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Conserved domains on  [gi|564388444|ref|XP_006252898|]
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unconventional myosin-IXb isoform X19 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-942 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


:

Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1337.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYL 319
Cdd:cd01385    81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385   161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARD 479
Cdd:cd01385   241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385   321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385   400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAeagvssp 719
Cdd:cd01385   480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  720 vtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknlldsks 799
Cdd:cd01385       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  800 lrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGM 879
Cdd:cd01385   553 -----SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388444  880 LETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01385   628 LETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
1659-1844 1.38e-127

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


The actual alignment was detected with superfamily member cd04407:

Pssm-ID: 445838 [Multi-domain]  Cd Length: 186  Bit Score: 397.83  E-value: 1.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRE 1738
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1739 LPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1818
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                         170       180
                  ....*....|....*....|....*.
gi 564388444 1819 PDNSDPLTSMKDVLKITTCVEMLIKE 1844
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
16-112 6.87e-53

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17217:

Pssm-ID: 452900  Cd Length: 96  Bit Score: 180.38  E-value: 6.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   16 TFHLHIYPQLpSAGSQTSCRVTATKDSTTSDVIRDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217     1 VYALQIYPQL-SAESSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                          90
                  ....*....|....*..
gi 564388444   96 QKEHPREDGYYFLLQER 112
Cdd:cd17217    80 QDDHPQSDGYYFLLQER 96
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1589-1646 1.77e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.77e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444 1589 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1646
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1001-1023 3.49e-05

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 42.31  E-value: 3.49e-05
                            10        20
                    ....*....|....*....|...
gi 564388444   1001 ERTRAAVYLQAAWRGYLQRQAYH 1023
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
Relaxase super family cl21589
Relaxase/Mobilisation nuclease domain; Relaxases/mobilisation proteins are required for the ...
953-1268 2.30e-04

Relaxase/Mobilisation nuclease domain; Relaxases/mobilisation proteins are required for the horizontal transfer of genetic information contained on plasmids that occurs during bacterial conjugation. The relaxase, in conjunction with several auxiliary proteins, forms the relaxation complex or relaxosome. Relaxases nick duplex DNA in a specific manner by catalyzing trans-esterification.


The actual alignment was detected with superfamily member PRK13863:

Pssm-ID: 451322 [Multi-domain]  Cd Length: 446  Bit Score: 46.09  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  953 LHGEVLRRILLLQSWFRmvLERRHfVQMKHAALTIQACWRSYRVRRTLERTRAAVylqaawRGYLQRQAYHHQrhsiirl 1032
Cdd:PRK13863  134 LHVVVNRRELLGHGWLK--ISRRH-PQLNYDALRIKMAEISLRHGIVLDATSRAE------RGITERPMTYAQ------- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1033 qslcrghlQRRsfsqmmLEKQKAEQAR------ETAGAEMSEGEPSP---VAAGEQPSEHPVEDPESLGVETETWMNSKS 1103
Cdd:PRK13863  198 --------YRR------LERQQANQIRfedadfEEFSPGEDHREPSQsfdTSPGEAPQGEPESAERPEKLQNESEVRLQE 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1104 PNGLSPKKEIP---SPEMETPAQ----KTVPAESHEKVPSSREKRESRRQRGLEHVERQNkhIQSCREENSTLREPSRKA 1176
Cdd:PRK13863  264 PAGSSIKADARirvSLESERRAQpsasKIPVADDFGIETSYVAEGDVRKLEGNSGTPRLA--TEVATHTTSERQQRRKRP 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1177 SLETGEsfPEDTKEPREDGLETWTETAApscpkQVPIVGDPPRSpSPLQRPASLDLDSRVSPVLPSSSLESPQD--EDKG 1254
Cdd:PRK13863  342 RDDEGE--PSGAKRTRLNGIAVGPEANA-----GEQDGRDDPIT-SPAQPPRSNPLADPVRASIATDSLPATADrqQQRE 413
                         330
                  ....*....|....
gi 564388444 1255 ENSTKVQDKPESPS 1268
Cdd:PRK13863  414 PSSKRPRDDDGEPS 427
PRK14950 super family cl36446
DNA polymerase III subunits gamma and tau; Provisional
1948-2063 6.39e-03

DNA polymerase III subunits gamma and tau; Provisional


The actual alignment was detected with superfamily member PRK14950:

Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1948 ASTESLLEERAVrgAAEGPPAPALPCPISPTPNPL-PAATAPPRGRPTSFVTVRVKTPRRTPIMPMANIKLPPGLPlhlt 2026
Cdd:PRK14950  354 AVIEALLVPVPA--PQPAKPTAAAPSPVRPTPAPStRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPES---- 427
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564388444 2027 swAPALQEAAVPV--KRREPPARRQDQVHSVYIAPGADL 2063
Cdd:PRK14950  428 --APKLTRAAIPVdeKPKYTPPAPPKEEEKALIADGDVL 464
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-942 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1337.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYL 319
Cdd:cd01385    81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385   161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARD 479
Cdd:cd01385   241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385   321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385   400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAeagvssp 719
Cdd:cd01385   480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  720 vtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknlldsks 799
Cdd:cd01385       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  800 lrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGM 879
Cdd:cd01385   553 -----SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388444  880 LETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01385   628 LETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
141-952 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 903.07  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    141 LPRPQADFDDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALAD 220
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    221 VAYYTMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKF 299
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    300 IQVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKH 379
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    380 DFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTI 459
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAS-TVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    460 TVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    620 YFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavl 698
Cdd:smart00242  475 HFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL------------------------ 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    699 reagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpWQGEDPRRllqslsrlqkprtff 778
Cdd:smart00242  531 ---------------------------------------------------------FPSGVSNA--------------- 538
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    779 lkskgikqkqiipknlldskslrliismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNA 858
Cdd:smart00242  539 -----------------------------------------GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNE 577
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    859 EKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC----REAIAALLEKLQVDRQNYQI 934
Cdd:smart00242  578 EKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWggdaKKACEALLQSLGLDEDEYQL 657
                           810
                    ....*....|....*...
gi 564388444    935 GKTKVFLKETERQALQER 952
Cdd:smart00242  658 GKTKVFLRPGQLAELEEL 675
Myosin_head pfam00063
Myosin head (motor domain);
149-942 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 689.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   149 DDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLR 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   229 KHVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVER---TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRleeQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   306 ESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQ 385
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKL 465
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKER--NDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGT 624
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHpHFQKPR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:pfam00063  476 LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL------------------------------ 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   705 raeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpWQGEDPRRLLQslsrlqkprtfFLKSKGI 784
Cdd:pfam00063  526 ---------------------------------------------------FPDYETAESAA-----------ANESGKS 543
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   785 KQKQIipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELC 864
Cdd:pfam00063  544 TPKRT-------------------------------KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGV 592
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   865 FDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVF 940
Cdd:pfam00063  593 FDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILapktWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIF 672

                   ..
gi 564388444   941 LK 942
Cdd:pfam00063  673 FR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
149-1044 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 661.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  149 DDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLR 228
Cdd:COG5022    69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLS 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTAL--SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:COG5022   149 EKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  307 SGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQ 386
Cdd:COG5022   229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLD 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKratGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLI 466
Cdd:COG5022   309 ALKTIGIDEEEQDQIFKILAAILHIGNIEFKE---DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIV 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:COG5022   386 VPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQ 460
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK-PTGLFYLLDEESNFPHATSHTLLAKFKQQ--HEDNKYFLG 623
Cdd:COG5022   461 FFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKK 540
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  624 TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagr 703
Cdd:COG5022   541 SRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKAST------------------------------------ 584
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  704 lraeraekaeagvsspvtrshveelprgantpseklyrdlhNQIIKSLkglpwqgedprrllqslsrlqkprtfFLKSKG 783
Cdd:COG5022   585 -----------------------------------------NEFVSTL--------------------------FDDEEN 597
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  784 IKqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 863
Cdd:COG5022   598 IE-----------------------------------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPW 642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  864 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP--------KDVQPCREAIAALLEKLQVDRQNYQIG 935
Cdd:COG5022   643 TFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPskswtgeyTWKEDTKNAVKSILEELVIDSSKYQIG 722
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  936 KTKVFLKeTERQALQERLHGEVLRRIL-LLQSWFRMVLERRHFVQMKHAALTIQACWRSYRVRRTLER---TRAAVYLQA 1011
Cdd:COG5022   723 NTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYelkWRLFIKLQP 801
                         890       900       910
                  ....*....|....*....|....*....|...
gi 564388444 1012 AWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 1044
Cdd:COG5022   802 LLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
PTZ00014 PTZ00014
myosin-A; Provisional
148-1017 7.70e-136

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 446.40  E-value: 7.70e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  148 FDDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYTM 226
Cdd:PTZ00014   98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  227 LRKHVNQCIVISGESGSGKTQSTNFLIhcltalsqKGYASGV--------ERTILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:PTZ00014  178 HGVKKSQTIIVSGESGAGKTEATKQIM--------RYFASSKsgnmdlkiQNAIMAANPVLEAFGNAKTIRNNNSSRFGR 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  299 FIQVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLK 378
Cdd:PTZ00014  250 FMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVK 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  379 hDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT-GRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTK 455
Cdd:PTZ00014  330 -DFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgGLTDAAAISDesLEVFNEACELLFLDYESLKKELTV 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  456 RKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQF 535
Cdd:PTZ00014  409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQL 483
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH 615
Cdd:PTZ00014  484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  616 EDNKYFLGTPV-LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraaira 694
Cdd:PTZ00014  564 KNNPKYKPAKVdSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF------------------- 624
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  695 MAVLREAGRLraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkp 774
Cdd:PTZ00014  625 EGVEVEKGKL---------------------------------------------------------------------- 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  775 rtfflkSKGikqkqiipkNLldskslrliismtlhdrttksllhlhkkkkppsISAQFQTSLNKLLEALGKAEPFFIRCI 854
Cdd:PTZ00014  635 ------AKG---------QL---------------------------------IGSQFLNQLDSLMSLINSTEPHFIRCI 666
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  855 RSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL-LP----KDVQPcREAIAALLEKLQVDR 929
Cdd:PTZ00014  667 KPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAvsndSSLDP-KEKAEKLLERSGLPK 745
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  930 QNYQIGKTKVFLKeteRQALQErlhgevLRRI--LLLQSWfrmvlerRHFVQMkhaaltIQACWRSYRVRRTL-ERTRAA 1006
Cdd:PTZ00014  746 DSYAIGKTMVFLK---KDAAKE------LTQIqrEKLAAW-------EPLVSV------LEALILKIKKKRKVrKNIKSL 803
                         890
                  ....*....|.
gi 564388444 1007 VYLQAAWRGYL 1017
Cdd:PTZ00014  804 VRIQAHLRRHL 814
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1659-1844 1.38e-127

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 397.83  E-value: 1.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRE 1738
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1739 LPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1818
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                         170       180
                  ....*....|....*....|....*.
gi 564388444 1819 PDNSDPLTSMKDVLKITTCVEMLIKE 1844
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1672-1845 2.01e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 199.41  E-value: 2.01e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   1672 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1750
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   1751 DFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1830
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159
                           170
                    ....*....|....*
gi 564388444   1831 VLKITTCVEMLIKEQ 1845
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1674-1823 6.43e-56

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 425782  Cd Length: 152  Bit Score: 191.25  E-value: 6.43e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  1674 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATV-KLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1752
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDSGEDVDlDLEEEDVHDVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388444  1753 LRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSD 1823
Cdd:pfam00620   81 IEAAKSEDEEERIEALRELLEKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPDSES 151
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 6.87e-53

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


Pssm-ID: 340737  Cd Length: 96  Bit Score: 180.38  E-value: 6.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   16 TFHLHIYPQLpSAGSQTSCRVTATKDSTTSDVIRDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217     1 VYALQIYPQL-SAESSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                          90
                  ....*....|....*..
gi 564388444   96 QKEHPREDGYYFLLQER 112
Cdd:cd17217    80 QDDHPQSDGYYFLLQER 96
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1589-1646 1.77e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.77e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444 1589 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1646
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-114 4.57e-16

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 75.06  E-value: 4.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    15 ATFHLHIYPQLPSAGSqTSCRVTATKDSTTSDVIRDVVASLHLDGSK-HYVLVEVKESGGEEWVLDASDSPVHRVLLWPr 93
Cdd:pfam00788    1 DDGVLKVYTEDGKPGT-TYKTILVSSSTTAEEVIEALLEKFGLEDDPrDYVLVEVLERGGGERRLPDDECPLQIQLQWP- 78
                           90       100
                   ....*....|....*....|.
gi 564388444    94 raqkehPREDGYYFLLQERNA 114
Cdd:pfam00788   79 ------RDASDSRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-113 7.03e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 71.56  E-value: 7.03e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444     15 ATFHLHIYPQLPSagSQTSCRVTATKDSTTSDVIRDVVASLHLDGS-KHYVLVEVKEsGGEEWVLDASDSPVHRVLLWPR 93
Cdd:smart00314    1 DTFVLRVYVDDLP--GGTYKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR 77
                            90       100
                    ....*....|....*....|
gi 564388444     94 raqkehpREDGYYFLLQERN 113
Cdd:smart00314   78 -------RGPNLRFVLRKRD 90
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1594-1642 1.96e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 1.96e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 564388444   1594 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1594-1642 2.18e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.36  E-value: 2.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564388444  1594 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1001-1023 3.49e-05

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 42.31  E-value: 3.49e-05
                            10        20
                    ....*....|....*....|...
gi 564388444   1001 ERTRAAVYLQAAWRGYLQRQAYH 1023
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
PRK13863 PRK13863
T-DNA border endonuclease VirD2;
953-1268 2.30e-04

T-DNA border endonuclease VirD2;


Pssm-ID: 237533 [Multi-domain]  Cd Length: 446  Bit Score: 46.09  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  953 LHGEVLRRILLLQSWFRmvLERRHfVQMKHAALTIQACWRSYRVRRTLERTRAAVylqaawRGYLQRQAYHHQrhsiirl 1032
Cdd:PRK13863  134 LHVVVNRRELLGHGWLK--ISRRH-PQLNYDALRIKMAEISLRHGIVLDATSRAE------RGITERPMTYAQ------- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1033 qslcrghlQRRsfsqmmLEKQKAEQAR------ETAGAEMSEGEPSP---VAAGEQPSEHPVEDPESLGVETETWMNSKS 1103
Cdd:PRK13863  198 --------YRR------LERQQANQIRfedadfEEFSPGEDHREPSQsfdTSPGEAPQGEPESAERPEKLQNESEVRLQE 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1104 PNGLSPKKEIP---SPEMETPAQ----KTVPAESHEKVPSSREKRESRRQRGLEHVERQNkhIQSCREENSTLREPSRKA 1176
Cdd:PRK13863  264 PAGSSIKADARirvSLESERRAQpsasKIPVADDFGIETSYVAEGDVRKLEGNSGTPRLA--TEVATHTTSERQQRRKRP 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1177 SLETGEsfPEDTKEPREDGLETWTETAApscpkQVPIVGDPPRSpSPLQRPASLDLDSRVSPVLPSSSLESPQD--EDKG 1254
Cdd:PRK13863  342 RDDEGE--PSGAKRTRLNGIAVGPEANA-----GEQDGRDDPIT-SPAQPPRSNPLADPVRASIATDSLPATADrqQQRE 413
                         330
                  ....*....|....
gi 564388444 1255 ENSTKVQDKPESPS 1268
Cdd:PRK13863  414 PSSKRPRDDDGEPS 427
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1003-1023 8.78e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 38.07  E-value: 8.78e-04
                           10        20
                   ....*....|....*....|.
gi 564388444  1003 TRAAVYLQAAWRGYLQRQAYH 1023
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1045-1295 2.44e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1045 FSQMMLEKQKAEQARETAGAEMSEGEPSPVAAGEQPSEHPVEDPESLGVETETWMNSKSPNGLSPKKEIPsPEMETPAQK 1124
Cdd:NF033839  275 FKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVK-PQLETPKPE 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1125 TVPAESHEKvPSSREKRESRRQRGLEHVERQNKHIQSCREENSTLREPSRKASLETGESFPEDTKEPREDGLETWTETAA 1204
Cdd:NF033839  354 VKPQPEKPK-PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVK 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1205 PSCPKQVPIVGDPPRSPSPLQRPASLDLDSRVSPVLPSSSLE-SPQDEDKGENSTKVQDKPESPSGSTQIQRYQHPDTER 1283
Cdd:NF033839  433 PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEvKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQA 512
                         250
                  ....*....|..
gi 564388444 1284 LATAVEIWRGKK 1295
Cdd:NF033839  513 STNEKATNKPKK 524
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
1948-2063 6.39e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1948 ASTESLLEERAVrgAAEGPPAPALPCPISPTPNPL-PAATAPPRGRPTSFVTVRVKTPRRTPIMPMANIKLPPGLPlhlt 2026
Cdd:PRK14950  354 AVIEALLVPVPA--PQPAKPTAAAPSPVRPTPAPStRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPES---- 427
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564388444 2027 swAPALQEAAVPV--KRREPPARRQDQVHSVYIAPGADL 2063
Cdd:PRK14950  428 --APKLTRAAIPVdeKPKYTPPAPPKEEEKALIADGDVL 464
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
979-998 7.03e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 7.03e-03
                            10        20
                    ....*....|....*....|
gi 564388444    979 QMKHAALTIQACWRSYRVRR 998
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARK 20
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-942 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1337.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYL 319
Cdd:cd01385    81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385   161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARD 479
Cdd:cd01385   241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385   321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385   400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAeagvssp 719
Cdd:cd01385   480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  720 vtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknlldsks 799
Cdd:cd01385       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  800 lrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGM 879
Cdd:cd01385   553 -----SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388444  880 LETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01385   628 LETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
141-952 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 903.07  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    141 LPRPQADFDDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALAD 220
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    221 VAYYTMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKF 299
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    300 IQVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKH 379
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    380 DFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTI 459
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAS-TVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    460 TVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    620 YFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavl 698
Cdd:smart00242  475 HFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL------------------------ 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    699 reagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpWQGEDPRRllqslsrlqkprtff 778
Cdd:smart00242  531 ---------------------------------------------------------FPSGVSNA--------------- 538
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    779 lkskgikqkqiipknlldskslrliismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNA 858
Cdd:smart00242  539 -----------------------------------------GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNE 577
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    859 EKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC----REAIAALLEKLQVDRQNYQI 934
Cdd:smart00242  578 EKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWggdaKKACEALLQSLGLDEDEYQL 657
                           810
                    ....*....|....*...
gi 564388444    935 GKTKVFLKETERQALQER 952
Cdd:smart00242  658 GKTKVFLRPGQLAELEEL 675
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
160-942 0e+00

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276950  Cd Length: 633  Bit Score: 785.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGK-LEPHVFALADVAYYTMLRKHVNQCIVIS 238
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSAdLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTALSQKG------YASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd00124    81 GESGAGKTETTKLVLKYLAALSGSGssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLN----QHNLNIEDGEDLKHDFERLQQAM 388
Cdd:cd00124   161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNdylnSSGCDRIDGVDDAEEFQELLDAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILP 468
Cdd:cd00124   241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd00124   321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDA---AESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLE 628
Cdd:cd00124   398 NQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  629 P-AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGsdssyvrqligmdpvavfrwavlraairamavlreagrlrae 707
Cdd:cd00124   478 KlEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS------------------------------------------ 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  708 raekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqk 787
Cdd:cd00124       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  788 qiipknlldskslrliismtlhdrttksllhlhkkkkppsiSAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDD 867
Cdd:cd00124   516 -----------------------------------------GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDP 554
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388444  868 ELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCR----EAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd00124   555 ELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASdskkAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
160-942 0e+00

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 704.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSqkGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYL 319
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAIS--GQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARD 479
Cdd:cd01381   239 DIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  480 SMAKSLYSALFDWIVLRINHALlnKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01381   319 AFVKGIYGRLFIWIVNKINSAI--YKPRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLgTP--VLEPAFIIQHFA 637
Cdd:cd01381   397 YDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL-KPksDLNTSFGINHFA 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavlraairamavlreagrlraeraekaeagvs 717
Cdd:cd01381   476 GVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFN----------------------------------------- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  718 spvtrshvEELPRGANTpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknllds 797
Cdd:cd01381   515 --------EDISMGSET--------------------------------------------------------------- 523
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  798 kslrliismtlhdrttksllhlhkKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYT 877
Cdd:cd01381   524 ------------------------RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYS 579
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  878 GMLETVRIRRSGYSAKYTFQDFTEQFQVLLPkDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01381   580 GMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIPPahktdCRAATRKICCAVLGGDADYQLGKTKIFLK 648
Myosin_head pfam00063
Myosin head (motor domain);
149-942 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 689.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   149 DDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLR 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   229 KHVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVER---TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRleeQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   306 ESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQ 385
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKL 465
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKER--NDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGT 624
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHpHFQKPR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:pfam00063  476 LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL------------------------------ 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   705 raeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpWQGEDPRRLLQslsrlqkprtfFLKSKGI 784
Cdd:pfam00063  526 ---------------------------------------------------FPDYETAESAA-----------ANESGKS 543
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   785 KQKQIipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELC 864
Cdd:pfam00063  544 TPKRT-------------------------------KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGV 592
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   865 FDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVF 940
Cdd:pfam00063  593 FDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILapktWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIF 672

                   ..
gi 564388444   941 LK 942
Cdd:pfam00063  673 FR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
149-1044 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 661.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  149 DDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLR 228
Cdd:COG5022    69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLS 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTAL--SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:COG5022   149 EKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  307 SGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQ 386
Cdd:COG5022   229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLD 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKratGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLI 466
Cdd:COG5022   309 ALKTIGIDEEEQDQIFKILAAILHIGNIEFKE---DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIV 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:COG5022   386 VPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQ 460
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK-PTGLFYLLDEESNFPHATSHTLLAKFKQQ--HEDNKYFLG 623
Cdd:COG5022   461 FFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKK 540
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  624 TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagr 703
Cdd:COG5022   541 SRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKAST------------------------------------ 584
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  704 lraeraekaeagvsspvtrshveelprgantpseklyrdlhNQIIKSLkglpwqgedprrllqslsrlqkprtfFLKSKG 783
Cdd:COG5022   585 -----------------------------------------NEFVSTL--------------------------FDDEEN 597
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  784 IKqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 863
Cdd:COG5022   598 IE-----------------------------------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPW 642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  864 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP--------KDVQPCREAIAALLEKLQVDRQNYQIG 935
Cdd:COG5022   643 TFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPskswtgeyTWKEDTKNAVKSILEELVIDSSKYQIG 722
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  936 KTKVFLKeTERQALQERLHGEVLRRIL-LLQSWFRMVLERRHFVQMKHAALTIQACWRSYRVRRTLER---TRAAVYLQA 1011
Cdd:COG5022   723 NTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYelkWRLFIKLQP 801
                         890       900       910
                  ....*....|....*....|....*....|...
gi 564388444 1012 AWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 1044
Cdd:COG5022   802 LLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
160-942 0e+00

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 645.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd01387     1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLESGIVRGAVVEKYL 319
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNQRRNNLVTEQ-ILEATPLLEAFGNAKTVRNDNSSRFGKYLEV-FFEGGVIVGAITSQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITAR 478
Cdd:cd01387   239 SIFRILASVLHLGNVYFHKRqLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDAR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  479 DSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd01387   319 DAIAKALYALLFSWLVTRVNAIVYSGTQ-----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  559 EYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAG 638
Cdd:cd01387   394 EYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAG 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  639 RVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraekaeagvSS 718
Cdd:cd01387   474 QVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHL------------------------------------------FS 511
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  719 PVTRSHVEELPRGANTPSEKLyrdlhnqiikslkglpwqgedprrllqslsrlqKPRTfflkskgikqkqiipknlldsk 798
Cdd:cd01387   512 SHRAQTDKAPPRLGKGRFVTM---------------------------------KPRT---------------------- 536
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  799 slrliismtlhdrttksllhlhkkkkpPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTG 878
Cdd:cd01387   537 ---------------------------PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSG 589
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  879 MLETVRIRRSGYSAKYTFQDFTEQFQVLL------PKDVQPCREAIAALLEklQVDRQNYQIGKTKVFLK 942
Cdd:cd01387   590 MLETIRIRKEGYPVRLPFQVFIDRYRCLValklprPAPGDMCVSLLSRLCT--VTPKDMYRLGATKVFLR 657
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
162-942 0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 636.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14883     3 INTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKgyASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYLLE 321
Cdd:cd14883    83 GAGKTETTKLILQYLCAVTNN--HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  322 KSRLVSQEKDERNYHVFYYLLLG--VSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd14883   161 QSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTYKKrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARD 479
Cdd:cd14883   241 GIFSVLSAILHLGNLTFED-IDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  480 SMAKSLYSALFDWIVLRINhallnkkdmeeavSCLS--------IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14883   320 AMAKALYSRTFAWLVNHIN-------------SCTNpgqknsrfIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHY 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFL-GTPVL-EP 629
Cdd:cd14883   387 VFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEkPDRRRwKT 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  630 AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraera 709
Cdd:cd14883   467 EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELF---------------------------------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  710 ekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgeDPRRLLqslsrlqkprtfflkskGIKQKQI 789
Cdd:cd14883   513 --------------------------------------------------TYPDLL-----------------ALTGLSI 525
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  790 IPKNLLDSKSlrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDEL 869
Cdd:cd14883   526 SLGGDTTSRG---------------------TSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDEL 584
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388444  870 VLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK--DVQPCREAIA--ALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14883   585 VLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRarSADHKETCGAvrALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
163-942 0e+00

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 624.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  163 LQSLKLRFVQQK-IYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd01380     4 LHNLKVRFCQRNaIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYLL 320
Cdd:cd01380    84 GAGKTVSAKYAMRYFATVGgSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  321 EKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQ 400
Cdd:cd01380   164 EKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  401 IFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARD 479
Cdd:cd01380   244 IFRILAAILHLGNVEIKAT---RNDSASISPDDEhLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  480 SMAKSLYSALFDWIVLRINHALLNKKDmEEAVSClsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASPVK-EKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  560 YQGEGISWHNIDYTDNVGCIHLISKKPtGLFYLLDEESNFPHATSHTLLAKFKQQHE--DNKYFLGTPVLEPAFIIQHFA 637
Cdd:cd01380   398 YVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLkkPNKHFKKPRFSNTAFIVKHFA 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraairamavlreagrlraeraekaeagvs 717
Cdd:cd01380   477 DDVEYQVEGFLEKNRDTVSEEHLNVLKASKN------------------------------------------------- 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  718 spvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknllds 797
Cdd:cd01380       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  798 kslrliismtlhdrttksllhlHKkkkpPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYT 877
Cdd:cd01380   508 ----------------------RK----KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRAC 561
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444  878 GMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDV---QPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01380   562 GVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEwlrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
162-942 0e+00

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276834  Cd Length: 647  Bit Score: 610.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYenQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd01383     3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSqkGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYLLE 321
Cdd:cd01383    81 GAGKTETAKIAMQYLAALG--GGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  322 KSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQI 401
Cdd:cd01383   159 KSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  402 FSVLSAILYLGNVTYKkrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDSM 481
Cdd:cd01383   239 FQMLAAVLWLGNISFQ--VIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDAL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  482 AKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQ 561
Cdd:cd01383   317 AKAIYASLFDWLVEQINKSL----EVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  562 GEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPvlEPAFIIQHFAGRVK 641
Cdd:cd01383   393 LDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGEVT 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  642 YQIKDFREKNMDYMRPDIVALLrGSDSSYVRQLIGmdpvavfrwAVLRAAIRAMAVLREAgrlraeraekaeagvsspvt 721
Cdd:cd01383   471 YDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFA---------SKMLDASRKALPLTKA-------------------- 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  722 rshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkSKGIKQKQiipknlldskslr 801
Cdd:cd01383   521 -----------------------------------------------------------SGSDSQKQ------------- 528
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  802 liismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLE 881
Cdd:cd01383   529 -------------------------SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLE 583
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444  882 TVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIA---ALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01383   584 VVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLStsvAILQQFNILPEMYQVGYTKLFFR 647
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
162-942 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 610.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd01379     3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKGYASgVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYLLE 321
Cdd:cd01379    83 GAGKTESANLLVQQLTVLGKANNRT-LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  322 KSRLVSQEKDERNYHVFYYLLLGVSEEER-QEFQLKQPQDYFYLNQHNLNIEDGEDL---KHDFERLQQAMEMVGFLPAT 397
Cdd:cd01379   162 KSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNsgnREKFEEIEQCFKVIGFTKEE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  398 KKQIFSVLSAILYLGNVTYKKRATG--RDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAI 475
Cdd:cd01379   242 VDSVYSILAAILHIGDIEFTEVESNhqTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEAT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  476 TARDSMAKSLYSALFDWIVLRINhALLnKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd01379   322 DARDAMAKALYGRLFSWIVNRIN-SLL-KPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAW 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  556 EQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFkqqhEDN---KYFLGTPVLEPAFI 632
Cdd:cd01379   400 EQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKF----HNNiksKYYWRPKSNALSFG 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQligmdpvavfrwavlraairamavlreagrlraeraeka 712
Cdd:cd01379   476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------------------------------- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  713 eagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipk 792
Cdd:cd01379       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  793 nlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQ 872
Cdd:cd01379   517 ----------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLK 562
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388444  873 QLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---LPKDVQPCREAIAALLEKLQVDrqNYQIGKTKVFLK 942
Cdd:cd01379   563 QLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLafkWNEEVVANRENCRLILERLKLD--NWALGKTKVFLK 633
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
160-942 0e+00

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 602.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVIS 238
Cdd:cd14873     1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTALSQ-------KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVR 311
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVISQqslelslKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMV 391
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  392 GFLPATKKQIFSVLSAILYLGNVTYKKRAtgrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSL 471
Cdd:cd14873   241 QFSKEEVREVSRLLAGILHLGNIEFITAG-----GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  472 SEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14873   316 QQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK------SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAF 631
Cdd:cd14873   390 IFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKK-LGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNF 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  632 IIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraeraEK 711
Cdd:cd14873   469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF----------------------------------EH 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  712 aeagVSSpvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiip 791
Cdd:cd14873   515 ----VSS------------------------------------------------------------------------- 517
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  792 knlldskslrliismtlhdRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVL 871
Cdd:cd14873   518 -------------------RNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVL 578
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388444  872 QQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP--KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14873   579 NQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnlALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
166-942 0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 586.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  166 LKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGESGSGK 245
Cdd:cd01378     7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  246 TQSTNFLIHCLTALSQKGYAS--GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYLLEKS 323
Cdd:cd01378    87 TEASKRIMQYIAAVSGGSESEveRVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  324 RLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQIFS 403
Cdd:cd01378   167 RVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFR 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  404 VLSAILYLGNVTYKKRATGrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDK---LILPYSLSEAITARDS 480
Cdd:cd01378   247 ILAAILHLGNIQFAEDEEG---NAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAYARDA 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  481 MAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEY 560
Cdd:cd01378   324 LAKAIYSRLFDWIVERINKSLAAKSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  561 QGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPH-ATSHTLLAKFKQQHEDNKYFLGTP----VLEPAFIIQH 635
Cdd:cd01378   400 VREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFECPSghfeLRRGEFRIKH 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  636 FAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraekaeag 715
Cdd:cd01378   480 YAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSL----------------------------------------- 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  716 vsspvtrshveeLPRGANTPSeklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknll 795
Cdd:cd01378   519 ------------FPEGVDLDS----------------------------------------------------------- 527
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  796 dskslrliismtlhdrttksllhlhkKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLR 875
Cdd:cd01378   528 --------------------------KKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVK 581
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444  876 YTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-------DVQpcrEAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01378   582 YLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKtwpawdgTWQ---GGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
163-942 0e+00

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.


Pssm-ID: 276835  Cd Length: 647  Bit Score: 582.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  163 LQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd01384     4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKGYASG--VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYL 319
Cdd:cd01384    84 GAGKTETTKMLMQYLAYMGGRAVTEGrsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01384   164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEEEQD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEV---LDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAIT 476
Cdd:cd01384   244 AIFRVVAAILHLGNIEFSKGE--EDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  477 ARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd01384   322 SRDALAKTIYSRLFDWLVDKINRSIGQDPN-----SKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKME 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFlGTPVLEP-AFIIQH 635
Cdd:cd01384   397 QEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRF-SKPKLSRtDFTIDH 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  636 FAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraeraekaeag 715
Cdd:cd01384   476 YAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF---------------------------------------- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  716 vsspvtrshvEELPRGANTPSEKLyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknll 795
Cdd:cd01384   516 ----------PPLPREGTSSSSKF-------------------------------------------------------- 529
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  796 dskslrliismtlhdrttksllhlhkkkkpPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLR 875
Cdd:cd01384   530 ------------------------------SSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLR 579
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  876 YTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KDVQPCREAIAALLEKLQVdrQNYQIGKTKVFLK 942
Cdd:cd01384   580 CGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPevlKGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
160-942 0e+00

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 580.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd01377     1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQST----NFLIHCLTALSQKGYASG----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVR 311
Cdd:cd01377    81 ESGAGKTENTkkviQYLASVAASSKKKKESGKkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQ-PQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEM 390
Cdd:cd01377   161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVDD-AEEFKLTDEAFDI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  391 VGFLPATKKQIFSVLSAILYLGNVTYKKRatGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTK------RKTITVNdk 464
Cdd:cd01377   240 LGFSEEEKMSIFKIVAAILHLGNIKFKQR--RREEQAELDGTEEADKAAHLLGVNSSDLLKALLKprikvgREWVTKG-- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  465 lilpYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQL 544
Cdd:cd01377   316 ----QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQ-----YFIGVLDIAGFEIFEFNSFEQLCINYTNEKL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  545 QYYFTQHIFKLEQEEYQGEGISWHNIDYtdnvG-----CIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:cd01377   387 QQFFNHHMFVLEQEEYKKEGIEWTFIDF----GldlqpTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKS 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  620 YFLGTPV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairama 696
Cdd:cd01377   463 KNFKKPKpkkSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLF--------------------- 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  697 vlreagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgEDPRRLLQSLSRLQKPRT 776
Cdd:cd01377   522 --------------------------------------------------------------KDYEESGGGGGKKKKKGG 539
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  777 FFlkskgikqkqiipknlldskslrliismtlhdRTtksllhlhkkkkppsISAQFQTSLNKLLEALGKAEPFFIRCIRS 856
Cdd:cd01377   540 SF--------------------------------RT---------------VSQLHKEQLNKLMTTLRSTHPHFVRCIIP 572
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  857 NAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC----REAIAALLEKLQVDRQNY 932
Cdd:cd01377   573 NEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGfddgKAACEKILKALQLDPELY 652
                         810
                  ....*....|
gi 564388444  933 QIGKTKVFLK 942
Cdd:cd01377   653 RIGNTKVFFK 662
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
160-942 2.43e-166

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276862 [Multi-domain]  Cd Length: 635  Bit Score: 524.64  E-value: 2.43e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQL-GKLEPHVFALADVAYYTMLRKHVNQCIVIS 238
Cdd:cd14897     1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKY 318
Cdd:cd14897    81 GESGAGKTESTKYMIKHLMKLSPSDDSDLLDK-IVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYL---NQHNLNIEDGEDLKHD---FERLQQAMEMVG 392
Cdd:cd14897   160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrddNRNRPVFNDSEELEYYrqmFHDLTNIMKLIG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  393 FLPATKKQIFSVLSAILYLGNVTYKKraTGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLS 472
Cdd:cd14897   240 FSEEDISVIFTILAAILHLTNIVFIP--DEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  473 EAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHI 552
Cdd:cd14897   318 QANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  553 FKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFI 632
Cdd:cd14897   398 FPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRVAFG 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagrlraeraeka 712
Cdd:cd14897   478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSN--------------------------------------------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  713 eagvsspvtrshveelprgantpseklyrdlhNQIIKSLkglpwqgedprrllqslsrlqkprtfFLKskgikqkqiipk 792
Cdd:cd14897   513 --------------------------------NEFISDL--------------------------FTS------------ 522
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  793 nlldskslrliismtlhdrttksllhlhkkkkppsisaQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQ 872
Cdd:cd14897   523 --------------------------------------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRR 564
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388444  873 QLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKdvqpCREAIAALLEKLQV-----DRQNYQIGKTKVFLK 942
Cdd:cd14897   565 QLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF----SNKVRSDDLGKCQKilktaGIKGYQFGKTKVFLK 635
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
162-942 6.20e-163

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 516.38  E-value: 6.20e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTML----RKHVNQCIVI 237
Cdd:cd14889     3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  238 SGESGSGKTQSTNFLIHCLTALSQKGyaSGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYlESGIVRGAVVEK 317
Cdd:cd14889    83 SGESGAGKTESTKLLLRQIMELCRGN--SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  318 YLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPAT 397
Cdd:cd14889   160 YLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  398 KKQIFSVLSAILYLGNVTYKKRATG--RDEGLEVGPpevLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAI 475
Cdd:cd14889   240 EVDMFTILAGILSLGNITFEMDDDEalKVENDSNGW---LKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  476 TARDSMAKSLYSALFDWIVLRINHALLNKKDMEeaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd14889   317 DARDSIAKVAYGRVFGWIVSKINQLLAPKDDSS--VELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLM 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  556 EQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQH 635
Cdd:cd14889   395 EQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVNH 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  636 FAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraAIRAMAVLREAGRLRaeraekaeag 715
Cdd:cd14889   475 YAGKVTYNASGFLEKNRDTIPASIRTLFINS------------------------ATPLLSVLFTATRSR---------- 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  716 vsspvtrshveelpRGANTPSEKlyrdlhnqiikslkgLPWQGEDprrllqslsrlqkprtfflkSKGIKQKQiipknll 795
Cdd:cd14889   521 --------------TGTLMPRAK---------------LPQAGSD--------------------NFNSTRKQ------- 544
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  796 dskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLR 875
Cdd:cd14889   545 -------------------------------SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLR 593
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444  876 YTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-DVQPCREAIAALLEKLQVdrQNYQIGKTKVFLK 942
Cdd:cd14889   594 YNGLLETIRIRREGFSWRPSFAEFAERYKILLCEpALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
160-942 5.05e-161

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 511.50  E-value: 5.05e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQ--------QLGKLEPHVFALADVAYYTMLRKH 230
Cdd:cd14907     1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  231 VNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYAS------------------GVERTILGAGPVLEAFGNAKTAHNNN 292
Cdd:cd14907    81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSeevltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  293 SSRFGKF--IQVNyLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQP--QD-YFYLNQ- 366
Cdd:cd14907   161 SSRFGKYvsILVD-KKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQlsGDrYDYLKKs 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  367 --HNLNIEDGEDLkhdFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKV 444
Cdd:cd14907   240 ncYEVDTINDEKL---FKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLLGI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  445 KRETLVEVLTKRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNK---KDMEEAVSCLSIGVLDI 521
Cdd:cd14907   317 DEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKdekDQQLFQNKYLSIGLLDI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  522 FGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWH--NIDYTDNVGCIHLISKKPTGLFYLLDEESNF 599
Cdd:cd14907   397 FGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYlnQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  600 PHATSHTLLAKFKQQHEDNKYFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmd 678
Cdd:cd14907   477 ATGTDEKLLNKIKKQHKNNSKLIFPNKInKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSK----------- 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  679 pvavfrwavlraairamavlreagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhNQIIKSLkglpWQG 758
Cdd:cd14907   546 ------------------------------------------------------------------NRIISSI----FSG 555
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  759 EDprrllQSLSRLQKPrtfflkskgIKQKQiipknlldskslrliismtlhdrttksllhlhKKKKppSISAQFQTSLNK 838
Cdd:cd14907   556 ED-----GSQQQNQSK---------QKKSQ--------------------------------KKDK--FLGSKFRNQMKQ 587
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  839 LLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLlpkdvqpcreai 918
Cdd:cd14907   588 LMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL------------ 655
                         810       820
                  ....*....|....*....|....
gi 564388444  919 aalleklqvdRQNYQIGKTKVFLK 942
Cdd:cd14907   656 ----------KKNVLFGKTKIFMK 669
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
160-942 3.89e-159

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 505.63  E-value: 3.89e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVIS 238
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTAlSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKY 318
Cdd:cd01382    81 GESGAGKTESTKYILRYLTE-SWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFqLKQPQdyfyLNQHNlniedgedlkhDFERLQQAMEMVGFLPATK 398
Cdd:cd01382   160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDPL----LDDVG-----------DFIRMDKAMKKIGLSDEEK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  399 KQIFSVLSAILYLGNVTYKKRATGRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTKRKTIT----VNDKLIL-PYSL 471
Cdd:cd01382   224 LDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPksEQSLEYAAELLGLDQDELRVSLTTRVMQTtrggAKGTVIKvPLKV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  472 SEAITARDSMAKSLYSALFDWIVLRINHALLNKKdmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd01382   304 EEANNARDALAKAIYSKLFDHIVNRINQCIPFET------SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNER 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNkYFLGTPVL---- 627
Cdd:cd01382   378 ILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKsklk 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  628 -------EPAFIIQHFAGRVKYQIKDFREKNMDymrpdivallrgsdssyvrqligmdpvavfrwavlraairamavlre 700
Cdd:cd01382   457 ihrnlrdDEGFLIRHFAGAVCYETAQFIEKNND----------------------------------------------- 489
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  701 agrlraeraekaeagvsspvtrshveelprgantpseklyrDLHNqiikSLKGLPWQGEDPrrLLQSLSRLQKPrtfflK 780
Cdd:cd01382   490 -----------------------------------------ALHA----SLESLICESKDK--FIRSLFESSTN-----N 517
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  781 SKGIKQKqiipknlldSKSLRLIismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEK 860
Cdd:cd01382   518 NKDSKQK---------AGKLSFI-----------------------SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKM 565
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  861 KELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDV---QP---CReaiaALLEKLQVDRQNYQI 934
Cdd:cd01382   566 TSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLarlDPrlfCK----ALFKALGLNENDFKF 641

                  ....*...
gi 564388444  935 GKTKVFLK 942
Cdd:cd01382   642 GLTKVFFR 649
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
160-939 7.31e-155

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276839  Cd Length: 644  Bit Score: 493.52  E-value: 7.31e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14872     1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNfliHCLTALSQ-KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKY 318
Cdd:cd14872    81 ESGAGKTEATK---QCLSFFAEvAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQhNLNIEdGEDLKHDFERLQQAMEMVGFLPATK 398
Cdd:cd14872   158 LLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLSG-CIEVE-GVDDVADFEEVVLAMEQLGFDDADI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  399 KQIFSVLSAILYLGNVTYKKRATGRD-EGLEVGPPEVLDTLSQLLKVKRETLVEVLT-KRKTITVNDKLILPYSLSEAIT 476
Cdd:cd14872   236 NNVMSLIAAILKLGNIEFASGGGKSLvSGSTVANRDVLKEVATLLGVDAATLEEALTsRLMEIKGCDPTRIPLTPAQATD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  477 ARDSMAKSLYSALFDWIVLRINHALlnkKDMEEAVSCLsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd14872   316 ACDALAKAAYSRLFDWLVKKINESM---RPQKGAKTTF-IGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL--EPAFIIQ 634
Cdd:cd14872   392 EALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRtsRTEFIVK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  635 HFAGRVKYQIKDFREKNMDymrpdivallrgsdssyvrqligmdpvavfrwavlraairamavlreagrlraeraekaea 714
Cdd:cd14872   472 HYAGDVTYDITGFLEKNKD------------------------------------------------------------- 490
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  715 gvsspvtrshveelprgantpseKLYRDLHnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipkNL 794
Cdd:cd14872   491 -----------------------TLQKDLY------------------------------------------------VL 499
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  795 LDSKSLRLIISMtlhdrttKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQL 874
Cdd:cd14872   500 LSSSKNKLIAVL-------FPPSEGDQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQL 572
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388444  875 RYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL-------PKDVqpcREAIAALLEKLQVDRQNYQIGKTKV 939
Cdd:cd14872   573 RYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVktiakrvGPDD---RQRCDLLLKSLKQDFSKVQVGKTRV 641
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
160-942 1.82e-152

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 487.36  E-value: 1.82e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHV----NQC 234
Cdd:cd14890     1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGVldpsNQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  235 IVISGESGSGKTQSTNFLIHCL---TALSQKGYASG--------------VERTILGAGPVLEAFGNAKTAHNNNSSRFG 297
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLariTSGFAQGASGEgeaaseaieqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  298 KFIQVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLnQHNLNIEDGEDL 377
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  378 KHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkrATGRDEGLE-VGPPEVLDTLSQLLKVKRETLVEVLTKR 456
Cdd:cd14890   240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFE--SENDTTVLEdATTLQSLKLAAELLGVNEDALEKALLTR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  457 kTITVNDKLIL-PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQF 535
Cdd:cd14890   318 -QLFVGGKTIVqPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWG-----FIGVLDIYGFEKFEWNTFEQL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPT---GLFYLLD-------EESNfphatsH 605
Cdd:cd14890   392 CINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgkpGIFITLDdcwrfkgEEAN------K 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  606 TLLAKFKQQH-------------EDNKYFLgTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSy 670
Cdd:cd14890   466 KFVSQLHASFgrksgsggtrrgsSQHPHFV-HPKFDADkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRS- 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  671 vrqligmdpvavfrwavlraairamavLREAgrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiiks 750
Cdd:cd14890   544 ---------------------------IREV------------------------------------------------- 547
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  751 lkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISA 830
Cdd:cd14890   548 ----------------------------------------------------------------------------SVGA 551
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  831 QFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPkD 910
Cdd:cd14890   552 QFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLP-T 630
                         810       820       830
                  ....*....|....*....|....*....|..
gi 564388444  911 VQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14890   631 AENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
160-942 3.64e-152

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 486.89  E-value: 3.64e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPiynpkyvKMYENQQLGKL-------EPHVFALADVAYYTMLRKHVN 232
Cdd:cd14888     1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIP-------GLYSDEMLLKFiqpsiskSPHVFSTASSAYQGMCNNKKS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  233 QCIVISGESGSGKTQSTNF---LIHCLTALSQKGYaSGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGI 309
Cdd:cd14888    74 QTILISGESGAGKTESTKYvmkFLACAGSEDIKKR-SLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  310 VR---------GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSE--------EERQE--------------FQLKQP 358
Cdd:cd14888   153 KRmsgdrgrlcGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREakntglsyEENDEklakgadakpisidMSSFEP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  359 QDYF-YLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtGRDEG--LEVGPPEVL 435
Cdd:cd14888   233 HLKFrYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNE-ACSEGavVSASCTDDL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  436 DTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMeeavSCLS 515
Cdd:cd14888   312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDN----SLLF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  516 IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDE 595
Cdd:cd14888   388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  596 ESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLI 675
Cdd:cd14888   468 ECFVPGGKDQGLCNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  676 gmdpvavfrwavlraairamavlreagrlraeraekaeagvsSPVTRSHVEelprgANTpseklyrdlhnqiikslkglp 755
Cdd:cd14888   548 ------------------------------------------SAYLRRGTD-----GNT--------------------- 559
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  756 wqgedprrllqslsrlqkprtfflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTS 835
Cdd:cd14888   560 -----------------------------------------------------------------KKKKFVTVSSEFRNQ 574
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  836 LNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDvqpcr 915
Cdd:cd14888   575 LDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGE----- 649
                         810       820
                  ....*....|....*....|....*..
gi 564388444  916 eaiaallEKLQVdrQNYQIGKTKVFLK 942
Cdd:cd14888   650 -------GKKQL--SIWAVGKTLCFFK 667
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
160-941 5.87e-149

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 477.36  E-value: 5.87e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYN----PKYVKMYENQQLG--KLEPHVFALADVAYYTMLRKHV-- 231
Cdd:cd14901     1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDdetkEAYYEHGERRAAGerKLPPHVYAVADKAFRAMLFASRgq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  232 --NQCIVISGESGSGKTQSTNFLIHCLTALS--QKGYASGVERT-----ILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 302
Cdd:cd14901    81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsaTTHGQNATEREnvrdrVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  303 NYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNI-EDGEDLKHDF 381
Cdd:cd14901   161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITV 461
Cdd:cd14901   241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVK-KDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  462 NDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALlnkKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYAN 541
Cdd:cd14901   320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESI---AYSESTGASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  542 EQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14901   397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASF 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  622 lGTPVLEPA---FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVrqligmdpvavfrwavlraairamavl 698
Cdd:cd14901   477 -SVSKLQQGkrqFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL--------------------------- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  699 reagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtff 778
Cdd:cd14901       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  779 lkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNA 858
Cdd:cd14901   529 ----------------------------------------------SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPND 562
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  859 EKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KDVQPCREAIAALLEKLQV------DR 929
Cdd:cd14901   563 VLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPdgaSDTWKVNELAERLMSQLQHselnieHL 642
                         810
                  ....*....|..
gi 564388444  930 QNYQIGKTKVFL 941
Cdd:cd14901   643 PPFQVGKTKVFL 654
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
160-942 3.16e-146

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 470.01  E-value: 3.16e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYN-PKYVKMYENQQLGKL-EPHVFALADVAYYTMLR----KHVN 232
Cdd:cd14892     1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKEEATASSpPPHVFSIAERAYRAMKGvgkgQGTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  233 QCIVISGESGSGKTQSTNFLIHCLTALSQ-----------KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14892    81 QSIVVSGESGAGKTEASKYIMKYLATASKlakgastskgaANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  302 VNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDF 381
Cdd:cd14892   161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITV 461
Cdd:cd14892   241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  462 NDK-LILPYSLSEAITARDSMAKSLYSALFDWIVLRINHA------LLNKKDMEEAVSCLsIGVLDIFGFEDFERNSFEQ 534
Cdd:cd14892   321 RGSvLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsGVTGGAASPTFSPF-IGILDIFGFEIMPTNSFEQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  535 FCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATS-HTLLAKFKQ 613
Cdd:cd14892   400 LCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTdKQLLTIYHQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  614 QHEDNKYFLGTPVLE-PAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGsdssyvrqligmdpvavfrwavlraai 692
Cdd:cd14892   480 THLDKHPHYAKPRFEcDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRS--------------------------- 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  693 ramavlreagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlq 772
Cdd:cd14892       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  773 kprtfflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsiSAQFQTSLNKLLEALGKAEPFFIR 852
Cdd:cd14892   533 --------------------------------------------------------SSKFRTQLAELMEVLWSTTPSYIK 556
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  853 CIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL-----------PKDVQPCREAIAAL 921
Cdd:cd14892   557 CIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvaaspdACDATTARKKCEEI 636
                         810       820
                  ....*....|....*....|.
gi 564388444  922 LEKlQVDRQNYQIGKTKVFLK 942
Cdd:cd14892   637 VAR-ALERENFQLGRTKVFLR 656
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
160-942 6.48e-144

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 463.48  E-value: 6.48e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVIS 238
Cdd:cd14903     1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTALsqkgyASGVE----RTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAV 314
Cdd:cd14903    81 GESGAGKTETTKILMNHLATI-----AGGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  315 VEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERqeFQLKQPQDYFYLNQH-NLNIEDGEDLKHdFERLQQAMEMVGF 393
Cdd:cd14903   156 CRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTGANkTIKIEGMSDRKH-FARTKEALSLIGV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  394 LPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSE 473
Cdd:cd14903   233 SEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  474 AITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIF 553
Cdd:cd14903   313 AEDCRDALAKAIYSNVFDWLVATINASLGNDAKMAN-----HIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  554 KLEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA-FI 632
Cdd:cd14903   388 KTVQIEYEEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTqFT 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavLRAAIRAmAVLREAGRLRAERAEKA 712
Cdd:cd14903   467 IKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK-----------EKVESPA-AASTSLARGARRRRGGA 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  713 eagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipk 792
Cdd:cd14903       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  793 nlldskslrliismtLHDRTtksllhlhkkkkppsISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQ 872
Cdd:cd14903   535 ---------------LTTTT---------------VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVS 584
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444  873 QLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KDVQPCREAIAALLEKLQVDR-QNYQIGKTKVFLK 942
Cdd:cd14903   585 QLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPegrNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
163-942 1.05e-142

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 459.63  E-value: 1.05e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  163 LQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGESG 242
Cdd:cd14896     4 LLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGHSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  243 SGKTQSTNFLIHCLTALSQKGyASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLESGIVRGAVVEKYLLEK 322
Cdd:cd14896    84 SGKTEAAKKIVQFLSSLYQDQ-TEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRL-HLQHGVIVGASVSHYLLET 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  323 SRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQIF 402
Cdd:cd14896   162 SRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIW 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  403 SVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDSMA 482
Cdd:cd14896   242 AVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDARDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  483 KSLYSALFDWIVLRINhALLNKKDMEEAVSclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQG 562
Cdd:cd14896   322 KTLYSRLFTWLLKRIN-AWLAPPGEAESDA--TIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  563 EGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKY 642
Cdd:cd14896   399 ELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAGTVTY 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  643 QIKDFREKNMDYMRPDIVALLrgsdssyvrqligmdpvavfrwavlraairamavlreagrlraeraekaeagvsspvtr 722
Cdd:cd14896   479 QVHKFLNRNRDQLDPAVVEML----------------------------------------------------------- 499
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  723 shveelprgantpseklyrdlhnqiikslkglpwqgedprrllqSLSRLQKPRTFFLKSKgikqkqiipknlldSKSlrl 802
Cdd:cd14896   500 --------------------------------------------AQSQLQLVGSLFQEAE--------------PQY--- 518
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  803 iismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLET 882
Cdd:cd14896   519 -----------------GLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEA 581
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444  883 VRIRRSGYSAKYTFQDFTEQFQVLLpKDVQPC---REAIAALLEK-LQVDRQNYQIGKTKVFLK 942
Cdd:cd14896   582 IGTRSEGFPVRVPFQAFLARFGALG-SERQEAlsdRERCGAILSQvLGAESPLYHLGATKVLLK 644
PTZ00014 PTZ00014
myosin-A; Provisional
148-1017 7.70e-136

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 446.40  E-value: 7.70e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  148 FDDLCNLPELNEANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYTM 226
Cdd:PTZ00014   98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  227 LRKHVNQCIVISGESGSGKTQSTNFLIhcltalsqKGYASGV--------ERTILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:PTZ00014  178 HGVKKSQTIIVSGESGAGKTEATKQIM--------RYFASSKsgnmdlkiQNAIMAANPVLEAFGNAKTIRNNNSSRFGR 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  299 FIQVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLK 378
Cdd:PTZ00014  250 FMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVK 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  379 hDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT-GRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTK 455
Cdd:PTZ00014  330 -DFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgGLTDAAAISDesLEVFNEACELLFLDYESLKKELTV 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  456 RKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQF 535
Cdd:PTZ00014  409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQL 483
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH 615
Cdd:PTZ00014  484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  616 EDNKYFLGTPV-LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraaira 694
Cdd:PTZ00014  564 KNNPKYKPAKVdSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF------------------- 624
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  695 MAVLREAGRLraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkp 774
Cdd:PTZ00014  625 EGVEVEKGKL---------------------------------------------------------------------- 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  775 rtfflkSKGikqkqiipkNLldskslrliismtlhdrttksllhlhkkkkppsISAQFQTSLNKLLEALGKAEPFFIRCI 854
Cdd:PTZ00014  635 ------AKG---------QL---------------------------------IGSQFLNQLDSLMSLINSTEPHFIRCI 666
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  855 RSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL-LP----KDVQPcREAIAALLEKLQVDR 929
Cdd:PTZ00014  667 KPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAvsndSSLDP-KEKAEKLLERSGLPK 745
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  930 QNYQIGKTKVFLKeteRQALQErlhgevLRRI--LLLQSWfrmvlerRHFVQMkhaaltIQACWRSYRVRRTL-ERTRAA 1006
Cdd:PTZ00014  746 DSYAIGKTMVFLK---KDAAKE------LTQIqrEKLAAW-------EPLVSV------LEALILKIKKKRKVrKNIKSL 803
                         890
                  ....*....|.
gi 564388444 1007 VYLQAAWRGYL 1017
Cdd:PTZ00014  804 VRIQAHLRRHL 814
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
160-942 5.49e-135

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276856  Cd Length: 645  Bit Score: 437.94  E-value: 5.49e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFV--QQKIYTYAGSILVAINPFKFLPiyNPKyVKMYENQQLGKLEPHVFALADVAYYTM-LRKHV--NQC 234
Cdd:cd14891     1 AGILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPD-KSDYINTPLDPCPPHPYAIAEMAYQQMcLGSGRmqNQS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  235 IVISGESGSGKTQSTNFLIHCLT-----------------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFG 297
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFLTtravggkkasgqdieqsSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  298 KFIQVNYLESGI-VRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGED 376
Cdd:cd14891   158 KFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  377 LKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT--GRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLT 454
Cdd:cd14891   238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTseGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  455 KRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFER-NSFE 533
Cdd:cd14891   318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-----PLPYIGVLDIFGFESFETkNDFE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  534 QFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQ 613
Cdd:cd14891   393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHK 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  614 QHEDNKYFLGTPV--LEPAFIIQHFAGRVKYQIKDFREKNMDymrpdivallrgsdssyvrqligmdpvavfrwavlraa 691
Cdd:cd14891   473 THKRHPCFPRPHPkdMREMFIVKHYAGTVSYTIGSFIDKNND-------------------------------------- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  692 iramavlreagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrl 771
Cdd:cd14891       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  772 qkprtfflkskgikqkqIIPKNLLDskslrLIISmtlhdrttksllhlhkkkkppsiSAQFQTSLNKLLEALGKAEPFFI 851
Cdd:cd14891   515 -----------------IIPEDFED-----LLAS-----------------------SAKFSDQMQELVDTLEATRCNFI 549
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  852 RCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREA-----IAALLEKLQ 926
Cdd:cd14891   550 RCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAEndrtlTQAILWAFR 629
                         810
                  ....*....|....*.
gi 564388444  927 VDRQNYQIGKTKVFLK 942
Cdd:cd14891   630 VPSDAYRLGRTRVFFR 645
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
160-942 2.72e-134

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276869  Cd Length: 653  Bit Score: 436.30  E-value: 2.72e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVIS 238
Cdd:cd14904     1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTIlGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKY 318
Cdd:cd14904    81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAKVI-DVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIE-DGEDLKHDFERLQQAMEMVGFLPAT 397
Cdd:cd14904   160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQiPGLDDAKLFASTQKSLSLIGLDNDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  398 KKQIFSVLSAILYLGNVTYKKRAtgrDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITA 477
Cdd:cd14904   240 QRTLFKILSGVLHLGEVMFDKSD---ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEEN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  478 RDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQ 557
Cdd:cd14904   317 RDALAKAIYSKLFDWMVVKINAAISTDDDRIKG----QIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  558 EEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHE---DNKYFLGTPVLEPAFIIQ 634
Cdd:cd14904   393 EEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkDNESIDFPKVKRTQFIIN 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  635 HFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSyvrqligmdpvavfrwavlraairamavlreagrLRAERAEKAEA 714
Cdd:cd14904   472 HYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLD----------------------------------LLTELFGSSEA 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  715 gvsspvtRSHVEELPRGantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknl 794
Cdd:cd14904   518 -------PSETKEGKSG--------------------------------------------------------------- 527
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  795 ldskslrliismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQL 874
Cdd:cd14904   528 -------------------------KGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQL 582
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444  875 RYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP-----KDV-QPCREAIAALLEKLQVDrqnYQIGKTKVFLK 942
Cdd:cd14904   583 RSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPpsmhsKDVrRTCSVFMTAIGRKSPLE---YQIGKSLIYFK 653
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-942 1.09e-132

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 432.51  E-value: 1.09e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14920     1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLT--ALSQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAhvASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD-KDNFQETMEAMHIMG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  393 FLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPE--VLDTLSQLLKVK-RETLVEVLTKRktITVNDKLILPY 469
Cdd:cd14920   240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM----PEntVAQKLCHLLGMNvMEFTRAILTPR--IKVGRDYVQKA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  470 SLSE-AITARDSMAKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14920   314 QTKEqADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGT- 624
Cdd:cd14920   390 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPr 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  625 -PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagr 703
Cdd:cd14920   470 qLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL----------------------------- 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  704 lraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpWQGEDprRLLQSLSRLQKPRTFFlkSKG 783
Cdd:cd14920   521 ----------------------------------------------------WKDVD--RIVGLDQVTGMTETAF--GSA 544
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  784 IKQKqiipKNLLdskslrliismtlhdRTTKSLlhlhkkkkppsisaqFQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 863
Cdd:cd14920   545 YKTK----KGMF---------------RTVGQL---------------YKESLTKLMATLRNTNPNFVRCIIPNHEKRAG 590
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  864 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKV 939
Cdd:cd14920   591 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKI 670

                  ...
gi 564388444  940 FLK 942
Cdd:cd14920   671 FFR 673
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
160-950 3.62e-132

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276867 [Multi-domain]  Cd Length: 716  Bit Score: 432.39  E-value: 3.62e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYE--------NQQLGKLEPHVFALADVAYYTMLR-K 229
Cdd:cd14902     1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  230 HVNQCIVISGESGSGKTQSTNFLIHCLTAL--------SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14902    81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  302 VNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDF 381
Cdd:cd14902   161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKRAVADKY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  382 ERLQ----QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKrATGRDEGLEVGPP--EVLDTLSQLLKVKRETLVEVLTK 455
Cdd:cd14902   241 AQLYvetvRAFEDTGVGELERLDIFKILAALLHLGNVNFTA-ENGQEDATAVTAAsrFHLAKCAELMGVDVDKLETLLSS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  456 RKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLR----INHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNS 531
Cdd:cd14902   320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRlsdeINYFDSAVSISDEDEELATIGILDIFGFESLNRNG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  532 FEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKF 611
Cdd:cd14902   400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  612 KQqhednkYFLGtpvlEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVrQLIGMDPvavfrwavlraa 691
Cdd:cd14902   480 YR------YHGG----LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV-VAIGADE------------ 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  692 iramavlreagrlraeraekaeaGVSSPVTrshveelprganTPSEKLYRdlhnqiikslkglpwqgedprrllqslsrl 771
Cdd:cd14902   537 -----------------------NRDSPGA------------DNGAAGRR------------------------------ 551
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  772 qkprtfflkskgikqkqiipknllDSKSLRLiismtlhdrttksllhlhkkkkpPSISAQFQTSLNKLLEALGKAEPFFI 851
Cdd:cd14902   552 ------------------------RYSMLRA-----------------------PSVSAQFKSQLDRLIVQIGRTEAHYV 584
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  852 RCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREA-------------- 917
Cdd:cd14902   585 RCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKCFLSTRDRAAkmnnhdlaqalvtv 664
                         810       820       830
                  ....*....|....*....|....*....|....
gi 564388444  918 -IAALLEKLQVDRQNYQIGKTKVFLKETERQALQ 950
Cdd:cd14902   665 lMDRVLLEDGVEREEKNPGALTAVTGDGSGTAFE 698
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
166-942 4.18e-129

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 423.21  E-value: 4.18e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  166 LKLRFVQQKIYTYAGSILVAINPFKFLP-IYNpkyVKMYENQQLG--KLEPHVFALADVAYYTMLRK-------HVNQCI 235
Cdd:cd14895     7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGwtALPPHVFSIAEGAYRSLRRRlhepgasKKNQTI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  236 VISGESGSGKTQSTNFLIHCLTALSQKGYA---SGVERTILG-----AGPVLEAFGNAKTAHNNNSSRFGKFIQVNY--- 304
Cdd:cd14895    84 LVSGESGAGKTETTKFIMNYLAESSKHTTAtssSKRRRAISGsellsANPILESFGNARTLRNDNSSRFGKFVRMFFegh 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  305 -LESGI-VRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLK--QPQDYFYLN-----QHNLNIEDGE 375
Cdd:cd14895   164 eLDTSLrMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISggqcyQRNDGVRDDK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  376 DlkhdFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTY---KKRATGRDEGLEVGPP-------------EVLDTLS 439
Cdd:cd14895   244 Q----FQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvasSEDEGEEDNGAASAPCrlasaspssltvqQHLDIVS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  440 QLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHAL--------LNKKDMEEAV 511
Cdd:cd14895   320 KLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnPNKAANKDTT 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  512 SClsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFY 591
Cdd:cd14895   400 PC--IAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFS 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  592 LLDEESNFPHATSHTLLAKFKQQHEDNKYFLG--TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSS 669
Cdd:cd14895   478 LLDEECVVPKGSDAGFARKLYQRLQEHSNFSAsrTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDA 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  670 YVRQLigMDPVAVfrwavlraairamavlreagrlraerAEKAEAGVSSPVTRShveelprgantpseklyrdlhnqiik 749
Cdd:cd14895   558 HLREL--FEFFKA--------------------------SESAELSLGQPKLRR-------------------------- 583
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  750 slkglpwqgedprrllqslsrlqkpRTFFLKSKGikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsIS 829
Cdd:cd14895   584 -------------------------RSSVLSSVG--------------------------------------------IG 594
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  830 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK 909
Cdd:cd14895   595 SQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA 674
                         810       820       830
                  ....*....|....*....|....*....|...
gi 564388444  910 DVQPCREAiAALLEKLQVDrqNYQIGKTKVFLK 942
Cdd:cd14895   675 KNASDATA-SALIETLKVD--HAELGKTRVFLR 704
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1659-1844 1.38e-127

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 397.83  E-value: 1.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRE 1738
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1739 LPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1818
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                         170       180
                  ....*....|....*....|....*.
gi 564388444 1819 PDNSDPLTSMKDVLKITTCVEMLIKE 1844
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
160-942 3.86e-127

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 416.69  E-value: 3.86e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14911     1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCL----------------TALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 303
Cdd:cd14911    81 ESGAGKTENTKKVIQFLayvaaskpkgsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  304 YLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEdGEDLKHDFER 383
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP-GVDDYAEFQA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  384 LQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPE--VLDTLSQLLKVKRETLVEVLTKRKtITV 461
Cdd:cd14911   240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATL----PDntVAQKIAHLLGLSVTDMTRAFLTPR-IKV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  462 NDKLILPYSLSEAIT-ARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYA 540
Cdd:cd14911   315 GRDFVTKAQTKEQVEfAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASF----IGILDMAGFEIFELNSFEQLCINYT 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  541 NEQLQYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:cd14911   391 NEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHP 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  620 YFLGTPVLEPA-FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmDPVAVFRWAvlRAAIRAMAVl 698
Cdd:cd14911   470 KFMKTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ----------DPFVVNIWK--DAEIVGMAQ- 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  699 reagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllQSLSRLQkprtff 778
Cdd:cd14911   537 -------------------------------------------------------------------QALTDTQ------ 543
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  779 lkskgikqkqiipknlldskslrliismtLHDRTTKSLLHlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNA 858
Cdd:cd14911   544 -----------------------------FGARTRKGMFR--------TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNH 586
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  859 EKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQI 934
Cdd:cd14911   587 EKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLtpnvIPKGFMDGKKACEKMIQALELDSNLYRV 666

                  ....*...
gi 564388444  935 GKTKVFLK 942
Cdd:cd14911   667 GQSKIFFR 674
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
160-942 4.80e-126

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 413.22  E-value: 4.80e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14929     1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIH---CLTALSQKGYASGV-ERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVV 315
Cdd:cd14929    81 ESGAGKTVNTKHIIQyfaTIAAMIESKKKLGAlEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  316 EKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKhDFERLQQAMEMVGFLP 395
Cdd:cd14929   161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAE-ELLATEQAMDILGFLP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  396 ATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAI 475
Cdd:cd14929   240 DEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  476 TARDSMAKSLYSALFDWIVLRINHALLNKkdmeeAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd14929   318 YAVGALSKSIYERMFKWLVARINRVLDAK-----LSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  556 EQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPV-----LEP 629
Cdd:cd14929   393 EQEEYRKEGIDWVSIDFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKpdkkkFEA 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  630 AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraairamavlreagrlraera 709
Cdd:cd14929   472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKS------------------------------------------- 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  710 ekaeagvsspvtrshveelprgantpSEKLYRDLHNQIIKSLKGLPWqGEDPRRllqslsrlqkprtfflksKGikqkqi 789
Cdd:cd14929   509 --------------------------SNRLLASLFENYISTDSAIQF-GEKKRK------------------KG------ 537
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  790 ipknlldsKSLRLIISmtlhdrttksllhLHKKkkppsisaqfqtSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDEL 869
Cdd:cd14929   538 --------ASFQTVAS-------------LHKE------------NLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYL 584
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444  870 VLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-----DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14929   585 VLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtfpksKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
163-942 7.09e-126

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 412.07  E-value: 7.09e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  163 LQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14876     4 LDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLtALSQKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL-ESGIVRGAVVeKYL 319
Cdd:cd14876    84 GAGKTEATKQIMRYF-ASAKSGNMDLrIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVAsEGGIRYGSVV-AFL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIeDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd14876   162 LEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDV-PGIDDVADFEEVLESLKSMGLTEEQID 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  400 QIFSVLSAILYLGNVTY-KKRATGRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAIT 476
Cdd:cd14876   241 TVFSIVSGVLLLGNVKItGKTEQGVDDAAAISNesLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  477 ARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd14876   321 LKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNF-----MGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLgtpvlePA------ 630
Cdd:cd14876   396 SKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFK------PAkvdsni 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  631 -FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraera 709
Cdd:cd14876   470 nFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF---------------------------------- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  710 ekaeAGVssPVTRShveelprgantpseklyrdlhnqiiKSLKGlpwqgedprrllqSLsrlqkprtfflkskgikqkqi 789
Cdd:cd14876   516 ----EGV--VVEKG-------------------------KIAKG-------------SL--------------------- 530
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  790 ipknlldskslrliismtlhdrttksllhlhkkkkppsISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDEL 869
Cdd:cd14876   531 --------------------------------------IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSK 572
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444  870 VLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP-----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14876   573 VLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLgiandKSLDP-KVAALKLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
162-663 3.52e-121

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276865  Cd Length: 627  Bit Score: 397.75  E-value: 3.52e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNP----KYVKMYE-------NQQLGKLEPHVFALADVAYYTMLR- 228
Cdd:cd14900     3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSdtmaKYLLSFEarssstrNKGSDPMPPHIYQVAGEAYKAMMLg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  229 ---KHVNQCIVISGESGSGKTQSTNFLIHCLT---------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRF 296
Cdd:cd14900    83 lngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  297 GKFIQVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQefqlkqpqdyfylnqhnlniedged 376
Cdd:cd14900   163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  377 lKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEG---LEVGPPEV--LDTLSQLLKVKRETLVE 451
Cdd:cd14900   218 -RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGqlkSDLAPSSIwsRDAAATLLSVDATKLEK 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  452 VLTKRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHaLLNKKDMEEAVSCLS-IGVLDIFGFEDFERN 530
Cdd:cd14900   297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNA-FLKMDDSSKSHGGLHfIGILDIFGFEVFPKN 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  531 SFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAK 610
Cdd:cd14900   376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLASK 455
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564388444  611 FKQQHEDNKYFLGTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALL 663
Cdd:cd14900   456 LYRACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLF 510
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
160-942 3.48e-120

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 396.71  E-value: 3.48e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14932     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTAL-----SQKGYASGV------ERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESG 308
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVassfkTKKDQSSIAlshgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14932   161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQD-KELFAETMEAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPEvlDTLSQ----LLKVKRETLVEVLTKRKTITVNDK 464
Cdd:cd14932   240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASM----PD--DTAAQkvchLLGMNVTDFTRAILSPRIKVGRDY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  465 LILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQL 544
Cdd:cd14932   314 VQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASF----IGILDIAGFEIFELNSFEQLCINYTNEKL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  545 QYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISKK--PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14932   390 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKF 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  622 LGTPVL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlRAAIRAMAVLR 699
Cdd:cd14932   470 QKPKKLkdDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSEL----------W---KDVDRIVGLDK 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  700 EAGrlraeraekaeagvsspvtrshVEELPRGAntpseklyrdlhnqiIKSLKGLpwqgedprrllqslsrlqkprtffl 779
Cdd:cd14932   537 VAG----------------------MGESLHGA---------------FKTRKGM------------------------- 554
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  780 kskgikqkqiipknlldskslrliismtlhDRTTKSLlhlhkkkkppsisaqFQTSLNKLLEALGKAEPFFIRCIRSNAE 859
Cdd:cd14932   555 ------------------------------FRTVGQL---------------YKEQLMNLMTTLRNTNPNFVRCIIPNHE 589
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  860 KKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIG 935
Cdd:cd14932   590 KKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACVLMVKALELDPNLYRIG 669

                  ....*..
gi 564388444  936 KTKVFLK 942
Cdd:cd14932   670 QSKVFFR 676
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
160-942 4.27e-120

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 396.63  E-value: 4.27e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14927     1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSQKGYASG-------------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAALGDGPGkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  307 SGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERQEFQL--KQPQDYFYLNQHNL---NIEDGEDLKhdf 381
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-KKPELQDMLLvsMNPYDYHFCSQGVTtvdNMDDGEELM--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  382 eRLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITV 461
Cdd:cd14927   237 -ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  462 NDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYAN 541
Cdd:cd14927   314 NEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQ-----FFIGVLDIAGFEIFEFNSFEQLCINFTN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  542 EQLQYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKY 620
Cdd:cd14927   389 EKLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSP 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  621 FLGTPVL------EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraaiRA 694
Cdd:cd14927   468 NFQKPRPdkkrkyEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQN------------------------KL 523
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  695 MAVLREaGRLRAERAEKAEAGVSspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkp 774
Cdd:cd14927   524 LATLYE-NYVGSDSTEDPKSGVK--------------------------------------------------------- 545
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  775 rtfflkskgikqkqiipknlldskslrliismtlhdrttksllhlHKKKKppsiSAQFQT-------SLNKLLEALGKAE 847
Cdd:cd14927   546 ---------------------------------------------EKRKK----AASFQTvsqlhkeNLNKLMTNLRATQ 576
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  848 PFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQP-----CREAIAALL 922
Cdd:cd14927   577 PHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdkfvdSRKATEKLL 656
                         810       820
                  ....*....|....*....|
gi 564388444  923 EKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14927   657 GSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
162-942 4.28e-120

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 396.34  E-value: 4.28e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14913     3 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKGYASG---------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd14913    83 GAGKTVNTKRVIQYFATIAATGDLAKkkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLlgvSEEERQEFQL----KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQ 385
Cdd:cd14913   163 ADIETYLLEKSRVTFQLKAERSYHIFYQIL---SNKKPELIELllitTNPYDYPFISQGEIlvaSIDDAEELL----ATD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKL 465
Cdd:cd14913   236 SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:cd14913   314 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF-----IGVLDIAGFEIFEYNSLEQLCINFTNEKLQ 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  546 YYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFL 622
Cdd:cd14913   389 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQK 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  623 GTPV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAvlr 699
Cdd:cd14913   468 PKVVkgrAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQ------------------------KSSNRLLA--- 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  700 eagRLRAERAekaeagvsspvtrshveelprGANTPSEklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtffl 779
Cdd:cd14913   521 ---HLYATFA---------------------TADADSG------------------------------------------ 534
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  780 KSKGIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAE 859
Cdd:cd14913   535 KKKVAKKK---------GSSFQ-------------------------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNET 580
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  860 KKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQI 934
Cdd:cd14913   581 KTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEgqfidSKKACEKLLASIDIDHTQYKF 660

                  ....*...
gi 564388444  935 GKTKVFLK 942
Cdd:cd14913   661 GHTKVFFK 668
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
160-942 3.26e-119

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 393.24  E-value: 3.26e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14934     1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSQKGYAS-----GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAV 314
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  315 VEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQL-KQPQDYFYLNQHNL---NIEDGEDLkhdfERLQQAMEM 390
Cdd:cd14934   161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTvvdNMDDGEEL----QITDVAFDV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  391 VGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYS 470
Cdd:cd14934   237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKP--REEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQN 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  471 LSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQ 550
Cdd:cd14934   315 MEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQ-----FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  551 HIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATShtllAKFKQQHEDNKYFLGTPVLEP 629
Cdd:cd14934   390 HMFVLEQEEYKREGIEWVFIDFgLDLQACIDLL-EKPMGIFSILEEQCVFPKATD----ATFKAALYDNHLGKSSNFLKP 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  630 A----------FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLR 699
Cdd:cd14934   465 KggkgkgpeahFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQ------------------------KSSLGLLALLF 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  700 EagrlraerAEKAEAGvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslSRLQKPRTFFL 779
Cdd:cd14934   521 K--------EEEAPAG-----------------------------------------------------SKKQKRGSSFM 539
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  780 kskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAE 859
Cdd:cd14934   540 -----------------------------------------------TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEF 572
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  860 KKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIG 935
Cdd:cd14934   573 KQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLnpnvIPQGFVDNKKASELLLGSIDLDVNEYKIG 652

                  ....*..
gi 564388444  936 KTKVFLK 942
Cdd:cd14934   653 HTKVFFR 659
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
157-666 3.31e-117

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 386.91  E-value: 3.31e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  157 LNEANLLQSLKLRFVQQKIYTYAGS-ILVAINPFKFLPIYNPKYVKMYEN-------QQLGKLEPHVFALADVAYYTMLR 228
Cdd:cd14879     1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYGSeyydttsGSKEPLPPHAYDLAARAYLRMRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  229 KHVNQCIVISGESGSGKT----QSTNFLIHcLTALSQKGYASGVErtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNY 304
Cdd:cd14879    81 RSEDQAVVFLGETGSGKSesrrLLLRQLLR-LSSHSKKGTKLSSQ--ISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  305 LESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYL---NQHNLNIEDGEDLKHDF 381
Cdd:cd14879   158 NERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLPLGPGSDDAEGF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLT-KRKTI- 459
Cdd:cd14879   238 QELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTyKTKLVr 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  460 ----TVndklilpysLSEAITA---RDSMAKSLYSALFDWIVLRINHALLNKkdmEEAVScLSIGVLDIFGFEDF---ER 529
Cdd:cd14879   318 kelcTV---------FLDPEGAaaqRDELARTLYSLLFAWVVETINQKLCAP---EDDFA-TFISLLDFPGFQNRsstGG 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  530 NSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEE-SNFPHATSHTLL 608
Cdd:cd14879   385 NSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQtRRMPKKTDEQML 464
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388444  609 AKFKQQHEDNKYF-----LGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGS 666
Cdd:cd14879   465 EALRKRFGNHSSFiavgnFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA 527
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
160-941 1.77e-116

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 387.41  E-value: 1.77e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLE-PHVFALADVAYYTMLRKHVNQCIVI 237
Cdd:cd14906     1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNKSPiPHIYAVALRAYQSMVSEKKNQSIII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  238 SGESGSGKTQSTNFLIHCLTALSQKGYASG---------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLES- 307
Cdd:cd14906    81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  308 GIVRGAVVEKYLLEKSRlVSQEKDERN--YHVFYYLLLGVSEEERQEFQLKQ-PQDYFYLNQH--------------NLN 370
Cdd:cd14906   161 GKIDGASIETYLLEKSR-ISHRPDNINlsYHIFYYLVYGASKDERSKWGLNNdPSKYRYLDARddvissfksqssnkNSN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  371 IEDGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGrDEGLEVGPP--EVLDTLSQLLKVKRET 448
Cdd:cd14906   240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDF-SKYAYQKDKvtASLESVSKLLGYIESV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  449 LVEVLTKRKTITVNDKLIL--PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLN---KKDMEEAVS---CLSIGVLD 520
Cdd:cd14906   319 FKQALLNRNLKAGGRGSVYcrPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqSNDLAGGSNkknNLFIGVLD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  521 IFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFP 600
Cdd:cd14906   399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMP 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  601 HATSHTLLAKFKQQ-HEDNKYFLGTpVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdp 679
Cdd:cd14906   479 KGSEQSLLEKYNKQyHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASS------------ 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  680 vavfrwavlraairamavlreagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhNQIIKSlkglpwqge 759
Cdd:cd14906   546 -----------------------------------------------------------------NFLKKS--------- 551
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  760 dprrlLQSLSRLQKPRTfflkskgikqkqiipknlldskslrliismtlHDRTTKSLlhlhkkkkppSISAQFQTSLNKL 839
Cdd:cd14906   552 -----LFQQQITSTTNT--------------------------------TKKQTQSN----------TVSGQFLEQLNQL 584
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  840 LEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL----------PK 909
Cdd:cd14906   585 IQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVdmynrknnnnPK 664
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444  910 D-VQPCREAIAALLEKLQV-----------------DRQNYQIGKTKVFL 941
Cdd:cd14906   665 LaSQLILQNIQSKLKTMGIsnnkkknnsnsnsnttnDKPLFQIGKTKIFI 714
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
160-942 1.64e-115

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 383.21  E-value: 1.64e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14921     1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLT--ALSQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAvvASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQD-DEMFQETLEAMSIMG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  393 FLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPEvlDTLSQ----LLKVKRETLVEVLTKRKTITVNDKLILP 468
Cdd:cd14921   240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASM----PD--NTAAQkvchLMGINVTDFTRSILTPRIKVGRDVVQKA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALlnKKDMEEAVSCLsiGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14921   314 QTKEQADFAIEALAKATYERLFRWILTRVNKAL--DKTHRQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTP 625
Cdd:cd14921   390 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPK 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  626 VL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLrgsdssyvrqligmdpvavfrwavlraairamavlreagr 703
Cdd:cd14921   470 QLkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLL---------------------------------------- 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  704 lraeraekaeagvsspvtrshveelprgaNTPSEKLYRDLhnqiikslkglpWQGEDprRLLqslsrlqkprtfflkskG 783
Cdd:cd14921   510 -----------------------------NASSDKFVADL------------WKDVD--RIV-----------------G 529
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  784 IKQKQIIPKNLLDSKSlrliismtlhdRTTKSLLHlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 863
Cdd:cd14921   530 LDQMAKMTESSLPSAS-----------KTKKGMFR--------TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSG 590
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  864 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKV 939
Cdd:cd14921   591 KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaanaIPKGFMDGKQACILMIKALELDPNLYRIGQSKI 670

                  ...
gi 564388444  940 FLK 942
Cdd:cd14921   671 FFR 673
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
160-942 2.00e-115

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 382.65  E-value: 2.00e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14909     1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTAL--SQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd14909    81 ESGAGKTENTKKVIAYFATVgaSKKTDEAAkskgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLG-VSEEERQEFQLKQPQDYFYLNQHNL---NIEDGEdlkhDFERLQQAM 388
Cdd:cd14909   161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGsVPGVKEMCLLSDNIYDYYIVSQGKVtvpNVDDGE----EFSLTDQAF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRatGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILP 468
Cdd:cd14909   237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQR--GREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14909   315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF-----IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHednkyfLG--TP 625
Cdd:cd14909   390 NHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTH------LGksAP 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  626 VLEPA----------FIIQHFAGRVKYQIKDFREKNMDymrpdivallrgsdssyvrqligmdpvavfrwavlraairam 695
Cdd:cd14909   463 FQKPKppkpgqqaahFAIAHYAGCVSYNITGWLEKNKD------------------------------------------ 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  696 avlreagrlraeraekaeagvssPVTRSHVEELPRGANTPSEKLYRDlHnqiikslkglPWQGEDPRrllqslsrlqkpr 775
Cdd:cd14909   501 -----------------------PLNDTVVDQFKKSQNKLLIEIFAD-H----------AGQSGGGE------------- 533
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  776 tfflKSKGIKQKqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIR 855
Cdd:cd14909   534 ----QAKGGRGK---------------------------------KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCII 576
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  856 SNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQP---CREAIAALLEKLQVDRQNY 932
Cdd:cd14909   577 PNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGeedPKKAAEIILESIALDPDQY 656
                         810
                  ....*....|
gi 564388444  933 QIGKTKVFLK 942
Cdd:cd14909   657 RLGHTKVFFR 666
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-942 4.11e-115

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 381.75  E-value: 4.11e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14919     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQST----NFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVV 315
Cdd:cd14919    81 ESGAGKTENTkkviQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  316 EKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVGFLP 395
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-KDMFQETMEAMRIMGIPE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  396 ATKKQIFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVE-VLTKRKTITvNDKLILPYSLSE 473
Cdd:cd14919   240 EEQMGLLRVISGVLQLGNIVFKKE---RNTDQASMPDNTaAQKVSHLLGINVTDFTRgILTPRIKVG-RDYVQKAQTKEQ 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  474 AITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIF 553
Cdd:cd14919   316 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASF----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  554 KLEQEEYQGEGISWHNIDY-TDNVGCIHLISKK--PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA 630
Cdd:cd14919   392 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  631 --FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQL-------IGMDPVAvfrwavlraairamavlrea 701
Cdd:cd14919   472 adFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriIGLDQVA-------------------- 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  702 grlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqSLSRLQKPRTFflks 781
Cdd:cd14919   532 -----------------------------------------------------------------GMSETALPGAF---- 542
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  782 kgikqkqiipknlldskslrliismtlhdRTTKSLLHlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKK 861
Cdd:cd14919   543 -----------------------------KTRKGMFR--------TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKK 585
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  862 ELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKT 937
Cdd:cd14919   586 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQS 665

                  ....*
gi 564388444  938 KVFLK 942
Cdd:cd14919   666 KVFFR 670
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
160-942 2.31e-113

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 377.33  E-value: 2.31e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQL---------GKLEPHVFALADVAYYTMLRK- 229
Cdd:cd14908     1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLlrsqgiespQALGPHVFAIADRSYRQMMSEi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  230 HVNQCIVISGESGSGKTQSTNFLIHCLTAL-----------SQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:cd14908    81 RASQSILISGESGAGKTESTKIVMLYLTTLgngeegapnegEELGKLSIMDR-VLQSNPILEAFGNARTLRNDNSSRFGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  299 FIQVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQ--------PQDYFYLNQ---- 366
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQggap 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  367 HNLNIEDgEDlkhDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYK-KRATGRDEGLEVGPPEVLDTLSQLLKVK 445
Cdd:cd14908   240 DLREFTD-ED---GLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFEsKEEDGAAEIAEEGNEKCLARVAKLLGVD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  446 RETLVEVLTKRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSClsiGVLDIFGFE 525
Cdd:cd14908   316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIRSSV---GVLDIFGFE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  526 DFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEE--------- 596
Cdd:cd14908   393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDEcrlgirgsd 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  597 SNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA--FIIQHFAGRVKYQIKD-FREKNMDymrpdivallrgsdssyvrq 673
Cdd:cd14908   473 ANYASRLYETYLPEKNQTHSENTRFEATSIQKTKliFAVRHFAGQVQYTVETtFCEKNKD-------------------- 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  674 ligmdpvavfrwavlraairamavlreagrlraeraekaeagvsspvtrshveELPrgantpseklyrdlhnqiikslkg 753
Cdd:cd14908   533 -----------------------------------------------------EIP------------------------ 535
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  754 lpwqgedprrllqslsrlqkprtfflkskgikqkqiipknlldskslrliismtlhdRTTKSLLhlhkkkkppSISAQFQ 833
Cdd:cd14908   536 ---------------------------------------------------------LTADSLF---------ESGQQFK 549
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  834 TSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KD 910
Cdd:cd14908   550 AQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipEV 629
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564388444  911 VQP----------------CREAIAALLEKLQVDRQNY-----QIGKTKVFLK 942
Cdd:cd14908   630 VLSwsmerldpqklcvkkmCKDLVKGVLSPAMVSMKNIpedtmQLGKSKVFMR 682
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1659-1844 2.95e-112

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 354.05  E-value: 2.95e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRE 1738
Cdd:cd04377     1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1739 LPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1818
Cdd:cd04377    81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRC 160
                         170       180
                  ....*....|....*....|....*.
gi 564388444 1819 PDNSDPLTSMKDVLKITTCVEMLIKE 1844
Cdd:cd04377   161 PDTADPLQSLQDVSKTTTCVETLIKE 186
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
160-942 1.23e-111

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 372.09  E-value: 1.23e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd15896     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALSQK-----------GYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESG 308
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQD-KDLFTETMEAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILP 468
Cdd:cd15896   240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKER--HTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd15896   318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASF----IGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTP 625
Cdd:cd15896   394 NHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPK 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  626 VL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQL-------IGMDPVavfrwavlraairama 696
Cdd:cd15896   474 KLkdEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELwkdvdriVGLDKV---------------- 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  697 vlreagrlraeraekaeAGVSspvtrshveELPrGANTPSEKLYRdlhnqiikslkglpwqgedprrllqslsrlqkprt 776
Cdd:cd15896   538 -----------------SGMS---------EMP-GAFKTRKGMFR----------------------------------- 555
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  777 fflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRS 856
Cdd:cd15896   556 --------------------------------------------------TVGQLYKEQLSKLMATLRNTNPNFVRCIIP 585
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  857 NAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNY 932
Cdd:cd15896   586 NHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACVLMIKSLELDPNLY 665
                         810
                  ....*....|
gi 564388444  933 QIGKTKVFLK 942
Cdd:cd15896   666 RIGQSKVFFR 675
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
160-941 1.42e-111

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 371.11  E-value: 1.42e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQ-QLGKLEPHVFALADVAYYTM--LRKHVNQCI 235
Cdd:cd14880     1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVksLIEPVNQSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  236 VISGESGSGKTQSTNFLIH-------CLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESG 308
Cdd:cd14880    81 VVSGESGAGKTWTSRCLMKfyavvaaSPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEdgEDlkhDFERLQQAM 388
Cdd:cd14880   161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLE--ED---CFEVTREAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKkratgrDEGLEVGPPEVLD-------TLSQLLKVKRETLVEVLTKRkTITV 461
Cdd:cd14880   236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFA------DSEDEAQPCQPMDdtkesvrTSALLLKLPEDHLLETLQIR-TIRA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  462 NDKLIL---PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCIN 538
Cdd:cd14880   309 GKQQQVfkkPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTF----IGLLDVYGFESFPENSLEQLCIN 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  539 YANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLakfkqQHEDN 618
Cdd:cd14880   385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSAAQL-----QTRIE 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  619 KYFLGTPVL-------EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPvavfrwavlraa 691
Cdd:cd14880   460 SALAGNPCLghnklsrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------------ 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  692 iramavlreagrlraeraekaeagvsspvtRSHVEELPRGANtpseklyrdlhnqiikslkglpwqgedprrllqslsrl 771
Cdd:cd14880   528 ------------------------------EEKTQEEPSGQS-------------------------------------- 539
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  772 qkprtfflKSKGIkqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFI 851
Cdd:cd14880   540 --------RAPVL------------------------------------------TVVSKFKASLEQLLQVLHSTTPHYI 569
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  852 RCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKdvQPCREAIAALLEKLQVDRQN 931
Cdd:cd14880   570 RCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRL--RPHTSSGPHSPYPAKGLSEP 647
                         810
                  ....*....|
gi 564388444  932 YQIGKTKVFL 941
Cdd:cd14880   648 VHCGRTKVFM 657
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
160-942 1.76e-111

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 371.06  E-value: 1.76e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQ-QKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQ-QLGKLEPHVFALADVAY-YTMLRKHVNQCIV 236
Cdd:cd14875     1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFnAIFVQGLGNQSVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  237 ISGESGSGKTQSTNFLIHCLTALS--------QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLE-- 306
Cdd:cd14875    81 ISGESGSGKTENAKMLIAYLGQLSymhssntsQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKL-YFDpt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  307 SGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEF-QLKQPQDYFYLNQHNLNIEDGEDLK-----HD 380
Cdd:cd14875   160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDGKtlddaHE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  381 FERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPpevLDTLSQLLKVKRETLVEV-LTKRKTI 459
Cdd:cd14875   240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETP---FLTACRLLQLDPAKLRECfLVKSKTS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  460 TVNdklILPySLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:cd14875   317 LVT---ILA-NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSG---CKYIGLLDIFGFENFTRNSFEQLCINY 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHED-N 618
Cdd:cd14875   390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANkS 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  619 KYFLGTPVLEP-AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPvavfrwavlraairamav 697
Cdd:cd14875   470 PYFVLPKSTIPnQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEK------------------ 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  698 lreagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqGEDPRrllqslsrlqkprtf 777
Cdd:cd14875   532 ------------------------------------------------------------GLARR--------------- 536
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  778 flkskgiKQkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSN 857
Cdd:cd14875   537 -------KQ----------------------------------------TVAIRFQRQLTDLRTELESTETQFIRCIKPN 569
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  858 AEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDV------QPCREAIAALLEKLQV---- 927
Cdd:cd14875   570 MEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTaslfkqEKYSEAAKDFLAYYQRlygw 649
                         810
                  ....*....|....*
gi 564388444  928 DRQNYQIGKTKVFLK 942
Cdd:cd14875   650 AKPNYAVGKTKVFLR 664
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-942 5.21e-110

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 367.13  E-value: 5.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14915     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIV 310
Cdd:cd14915    83 GAGKTVNTKRVIQYFATIAVTGekkkeeAASGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLK-QPQDYFYLNQHNLNIEDGEDlKHDFERLQQAME 389
Cdd:cd14915   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQGEITVPSIDD-QEELMATDSAVD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  390 MVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPY 469
Cdd:cd14915   242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14915   320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGTPV 626
Cdd:cd14915   395 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNFQKPKPA 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  627 ---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLREAGr 703
Cdd:cd14915   474 kgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSGMKTLAFLFSGG- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  704 lraeRAEKAEAGvsspvtrshveelprGANTPSEKlyrdlhnqiikslKGLPWQgedprrllqslsrlqkprtfflkskg 783
Cdd:cd14915   529 ----QTAEAEGG---------------GGKKGGKK-------------KGSSFQ-------------------------- 550
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  784 ikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 863
Cdd:cd14915   551 -------------------------------------------TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPG 587
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  864 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTK 938
Cdd:cd14915   588 AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTK 667

                  ....
gi 564388444  939 VFLK 942
Cdd:cd14915   668 VFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
162-942 3.31e-109

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 364.82  E-value: 3.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14912     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIV 310
Cdd:cd14912    83 GAGKTVNTKRVIQYFATIAVTGekkkeeITSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLK-QPQDYFYLNQHNLNIEDGEDlKHDFERLQQAME 389
Cdd:cd14912   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDD-QEELMATDSAID 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  390 MVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPY 469
Cdd:cd14912   242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14912   320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL- 627
Cdd:cd14912   395 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVv 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  628 ----EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLREAgr 703
Cdd:cd14912   474 kgkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQ------------------------KSAMKTLAYLFSG-- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  704 lrAERAEKAEAGvsspvtrshveelpRGANTPSEKlyrdlhnqiikslKGLPWQgedprrllqslsrlqkprtfflkskg 783
Cdd:cd14912   528 --AQTAEGASAG--------------GGAKKGGKK-------------KGSSFQ-------------------------- 552
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  784 ikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 863
Cdd:cd14912   553 -------------------------------------------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPG 589
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  864 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTK 938
Cdd:cd14912   590 AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTK 669

                  ....
gi 564388444  939 VFLK 942
Cdd:cd14912   670 VFFK 673
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
162-942 5.83e-109

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 364.05  E-value: 5.83e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14910     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIV 310
Cdd:cd14910    83 GAGKTVNTKRVIQYFATIAVTGekkkeeATSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLK-QPQDYFYLNQHNLNIEDGEDlKHDFERLQQAME 389
Cdd:cd14910   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDD-QEELMATDSAIE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  390 MVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPY 469
Cdd:cd14910   242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14910   320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGTPV 626
Cdd:cd14910   395 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNFQKPKPA 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  627 ---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLreagr 703
Cdd:cd14910   474 kgkVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSSMKTLALL----- 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  704 LRAERAEKAEAGvsspvtrshveelprGANTPSEKlyrdlhnqiikslKGLPWQgedprrllqslsrlqkprtfflkskg 783
Cdd:cd14910   525 FSGAAAAEAEEG---------------GGKKGGKK-------------KGSSFQ-------------------------- 550
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  784 ikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 863
Cdd:cd14910   551 -------------------------------------------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPG 587
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  864 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTK 938
Cdd:cd14910   588 AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTK 667

                  ....
gi 564388444  939 VFLK 942
Cdd:cd14910   668 VFFK 671
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
162-942 3.62e-108

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 361.74  E-value: 3.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14918     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALS--------QKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd14918    83 GAGKTVNTKRVIQYFATIAvtgekkkeESGKMQGtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLllgVSEEERQEFQL----KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14918   163 ADIETYLLEKSRVTFQLKAERSYHIFYQI---TSNKKPDLIEMllitTNPYDYAFVSQGEITVPSIDD-QEELMATDSAI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILP 468
Cdd:cd14918   239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14918   317 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL 627
Cdd:cd14918   392 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  628 -----EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLREAg 702
Cdd:cd14918   471 vkgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQ------------------------KSAMKTLASLFST- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  703 rlraerAEKAEAGVSSpvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkSK 782
Cdd:cd14918   526 ------YASAEADSGA--------------------------------------------------------------KK 537
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  783 GIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKE 862
Cdd:cd14918   538 GAKKK---------GSSFQ-------------------------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 583
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  863 LCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKT 937
Cdd:cd14918   584 GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnasaIPEgQFIDSKKASEKLLASIDIDHTQYKFGHT 663

                  ....*
gi 564388444  938 KVFLK 942
Cdd:cd14918   664 KVFFK 668
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
162-942 7.08e-108

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 360.96  E-value: 7.08e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14917     3 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTAL------SQKGYASG---VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd14917    83 GAGKTVNTKRVIQYFAVIaaigdrSKKDQTPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQL-KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQAM 388
Cdd:cd14917   163 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETtvaSIDDAEELM----ATDNAF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILP 468
Cdd:cd14917   239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQ--REEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14917   317 QNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH-------EDNKY 620
Cdd:cd14917   392 NHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgksnnfQKPRN 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  621 FLGTPvlEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavlraairamavlre 700
Cdd:cd14917   471 IKGKP--EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFA------------------------ 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  701 agrlraeraekAEAGVSSPVTRShveelpRGantpseklyrdlhnqiiKSLKGLPWQgedprrllqslsrlqkprtfflk 780
Cdd:cd14917   525 -----------NYAGADAPIEKG------KG-----------------KAKKGSSFQ----------------------- 547
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  781 skgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEK 860
Cdd:cd14917   548 ----------------------------------------------TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETK 581
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  861 KELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIG 935
Cdd:cd14917   582 SPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEgqfidSRKGAEKLLSSLDIDHNQYKFG 661

                  ....*..
gi 564388444  936 KTKVFLK 942
Cdd:cd14917   662 HTKVFFK 668
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
162-942 1.19e-106

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 357.45  E-value: 1.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14916     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALSQKGY----------ASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVR 311
Cdd:cd14916    83 GAGKTVNTKRVIQYFASIAAIGDrskkenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQL-KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEM 390
Cdd:cd14916   163 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASIDD-SEELLATDSAFDV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  391 VGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYS 470
Cdd:cd14916   242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQ--REEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  471 LSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQ 550
Cdd:cd14916   320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  551 HIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTP---- 625
Cdd:cd14916   395 HMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPrnvk 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  626 -VLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLREAgrl 704
Cdd:cd14916   474 gKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQ------------------------KSSLKLMATLFST--- 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  705 raerAEKAEAGVSSpvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflKSKGI 784
Cdd:cd14916   527 ----YASADTGDSG-------------------------------------------------------------KGKGG 541
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  785 KQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELC 864
Cdd:cd14916   542 KKK---------GSSFQ-------------------------TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGV 587
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  865 FDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKV 939
Cdd:cd14916   588 MDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEgqfidSRKGAEKLLGSLDIDHNQYKFGHTKV 667

                  ...
gi 564388444  940 FLK 942
Cdd:cd14916   668 FFK 670
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-942 3.38e-106

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 355.94  E-value: 3.38e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14930     1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIHCLTALS-------QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRG 312
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVAsspkgrkEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNqHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPGQE-RELFQETLESLRVLG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  393 FLPATKKQIFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSL 471
Cdd:cd14930   239 FSHEEITSMLRMVSAVLQFGNIVLKRE---RNTDQATMPDNTaAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  472 SEAITARDSMAKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14930   316 EQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  552 IFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL- 627
Cdd:cd14930   392 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLr 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  628 -EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraairamavlreagRLRA 706
Cdd:cd14930   472 dQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTD----------------------------------RLTA 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  707 ERAEKAEAGVSspvtrshVEElprgantpseklyrdlhnqiIKSLKGLPWQGEDPRRLLQSLSRLqkprtfflkskgikq 786
Cdd:cd14930   518 EIWKDVEGIVG-------LEQ--------------------VSSLGDGPPGGRPRRGMFRTVGQL--------------- 555
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  787 kqiipknlldskslrliismtlhdrttksllhlhkkkkppsisaqFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFD 866
Cdd:cd14930   556 ---------------------------------------------YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 590
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  867 DELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14930   591 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
160-942 6.50e-104

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276851  Cd Length: 650  Bit Score: 348.80  E-value: 6.50e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYE--NQQLG---KLEPHVFALADVAYYTMLRKHVNQ 233
Cdd:cd14886     1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRqaDTSRGfpsDLPPHSYAVAQSALNGLISDGISQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  234 CIVISGESGSGKTQSTNFLIHCLtALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGA 313
Cdd:cd14886    81 SCIVSGESGAGKTETAKQLMNFF-AYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  314 VVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVgF 393
Cdd:cd14886   160 KITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  394 LPATKKQIFSVLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLS 472
Cdd:cd14886   239 SKNEIDSFYKCISGILLAGNIEFSEEgDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  473 EAITARDSMAKSLYSALFDWIVLRINHALlnkkdMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHI 552
Cdd:cd14886   319 QAEVNIRAVAKDLYGALFELCVDTLNEII-----QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  553 FKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVlEPAFI 632
Cdd:cd14886   394 FKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSFIPGKGS-QCNFT 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRqligmdpvavfrwavlraairamavlreagrlraeraeka 712
Cdd:cd14886   473 IVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN---------------------------------------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  713 eagvsspvtrshveelprgantpseklyrdlhnqiiKSLKGLPwqGEDPrrllqslsrLQKPRtfFLKSKgikqkqiipk 792
Cdd:cd14886   513 ------------------------------------KAFSDIP--NEDG---------NMKGK--FLGST---------- 533
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  793 nlldskslrliismtlhdrttksllhlhkkkkppsisaqFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQ 872
Cdd:cd14886   534 ---------------------------------------FQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYN 574
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388444  873 QLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL---------PKDVqpcREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14886   575 QLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshnsssqnaGEDL---VEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-942 7.78e-104

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 349.37  E-value: 7.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14923     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLTALS---------QKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVR 311
Cdd:cd14923    83 GAGKTVNTKRVIQYFATIAvtgdkkkeqQPGKMQGtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLK-QPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQA 387
Cdd:cd14923   163 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVtvaSIDDSEELL----ATDNA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  388 MEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLIL 467
Cdd:cd14923   239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  468 PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYY 547
Cdd:cd14923   317 GQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  548 FTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGT 624
Cdd:cd14923   392 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKPK 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  625 PV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLrea 701
Cdd:cd14923   471 PAkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSSLKLLSFL--- 523
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  702 grlrAERAEKAEAGVSSpvtrshveelprGANTPSEKlyrdlhnqiikslKGLPWQgedprrllqslsrlqkprtfflks 781
Cdd:cd14923   524 ----FSNYAGAEAGDSG------------GSKKGGKK-------------KGSSFQ------------------------ 550
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  782 kgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKK 861
Cdd:cd14923   551 ---------------------------------------------TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKT 585
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  862 ELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGK 936
Cdd:cd14923   586 PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEgqfidSKNASEKLLNSIDVDREQYRFGH 665

                  ....*.
gi 564388444  937 TKVFLK 942
Cdd:cd14923   666 TKVFFK 671
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
160-942 1.21e-96

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276897  Cd Length: 637  Bit Score: 326.97  E-value: 1.21e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYnpkyVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISG 239
Cdd:cd14937     1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  240 ESGSGKTQSTNFLIhcltalsqKGYASGVER------TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGA 313
Cdd:cd14937    77 ESGSGKTEASKLVI--------KYYLSGVKEdneisnTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  314 VVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKhDFERLqqameMVGF 393
Cdd:cd14937   149 SIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAK-DFGNL-----MISF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  394 ----LPATKKQIFSVLSAILYLGNVTYKKRATGRDEG---LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLI 466
Cdd:cd14937   223 dkmnMHDMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNcseLDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIE 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:cd14937   303 IPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNN-----YIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGTP 625
Cdd:cd14937   378 IYLYIVYEKETELYKAEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVKNDESIVSVYTNKFSKHeKYASTKK 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  626 VLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQligmdpvavfrwavlraairamavlreagrlr 705
Cdd:cd14937   457 DINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRS-------------------------------- 504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  706 aeraekaeagvsspvtrshveelprgantpsekLYRDLhnqiikslkglpwqgedprRLLQSLSRlqkprtfflkskgik 785
Cdd:cd14937   505 ---------------------------------LYEDV-------------------EVSESLGR--------------- 517
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  786 qkqiipKNLLDSKSLRliismtlhdrttksllhlhkkkkppsisaqfqtSLNKLLEALGKAEPFFIRCIRSNAEKKELCF 865
Cdd:cd14937   518 ------KNLITFKYLK---------------------------------NLNNIISYLKSTNIYFIKCIKPNENKEKNNF 558
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  866 DDELVLQQLRYTGMLETVRIRRSgYSAKYTFQDFTEQFQVL---LPKDVQPC-REAIAALLEKlQVDRQNYQIGKTKVFL 941
Cdd:cd14937   559 NQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdysTSKDSSLTdKEKVSMILQN-TVDPDLYKVGKTMVFL 636

                  .
gi 564388444  942 K 942
Cdd:cd14937   637 K 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
160-942 2.27e-96

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276852  Cd Length: 725  Bit Score: 329.30  E-value: 2.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQ--------QKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHV 231
Cdd:cd14887     1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  232 NQCIVISGESGSGKTQSTNFLIHCLTALS--QKGYAS-GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESG 308
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSdrRHGADSqGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLlgVSEEERQEFQLKQPQDYFYLnqhnlniedgedlkHDFERLQQAM 388
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALC--NAAVAAATQKSSAGEGDPES--------------TDLRRITAAM 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  389 EMVGFLPATKKQIFSVLSAILYLGNV---------TYKKRatgRDEGLEVGPPEVLDTLSQLLKVKRET---LVEVLTKR 456
Cdd:cd14887   225 KTVGIGGGEQADIFKLLAAILHLGNVefttdqepeTSKKR---KLTSVSVGCEETAADRSHSSEVKCLSsglKVTEASRK 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  457 KTITVNDKLILP------------------------YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVS 512
Cdd:cd14887   302 HLKTVARLLGLPpgvegeemlrlalvsrsvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESDS 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  513 ---------CLSIGVLDIFGFEDFE---RNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGcih 580
Cdd:cd14887   382 dedtpsttgTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFS--- 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  581 liskkptglFYLLDEESNFPHATSHtllakfkqqhednkyFLGTPvlepafiiqhfagrvkyQIKDFREKNMDYMRPDIV 660
Cdd:cd14887   459 ---------FPLASTLTSSPSSTSP---------------FSPTP-----------------SFRSSSAFATSPSLPSSL 497
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  661 ALLRGSDSSYVRQLIGMDPVAVFrwaVLRAAIRAMAVLREAGRLRAERAEKAEAGVSspvtrshveelprgaNTPSEKLY 740
Cdd:cd14887   498 SSLSSSLSSSPPVWEGRDNSDLF---YEKLNKNIINSAKYKNITPALSRENLEFTVS---------------HFACDVTY 559
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  741 --RDLHNQIIKSLKglpwqgEDPRRLLQSLSrlqkprTFflkskgikqkqiIPKNLLDSKSLRLIISmtlhdrttksllh 818
Cdd:cd14887   560 daRDFCRANREATS------DELERLFLACS------TY------------TRLVGSKKNSGVRAIS------------- 602
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  819 lhkkKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQD 898
Cdd:cd14887   603 ----SRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVE 678
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*..
gi 564388444  899 FTEQFQVLLPKDVQ---PCREAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd14887   679 LWRRYETKLPMALRealTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
162-942 1.57e-94

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276863  Cd Length: 578  Bit Score: 319.15  E-value: 1.57e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKflPIYNPKYVKMYENQQlGKLEPHVFALADVAYYTMLrKHVNQCIVISGES 241
Cdd:cd14898     3 TLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYLKNY-SHVEPHVYDVAEASVQDLL-VHGNQTIVISGES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCLtaLSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYleSGIVRGAVVEKYLLE 321
Cdd:cd14898    79 GSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLLE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  322 KSRLVSQEKDERNYHVFYYLLlgvseeERQEFQLKQpqDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFlpATKKQI 401
Cdd:cd14898   155 KSRVTHHEKGERNFHIFYQFC------ASKRLNIKN--DFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGI--ANFKSI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  402 FSVLSAILYLGNVTYKkratgrDEG-LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDS 480
Cdd:cd14898   225 EDCLLGILYLGSIQFV------NDGiLKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNS 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  481 MAKSLYSALFDWIVLRINHALlnkkdmeEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEY 560
Cdd:cd14898   299 MARLLYSNVFNYITASINNCL-------EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  561 QGEGISWHNIDYTDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQhedNKYFLGTPVlEPAFIIQHFAGRV 640
Cdd:cd14898   372 KEEGIEWPDVEFFDNNQCIRDF-EKPCGLMDLISEESFNAWGNVKNLLVKIKKY---LNGFINTKA-RDKIKVSHYAGDV 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  641 KYQIKDFREKNmdymrpdivallrgsdssyvrqligmdpvavfrwavlraairamavlREAGRLRaeraekaeagvsspv 720
Cdd:cd14898   447 EYDLRDFLDKN-----------------------------------------------REKGQLL--------------- 464
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  721 trshveelprgantpseklyrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiIPKNLLdsksl 800
Cdd:cd14898   465 ---------------------------------------------------------------------IFKNLL----- 470
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  801 rliismtlhdrttksllhLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGML 880
Cdd:cd14898   471 ------------------INDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGIL 532
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388444  881 ETVRIRRSGYSAKYTFQDFTEQFQVLlpkdvQPCREaiaalleklqvDRQNYQIGKTKVFLK 942
Cdd:cd14898   533 ETIRLSKQCFPQEIPKDRFEERYRIL-----GITLF-----------EVVDYRKGRTRYFMK 578
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
160-907 2.22e-92

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276864 [Multi-domain]  Cd Length: 717  Bit Score: 317.42  E-value: 2.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMY---ENQQLGK-------LEPHVFALADVAYYTMLR 228
Cdd:cd14899     1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydHNSQFGDrvtstdpREPHLFAVARAAYIDIVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  229 KHVNQCIVISGESGSGKTQSTN-----FLIHCLTALSQKGYASG-----------VERTILGAGPVLEAFGNAKTAHNNN 292
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKiimtyFAVHCGTGNNNLTNSESisppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  293 SSRFGKFIQVNYL-ESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLG----VSEEERQEFQLKQ-PQDYFYLNQ 366
Cdd:cd14899   161 SSRFGKFIELRFRdERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGgPQSFRLLNQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  367 HNLNIE-DGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDT-------- 437
Cdd:cd14899   241 SLCSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVFADEARVMSSttgafdhf 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  438 --LSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHAL----------LNKK 505
Cdd:cd14899   321 tkAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgaDESD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  506 DMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK 585
Cdd:cd14899   401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  586 PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK---YFLGTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIV 660
Cdd:cd14899   481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshpHFRSAPLIQRTtqFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  661 ALLRGSDSSYVRQLIGmdpvavfrwAVLRAAIRAMAVLREAGRLRAERAEKAEAGVsspvtrshveelprgantpsekly 740
Cdd:cd14899   561 QLLAGSSNPLIQALAA---------GSNDEDANGDSELDGFGGRTRRRAKSAIAAV------------------------ 607
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  741 rdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikqkqiipknlldskslrliismtlhdrttksllhlh 820
Cdd:cd14899       --------------------------------------------------------------------------------
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  821 kkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 900
Cdd:cd14899   608 ------SVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFL 681

                  ....*..
gi 564388444  901 EQFQVLL 907
Cdd:cd14899   682 GRYRRVL 688
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
160-942 4.38e-92

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 314.45  E-value: 4.38e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN---QQLGKLEPHVFALADVAYYTMLRKHVNQCIV 236
Cdd:cd14878     1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  237 ISGESGSGKTQSTNFLIHCLTAlsqkgyASGVERTILG-----AGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE-SGIV 310
Cdd:cd14878    81 LSGERGSGKTEASKQIMKHLTC------RASSSRTTFDsrfkhVNCILEAFGHAKTTLNDLSSCFIKYFELQFCErKKHL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLniEDGEDLKHDFER-----LQ 385
Cdd:cd14878   155 TGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMR--EDVSTAERSLNReklavLK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKL 465
Cdd:cd14878   233 QALNVVGFSSLEVENLFVILSAILHLGDIRFT--ALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:cd14878   311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQ-DEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDN-VGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHED---NKYF 621
Cdd:cd14878   390 HYINEVLFLQEQTECVQEGVTMETAYSPGNqTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESsntNAVY 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  622 L------GTPVLE---PAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQligmdpvavfrwavlraai 692
Cdd:cd14878   470 SpmkdgnGNVALKdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINH------------------- 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  693 ramavlreagrlraeraekaeagvsspvtrshveelprgantpseklyrdlhnqiikslkglpwqgedprrLLQSlsrlq 772
Cdd:cd14878   531 -----------------------------------------------------------------------LFQS----- 534
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  773 kprtfflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkKPPSISAQFQTSLNKLLEALGKAEPFFIR 852
Cdd:cd14878   535 ---------------------------------------------------KLVTIASQLRKSLADIIGKLQKCTPHFIH 563
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  853 CIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLpkDVQPCREAIAALLEK-----LQV 927
Cdd:cd14878   564 CIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA--DTLLGEKKKQSAEERcrlvlQQC 641
                         810
                  ....*....|....*
gi 564388444  928 DRQNYQIGKTKVFLK 942
Cdd:cd14878   642 KLQGWQMGVRKVFLK 656
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
160-942 6.71e-85

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 292.55  E-value: 6.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYenqqlgklepHVFALADVAYYTMLRKHVN-QCIVIS 238
Cdd:cd14874     1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTIlgaGPVLEAFGNAKTAHNNNSSRFGKFIQVNYlESGIVRGAVVeKY 318
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAI---ESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNL-KY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  319 L--LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHdFERLQQAMEMVGFLPA 396
Cdd:cd14874   146 TvpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNH-FKHLEDALHVLGFSDD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  397 TKKQIFSVLSAILYLGNVTYKKRATGRDEG--LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVndklilPYSLSEA 474
Cdd:cd14874   225 HCISIYKIISTILHIGNIYFRTKRNPNVEQdvVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSEDGT------TIDLNAA 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  475 ITARDSMAKSLYSALFDWIVLRINHALlnKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFK 554
Cdd:cd14874   299 LDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTGV----ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  555 LEQEEYQGEGISwhnIDYT-----DNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEP 629
Cdd:cd14874   373 DQLVDYAKDGIS---VDYKvpnsiENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKER 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  630 -AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraer 708
Cdd:cd14874   450 lEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF--------------------------------- 496
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  709 aekaeagvsspvtRSHveelprGANTPSEKLYrdlhnqiikslkglpwqgedprrllqslsrlqkprtfflkskgikQKQ 788
Cdd:cd14874   497 -------------ESY------SSNTSDMIVS---------------------------------------------QAQ 512
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  789 IIPKNlldskslrliiSMTLHDRTTKSLLHlhkkkkppsisaqfqtslnkllealgkaepfFIRCIRSNAEKKELCFDDE 868
Cdd:cd14874   513 FILRG-----------AQEIADKINGSHAH-------------------------------FVRCIKSNNERQPKKFDIP 550
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444  869 LVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC---REAIAALLEKLQVDRQN-YQIGKTKVFLK 942
Cdd:cd14874   551 LVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCqneKEIIQDILQGQGVKYENdFKIGTEYVFLR 628
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
162-942 9.42e-81

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276870  Cd Length: 673  Bit Score: 281.98  E-value: 9.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGkLEPHVFALADVAYYTMLRKHVNQCIVISGES 241
Cdd:cd14905     3 LINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  242 GSGKTQSTNFLIHCL--TALSQKGYasgVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYL 319
Cdd:cd14905    82 GSGKSENTKIIIQYLltTDLSRSKY---LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQ-HNLNIEDGEDlKHDFERLQQAMEMVGFLPATK 398
Cdd:cd14905   159 LDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDD-NRVFDRLKMSFVFFDFPSEKI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  399 KQIFSVLSAILYLGNVTYKKratgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNdklilpyslsEAITAR 478
Cdd:cd14905   238 DLIFKTLSFIIILGNVTFFQ----KNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVN----------EAVENR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  479 DSMAKSLYSALFDWIVlrinhALLNKKdMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd14905   304 DSLARSLYSALFHWII-----DFLNSK-LKPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  559 EYQGEGISWHN-IDYTDNVGCIHLISKkptgLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPvlePAFIIQHFA 637
Cdd:cd14905   378 EYQTERIPWMTpISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP---NKFGIEHYF 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvaVFRWAVLRAAIRAMAVLREAGRlraeraekaeagvS 717
Cdd:cd14905   451 GQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSRDG-----VFNINATVAELNQMFDAKNTAK-------------K 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  718 SPVTRSHVeELPRGANTPSeklyrDLHNQIIKSLKGlpwqGEDPRRLLQSLSRLQKPRTFFLKSKGIKQKQiipknllds 797
Cdd:cd14905   513 SPLSIVKV-LLSCGSNNPN-----NVNNPNNNSGGG----GGGGNSGGGSGSGGSTYTTYSSTNKAINNSN--------- 573
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  798 kslrliismtlhdrttksllhlhkkkkppsisaqfqtslnkllealgkAEPFFIRCIRSNAEKKELCFDDELVLQQLRYT 877
Cdd:cd14905   574 ------------------------------------------------CDFHFIRCIKPNSKKTHLTFDVKSVNEQIKSL 605
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388444  878 GMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKdvqpcREAIAALLEKLQVDRQN--------YQIGKTKVFLK 942
Cdd:cd14905   606 CLLETTRIQRFGYTIHYNNKIFFDRFSFFFQN-----QRNFQNLFEKLKENDINidsilpppIQVGNTKIFLR 673
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
163-941 1.11e-79

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 277.38  E-value: 1.11e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  163 LQSLKLRFVQQKIYTYAGSILVAINPFKFLPiyNPKYVKMYENQQLGKLEPHVFaladvayYTMLRKHVN----QCIVIS 238
Cdd:cd14881     4 MKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLAPQLLKVV-------QEAVRQQSEtgypQAIILS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVvEKY 318
Cdd:cd14881    75 GTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTDGALYRTKI-HCY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLK--QPQDYFYLNQHnlniEDGEDLKHDFERLQQAMEMVGFLPA 396
Cdd:cd14881   154 FLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHG----DTRQNEAEDAARFQAWKACLGILGI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  397 TKKQIFSVLSAILYLGNVTYKKRATGrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRktiTVNDKLILPYSLSEAIT 476
Cdd:cd14881   230 PFLDVVRVLAAVLLLGNVQFIDGGGL---EVDVKGETELKSVAALLGVSGAALFRGLTTR---THNARGQLVKSVCDANM 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  477 A---RDSMAKSLYSALFDWIVLRIN-----HALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14881   304 SnmtRDALAKALYCRTVATIVRRANslkrlGSTLGTHATDG-----FIGILDMFGFEDPKPSQLEHLCINLCAETMQHFY 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWH-NIDYTDNVGCIHLISKKPTGLFYLLDEESNfPHATSHTLLAKFKQQHEDNKYFLGT-PV 626
Cdd:cd14881   379 NTHIFKSSIESCRDEGIQCEvEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAkPQ 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  627 LEPAFIIQHFAGRVKYQIKDFREKNMDYMrPDivallrgsdssyvrqligmDPVAVFrwavlraairamavlreagrlra 706
Cdd:cd14881   458 DDRMFGIRHFAGRVVYDASDFLDTNRDVV-PD-------------------DLVAVF----------------------- 494
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  707 eRAEKAEAGVSSpvtrshveelprgantpseklyrdlHNQiikslkglpwqgedprrllqslsrlqkprtfflkskgikq 786
Cdd:cd14881   495 -YKQNCNFGFAT-------------------------HTQ---------------------------------------- 508
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  787 kqiipknlldskslrliismtlhdrttksllhlhkkkkppsisaQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFD 866
Cdd:cd14881   509 --------------------------------------------DFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFD 544
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  867 DELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---------KDVQPCR----EAIAALLEKLQVDRQNYQ 933
Cdd:cd14881   545 RGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPfrllrrveeKALEDCAlilqFLEAQPPSKLSSVSTSWA 624

                  ....*...
gi 564388444  934 IGKTKVFL 941
Cdd:cd14881   625 LGKRHIFL 632
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
161-942 6.66e-78

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 272.38  E-value: 6.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  161 NLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGE 240
Cdd:cd14882     2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  241 SGSGKTqsTNFLiHCLTALSQKGYA-SGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYL 319
Cdd:cd14882    82 SYSGKT--TNAR-LLIKHLCYLGDGnRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEER-QEFQLKQPQDYFYLNQHNLNIEDG-----EDLKHDFERLQQAMEMVGF 393
Cdd:cd14882   159 LEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYLRIPPEVPPSKlkyrrDDPEGNVERYKEFEEILKD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  394 LPATKKQ---IFSVLSAILYLGNVTYKKratGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYS 470
Cdd:cd14882   239 LDFNEEQletVRKVLAAILNLGEIRFRQ---NGGYA-ELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  471 LSEAITARDSMAKSLYSALFDWIVLRINHALLnkkdMEEAV--SCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14882   315 TEEARDARDVLASTLYSRLVDWIINRINMKMS----FPRAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHY 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  549 TQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLlakfKQQHEDNKYFLgTPVLE 628
Cdd:cd14882   391 NQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQNYIM----DRIKEKHSQFV-KKHSA 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  629 PAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraer 708
Cdd:cd14882   466 HEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF--------------------------------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  709 aekaeagvsspvTRSHVEELPRGANTpseklYRDLHNQIIKSLkglpwqgedprrllqslsrlqkprtfflkskgikqkq 788
Cdd:cd14882   513 ------------TNSQVRNMRTLAAT-----FRATSLELLKML------------------------------------- 538
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  789 iipknlldskslrliismtlhdrttksllhlhkkkkppSISAqfqtslnkllealGKAEPFFIRCIRSNAEKKELCFDDE 868
Cdd:cd14882   539 --------------------------------------SIGA-------------NSGGTHFVRCIRSDLEYKPRGFHSE 567
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388444  869 LVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---LPKDVQPCREAIAALLEKLQVdrQNYQIGKTKVFLK 942
Cdd:cd14882   568 VVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLafdFDETVEMTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
163-942 8.56e-75

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 264.56  E-value: 8.56e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  163 LQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGESG 242
Cdd:cd01386     4 LHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  243 SGKTQSTNFLIH--CLTALSQKGYASgVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYLL 320
Cdd:cd01386    84 SGKTTNCRHILEylVTAAGSVGGVLS-VEK-LNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  321 EKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQ--PQDYFYLNQHnLNIEDGEDLKHDFERLQQAMEMVGFLPATK 398
Cdd:cd01386   162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQlaESNSFGIVPL-QKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  399 KQIFSVLSAILYLGnvtykkrATGRDEGLEVGPPEVLD-------------TLSQLLK-VKRETLVEVLTKRKTITVNDK 464
Cdd:cd01386   241 RAIWSILAAIYHLG-------AAGATKAASAGRKQFARpewaqraayllgcTLEELSSaIFKHHLSGGPQQSTTSSGQES 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  465 LILPYSLSEAITAR---DSMAKSLYSALFDWIVlrinhALLNKKDMEEAVSCLSIGVLDIFGFED-----FERNS-FEQF 535
Cdd:cd01386   314 PARSSSGGPKLTGVealEGFAAGLYSELFAAVV-----SLINRSLSSSHHSTSSITIVDTPGFQNpahsgSQRGAtFEDL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGIswhNIDYTDNVGCIH----LISKKPT--------------GLFYLLDEES 597
Cdd:cd01386   389 CHNYAQERLQLLFHERTFVAPLERYKQENV---EVDFDLPELSPGalvaLIDQAPQqalvrsdlrdedrrGLLWLLDEEA 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  598 NFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA-----FIIQHfagrvkyqikdfreknmdymrpdivallrgsdssyvr 672
Cdd:cd01386   466 LYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSegplqFVLGH------------------------------------- 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  673 qLIGMDPVavfRWAVlraairamavlreAGRLRAERaekaeagvSSPVTRShveelprgantpseklyrdlhnqiikslk 752
Cdd:cd01386   509 -LLGTNPV---EYDV-------------SGWLKAAK--------ENPSAQN----------------------------- 534
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  753 glpwqgedPRRLLQSLSRlqkprtfflKSKGIKQKqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQF 832
Cdd:cd01386   535 --------ATQLLQESQK---------ETAAVKRK---------------------------------------SPCLQI 558
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  833 QTSLNKLLEALGKAEPFFIRCI--RSNAEKKE----LCFDDELVLQ------QLRYTGMLETVRIRRSGYSAKYTFQDFT 900
Cdd:cd01386   559 KFQVDALIDTLRRTGLHFVHCLlpQHNAGKDErstsSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFR 638
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564388444  901 EQFQVLLPKDVQPC---------REAIAALLEKLQVDRQNYQIGKTKVFLK 942
Cdd:cd01386   639 RRFQVLAPPLTKKLglnsevadeRKAVEELLEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
160-673 7.77e-71

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 252.90  E-value: 7.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  160 ANLLQSLKLRFVQQKIYTYAGSILVAINPFKFLP-IYNPK----YVKMYENQQLGK---LEPHVFALADVAYYTMLRKHV 231
Cdd:cd14884     1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDvmnvYLHKKSNSAASAapfPKAHIYDIANMAYKNMRGKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  232 NQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE----- 306
Cdd:cd14884    81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  307 ----SGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQL-KQPQDYFYLNQHNLNIEDG------- 374
Cdd:cd14884   161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLvRNCGVYGLLNPDESHQKRSvkgtlrl 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  375 EDLKHDFERLQQAMEMVGF------LPATK------KQIFSVLSAILYLGNVTYKkratgrdeglevgppevldTLSQLL 442
Cdd:cd14884   241 GSDSLDPSEEEKAKDEKNFvallhgLHYIKyderqiNEFFDIIAGILHLGNRAYK-------------------AAAECL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  443 KVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLS------- 515
Cdd:cd14884   302 QIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDIysineai 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  516 IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKkptgLFYLLDE 595
Cdd:cd14884   382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRRLDD 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  596 ESNFpHATSHT---------LLAKFKQQHEDNKYFLG-------------TPVLEPAFIIQHFAGRVKYQIKDFREKNMD 653
Cdd:cd14884   458 ITKL-KNQGQKktddhffryLLNNERQQQLEGKVSYGfvlnhdadgtakkQNIKKNIFFIRHYAGLVTYRINNWIDKNSD 536
                         570       580
                  ....*....|....*....|
gi 564388444  654 YMRPDIVALLRGSDSSYVRQ 673
Cdd:cd14884   537 KIETSIETLISCSSNRFLRE 556
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1659-1844 1.22e-69

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 232.20  E-value: 1.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRE 1738
Cdd:cd04406     1 FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1739 LPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1818
Cdd:cd04406    81 LPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRC 160
                         170       180
                  ....*....|....*....|....*.
gi 564388444 1819 PDNSDPLTSMKDVLKITTCVEMLIKE 1844
Cdd:cd04406   161 PDTTDPLQSVQDISKTTTCVELIVCE 186
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
162-941 8.22e-60

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 221.38  E-value: 8.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQ----------LGKLEPHVFALADVAYYTMLRKHV 231
Cdd:cd14893     3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  232 NQCIVISGESGSGKTQSTNFLIHCLT-----------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFI 300
Cdd:cd14893    83 DQAVILLGGMGAGKSEAAKLIVQYLCeigdeteprpdSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  301 QVNYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEE--RQEFQL-KQPQDYFYLNQHNLNIEDGEDL 377
Cdd:cd14893   163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMnKCVNEFVMLKQADPLATNFALD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  378 KHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGrdeGLEVG-----------------PPEVLdTLSQ 440
Cdd:cd14893   243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEG---GKSVGgansttvsdaqscalkdPAQIL-LAAK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  441 LLKVKRETLVEVLTKRKTITV-NDKLILPY---SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEE----AVS 512
Cdd:cd14893   319 LLEVEPVVLDNYFRTRQFFSKdGNKTVSSLkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRYEksniVIN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  513 CLSIGVLDIFGFEDFE--RNSFEQFCINYANEQLQYYFTQHIFK-----LEQEEYQGEG-ISWH-NIDYT-DNVGCIHLI 582
Cdd:cd14893   399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrLTVNsNVDITsEQEKCLQLF 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  583 SKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHED---------NKYFLGTPVLEPA-----FIIQHFAGRVKYQIKDFR 648
Cdd:cd14893   479 EDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnmGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLS 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  649 EKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwAVLRAAiramavlrEAGRLRAERAEKAEagvsspvtrshveel 728
Cdd:cd14893   559 SKNMLSISSTCAAIMQSSKN-----------------AVLHAV--------GAAQMAAASSEKAA--------------- 598
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  729 prgantpseklyrdlhnqiikslkglpwqgedprrllQSLSRLQKPRTFFLKSKGIKQKQiipKNLLDSKSLRLiismtl 808
Cdd:cd14893   599 -------------------------------------KQTEERGSTSSKFRKSASSARES---KNITDSAATDV------ 632
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  809 hdrttksllhlhkkkkppsisaqfQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRS 888
Cdd:cd14893   633 ------------------------YNQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRS 688
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564388444  889 GYSAKYTFQDFTEQFqvllpKDVQPCREAIAALLEKLQ----VDRQNYQIGKTKVFL 941
Cdd:cd14893   689 IFTVHLTYGHFFRRY-----KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1672-1845 2.01e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 199.41  E-value: 2.01e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   1672 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1750
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   1751 DFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1830
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159
                           170
                    ....*....|....*
gi 564388444   1831 VLKITTCVEMLIKEQ 1845
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1674-1823 6.43e-56

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 425782  Cd Length: 152  Bit Score: 191.25  E-value: 6.43e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  1674 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATV-KLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1752
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDSGEDVDlDLEEEDVHDVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388444  1753 LRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSD 1823
Cdd:pfam00620   81 IEAAKSEDEEERIEALRELLEKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPDSES 151
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
1674-1844 1.34e-53

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090  Cd Length: 169  Bit Score: 185.58  E-value: 1.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1674 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1753
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1754 RAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDplTSMKDVLK 1833
Cdd:cd00159    81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDD--ELLEDIKK 158
                         170
                  ....*....|.
gi 564388444 1834 ITTCVEMLIKE 1844
Cdd:cd00159   159 LNEIVEFLIEN 169
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 6.87e-53

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


Pssm-ID: 340737  Cd Length: 96  Bit Score: 180.38  E-value: 6.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   16 TFHLHIYPQLpSAGSQTSCRVTATKDSTTSDVIRDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217     1 VYALQIYPQL-SAESSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                          90
                  ....*....|....*..
gi 564388444   96 QKEHPREDGYYFLLQER 112
Cdd:cd17217    80 QDDHPQSDGYYFLLQER 96
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
162-941 1.87e-52

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 198.52  E-value: 1.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  162 LLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMY---ENQQLGKLEPHVFALADVAYYTMLRKhvNQCIVIS 238
Cdd:cd14938     3 VLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYkciDCIEDLSLNEYHVVHNALKNLNELKR--NQSIIIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  239 GESGSGKTQSTNFLIHCL----------------------TALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRF 296
Cdd:cd14938    81 GESGSGKSEIAKNIINFIayqvkgsrrlptnlndqeedniHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  297 GKFIQVnYLESGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYfylnqHNLNIEDGED 376
Cdd:cd14938   161 SKFCTI-HIENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENY-----SMLNNEKGFE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  377 LKHDFE-RLQQAMEMVGFLPATKKQI---FSVLSAILYLGNV----TYKKRAT---GRDEGLEVGPPEVLDTLS------ 439
Cdd:cd14938   235 KFSDYSgKILELLKSLNYIFDDDKEIdfiFSVLSALLLLGNTeivkAFRKKSLlmgKNQCGQNINYETILSELEnsedig 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  440 ------------QLLKVKRETLVEVLTKRKTItvNDKLILPYSLSEAITAR-DSMAKSLYSALFDWIVLRINHALLNKKD 506
Cdd:cd14938   315 ldenvknlllacKLLSFDIETFVKYFTTNYIF--NDSILIKVHNETKIQKKlENFIKTCYEELFNWIIYKINEKCTQLQN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  507 MEEAVSclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISW-HNIDYTDNVG-CIHLISK 584
Cdd:cd14938   393 ININTN--YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCeYNSENIDNEPlYNLLVGP 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  585 KPTGLFYLLDEESN---FPHATSHTL-LAKFKQqheDNKYFLGTPVLE--PAFIIQHFAGRVKYQIKDFREKNMDYMRPD 658
Cdd:cd14938   471 TEGSLFSLLENVSTktiFDKSNLHSSiIRKFSR---NSKYIKKDDITGnkKTFVITHSCGDIIYNAENFVEKNIDILTNR 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  659 IVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraeraekaeAGVSSPVTRSHVEELPRGANTPSEK 738
Cdd:cd14938   548 FIDMVKQSENEYMRQFC--------------------------------------MFYNYDNSGNIVEEKRRYSIQSALK 589
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  739 LYR---DLHNQIIKSLKglpwqgedpRRLLQSLSRLQKprtfflkskgikqkqiipknlldskslrliismtlhdrttKS 815
Cdd:cd14938   590 LFKrryDTKNQMAVSLL---------RNNLTELEKLQE----------------------------------------TT 620
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  816 LLHlhkkkkppsisaqfqtslnkllealgkaepfFIRCIRSNAEKKELC-FDDELVLQQLRYTGMLETVRIRRSGYSAKY 894
Cdd:cd14938   621 FCH-------------------------------FIVCMKPNESKRELCsFDANIVLRQVRNFSIVEASQLKVGYYPHKF 669
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 564388444  895 TFQDFTEQFQVLlpkdvQPC-REAIAALLEKLQVDRQNYQIGKTKVFL 941
Cdd:cd14938   670 TLNEFLSIFDIK-----NEDlKEKVEALIKSYQISNYEWMIGNNMIFL 712
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1666-1816 2.92e-38

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 142.06  E-value: 2.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1666 LTSDkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKL---EDFPiHAITGVLKQWLRELPEP 1742
Cdd:cd04385    10 LTDN--DIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLregEYTV-HDVADVLKRFLRDLPDP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444 1743 LMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLL 1816
Cdd:cd04385    87 LLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLF 160
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1589-1646 1.77e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.77e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444 1589 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1646
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1844 1.87e-35

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 134.89  E-value: 1.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCV-DSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDF---PiHAITGVLKQ 1734
Cdd:cd04386     5 FGTPLeEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFysdP-HAVASALKS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1735 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1814
Cdd:cd04386    84 YLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPN 163
                         170       180       190
                  ....*....|....*....|....*....|.
gi 564388444 1815 LLRCP-DNSDPLTSMKDVLKITTCVEMLIKE 1844
Cdd:cd04386   164 LLWAKnEGSLAEMAAGTSVHVVAIVELIISH 194
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1828 7.52e-35

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 132.53  E-value: 7.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKL---EDF--PIHAITGVL 1732
Cdd:cd04398     1 FGVPLEDLILrEGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLispEDYesDIHSVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1733 KQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFA 1812
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                         170
                  ....*....|....*.
gi 564388444 1813 PCLLrcPDNSDPLTSM 1828
Cdd:cd04398   161 PTLM--NAAPDNAADM 174
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
18-112 1.80e-34

Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system.


Pssm-ID: 340477  Cd Length: 97  Bit Score: 127.82  E-value: 1.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   18 HLHIYPQLPSAgSQTSCRVTATKDSTTSDVIRDVVASLHLDGSKHYVLVEVKESGG---EEWVLDASDSPVHRVLLWPRR 94
Cdd:cd01779     1 MVRVYPGALSP-ETEFLSVEATKQTTASEVIECLVAKLRLDKAECYELAEVCGSGGqgcKERRLGPSENPVQVQLLWPKM 79
                          90
                  ....*....|....*...
gi 564388444   95 AQKEHPREDGYYFLLQER 112
Cdd:cd01779    80 AGDSDNQVTSYRFFLREK 97
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1659-1828 8.13e-34

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 129.43  E-value: 8.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAT----VKLEDfpIHAITGVLK 1733
Cdd:cd04403     1 FGCHLEALCQrENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLdlddSKWED--IHVITGALK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1734 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1813
Cdd:cd04403    79 LFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGP 158
                         170
                  ....*....|....*..
gi 564388444 1814 CLLRcP--DNSDPLTSM 1828
Cdd:cd04403   159 TLLR-PeqETGNIAVHM 174
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1666-1843 1.10e-32

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837  Cd Length: 194  Bit Score: 126.48  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1666 LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PATVKLEDFP-IHAITGVLKQWLRELPEP 1742
Cdd:cd04372     9 VKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDgeKADISATVYPdINVITGALKLYFRDLPIP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1743 LMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDnS 1822
Cdd:cd04372    89 VITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPE-D 167
                         170       180
                  ....*....|....*....|.
gi 564388444 1823 DPLTSMKDVLKITTCVEMLIK 1843
Cdd:cd04372   168 SALTTLNDMRYQILIVQLLIT 188
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
182-302 1.01e-30

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 119.76  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  182 ILVAINPFKFLPIYNP-KYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS 260
Cdd:cd01363     1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564388444  261 QKGYASG--------------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 302
Cdd:cd01363    81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
272-675 1.35e-30

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 131.79  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  272 ILGAGPVLEAFGNAKTAHNNNSSRFGKF--IQVNYlesGI------VRGAVVEKYLLEKSRLVSQ------EKDERNYHV 337
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAF---GLhpwefqICGCHISPFLLEKSRVTSErgresgDQNELNFHI 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  338 FYYLLLGVSEEERQEFQLKQPQ---------DYFYLNQHNLN--IEDGEDLKHDFERLQQAMEMVGFL---PATKKQIFS 403
Cdd:cd14894   326 LYAMVAGVNAFPFMRLLAKELHldgidcsalTYLGRSDHKLAgfVSKEDTWKKDVERWQQVIDGLDELnvsPDEQKTIFK 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  404 VLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITV---NDKLILPYSLSEAITARD 479
Cdd:cd14894   406 VLSAVLWLGNIELDYReVSGKLVMSSTGALNAPQKVVELLELGSVEKLERMLMTKSVSLqstSETFEVTLEKGQVNHVRD 485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  480 SMAKSLYSALFDWIVLRINHALL--------NKKDME------EAVSCLSIgvLDIFGFEDFERNSFEQFCINYANEQLq 545
Cdd:cd14894   486 TLARLLYQLAFNYVVFVMNEATKmsalstdgNKHQMDsnasapEAVSLLKI--VDVFGFEDLTHNSLDQLCINYLSEKL- 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  546 yyftqhiFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLdEESNFPHATSHTllaKFKQQHEDNKYFL--- 622
Cdd:cd14894   563 -------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENM---NAQQEEKRNKLFVrni 631
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388444  623 --------------------GTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLI 675
Cdd:cd14894   632 ydrnssrlpepprvlsnakrHTPVLLNVlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML 706
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1659-1826 9.77e-30

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 118.34  E-value: 9.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLT---SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKL--EDFP-IHAITGVL 1732
Cdd:cd04379     1 FGVPLSRLVereGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELseELYPdINVITGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1733 KQWLRELPEPLMTFAQYGDFLRA--VELPEKQEQLAA-IYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1809
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEAlaVALPNDVQTNTHlTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                         170
                  ....*....|....*..
gi 564388444 1810 IFAPCLLRCPDNSDPLT 1826
Cdd:cd04379   161 CFGPVLMFCSQEFSRYG 177
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1842 3.10e-29

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 116.73  E-value: 3.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDS--LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLED---FPIHAITGVLK 1733
Cdd:cd04395     2 FGVPLDDcpPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDprwRDVNVVSSLLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1734 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1813
Cdd:cd04395    82 SFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGP 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 564388444 1814 CLLRCPDNS--DPLTSMKDVLKIttcVEMLI 1842
Cdd:cd04395   162 TLVRTSDDNmeTMVTHMPDQCKI---VETLI 189
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1842 3.24e-29

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 116.24  E-value: 3.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDkASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDpATVKLEDFPIHAITGVLKQWLRE 1738
Cdd:cd04402     2 FGQPLSNICED-DNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSG-VEVDLKAEPVLLLASVLKDFLRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1739 LPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1818
Cdd:cd04402    80 IPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWP 159
                         170       180
                  ....*....|....*....|....
gi 564388444 1819 PDNSDPLtsMKDVLKITTCVEMLI 1842
Cdd:cd04402   160 PASSELQ--NEDLKKVTSLVQFLI 181
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1672-1843 1.25e-28

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 115.21  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1672 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1751
Cdd:cd04378    15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYND 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1752 FL----RAVELPEKQEQ----------LAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1817
Cdd:cd04378    95 FIalakEIQRDTEEDKApntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIR 174
                         170       180
                  ....*....|....*....|....*...
gi 564388444 1818 CPDNSDP--LTSMKDVLKITTCVEMLIK 1843
Cdd:cd04378   175 PRPGDADvsLSSLVDYGYQARLVEFLIT 202
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
1591-1646 1.64e-28

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410368  Cd Length: 56  Bit Score: 109.31  E-value: 1.64e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564388444 1591 HNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1646
Cdd:cd20818     1 HNGHKFATVQFNIPTYCEVCNSFIWLMEKGLVCQVCKFTCHKKCYSKITAPCKGNS 56
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1846 3.68e-28

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869  Cd Length: 195  Bit Score: 113.59  E-value: 3.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTS---DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL-QTDPatVKLEDFP-IHAITGVLK 1733
Cdd:cd04404     6 FGVSLQFLKEknpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYnMGEP--VDFDQYEdVHLPAVILK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1734 QWLRELPEPLMTFAQYGDFLRAVELPeKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1813
Cdd:cd04404    84 TFLRELPEPLLTFDLYDDIVGFLNVD-KEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 564388444 1814 CLLRCPDNSdplTSMKDVLKITTCVEMLIKEQM 1846
Cdd:cd04404   163 NLLWAKDAS---MSLSAINPINTFTKFLLDHQD 192
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1660-1831 4.48e-28

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 113.16  E-value: 4.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1660 GVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLREL 1739
Cdd:cd04382     4 GELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1740 PEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDvNRMSPGALAIIFAPCLLRCP 1819
Cdd:cd04382    84 KEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYS 162
                         170
                  ....*....|...
gi 564388444 1820 D-NSDPLTSMKDV 1831
Cdd:cd04382   163 VpNPDPMTILQDT 175
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
1659-1842 6.68e-27

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 109.91  E-value: 6.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSD-KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLR 1737
Cdd:cd04408     1 FGVDFSQLPRDfPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1738 ELPEPLMTFAQYGDFL-----------RAVELPE-KQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPG 1805
Cdd:cd04408    81 ELPEPVLPFQLYDDFIalakelqrdseKAAESPSiVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 564388444 1806 ALAIIFAPCLLRCPDNSD-PLTSMKDVLKITTCVEMLI 1842
Cdd:cd04408   161 NLGIVFGPTLLRPLVGGDvSMICLLDTGYQAQLVEFLI 198
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1842 2.48e-26

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 107.93  E-value: 2.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTREL-RQALQTDPATVKLEDFPIHAITGVLKQWLR 1737
Cdd:cd04373     1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLqKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1738 ELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1817
Cdd:cd04373    81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160
                         170       180
                  ....*....|....*....|....*..
gi 564388444 1818 cPD--NSDPLTSMKDVlkiTTCVEMLI 1842
Cdd:cd04373   161 -PDftSMEALSATRIY---QTIIETFI 183
RA_Myosin-IXa cd17216
Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is ...
17-112 3.12e-26

Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function.


Pssm-ID: 340736  Cd Length: 96  Bit Score: 104.24  E-value: 3.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444   17 FHLHIYPQLPSAGSqTSCRVTATKDSTTSDVIRDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRAQ 96
Cdd:cd17216     2 FTLRIYPGNIAEGT-IYCPVPARKNTTAAEVIESLINKLQLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMAL 80
                          90
                  ....*....|....*.
gi 564388444   97 KEHPREDGYYFLLQER 112
Cdd:cd17216    81 ENRFSGEDYRFLLREK 96
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
1669-1842 5.33e-26

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 107.48  E-value: 5.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1669 DKASVPIVlEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL----QTDPATVKLE--DFPIHAITGVLKQWLRELPEP 1742
Cdd:cd04374    25 DDIGFKFV-RKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpkTSTPGDVDLDnsEWEIKTITSALKTYLRNLPEP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1743 LMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1822
Cdd:cd04374   104 LMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEET 183
                         170       180
                  ....*....|....*....|
gi 564388444 1823 dpLTSMKDVLKITTCVEMLI 1842
Cdd:cd04374   184 --VAAIMDIKFQNIVVEILI 201
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1659-1830 1.03e-25

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 106.55  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSDKAS-VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PATVKLEDFPIHAITGVLKQW 1735
Cdd:cd04387     1 FGVKISTVTKRERSkVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNnkDVSVMLSEMDVNAIAGTLKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1736 LRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1815
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
                         170
                  ....*....|....*..
gi 564388444 1816 LRCP--DNSDPLTSMKD 1830
Cdd:cd04387   161 LRPSekESKIPTNTMTD 177
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1673-1819 1.16e-24

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 103.35  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1673 VPIVLEKLLEHVEMHGLYTeGLYRKSGAANRTRELRQALQTDpATVKLEDFP----IHAITGVLKQWLRELPEPLMTFAQ 1748
Cdd:cd04384    18 VPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSE-QIPDLTKDVyiqdIHSVSSLCKLYFRELPNPLLTYQL 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388444 1749 YGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCP 1819
Cdd:cd04384    96 YEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAPNLLRSK 166
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1845 1.67e-24

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 103.58  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSL------TSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PATVKLEDFPIHAITG 1730
Cdd:cd04391     2 FGVPLSTLlerdqkKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKfyEGTFLWDQVKQHDAAS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1731 VLKQWLRELPEPLMTfAQYGDFLRAVE-LPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1809
Cdd:cd04391    82 LLKLFIRELPQPLLT-VEYLPAFYSVQgLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAM 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 564388444 1810 IFAPCLLRC--PDNSDPLTSMKDVLKITTC---VEMLIKEQ 1845
Cdd:cd04391   161 IMAPNLFPPrgKHSKDNESLQEEVNMAAGCaniMRLLIRYQ 201
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1673-1844 3.63e-23

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 99.05  E-value: 3.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1673 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1752
Cdd:cd04390    22 VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYEDF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1753 LRAVELPEKQEQ--LAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRcPDNSDPLTSMKD 1830
Cdd:cd04390   102 LSCAQLLSKDEEkgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILR-PKVEDPATIMEG 180
                         170
                  ....*....|....
gi 564388444 1831 VLKITTCVEMLIKE 1844
Cdd:cd04390   181 TPQIQQLMTVMISK 194
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1842 1.12e-22

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 97.93  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLT----SDKASVPIVLEKLLEHVEMHgLYTEGLYRKSGAANRTRELRQALQTDPATvkLEDFPIHAITGVLKQ 1734
Cdd:cd04394     2 FGVPLHSLPhstvPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEAC--LSSALPCDVAGLLKQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1735 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1814
Cdd:cd04394    79 FFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPN 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 564388444 1815 LLRCPDNSDPLTS--MKDVLKITTCVEMLI 1842
Cdd:cd04394   159 LFQSEEGGEKMSSstEKRLRLQAAVVQTLI 188
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1673-1843 2.61e-22

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 97.19  E-value: 2.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1673 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1752
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1753 L-------------RAVELPEKQEQ---------LAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAII 1810
Cdd:cd04409    96 IglakesqhvnetqEAKKNSDKKWPnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGII 175
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 564388444 1811 FAPCLLRcPDNSDP---LTSMKDVLKITTCVEMLIK 1843
Cdd:cd04409   176 FGPTLIR-PRPTDAtvsLSSLVDYPHQARLVELLIT 210
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1679-1851 1.94e-21

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 94.45  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1679 KLLEHVEMHgLYTEGLYRKSGAANRTRELRQALQTD-PATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVE 1757
Cdd:cd04392    15 QLIEYLEKN-LRVEGLFRKPGNSARQQELRDLLNSGtDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIAD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1758 L------------PEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLrCPDNSDPL 1825
Cdd:cd04392    94 LcqfdekgnktsaPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI-CPRNLTPE 172
                         170       180
                  ....*....|....*....|....*.
gi 564388444 1826 TSMKDVLKITTCVEMLIKEQMRKYKV 1851
Cdd:cd04392   173 DLHENAQKLNSIVTFMIKHSQKLFKA 198
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1672-1854 1.98e-21

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 94.43  E-value: 1.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1672 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1751
Cdd:cd04376     8 QVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1752 FLRAVELpEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVAL-LEDV----------NRMSPGALAIIFAPCLLRCPD 1820
Cdd:cd04376    88 FIGTALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhAADSidedgqevsgNKMTSLNLATIFGPNLLHKQK 166
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564388444 1821 NSDPLTS-----MKDVLKITTCVEMLIKEQMRKYKVKME 1854
Cdd:cd04376   167 SGEREFVqaslrIEESTAIINVVQTMIDNYEELFMVSPE 205
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1835 1.45e-20

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 91.37  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLTSD---KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQW 1735
Cdd:cd04393     3 FGVPLQELQQAgqpENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLRLF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1736 LRELPEPLMTFAQYGDFLRAV-ELPEKQEQLAAIYAVLDHLPEANHtSLERLIFH-LVKVALLEDVNRMSPGALAIIFAP 1813
Cdd:cd04393    83 LQELPEGLIPASLQIRLMQLYqDYNGEDEFGRKLRDLLQQLPPVNY-SLLKFLCHfLSNVASQHHENRMTAENLAAVFGP 161
                         170       180
                  ....*....|....*....|..
gi 564388444 1814 CLLRCPDNSDPLTSMKDVLKIT 1835
Cdd:cd04393   162 DVFHVYTDVEDMKEQEICSRIM 183
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
1672-1815 1.52e-20

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 91.27  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1672 SVPIVLEKLLEHVEMHG-LYTEGLYRKSGAANRTRELRQALQTDpATVKL----EDFPIHAITGVLKQWLRELPEPLMTF 1746
Cdd:cd04400    21 DLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTE-YDVDLfsssLYPDVHTVAGLLKLYLRELPTLILGG 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1747 AQYGDFLRAVELPEKQEQLAAIYAVL-DHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1815
Cdd:cd04400   100 ELHNDFKRLVEENHDRSQRALELKDLvSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNVCIVFSPTL 169
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1673-1843 2.23e-19

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 87.83  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1673 VPIVLEKLLEHV-EMHGLYTEGLYRKSGAANRTRELRqaLQTDPATV---KLEDfpIHAITGVLKQWLRELPEPLMTFAQ 1748
Cdd:cd04389    21 LPWILTFLSEKVlALGGFQTEGIFRVPGDIDEVNELK--LRVDQWDYplsGLED--PHVPASLLKLWLRELEEPLIPDAL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1749 YGDFLRAVELPEKqeqlaaIYAVLDHLPEANHTSLERLIfHLVKVALLEDV---NRMSPGALAIIFAPCLLRCpDNSDPL 1825
Cdd:cd04389    97 YQQCISASEDPDK------AVEIVQKLPIINRLVLCYLI-NFLQVFAQPENvahTKMDVSNLAMVFAPNILRC-TSDDPR 168
                         170
                  ....*....|....*...
gi 564388444 1826 TSMKDVLKITTCVEMLIK 1843
Cdd:cd04389   169 VIFENTRKEMSFLRTLIE 186
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
1589-1643 2.38e-19

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410433  Cd Length: 58  Bit Score: 83.48  E-value: 2.38e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564388444 1589 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20883     1 EEHNGHIFKSTQYSIPTYCEYCSSLIWMMDRAYVCKLCRYACHKKCCLKTTTKCS 55
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1659-1815 3.64e-19

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 87.11  E-value: 3.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVD-----SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRqALQTDPATVKLEDFPIHAITGVLK 1733
Cdd:cd04381     1 FGASLSlaverSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELK-AAYNRRESPNLEEYEPPTVASLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1734 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1813
Cdd:cd04381    80 QYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSP 159

                  ..
gi 564388444 1814 CL 1815
Cdd:cd04381   160 TV 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1851 7.10e-19

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 87.47  E-value: 7.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVD-SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLR 1737
Cdd:cd04375     5 FGVPLLvNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYFR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1738 ELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1817
Cdd:cd04375    85 DLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSLFH 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1818 CP----DNSDPLTSMKDV--------------LKITTCVEMLIKEQMRKYKV 1851
Cdd:cd04375   165 LNtsrrENSSPARRMQRKkslgkpdqkelsenKAAHQCLAYMIEECNTLFMV 216
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1674-1824 3.95e-18

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 84.93  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1674 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTrELRQALQTDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1753
Cdd:cd04388    16 PPLLIKLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMI 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444 1754 RAVELPEKQEQLAAIYAVL---DHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1824
Cdd:cd04388    95 SRAQEVQSSDEYAQLLRKLirsPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSD 168
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1673-1824 1.37e-16

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 79.77  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1673 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQ--TDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1750
Cdd:cd04383    18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFErgEDPLADDQNDHDINSVAGVLKLYFRGLENPLFPKERFE 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388444 1751 DFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1824
Cdd:cd04383    98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPVPEGQDQ 171
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-114 4.57e-16

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 75.06  E-value: 4.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444    15 ATFHLHIYPQLPSAGSqTSCRVTATKDSTTSDVIRDVVASLHLDGSK-HYVLVEVKESGGEEWVLDASDSPVHRVLLWPr 93
Cdd:pfam00788    1 DDGVLKVYTEDGKPGT-TYKTILVSSSTTAEEVIEALLEKFGLEDDPrDYVLVEVLERGGGERRLPDDECPLQIQLQWP- 78
                           90       100
                   ....*....|....*....|.
gi 564388444    94 raqkehPREDGYYFLLQERNA 114
Cdd:pfam00788   79 ------RDASDSRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-113 7.03e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 71.56  E-value: 7.03e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444     15 ATFHLHIYPQLPSagSQTSCRVTATKDSTTSDVIRDVVASLHLDGS-KHYVLVEVKEsGGEEWVLDASDSPVHRVLLWPR 93
Cdd:smart00314    1 DTFVLRVYVDDLP--GGTYKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR 77
                            90       100
                    ....*....|....*....|
gi 564388444     94 raqkehpREDGYYFLLQERN 113
Cdd:smart00314   78 -------RGPNLRFVLRKRD 90
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1672-1820 2.39e-13

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 71.29  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1672 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDP---ATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQ 1748
Cdd:cd04396    31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPdygKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1749 YGDFLRAVELPEKQEQL--------------AAI--Y-AVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIF 1811
Cdd:cd04396   111 YEEFRNPLRKRPRILQYmkgrineplntdidQAIkeYrDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIF 190

                  ....*....
gi 564388444 1812 APCLLRCPD 1820
Cdd:cd04396   191 QPGILSHPD 199
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1650-1842 2.60e-13

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 71.24  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1650 SELGAEPGHFgvcvdsltsdkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDP-ATVKLEDFPIHAI 1728
Cdd:cd04397    16 STLGVGPGKL------------RIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPtEVPDLSKENPVQL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1729 TGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDV-----NRMS 1803
Cdd:cd04397    84 AALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKMD 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564388444 1804 PGALAIIFAPCLLRcPDNSDPLTSMKDVLKITTcVEMLI 1842
Cdd:cd04397   164 IHNLATVITPNILY-SKTDNPNTGDEYFLAIEA-VNYLI 200
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1594-1642 1.96e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 1.96e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 564388444   1594 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1594-1642 7.74e-12

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 61.76  E-value: 7.74e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWgLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
1591-1644 2.48e-11

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410375  Cd Length: 55  Bit Score: 60.37  E-value: 2.48e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564388444 1591 HNGHVFASYQVNIPQSCEQCLSYIWLMDkALLCSVCKMTCHKKCVHKIQ--SYCSY 1644
Cdd:cd20825     1 EGKHDFVLTQFQNATYCDFCKKKIWLKE-AFQCRLCGMICHKKCLDKCQaeTLCTR 55
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
1593-1643 1.97e-09

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 55.09  E-value: 1.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564388444 1593 GHVFASYQVNIPQSCEQCLSYIWlmDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20826     2 SHSFKEKSFRKPRTCDVCKQIIW--NEGSSCRVCKYACHRKCEPKVTAACS 50
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1672-1822 1.26e-08

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 57.35  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1672 SVPIVLEKLLEHVEMHGLYTEGLYRKSG----AANRTRELRQALQTDpaTVKLEDFPIHAITGVLKQWLRELPEPLMTFA 1747
Cdd:cd04380    49 SIPKEIWRLVDYLYTRGLAQEGLFEEPGlpsePGELLAEIRDALDTG--SPFNSPGSAESVAEALLLFLESLPDPIIPYS 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388444 1748 QYGDFLRAVELPEKQeqlaaIYAVLD-HLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1822
Cdd:cd04380   127 LYERLLEAVANNEED-----KRQVIRiSLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRA 197
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
19-95 6.72e-08

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 51.93  E-value: 6.72e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388444   19 LHIYPQLPSAGSQtSCRVTATKDSTTSDVIRDVVASLHLDGS-KHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17043     2 LKVYDDDLAPGSA-YKSILVSSTTTAREVVQLLLEKYGLEEDpEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQG 78
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
1594-1643 1.06e-07

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 50.01  E-value: 1.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20824     2 HNFKPHSFSIPTKCDYCGEKIWgLSKKGLSCKDCGFNCHIKCELKVPPECP 52
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
1592-1642 1.16e-07

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 50.36  E-value: 1.16e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564388444 1592 NGHVFASYQVNIP--QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20819     4 LGHHFVLQKSKSSskQYCDKCCGIIWgLLQTWYRCTDCGYRCHSKCLNSITRTC 57
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1594-1642 2.18e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.36  E-value: 2.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564388444  1594 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
1593-1643 4.64e-07

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 48.14  E-value: 4.64e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1593 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20832     1 GHQFVLQHYYQVTFCNHCSGLLWgIGYQGYQCSDCEFNIHKQCIEVIEESCP 52
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
1592-1642 1.23e-06

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410372  Cd Length: 52  Bit Score: 46.90  E-value: 1.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564388444 1592 NGHVFAS---YQVNipqSCEQCLSYiwLMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20822     1 RGHKFVQkqfYQIM---RCAVCGEF--LVNAGYQCEDCKYTCHKKCYEKVVTKC 49
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
1593-1642 1.53e-06

protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410370  Cd Length: 52  Bit Score: 46.67  E-value: 1.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564388444 1593 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20820     1 GHRFVPLELEQPTWCDLCGSVILgLFRKCLRCANCKMTCHPRCRSLVCLTC 51
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
1591-1643 2.18e-06

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410435  Cd Length: 54  Bit Score: 46.49  E-value: 2.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564388444 1591 HNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20885     1 GEGHDFQPCSLTNPTWCDLCGDFIWgLYKQCLRCTHCKYTCHLRCRDLVTLDCS 54
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1588-1646 3.74e-06

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 46.16  E-value: 3.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1588 VQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1646
Cdd:cd20834     2 VHEVKGHEFIAKFFRQPTFCSVCKEFLWgFNKQGYQCRQCNAAVHKKCHDKILGKCPGSA 61
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
1593-1643 5.16e-06

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 45.38  E-value: 5.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1593 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20803     1 GHSFRKKTFHKPTYCHHCTDLLWgLLNQGYQCEVCNFVSHERCLKTVVTPCS 52
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
1592-1643 6.12e-06

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 44.94  E-value: 6.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1592 NGHVFAsyQVNIPQSCEQCLSYIWLmdKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20816     1 QTHRFR--RLRTPSKCRECDSYVYF--NGAECEECGLACHKKCLETLAIQCG 48
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
1594-1634 6.68e-06

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 45.09  E-value: 6.68e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKC 1634
Cdd:cd20821     3 HRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDC 43
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1594-1642 8.20e-06

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 44.73  E-value: 8.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20837     1 HRFKVYNYMSPTFCDHCGSLLWgLFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
1594-1644 1.14e-05

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 44.36  E-value: 1.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1644
Cdd:cd20828     6 HNFEPHSFVTPTNCDYCLQILWgIVKKGMKCSECGYNCHEKCQPQVPKQCSK 57
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1593-1643 1.70e-05

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 43.77  E-value: 1.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1593 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20792     1 GHKFVATFFKQPTFCSHCKDFIWgLGKQGYQCQVCRFVVHKRCHEYVVFKCP 52
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
1591-1643 2.08e-05

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 43.87  E-value: 2.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564388444 1591 HNGHVFASYQVNIPQSCEQC-LSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20831     3 YNDHTFVATHFKGGPSCAVCnKLIPGRFGKqGYQCRDCGLICHKRCHVKVETHCP 57
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1001-1023 3.49e-05

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 42.31  E-value: 3.49e-05
                            10        20
                    ....*....|....*....|...
gi 564388444   1001 ERTRAAVYLQAAWRGYLQRQAYH 1023
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1586-1642 3.61e-05

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 43.22  E-value: 3.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564388444 1586 RAVQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDK-ALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20835     2 RRVHQVNGHKFMATYLRQPTYCSHCKDFIWgVIGKqGYQCQVCTCVVHKRCHQLVVTKC 60
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
1592-1643 6.20e-05

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 42.25  E-value: 6.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564388444 1592 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20794     1 NGHLFQAKRFNRRAVCAYCSDRIWgLGRQGYKCINCKLLVHKKCHKLVKVACG 53
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1594-1642 8.55e-05

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 41.87  E-value: 8.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20838     3 HRFSVHNYKRPTFCDHCGSLLYgLYKQGLQCKVCKMNVHKRCQKNVANNC 52
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
1594-1642 9.54e-05

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410414  Cd Length: 60  Bit Score: 41.93  E-value: 9.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLS-YIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20864     3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKAPSVC 52
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1591-1632 1.22e-04

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410425  Cd Length: 71  Bit Score: 41.94  E-value: 1.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 564388444 1591 HNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHK 1632
Cdd:cd20875     9 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 53
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1659-1818 1.54e-04

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 45.02  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1659 FGVCVDSLT-SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGA------ANRTRELRQALQTDPATVK----LEDFPIHA 1727
Cdd:cd04399     1 FGVDLETRCrLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVwtdpvsLKETHQLRNLLNKPKKPDKeviiLKKFEPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1728 ITGVLKQWLRELPEPLMTfAQYGDFLRAV-------ELPEKQEQLAAIYAVLDHLPEANHTSLERLIFHLVKvalLEDVN 1800
Cdd:cd04399    81 VASVLKLYLLELPDSLIP-HDIYDLIRSLysayppsQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYR---LIEIT 156
                         170       180
                  ....*....|....*....|....
gi 564388444 1801 RMSPGA------LAIIFAPCLLRC 1818
Cdd:cd04399   157 KMGESEeeyadkLATSLSREILRP 180
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
1593-1643 1.77e-04

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410436  Cd Length: 50  Bit Score: 40.83  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564388444 1593 GHVFASYQVnIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20886     3 GHRFEPGAL-GPGWCDLCGRYI--LSQALRCTNCKYTCHSECRDLVQLDCN 50
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
1607-1645 1.83e-04

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410350  Cd Length: 60  Bit Score: 41.15  E-value: 1.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564388444 1607 CEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1645
Cdd:cd20800    21 CREALSGV--TSHGLSCEVCKFKAHKRCAVKAPNNCKWT 57
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
1594-1642 2.27e-04

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 40.73  E-value: 2.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20796     2 HTFVVHTYTKPTVCQHCKKLLKgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
PRK13863 PRK13863
T-DNA border endonuclease VirD2;
953-1268 2.30e-04

T-DNA border endonuclease VirD2;


Pssm-ID: 237533 [Multi-domain]  Cd Length: 446  Bit Score: 46.09  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444  953 LHGEVLRRILLLQSWFRmvLERRHfVQMKHAALTIQACWRSYRVRRTLERTRAAVylqaawRGYLQRQAYHHQrhsiirl 1032
Cdd:PRK13863  134 LHVVVNRRELLGHGWLK--ISRRH-PQLNYDALRIKMAEISLRHGIVLDATSRAE------RGITERPMTYAQ------- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1033 qslcrghlQRRsfsqmmLEKQKAEQAR------ETAGAEMSEGEPSP---VAAGEQPSEHPVEDPESLGVETETWMNSKS 1103
Cdd:PRK13863  198 --------YRR------LERQQANQIRfedadfEEFSPGEDHREPSQsfdTSPGEAPQGEPESAERPEKLQNESEVRLQE 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1104 PNGLSPKKEIP---SPEMETPAQ----KTVPAESHEKVPSSREKRESRRQRGLEHVERQNkhIQSCREENSTLREPSRKA 1176
Cdd:PRK13863  264 PAGSSIKADARirvSLESERRAQpsasKIPVADDFGIETSYVAEGDVRKLEGNSGTPRLA--TEVATHTTSERQQRRKRP 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1177 SLETGEsfPEDTKEPREDGLETWTETAApscpkQVPIVGDPPRSpSPLQRPASLDLDSRVSPVLPSSSLESPQD--EDKG 1254
Cdd:PRK13863  342 RDDEGE--PSGAKRTRLNGIAVGPEANA-----GEQDGRDDPIT-SPAQPPRSNPLADPVRASIATDSLPATADrqQQRE 413
                         330
                  ....*....|....
gi 564388444 1255 ENSTKVQDKPESPS 1268
Cdd:PRK13863  414 PSSKRPRDDDGEPS 427
C1_DGKbeta_rpt1 cd20845
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG ...
1588-1645 2.57e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase beta contains two copies of the C1 domain. This model corresponds to the first one. DGK-beta contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410395  Cd Length: 66  Bit Score: 40.99  E-value: 2.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564388444 1588 VQEHNGHVFASYQVNIPQSCEQCLSY-IWLMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1645
Cdd:cd20845     2 VKDDGQHVWRLKHFNKPAYCNLCLNMlVGLGKQGLCCSFCKYTVHERCVQRAPASCIKT 60
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
1591-1645 3.08e-04

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 40.36  E-value: 3.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564388444 1591 HNGHVfASYQVniPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1645
Cdd:cd20795     4 HSLFV-HSYKS--PTFCDFCGEMLFgLVRQGLKCEGCGLNFHKRCAYKIPNNCTGS 56
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
1594-1642 4.59e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410439  Cd Length: 56  Bit Score: 39.87  E-value: 4.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20889     3 HTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKVVTPC 49
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
1594-1643 7.31e-04

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 39.23  E-value: 7.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVnIPQSCEQCLSYIWLmdkALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20812     3 HRFSKKLF-MRQTCDYCHKQMFF---GLKCKDCKYKCHKKCAKKAPPSCG 48
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1003-1023 8.78e-04

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 38.07  E-value: 8.78e-04
                           10        20
                   ....*....|....*....|.
gi 564388444  1003 TRAAVYLQAAWRGYLQRQAYH 1023
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1594-1642 9.29e-04

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 38.80  E-value: 9.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20793     1 HKFKVHTYYSPTFCDHCGSLLYgLVRQGLKCKDCGMNVHHRCKENVPHLC 50
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
1594-1645 9.36e-04

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 39.28  E-value: 9.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCSYT 1645
Cdd:cd20799     6 HVWRLKHFNKPAYCNVCENMLVGLRKqGLCCTFCKYTVHERCVSRAPASCIRT 58
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1594-1649 9.56e-04

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 39.62  E-value: 9.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRRK 1649
Cdd:cd20839     8 HALFVHSYRAPAFCDHCGEMLWgLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRR 64
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
1621-1643 1.02e-03

protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity, and interferes with AKT1 signaling. It contains an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410437  Cd Length: 53  Bit Score: 38.99  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|...
gi 564388444 1621 LLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20887    28 LVCRVCKVASHKKCEAKVTSACQ 50
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
1594-1643 1.05e-03

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 38.94  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20827     2 HRFEKHNFTTPTYCDYCSSLLWgLVKTGMRCADCGYSCHEKCLEHVPKNCT 52
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
1594-1644 1.25e-03

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 38.79  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1644
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVgLVRQGLVCEVCGYACHVSCADKAPQVCPV 52
C1_betaCHN cd20857
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ...
1594-1648 2.16e-03

protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410407  Cd Length: 61  Bit Score: 38.10  E-value: 2.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRR 1648
Cdd:cd20857     6 HNFKVHTFRGPHWCEYCANFMWgLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKR 61
RA_RASSF2_like cd01784
Ras-associating (RA) domain found in Ras-association domain family members, RASSF2, RASSF4, ...
26-92 2.29e-03

Ras-associating (RA) domain found in Ras-association domain family members, RASSF2, RASSF4, and RASSF6; The RASSF family of proteins shares a conserved RalGDS/AF6 RA domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). The classical family members (RASSF1-6) contain a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that functions as scaffolding and regulatory interactions. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. Classical RASSF members interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. The classical RASSF protein family seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. This family contains RASSF2, RASSF4, and RASSF6.


Pssm-ID: 340482  Cd Length: 87  Bit Score: 38.77  E-value: 2.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388444   26 PSAGSQTSCRVTATkdSTTSDVIRDVVASLH-LDGSKHYVLVEVKESGGEEwVLDASDSP-VHRVLLWP 92
Cdd:cd01784     9 PPYGSVTNVRVTSL--MTTPEVIKLLLEKFKvENSPEEFALYVVKDSGERR-RLKDDDYPlLTRVLLGP 74
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1045-1295 2.44e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 411408 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1045 FSQMMLEKQKAEQARETAGAEMSEGEPSPVAAGEQPSEHPVEDPESLGVETETWMNSKSPNGLSPKKEIPsPEMETPAQK 1124
Cdd:NF033839  275 FKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVK-PQLETPKPE 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1125 TVPAESHEKvPSSREKRESRRQRGLEHVERQNKHIQSCREENSTLREPSRKASLETGESFPEDTKEPREDGLETWTETAA 1204
Cdd:NF033839  354 VKPQPEKPK-PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVK 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1205 PSCPKQVPIVGDPPRSPSPLQRPASLDLDSRVSPVLPSSSLE-SPQDEDKGENSTKVQDKPESPSGSTQIQRYQHPDTER 1283
Cdd:NF033839  433 PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEvKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQA 512
                         250
                  ....*....|..
gi 564388444 1284 LATAVEIWRGKK 1295
Cdd:NF033839  513 STNEKATNKPKK 524
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1589-1637 2.49e-03

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410424  Cd Length: 69  Bit Score: 38.46  E-value: 2.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1589 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHKKCVHK 1637
Cdd:cd20874     3 LPHKGHEFIPTLYHFPANCEACAKPLWHVFKpppALECRRCHVKCHKDHLDK 54
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
1594-1642 3.86e-03

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410364  Cd Length: 56  Bit Score: 37.23  E-value: 3.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20814     5 HRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTC 53
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
1592-1643 3.88e-03

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410438  Cd Length: 57  Bit Score: 37.54  E-value: 3.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564388444 1592 NGHVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1643
Cdd:cd20888     4 HTHTFKVKTFKKVKSCGICKQAI--TREGSTCRVCKLSCHKKCEAKVATPCV 53
C1_AKAP13 cd20878
protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...
1592-1634 3.93e-03

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) and similar proteins; AKAP-13, also called AKAP-Lbc, breast cancer nuclear receptor-binding auxiliary protein (Brx-1), guanine nucleotide exchange factor Lbc, human thyroid-anchoring protein 31, lymphoid blast crisis oncogene (LBC oncogene), non-oncogenic Rho GTPase-specific GTP exchange factor, protein kinase A-anchoring protein 13 (PRKA13), or p47, is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors (GPCRs). It activates RhoA in response to GPCR signaling via its function as a Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Its Rho-GEF activity is regulated by protein kinase A (PKA), through binding and phosphorylation. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, and Brx) that contain a C1 domain followed by a dbl oncogene homology (DH) domain and a PH domain which are required for full transforming activity. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410428  Cd Length: 60  Bit Score: 37.32  E-value: 3.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564388444 1592 NGHVFASYQVNIPQSCEQClSYIWLMDKALLCSVCKMTCHKKC 1634
Cdd:cd20878     6 NGHVFSPVSSVGPTQCYHC-SKPLNTKDAFLCANCNVQVHKGC 47
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
1605-1636 4.77e-03

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 36.84  E-value: 4.77e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564388444 1605 QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVH 1636
Cdd:cd20830    12 QWCDKCGKFLFgLVHQGLQCQDCGLVCHRTCAA 44
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
1594-1642 4.94e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 37.65  E-value: 4.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20843    12 HTFVIHSYTRPTVCQFCKKLLkGLFRQGLQCKDCKFNCHKRCATRVPNDC 61
C1_ScPKC1-like_rpt2 cd20823
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
1591-1642 5.23e-03

second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410373  Cd Length: 59  Bit Score: 36.90  E-value: 5.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564388444 1591 HNGHVFASYQVNIPQSCEQClSYI--WLMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20823     2 RIPHRFEPFTNLGANWCCHC-GQMlpLGRKQIRKCTECGKTAHAQCAHLVPNFC 54
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
1592-1634 5.46e-03

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. Members of this family contain C1 domain found in aPKC isoform zeta. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410448  Cd Length: 55  Bit Score: 36.89  E-value: 5.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 564388444 1592 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKC 1634
Cdd:cd21095     1 NGHLFQAKRFNRRAYCGQCSERIWgLGRQGYKCINCKLLVHKRC 44
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1594-1642 5.50e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 38.07  E-value: 5.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20842    35 HTFVIHSYTRPTVCQYCKKLLkGLFRQGLQCKDCKFNCHKRCAPKVPNNC 84
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
1594-1643 5.64e-03

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 36.92  E-value: 5.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIqSYCS 1643
Cdd:cd20817     1 HSFQEHTFKKPTFCDVCKELLVgLSKQGLRCKNCKMNVHHKCQEGV-PDCS 50
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
1948-2063 6.39e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388444 1948 ASTESLLEERAVrgAAEGPPAPALPCPISPTPNPL-PAATAPPRGRPTSFVTVRVKTPRRTPIMPMANIKLPPGLPlhlt 2026
Cdd:PRK14950  354 AVIEALLVPVPA--PQPAKPTAAAPSPVRPTPAPStRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPES---- 427
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564388444 2027 swAPALQEAAVPV--KRREPPARRQDQVHSVYIAPGADL 2063
Cdd:PRK14950  428 --APKLTRAAIPVdeKPKYTPPAPPKEEEKALIADGDVL 464
C1_PIK3R-like_rpt1 cd20829
first protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
1594-1635 6.46e-03

first protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410379  Cd Length: 53  Bit Score: 36.56  E-value: 6.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIWLMDKAL-LCSVCKMTCHKKCV 1635
Cdd:cd20829     1 HRLVDVYFVTPILCRHCKDYIWGKGKVGvRCEDCHACFHLVCA 43
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
1594-1642 6.54e-03

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 36.55  E-value: 6.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564388444 1594 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1642
Cdd:cd20836     1 HKFKVHTYSSPTFCDHCGSLLYgLIHQGMKCDTCDMNVHKRCVKNVPSLC 50
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
979-998 7.03e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 7.03e-03
                            10        20
                    ....*....|....*....|
gi 564388444    979 QMKHAALTIQACWRSYRVRR 998
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARK 20
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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