NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157738625|ref|NP_001099036|]
View 

kinesin-like protein KIF13A isoform b [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 5-359 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 592.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQ-TVLHPPPSNTKQG-ERKPPKVFAFDYCFWSMDeSNTTKYAGQEVVFKCL 82
Cdd:cd01365     2 NVKVAVRVRPFNSREKERNSKCIVQMSGKEtTLKNPKQADKNNKaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYEDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   83 GEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISLEQNESQTFKVEVSYMEIYNEKVRDLLD 162
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  163 PK--GSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGN 240
Cdd:cd01365   161 PKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETNL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  241 SGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGK--GKSKFVPYRDSVLTWLLKDNLG 318
Cdd:cd01365   241 TTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKENLG 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 157738625  319 GNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVN 359
Cdd:cd01365   321 GNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 446-554 8.34e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 252.12  E-value: 8.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  446 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTPKENARSCVNGTLVCSTTQL 525
Cdd:cd22729     1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80

                          90       100
                  ....*....|....*....|....*....
gi 157738625  526 WHGDRILWGNNHFFRINLPKRKRRDWLKD 554
Cdd:cd22729    81 WHGDRILWGNNHFFRINLPKRKRRDWLKE 109
Kinesin_assoc super family cl24686
Kinesin-associated;
356-468 1.48e-21

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 93.75  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   356 AVVNEDPNAKVIRELREEVEKLREQL-SQA--EAMKAPELKEKLEESEKL------------------------------ 402
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyAQGlgDIIDTIAHPTKKRANTPAanasaataamagaspspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   403 -------------------------IKELTVTWEEKLRKTEEIAQERQRQLESMGISLEMSGIKVG----DDKCYLVNLN 453
Cdd:pfam16183   81 slherimftpgseeaierlketekiIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 157738625   454 ADPALNELLVYYLKD 468
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 748-792 1.45e-15

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


:

Pssm-ID: 463574  Cd Length: 43  Bit Score: 71.86  E-value: 1.45e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157738625   748 LENKLIDMRDLYQEWKEKVPEAKrlYGKRGDPFYEAQENHNLIGV 792
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQH--FEVDRDPFYEPPENHNLIGV 43
DUF3694 super family cl13857
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1215-1279 1.15e-10

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


The actual alignment was detected with superfamily member pfam12473:

Pssm-ID: 463599  Cd Length: 149  Bit Score: 61.45  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738625  1215 PIIKHSDD---EVSATASWDSSVHDSVHLNRVTPQNERIYLIVKTTVQLSHpAAMELVLRKRIAANIY 1279
Cdd:pfam12473   79 PVVRFNADgtsSYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEK-CAEPVRFSMDTAVQIY 145
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 552-770 1.51e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   552 LKDFEKETGPPEHDLDAASEASSEPDynyefAQMEVIMKTLNSNDPvqnvvqvlEKQYLEEKRSALEEQRLMYERELEQL 631
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELE-----AEIEELEERLEEAEE--------ELAEAEAEIEELEAQIEQLKEELKAL 801

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   632 RQQLSPDRQPQSSGPDRLAYSSQTAQQKVTQWAEERDELFR--QSLAKLREQLVKantlvreanfLAEEMSKLTDYQVTL 709
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleEQIEELSEDIES----------LAAEIEELEELIEEL 871

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738625   710 QIPAANLSANRKrgaiVSEPAIQVRRKGKSTQVWTIEKLENKLIDMRDLYQEWKEKVPEAK 770
Cdd:TIGR02168  872 ESELEALLNERA----SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 5-359 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 592.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQ-TVLHPPPSNTKQG-ERKPPKVFAFDYCFWSMDeSNTTKYAGQEVVFKCL 82
Cdd:cd01365     2 NVKVAVRVRPFNSREKERNSKCIVQMSGKEtTLKNPKQADKNNKaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYEDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   83 GEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISLEQNESQTFKVEVSYMEIYNEKVRDLLD 162
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  163 PK--GSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGN 240
Cdd:cd01365   161 PKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETNL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  241 SGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGK--GKSKFVPYRDSVLTWLLKDNLG 318
Cdd:cd01365   241 TTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKENLG 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 157738625  319 GNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVN 359
Cdd:cd01365   321 GNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-359 1.94e-150

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 465.12  E-value: 1.94e-150
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625      6 VKVAVRVRPMNRRELELNTKCVVEMEGN--QTVLHPPPSNtkqgeRKPPKVFAFDYCFwsmDESNTtkyagQEVVFKCLG 83
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKvgKTLTVRSPKN-----RQGEKKFTFDKVF---DATAS-----QEDVFEETA 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625     84 EGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISlEQNESQTFKVEVSYMEIYNEKVRDLLDP 163
Cdd:smart00129   69 APLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKID-KREEGWQFSVKVSYLEIYNEKIRDLLNP 147

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    164 kgSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTlyDLQSGNSGE 243
Cdd:smart00129  148 --SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQK--IKNSSSGSG 223

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    244 KVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQaagkGKSKFVPYRDSVLTWLLKDNLGGNSQT 323
Cdd:smart00129  224 KASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQH----SKSRHIPYRDSKLTRLLQDSLGGNSKT 299

                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 157738625    324 SMIATISPAADNYEETLSTLRYADRAKRIVNHAVVN 359
Cdd:smart00129  300 LMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-352 2.06e-143

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 445.86  E-value: 2.06e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    11 RVRPMNRRELELNTKCVVEMEGnqtVLHPPPSNTKQGERKPPKVFAFDYCFWSmdesNTTkyagQEVVFKCLGEGILEKA 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES---VDSETVESSHLTNKNRTKTFTFDKVFDP----EAT----QEDVYEETAKPLVESV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    91 FQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISlEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQ-S 169
Cdd:pfam00225   70 LEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQ-KTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKrK 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   170 LKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGeKVSKVS 249
Cdd:pfam00225  149 LRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKLN 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   250 LVDLAGSERVSKTGAA-GERLKEGSNINKSLTTLGLVISSLADqaagkGKSKFVPYRDSVLTWLLKDNLGGNSQTSMIAT 328
Cdd:pfam00225  228 LVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIAN 302

                          330       340
                   ....*....|....*....|....
gi 157738625   329 ISPAADNYEETLSTLRYADRAKRI 352
Cdd:pfam00225  303 ISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-383 2.21e-87

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 297.42  E-value: 2.21e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   47 GERKPPKVFAFDYCFwsmDESNTtkyagQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLC 126
Cdd:COG5059    50 LEKSKEGTYAFDKVF---GPSAT-----QEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  127 CALFKRISLeQNESQTFKVEVSYMEIYNEKVRDLLDPKgsRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKS 206
Cdd:COG5059   122 KELFSKLED-LSMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKN 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  207 RTVAATNMNEESSRSHAVFNIIITQTlydlQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVI 286
Cdd:COG5059   199 RTTASTEINDESSRSHSIFQIELASK----NKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVI 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  287 SSLADqaagKGKSKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNE--DPNA 364
Cdd:COG5059   275 NALGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssDSSR 350

                         330       340
                  ....*....|....*....|....*
gi 157738625  365 KV------IRELREEVEKLREQLSQ 383
Cdd:COG5059   351 EIeeikfdLSEDRSEIEILVFREQS 375
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 446-554 8.34e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 252.12  E-value: 8.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  446 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTPKENARSCVNGTLVCSTTQL 525
Cdd:cd22729     1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80

                          90       100
                  ....*....|....*....|....*....
gi 157738625  526 WHGDRILWGNNHFFRINLPKRKRRDWLKD 554
Cdd:cd22729    81 WHGDRILWGNNHFFRINLPKRKRRDWLKE 109
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 1-378 8.24e-75

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 274.89  E-value: 8.24e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    1 MSDTKVKVAVRVRPMNRRELElnTKCVVEMEGNqtvlhpppSNTKQGErkppkVFAFDycfwSMDESNTTkyagQEVVFK 80
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGEEG--EMIVQKMSND--------SLTINGQ-----TFTFD----SIADPEST----QEDIFQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   81 CLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHA----------EQLGLIPRLCCALFKRISLEQ---NESQ-TFKVE 146
Cdd:PLN03188  152 LVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhADRQlKYQCR 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  147 VSYMEIYNEKVRDLLDPkgSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFN 226
Cdd:PLN03188  232 CSFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  227 IIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLAdQAAGKGKSKFVPYRD 306
Cdd:PLN03188  310 CVVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILA-EISQTGKQRHIPYRD 388

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738625  307 SVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNE----DPN--AKVIRELREEVEKLR 378
Cdd:PLN03188  389 SRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
Kinesin_assoc pfam16183
Kinesin-associated;
356-468 1.48e-21

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 93.75  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   356 AVVNEDPNAKVIRELREEVEKLREQL-SQA--EAMKAPELKEKLEESEKL------------------------------ 402
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyAQGlgDIIDTIAHPTKKRANTPAanasaataamagaspspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   403 -------------------------IKELTVTWEEKLRKTEEIAQERQRQLESMGISLEMSGIKVG----DDKCYLVNLN 453
Cdd:pfam16183   81 slherimftpgseeaierlketekiIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 157738625   454 ADPALNELLVYYLKD 468
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 748-792 1.45e-15

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 71.86  E-value: 1.45e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157738625   748 LENKLIDMRDLYQEWKEKVPEAKrlYGKRGDPFYEAQENHNLIGV 792
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQH--FEVDRDPFYEPPENHNLIGV 43
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1215-1279 1.15e-10

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 61.45  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738625  1215 PIIKHSDD---EVSATASWDSSVHDSVHLNRVTPQNERIYLIVKTTVQLSHpAAMELVLRKRIAANIY 1279
Cdd:pfam12473   79 PVVRFNADgtsSYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEK-CAEPVRFSMDTAVQIY 145
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 470-533 3.18e-08

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 51.81  E-value: 3.18e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738625   470 TRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTP-KENARSCVNGTLVCST-TQLWHGDRILW 533
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDlGSTNGTFVNGQRLGPEpVRLKDGDVIRL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 552-770 1.51e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   552 LKDFEKETGPPEHDLDAASEASSEPDynyefAQMEVIMKTLNSNDPvqnvvqvlEKQYLEEKRSALEEQRLMYERELEQL 631
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELE-----AEIEELEERLEEAEE--------ELAEAEAEIEELEAQIEQLKEELKAL 801

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   632 RQQLSPDRQPQSSGPDRLAYSSQTAQQKVTQWAEERDELFR--QSLAKLREQLVKantlvreanfLAEEMSKLTDYQVTL 709
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleEQIEELSEDIES----------LAAEIEELEELIEEL 871

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738625   710 QIPAANLSANRKrgaiVSEPAIQVRRKGKSTQVWTIEKLENKLIDMRDLYQEWKEKVPEAK 770
Cdd:TIGR02168  872 ESELEALLNERA----SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 470-519 4.15e-03

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 36.77  E-value: 4.15e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 157738625    470 TRVG-ADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTP-KENARSCVNGTLV 519
Cdd:smart00240    1 VTIGrSSEDCDIQLDGPSISRRHAVIVYDGGGRFYLIDlGSTNGTFVNGKRI 52
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
591-761 5.05e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  591 TLNSNDP------VQNVVQVLEKQYLEEKRSALEEQRLMYERELEQLRQQLspdrqpqssgpdrlayssQTAQQKVTQ-- 662
Cdd:COG3206   141 SYTSPDPelaaavANALAEAYLEQNLELRREEARKALEFLEEQLPELRKEL------------------EEAEAALEEfr 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  663 ------WAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLtdyqvtLQIPAANLSanrkrgAIVSEPAIQVRRK 736
Cdd:COG3206   203 qknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ------LGSGPDALP------ELLQSPVIQQLRA 270

                         170       180
                  ....*....|....*....|....*
gi 157738625  737 gkstqvwTIEKLENKLIDMRDLYQE 761
Cdd:COG3206   271 -------QLAELEAELAELSARYTP 288
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 5-359 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 592.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQ-TVLHPPPSNTKQG-ERKPPKVFAFDYCFWSMDeSNTTKYAGQEVVFKCL 82
Cdd:cd01365     2 NVKVAVRVRPFNSREKERNSKCIVQMSGKEtTLKNPKQADKNNKaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYEDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   83 GEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISLEQNESQTFKVEVSYMEIYNEKVRDLLD 162
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLLN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  163 PK--GSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGN 240
Cdd:cd01365   161 PKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETNL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  241 SGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGK--GKSKFVPYRDSVLTWLLKDNLG 318
Cdd:cd01365   241 TTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKENLG 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 157738625  319 GNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVN 359
Cdd:cd01365   321 GNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-359 1.94e-150

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 465.12  E-value: 1.94e-150
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625      6 VKVAVRVRPMNRRELELNTKCVVEMEGN--QTVLHPPPSNtkqgeRKPPKVFAFDYCFwsmDESNTtkyagQEVVFKCLG 83
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKvgKTLTVRSPKN-----RQGEKKFTFDKVF---DATAS-----QEDVFEETA 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625     84 EGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISlEQNESQTFKVEVSYMEIYNEKVRDLLDP 163
Cdd:smart00129   69 APLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKID-KREEGWQFSVKVSYLEIYNEKIRDLLNP 147

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    164 kgSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTlyDLQSGNSGE 243
Cdd:smart00129  148 --SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQK--IKNSSSGSG 223

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    244 KVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQaagkGKSKFVPYRDSVLTWLLKDNLGGNSQT 323
Cdd:smart00129  224 KASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQH----SKSRHIPYRDSKLTRLLQDSLGGNSKT 299

                           330       340       350
                    ....*....|....*....|....*....|....*.
gi 157738625    324 SMIATISPAADNYEETLSTLRYADRAKRIVNHAVVN 359
Cdd:smart00129  300 LMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-352 2.06e-143

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 445.86  E-value: 2.06e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    11 RVRPMNRRELELNTKCVVEMEGnqtVLHPPPSNTKQGERKPPKVFAFDYCFWSmdesNTTkyagQEVVFKCLGEGILEKA 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVES---VDSETVESSHLTNKNRTKTFTFDKVFDP----EAT----QEDVYEETAKPLVESV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    91 FQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISlEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQ-S 169
Cdd:pfam00225   70 LEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQ-KTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKrK 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   170 LKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGeKVSKVS 249
Cdd:pfam00225  149 LRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKLN 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   250 LVDLAGSERVSKTGAA-GERLKEGSNINKSLTTLGLVISSLADqaagkGKSKFVPYRDSVLTWLLKDNLGGNSQTSMIAT 328
Cdd:pfam00225  228 LVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIAN 302

                          330       340
                   ....*....|....*....|....
gi 157738625   329 ISPAADNYEETLSTLRYADRAKRI 352
Cdd:pfam00225  303 ISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 5-350 1.72e-141

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 440.54  E-value: 1.72e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPpsntkQGERKPPKVFAFDYCFWSmdesNTTkyagQEVVFKCLGE 84
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPP-----KNRVAPPKTFAFDAVFDS----TST----QEEVYEGTAK 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   85 GILEKAFQGYNACIFAYGQTGSGKSFSMMG-HAEQLGLIPRLCCALFKRISLEQNESQTFKVEVSYMEIYNEKVRDLLDP 163
Cdd:cd00106    68 PLVDSALEGYNGTIFAYGQTGSGKTYTMLGpDPEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLLSP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  164 KgSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQtlYDLQSGNSGE 243
Cdd:cd00106   148 V-PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGESV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  244 KVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaagkGKSKFVPYRDSVLTWLLKDNLGGNSQT 323
Cdd:cd00106   225 TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTRLLQDSLGGNSKT 299

                         330       340
                  ....*....|....*....|....*..
gi 157738625  324 SMIATISPAADNYEETLSTLRYADRAK 350
Cdd:cd00106   300 IMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 6-352 1.53e-117

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 374.88  E-value: 1.53e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    6 VKVAVRVRPMNRRELELNTKCVVEME--GNQTVLHPPpsntKQGERKPPKVFAFDYCF-WSmdesnttkyAGQEVVFKCL 82
Cdd:cd01371     3 VKVVVRCRPLNGKEKAAGALQIVDVDekRGQVSVRNP----KATANEPPKTFTFDAVFdPN---------SKQLDVYDET 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   83 GEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQL---GLIPRLCCALFKRISLEQNeSQTFKVEVSYMEIYNEKVRD 159
Cdd:cd01371    70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQN-NQQFLVRVSYLEIYNEEIRD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  160 LLDpKGSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIItQTLYDLQSG 239
Cdd:cd01371   149 LLG-KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI-ECSEKGEDG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  240 NSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaagkGKSKFVPYRDSVLTWLLKDNLGG 319
Cdd:cd01371   227 ENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGG 301

                         330       340       350
                  ....*....|....*....|....*....|...
gi 157738625  320 NSQTSMIATISPAADNYEETLSTLRYADRAKRI 352
Cdd:cd01371   302 NSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 3-352 1.22e-109

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 352.02  E-value: 1.22e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    3 DTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLhpppSNTKQGErkppKVFAFDYCFwsmdESNTTkyagQEVVFKCL 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVV----IATSETG----KTFSFDRVF----DPNTT----QEDVYNFA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   83 GEGILEKAFQGYNACIFAYGQTGSGKSFSMMG---HAEQLGLIPRLCCALFKRISLeQNESQTFKVEVSYMEIYNEKVRD 159
Cdd:cd01369    65 AKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGklgDPESMGIIPRIVQDIFETIYS-MDENLEFHVKVSYFEIYMEKIRD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  160 LLDPkgSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTlyDLQSG 239
Cdd:cd01369   144 LLDV--SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETE 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  240 NSgeKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaagkGKSKFVPYRDSVLTWLLKDNLGG 319
Cdd:cd01369   220 KK--KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLGG 292

                         330       340       350
                  ....*....|....*....|....*....|...
gi 157738625  320 NSQTSMIATISPAADNYEETLSTLRYADRAKRI 352
Cdd:cd01369   293 NSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 5-352 7.09e-109

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 349.71  E-value: 7.09e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTkqgerkppkvFAFDYCFwsmDESNTTKyagqeVVFKCLGE 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPPSTS----------FTFDHVF---GGDSTNR-----EVYELIAK 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   85 GILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRIslEQNESQTFKVEVSYMEIYNEKVRDLLDPK 164
Cdd:cd01374    63 PVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKI--QDTPDREFLLRVSYLEIYNEKINDLLSPT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  165 GsrQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTlYDLQSGNSGEK 244
Cdd:cd01374   141 S--QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESS-ERGELEEGTVR 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  245 VSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaagKGKSKFVPYRDSVLTWLLKDNLGGNSQTS 324
Cdd:cd01374   218 VSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----GKVGGHIPYRDSKLTRILQPSLGGNSRTA 293

                         330       340
                  ....*....|....*....|....*...
gi 157738625  325 MIATISPAADNYEETLSTLRYADRAKRI 352
Cdd:cd01374   294 IICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 6-352 1.03e-108

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 350.09  E-value: 1.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    6 VKVAVRVRPMNRRELELNTKCVVE-MEGNQTVlhpppsntkQGERKppKVFAFDYCFWSMDEsnttkyagQEVVFKCLGE 84
Cdd:cd01372     3 VRVAVRVRPLLPKEIIEGCRICVSfVPGEPQV---------TVGTD--KSFTFDYVFDPSTE--------QEEVYNTCVA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   85 GILEKAFQGYNACIFAYGQTGSGKSFSM-MGHA-----EQLGLIPRLCCALFKRISLEQNESQtFKVEVSYMEIYNEKVR 158
Cdd:cd01372    64 PLVDGLFEGYNATVLAYGQTGSGKTYTMgTAYTaeedeEQVGIIPRAIQHIFKKIEKKKDTFE-FQLKVSFLEIYNEEIR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  159 DLLDPKGSRQS-LKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQ 237
Cdd:cd01372   143 DLLDPETDKKPtISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGP 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  238 SGNSGEK------VSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaaGKGKSKFVPYRDSVLTW 311
Cdd:cd01372   223 IAPMSADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD---ESKKGAHVPYRDSKLTR 299

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 157738625  312 LLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRI 352
Cdd:cd01372   300 LLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 6-352 3.33e-103

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 334.70  E-value: 3.33e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    6 VKVAVRVRPMNRRELELNTKCVVE-MEGNQTVLHPP-----------PSNTKQGERKPPKVFAFDYCFwsmDESNTtkya 73
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVKvMDNHMLVFDPKdeedgffhggsNNRDRRKRRNKELKYVFDRVF---DETST---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   74 gQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISlEQNESQTFKVEVSYMEIY 153
Cdd:cd01370    75 -QEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIE-SLKDEKEFEVSMSYLEIY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  154 NEKVRDLLDPKGSRqsLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTl 233
Cdd:cd01370   153 NETIRDLLNPSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  234 YDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaaGKGKSKFVPYRDSVLTWLL 313
Cdd:cd01370   230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTRLL 306

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 157738625  314 KDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRI 352
Cdd:cd01370   307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 5-354 3.79e-102

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 331.10  E-value: 3.79e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQgerkppKVFAFDYCFwSMDESnttkyagQEVVFKCLgE 84
Cdd:cd01366     3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIGAKQ------KEFSFDKVF-DPEAS-------QEDVFEEV-S 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   85 GILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISLEQNESQTFKVEVSYMEIYNEKVRDLLDP- 163
Cdd:cd01366    68 PLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAPg 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  164 KGSRQSLKVREHKVLGP-YVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQtlYDLQSGNSg 242
Cdd:cd01366   148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISG--RNLQTGEI- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  243 eKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaagkgKSKFVPYRDSVLTWLLKDNLGGNSQ 322
Cdd:cd01366   225 -SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQ------KQSHIPYRNSKLTYLLQDSLGGNSK 297

                         330       340       350
                  ....*....|....*....|....*....|..
gi 157738625  323 TSMIATISPAADNYEETLSTLRYADRAKRIVN 354
Cdd:cd01366   298 TLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 6-361 1.13e-99

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 324.85  E-value: 1.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    6 VKVAVRVRPMNRRELELN-TKCVVEMEGNQTVLHPppsntkqgerKPPKVFAFDYCFwsmdESNTTkyagQEVVFKCLGE 84
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEyGQCLKKLSSDTLVLHS----------KPPKTFTFDHVA----DSNTN----QESVFQSVGK 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   85 GILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQL--------GLIPRLCCALFKRISLEQNESQ---TFKVEVSYMEIY 153
Cdd:cd01373    65 PIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEKAGegkSFLCKCSFLEIY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  154 NEKVRDLLDPkgSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQtl 233
Cdd:cd01373   145 NEQIYDLLDP--ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES-- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  234 YDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAagKGKSKFVPYRDSVLTWLL 313
Cdd:cd01373   221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVA--HGKQRHVCYRDSKLTFLL 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 157738625  314 KDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNED 361
Cdd:cd01373   299 RDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 3-361 1.01e-90

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 299.24  E-value: 1.01e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    3 DTKVKVAVRVRPMNRRELELNTKCVVEMEGNQ---TVLHPPPSNTKQgerkpPKVFAFDYCFWSmdesnttkYAGQEVVF 79
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRkevSVRTGGLADKSS-----TKTYTFDMVFGP--------EAKQIDVY 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   80 KCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMG-----------HAEQLGLIPRLCCALFKRISLEQNEsqtFKVEVS 148
Cdd:cd01364    68 RSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE---YSVKVS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  149 YMEIYNEKVRDLLDPKGS-RQSLKVRE--HKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVF 225
Cdd:cd01364   145 YLEIYNEELFDLLSPSSDvSERLRMFDdpRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  226 NIiitqTLYDLQSGNSGE---KVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADqaagkgKSKFV 302
Cdd:cd01364   225 SI----TIHIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHV 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157738625  303 PYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNED 361
Cdd:cd01364   295 PYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
47-383 2.21e-87

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 297.42  E-value: 2.21e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   47 GERKPPKVFAFDYCFwsmDESNTtkyagQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLC 126
Cdd:COG5059    50 LEKSKEGTYAFDKVF---GPSAT-----QEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  127 CALFKRISLeQNESQTFKVEVSYMEIYNEKVRDLLDPKgsRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKS 206
Cdd:COG5059   122 KELFSKLED-LSMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKN 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  207 RTVAATNMNEESSRSHAVFNIIITQTlydlQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVI 286
Cdd:COG5059   199 RTTASTEINDESSRSHSIFQIELASK----NKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVI 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  287 SSLADqaagKGKSKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNE--DPNA 364
Cdd:COG5059   275 NALGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssDSSR 350

                         330       340
                  ....*....|....*....|....*
gi 157738625  365 KV------IRELREEVEKLREQLSQ 383
Cdd:COG5059   351 EIeeikfdLSEDRSEIEILVFREQS 375
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 5-350 4.47e-82

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 274.27  E-value: 4.47e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQTV-LHPPP-----SNTKQGERKPPKvFAFDYCFwsmdESNTTkyagQEVV 78
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVvLHPPKgsaanKSERNGGQKETK-FSFSKVF----GPNTT----QKEF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   79 FKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRIsleqnesQTFKVEVSYMEIYNEKVR 158
Cdd:cd01368    73 FQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSI-------GGYSVFVSYIEIYNEYIY 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  159 DLLDPKGS-----RQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTL 233
Cdd:cd01368   146 DLLEPSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAP 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  234 YDLQSGNSGEK----VSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQaAGKGKSKFVPYRDSVL 309
Cdd:cd01368   226 GDSDGDVDQDKdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREN-QLQGTNKMVPFRDSKL 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 157738625  310 TWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAK 350
Cdd:cd01368   305 THLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 446-554 8.34e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 252.12  E-value: 8.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  446 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTPKENARSCVNGTLVCSTTQL 525
Cdd:cd22729     1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80

                          90       100
                  ....*....|....*....|....*....
gi 157738625  526 WHGDRILWGNNHFFRINLPKRKRRDWLKD 554
Cdd:cd22729    81 WHGDRILWGNNHFFRINLPKRKRRDWLKE 109
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 1-378 8.24e-75

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 274.89  E-value: 8.24e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    1 MSDTKVKVAVRVRPMNRRELElnTKCVVEMEGNqtvlhpppSNTKQGErkppkVFAFDycfwSMDESNTTkyagQEVVFK 80
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGEEG--EMIVQKMSND--------SLTINGQ-----TFTFD----SIADPEST----QEDIFQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   81 CLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHA----------EQLGLIPRLCCALFKRISLEQ---NESQ-TFKVE 146
Cdd:PLN03188  152 LVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhADRQlKYQCR 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  147 VSYMEIYNEKVRDLLDPkgSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFN 226
Cdd:PLN03188  232 CSFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  227 IIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLAdQAAGKGKSKFVPYRD 306
Cdd:PLN03188  310 CVVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILA-EISQTGKQRHIPYRD 388

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738625  307 SVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNE----DPN--AKVIRELREEVEKLR 378
Cdd:PLN03188  389 SRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 5-350 7.19e-73

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 247.11  E-value: 7.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELntkcVVEMEGNQTV-LHPP------PSNTKQGERKppkvFAFDYCFwsmdesnttKYAGQEV 77
Cdd:cd01375     1 KVQAFVRVRPTDDFAHEM----IKYGEDGKSIsIHLKkdlrrgVVNNQQEDWS----FKFDGVL---------HNASQEL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   78 VFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQL---GLIPRLCCALFKRIslEQNESQTFKVEVSYMEIYN 154
Cdd:cd01375    64 VYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMI--EERPTKAYTVHVSYLEIYN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  155 EKVRDLLDPK----GSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIIT 230
Cdd:cd01375   142 EQLYDLLSTLpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLE 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  231 QTLYDLQSgnsgEKV--SKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQaagkgKSKFVPYRDSV 308
Cdd:cd01375   222 AHSRTLSS----EKYitSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-----DRTHVPFRQSK 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 157738625  309 LTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAK 350
Cdd:cd01375   293 LTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 5-350 1.57e-72

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 246.05  E-value: 1.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    5 KVKVAVRVRPMNRRELELNTKCVVEMEGNQTVL-HPPPSN---TKQGERKppkVFAFDYCFwsmDESNTTkyagqEVVFK 80
Cdd:cd01367     1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIvHEPKLKvdlTKYIENH---TFRFDYVF---DESSSN-----ETVYR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   81 CLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMG----HAEQLGLIPRLCCALFKRISlEQNESQTFKVEVSYMEIYNEK 156
Cdd:cd01367    70 STVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLN-KLPYKDNLGVTVSFFEIYGGK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  157 VRDLLDPKgsrQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIItqtlydl 236
Cdd:cd01367   149 VFDLLNRK---KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  237 QSGNSGEKVSKVSLVDLAGSERVSKTGAAG-ERLKEGSNINKSLTTLGLVISSLADQaagkgkSKFVPYRDSVLTWLLKD 315
Cdd:cd01367   219 RDRGTNKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQN------KAHIPFRGSKLTQVLKD 292

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 157738625  316 NL-GGNSQTSMIATISPAADNYEETLSTLRYADRAK 350
Cdd:cd01367   293 SFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 6-350 1.50e-68

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 234.32  E-value: 1.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    6 VKVAVRVRP-MNRRELELNTKCVVEMEGNQTVLHPPpsnTKQGErkpPKVFAFDYCFWsmDESNTTK-YAGQevvFKCLG 83
Cdd:cd01376     2 VRVAVRVRPfVDGTAGASDPSCVSGIDSCSVELADP---RNHGE---TLKYQFDAFYG--EESTQEDiYARE---VQPIV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   84 EGILEkafqGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALfkrISLEQNESQTFKVEVSYMEIYNEKVRDLLDP 163
Cdd:cd01376    71 PHLLE----GQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDL---LQMTRKEAWALSFTMSYLEIYQEKILDLLEP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  164 KGSrqSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLydlQSGNSGE 243
Cdd:cd01376   144 ASK--ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE---RLAPFRQ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  244 KVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLadqaaGKGKSKfVPYRDSVLTWLLKDNLGGNSQT 323
Cdd:cd01376   219 RTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL-----NKNLPR-IPYRDSKLTRLLQDSLGGGSRC 292

                         330       340
                  ....*....|....*....|....*..
gi 157738625  324 SMIATISPAADNYEETLSTLRYADRAK 350
Cdd:cd01376   293 IMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
 446-544 1.81e-59

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 199.44  E-value: 1.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  446 KCYLVNLNADPALNELLVYYLKDHTRVG---ADTSQDIQLFGIGIQPQHCEIDIaSDGDVTLTPKENARSCVNGTLVCST 522
Cdd:cd22706     1 KYYLVNLNADPSLNELLVYYLKEHTLIGrsdAPTQQDIQLSGLGIQPEHCIITI-ENEDVYLTPLEGARTCVNGSIVTEK 79

                          90       100
                  ....*....|....*....|..
gi 157738625  523 TQLWHGDRILWGNNHFFRINLP 544
Cdd:cd22706    80 TQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 446-544 1.26e-53

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 182.42  E-value: 1.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  446 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTPKENARSCVNGTLVCSTTQL 525
Cdd:cd22730     1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80

                          90
                  ....*....|....*....
gi 157738625  526 WHGDRILWGNNHFFRINLP 544
Cdd:cd22730    81 HHGDRILWGNNHFFRINLP 99
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
 448-542 9.46e-33

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 123.11  E-value: 9.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYYLKD-HTRVG---ADTSQDIQLFGIGIQPQHCEIDiASDGDVTLTPKENARSCVNGTLVCSTT 523
Cdd:cd22705     3 HLVNLNEDPLMSECLLYYIKPgITRVGradADVPQDIQLSGTHILEEHCTFE-NEDGVVTLEPCEGALTYVNGKRVTEPT 81

                          90
                  ....*....|....*....
gi 157738625  524 QLWHGDRILWGNNHFFRIN 542
Cdd:cd22705    82 RLKTGSRVILGKNHVFRFN 100
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
 449-544 2.43e-28

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 110.43  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  449 LVNLNADPALNELLVYYLKD-HTRVG---ADTSQDIQLFGIGIQPQHCEIdIASDGDVTLTPKENARSCVNGTLVCSTTQ 524
Cdd:cd22707    10 LVNLNEDPQLSEMLLYMLKEgQTRVGrskASSSHDIQLSGALIADDHCTI-ENNGGKVTIIPVGDAETYVNGELISEPTV 88

                          90       100
                  ....*....|....*....|
gi 157738625  525 LWHGDRILWGNNHFFRINLP 544
Cdd:cd22707    89 LHHGDRVILGGDHYFRFNHP 108
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 447-544 1.64e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 102.29  E-value: 1.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  447 CYLVNLNADPALNELLVYYLKD-HTRVG---ADTSQDIQLFGIGIQPQHCEIdIASDGDVTLTPKEN-ARSCVNGTLVCS 521
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEgETTIGradAEPEPDIVLSGLSIQKQHAVI-TNTDGKVTIEPVSPgAKVIVNGVPVTG 79

                          90       100
                  ....*....|....*....|...
gi 157738625  522 TTQLWHGDRILWGNNHFFRINLP 544
Cdd:cd22709    80 ETELHHLDRVILGSNHLYVFVGP 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 71-288 3.02e-22

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: 95.49  E-value: 3.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   71 KYAGQEVVFKCLGEgILEKAFQGYN-ACIFAYGQTGSGKSFSMMGhaeqlgLIPRLCCALFKRISLEQNESQtfkvevsy 149
Cdd:cd01363    28 RSESQPHVFAIADP-AYQSMLDGYNnQSIFAYGESGAGKTETMKG------VIPYLASVAFNGINKGETEGW-------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  150 meiynekvrdlldpkgsrqslkvrehkvlgpyvDGLSQLAVTSFEDIESLMSEGNKSRTvAATNMNEESSRSHAVFNIii 229
Cdd:cd01363    93 ---------------------------------VYLTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEI-- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157738625  230 tqtlydlqsgnsgekvskvsLVDLAGSERvsktgaagerlkegsnINKSLTTLGLVISS 288
Cdd:cd01363   137 --------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
 448-546 1.16e-21

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 91.64  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYYLKDH-TRVG---ADTSQDIQLFGIGIQPQHCEI--DIASDGDV--TLTPKENARSCVNGTLV 519
Cdd:cd22727     4 HLVNLNEDPLMSECLLYYIKDGiTRVGqadAERRQDIVLSGAHIKEEHCIFrsERNNNGEVivTLEPCERSETYVNGKRV 83

                          90       100
                  ....*....|....*....|....*..
gi 157738625  520 CSTTQLWHGDRILWGNNHFFRINLPKR 546
Cdd:cd22727    84 VQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
Kinesin_assoc pfam16183
Kinesin-associated;
356-468 1.48e-21

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 93.75  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   356 AVVNEDPNAKVIRELREEVEKLREQL-SQA--EAMKAPELKEKLEESEKL------------------------------ 402
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyAQGlgDIIDTIAHPTKKRANTPAanasaataamagaspspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   403 -------------------------IKELTVTWEEKLRKTEEIAQERQRQLESMGISLEMSGIKVG----DDKCYLVNLN 453
Cdd:pfam16183   81 slherimftpgseeaierlketekiIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 157738625   454 ADPALNELLVYYLKD 468
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
 448-550 5.85e-20

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 86.91  E-value: 5.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYYLKDH-TRVG---ADTSQDIQLFGIGIQPQHC--EIDIASDGD--VTLTPKENARSCVNGTLV 519
Cdd:cd22726     3 HLVNLNEDPLMSECLLYYIKDGiTRVGredAERRQDIVLSGHFIKEEHCifRSDTRSGGEavVTLEPCEGADTYVNGKKV 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 157738625  520 CSTTQLWHGDRILWGNNHFFRINLPKRKRRD 550
Cdd:cd22726    83 TEPSILRSGNRIIMGKSHVFRFNHPEQARQE 113
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 447-544 9.46e-19

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 83.14  E-value: 9.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  447 CYLVNLNADPALNELL-VYYLKDH-TRVGADTS-----QDIQLFGIGIQPQHCeiDIAS-DGDVTLTP-KENARSCVNGT 517
Cdd:cd22711     2 PYLLELSPDGSDRDKPrRHRLQPNvTEVGSERSpansgQFIQLFGPDILPRHC--VITHmEGVVTVTPaSQDAETYVNGQ 79

                          90       100
                  ....*....|....*....|....*..
gi 157738625  518 LVCSTTQLWHGDRILWGNNHFFRINLP 544
Cdd:cd22711    80 RIYETTMLQHGMVVQFGRSHTFRFCDP 106
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 5-161 2.65e-18

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 83.04  E-value: 2.65e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625     5 KVKVAVRVRPMNRRELELNTkcvvemegnqtvlhPPPSNTKQGERKPPKVFAFDYCFwsmdESNTTkyagQEVVF---KC 81
Cdd:pfam16796   21 NIRVFARVRPELLSEAQIDY--------------PDETSSDGKIGSKNKSFSFDRVF----PPESE----QEDVFqeiSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625    82 LgegiLEKAFQGYNACIFAYGQTGSGKSFSMmghaeqlglIPRLCCALFKRISlEQNESQTFKVEVSYMEIYNEKVRDLL 161
Cdd:pfam16796   79 L----VQSCLDGYNVCIFAYGQTGSGSNDGM---------IPRAREQIFRFIS-SLKKGWKYTIELQFVEIYNESSQDLL 144
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
 448-542 2.43e-17

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 79.14  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYYLKDH-TRVGaDTSQDIQLFGIGIQPQHCEIDIASDGD----VTLTPKENARSCVNGTLVCST 522
Cdd:cd22728     3 HLVNLNEDPLMSECLLYHIKDGvTRVG-QVDVDIKLSGQFIREQHCLFRSIPNPSgevvVTLEPCEGAETYVNGKQVTEP 81

                          90       100
                  ....*....|....*....|
gi 157738625  523 TQLWHGDRILWGNNHFFRIN 542
Cdd:cd22728    82 LVLKSGNRIVMGKNHVFRFN 101
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
 448-544 4.87e-16

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 75.39  E-value: 4.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYYLKD-HTRVG---ADTSQDIQLFGIGIQPQHCEIDIAsDGDVTLTPKENARSCVNGTLVCSTT 523
Cdd:cd22708    10 HLIGIDDDLLSTGVVLYHLKEgKTRIGredAPQEQDIVLDGEDIEAEHCIIENV-GGVVTLHPLPGALCAVNGQVITQPT 88

                          90       100
                  ....*....|....*....|.
gi 157738625  524 QLWHGDRILWGNNHFFRINLP 544
Cdd:cd22708    89 RLTQGDVILLGKTNMFRFNHP 109
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 748-792 1.45e-15

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 71.86  E-value: 1.45e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157738625   748 LENKLIDMRDLYQEWKEKVPEAKrlYGKRGDPFYEAQENHNLIGV 792
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQH--FEVDRDPFYEPPENHNLIGV 43
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 448-545 1.06e-11

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 63.41  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYYLKD-HTRVGAD---TSQDIQLFGIGIQPQHCEIDiASDGDVTLTPKENARSCVNGTLVCSTT 523
Cdd:cd22732    10 HLIGIDDDLLSTGIILYHLKEgRTYVGRDdatTEQDIVLHGLDLESEHCIFE-NLNGTVTLIPLNGAQCSVNGVQITEAT 88

                          90       100
                  ....*....|....*....|..
gi 157738625  524 QLWHGDRILWGNNHFFRINLPK 545
Cdd:cd22732    89 QLNQGAVILLGRTNMFRFNHPK 110
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
 448-549 2.33e-11

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 62.48  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYYLKDHT----RVGADTSQDIQLFGIGIQPQHCEIDiASDGDVTLTPKENARSCVNGTLVCSTT 523
Cdd:cd22731    10 HLIAMDDDILSTGVVLYHLREGTtkigRSDSEQEQDIVLQGPWIERDHCMIH-NECGVVTLRPAQGAQCTVNGREVTESC 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 157738625  524 QLWHGDRILWGNNHFFRINLPK-----RKRR 549
Cdd:cd22731    89 RLSQGAVIVLGKTHKFRFNHPAeaailRQRR 119
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1215-1279 1.15e-10

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 61.45  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157738625  1215 PIIKHSDD---EVSATASWDSSVHDSVHLNRVTPQNERIYLIVKTTVQLSHpAAMELVLRKRIAANIY 1279
Cdd:pfam12473   79 PVVRFNADgtsSYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEK-CAEPVRFSMDTAVQIY 145
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
 445-539 7.46e-10

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 58.08  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  445 DKCYLVNLNADPALNELLVYYLKDHTR-VGADTSQ----DIQLFGIGIQPQHCEI--------------DIASDGDVTLT 505
Cdd:cd22712     2 DYPYLLTLRGFSPKQDLLVYPLLEQVIlVGSRTEGarkvDISLRAPDILPQHCWIrrkpeplsddedsdKESADYRVVLS 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 157738625  506 PKENARSCVNGTLVCSTTQLWHGDRILWGNNHFF 539
Cdd:cd22712    82 PLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLF 115
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
 438-549 1.10e-09

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 57.72  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  438 SGIKVGDDKCYLVNLNADPALNELLVYYLKD-HTRVGADTSQDIQLFGIGIQPQHCEIDiASDGDVTLTPKENARScVNG 516
Cdd:cd22713     8 KALKVQTEKPHLVSLGSGRLSTAVTLLPLPEgKTTIGTAASDIISLQGPGVEPEHCYIE-NINGTVTLYPCGNLCS-VDG 85

                          90       100       110
                  ....*....|....*....|....*....|...
gi 157738625  517 TLVCSTTQLWHGDRILWGNNHFFRINLPKRKRR 549
Cdd:cd22713    86 LPITEPTRLTQGCMICLGRSNYFRFNHPAEAKR 118
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 470-533 3.18e-08

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 51.81  E-value: 3.18e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157738625   470 TRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTP-KENARSCVNGTLVCST-TQLWHGDRILW 533
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDlGSTNGTFVNGQRLGPEpVRLKDGDVIRL 66
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 448-538 3.66e-08

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 52.66  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  448 YLVNLNADPALNELLVYylKDHTRVGADTSQDIQLFGIGIQPQHCEIDIaSDGDVTLTPKE-NARSCVNGTLVCSTTQLW 526
Cdd:cd00060     1 RLIVLDGDGGGREFPLT--KGVVTIGRSPDCDIVLDDPSVSRRHARIEV-DGGGVYLEDLGsTNGTFVNGKRITPPVPLQ 77

                          90
                  ....*....|..
gi 157738625  527 HGDRILWGNNHF 538
Cdd:cd00060    78 DGDVIRLGDTTF 89
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 467-538 7.43e-08

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 51.83  E-value: 7.43e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157738625  467 KDHTRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTPK-ENARSCVNGTLVCSTTQLWHGDRILWGNNHF 538
Cdd:cd22673    20 KKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGKAYLENLsTTNPTLVNGKAIEKSAELKDGDVITIGGRSF 92
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
98-289 2.61e-06

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 52.43  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   98 IFAYGQTGSGKSFSMMghaEQLGLIPRLCC-ALFKRISLEQNESQTFKVEVSYMEIY-NEKVRDLLDPKGSRQSLKVREH 175
Cdd:COG5059   385 IFAYMQSLKKETETLK---SRIDLIMKSIIsGTFERKKLLKEEGWKYKSTLQFLRIEiDRLLLLREEELSKKKTKIHKLN 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  176 KVLGPYVDGLSQLavtSFEDIESLMSEGNKS-RTVAATNMNEESSRSHAVFNIIITQTlydlqsgNSGEKVSKVSLVDLA 254
Cdd:COG5059   462 KLRHDLSSLLSSI---PEETSDRVESEKASKlRSSASTKLNLRSSRSHSKFRDHLNGS-------NSSTKELSLNQVDLA 531

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 157738625  255 GSERVSKTgAAGERLKEGSNINKSLTTLGLVISSL 289
Cdd:COG5059   532 GSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 552-770 1.51e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   552 LKDFEKETGPPEHDLDAASEASSEPDynyefAQMEVIMKTLNSNDPvqnvvqvlEKQYLEEKRSALEEQRLMYERELEQL 631
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELE-----AEIEELEERLEEAEE--------ELAEAEAEIEELEAQIEQLKEELKAL 801

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625   632 RQQLSPDRQPQSSGPDRLAYSSQTAQQKVTQWAEERDELFR--QSLAKLREQLVKantlvreanfLAEEMSKLTDYQVTL 709
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleEQIEELSEDIES----------LAAEIEELEELIEEL 871

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157738625   710 QIPAANLSANRKrgaiVSEPAIQVRRKGKSTQVWTIEKLENKLIDMRDLYQEWKEKVPEAK 770
Cdd:TIGR02168  872 ESELEALLNERA----SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 470-519 4.15e-03

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 36.77  E-value: 4.15e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 157738625    470 TRVG-ADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTP-KENARSCVNGTLV 519
Cdd:smart00240    1 VTIGrSSEDCDIQLDGPSISRRHAVIVYDGGGRFYLIDlGSTNGTFVNGKRI 52
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
591-761 5.05e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  591 TLNSNDP------VQNVVQVLEKQYLEEKRSALEEQRLMYERELEQLRQQLspdrqpqssgpdrlayssQTAQQKVTQ-- 662
Cdd:COG3206   141 SYTSPDPelaaavANALAEAYLEQNLELRREEARKALEFLEEQLPELRKEL------------------EEAEAALEEfr 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157738625  663 ------WAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLtdyqvtLQIPAANLSanrkrgAIVSEPAIQVRRK 736
Cdd:COG3206   203 qknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ------LGSGPDALP------ELLQSPVIQQLRA 270

                         170       180
                  ....*....|....*....|....*
gi 157738625  737 gkstqvwTIEKLENKLIDMRDLYQE 761
Cdd:COG3206   271 -------QLAELEAELAELSARYTP 288
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH