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Conserved domains on  [gi|300798152|ref|NP_001179823|]
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calpain-5 [Bos taurus]

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C2 pfam00648
Calpain family cysteine protease;
27-341 0e+00

Calpain family cysteine protease;


:

Pssm-ID: 279042  Cd Length: 292  Bit Score: 517.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   27 FEDPNFPATDDSLYYKGSPGPTVRWKRPKDICEDPRLFVDGISSHDLHQGQVGNCWFVAACSSLASRESLWQKVIPDwke 106
Cdd:pfam00648   1 FEDPEFPADDSSLGYSPKPPRKIEWKRPKEICSNPQFFVDGASRFDICQGELGDCWFLAALASLTLRPDLLKRVVPP--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  107 qewDPEKPNAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEKAYAKLAGCYQALDGGNTADAL 186
Cdd:pfam00648  78 ---DQSFEENYAGIFHFRFWRFGEWVDVVIDDRLPTINGRLLFVHSADKNEFWSALLEKAYAKLHGSYEALKGGSTSEAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  187 VDFTGGVSEPIDLTEgdfandeaKRNQLFERVLKVHSRGGLISASIKAvTAADMEARLACGLVKGHAYAITDVRKVRLgh 266
Cdd:pfam00648 155 EDFTGGVTESIDLKK--------APPDLWEILLKALKRGSLMGCSIDA-TPTEEEAVLPNGLVKGHAYSVTGVREVNY-- 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798152  267 gllaffKSEKLDMIRLRNPWGEREWNGPWSDTSEEWQKVSKSEREKLGVTVQDDGEFWMTFEDLCRYFTDIIKCR 341
Cdd:pfam00648 224 ------KGGKVRLVRLRNPWGEVEWNGAWSDGSPEWQSVSPEEKKKLGLTFADDGEFWMSFEDFLKNFTDLEICN 292
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
515-638 1.35e-60

C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 176011  Cd Length: 126  Bit Score: 199.81  E-value: 1.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 515 PQQVTQVHVLGAAGLK--DSPTGANSYVIIKCEGDKVRSAVQKGTSTPEYDVKGVFYRKKPSQPITVQIWNHRVLKDEFL 592
Cdd:cd04046    1 PQVVTQVHVHSAEGLSkqDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300798152 593 GQVHLKANADDLQALHTLHLRDRNSRQPSDLPGTVAVRVLSSASLT 638
Cdd:cd04046   81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
354-493 3.23e-57

Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.


:

Pssm-ID: 279416  Cd Length: 146  Bit Score: 191.22  E-value: 3.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  354 WEEARLRGAWTRHEdplqnRSGGCINHKDSFFQNPQYIFDVKKPED-------EVLISIQQRPKQSTRRDGKgENLAIGF 426
Cdd:pfam01067   1 WEESVFEGRWVRGS-----TAGGCRNYPDTFWTNPQYRITLTEPDDddddgecTVLVSLMQKNRRRLRREGL-DLLTIGF 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300798152  427 DIYKV--EENRQYRMHSLQHR---AASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPS 493
Cdd:pfam01067  75 AIYKVpkEQNRKLRRHFFLRNqpvARSSTFINLREVSLRFRLPPGEYVIVPSTFEPNEEGEFLLRIFSEKES 146
 
Name Accession Description Interval E-value
Peptidase_C2 pfam00648
Calpain family cysteine protease;
27-341 0e+00

Calpain family cysteine protease;


Pssm-ID: 279042  Cd Length: 292  Bit Score: 517.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   27 FEDPNFPATDDSLYYKGSPGPTVRWKRPKDICEDPRLFVDGISSHDLHQGQVGNCWFVAACSSLASRESLWQKVIPDwke 106
Cdd:pfam00648   1 FEDPEFPADDSSLGYSPKPPRKIEWKRPKEICSNPQFFVDGASRFDICQGELGDCWFLAALASLTLRPDLLKRVVPP--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  107 qewDPEKPNAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEKAYAKLAGCYQALDGGNTADAL 186
Cdd:pfam00648  78 ---DQSFEENYAGIFHFRFWRFGEWVDVVIDDRLPTINGRLLFVHSADKNEFWSALLEKAYAKLHGSYEALKGGSTSEAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  187 VDFTGGVSEPIDLTEgdfandeaKRNQLFERVLKVHSRGGLISASIKAvTAADMEARLACGLVKGHAYAITDVRKVRLgh 266
Cdd:pfam00648 155 EDFTGGVTESIDLKK--------APPDLWEILLKALKRGSLMGCSIDA-TPTEEEAVLPNGLVKGHAYSVTGVREVNY-- 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798152  267 gllaffKSEKLDMIRLRNPWGEREWNGPWSDTSEEWQKVSKSEREKLGVTVQDDGEFWMTFEDLCRYFTDIIKCR 341
Cdd:pfam00648 224 ------KGGKVRLVRLRNPWGEVEWNGAWSDGSPEWQSVSPEEKKKLGLTFADDGEFWMSFEDFLKNFTDLEICN 292
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
13-351 1.66e-175

Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).


Pssm-ID: 128526  Cd Length: 318  Bit Score: 504.55  E-value: 1.66e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152    13 YSALKRACLRRKVLFEDPNFPATDDSLYYKGSPGPTVRWKRPKDICEDPRLFVDGISSHDLHQGQVGNCWFVAACSSLAS 92
Cdd:smart00230   1 YEALRQYCKESGTLFEDPLFPANNGSLFFSQRQRKFVVWKRPHEIFENPPFIVGGASRTDICQGVLGDCWLLAALASLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152    93 RESLWQKVIPdwKEQEWDPekpnAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEKAYAKLAG 172
Cdd:smart00230  81 REKLLDRVIP--HDQEFSE----NYAGIFHFRFWRFGKWVDVVIDDRLPTYNGELVFMHSNSRNEFWSALLEKAYAKLNG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   173 CYQALDGGNTADALVDFTGGVSEPIDLTEGDFandeaKRNQLFERVLKVHSRGGLISASIKAVTAADMEARLACGLVKGH 252
Cdd:smart00230 155 CYEALKGGSTTEALEDLTGGVAESIDLKEASK-----DPDNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   253 AYAITDVRKVRLGHgllaffksekLDMIRLRNPWGEREWNGPWSDTSEEWQKVSKSEREKLGVTVQDDGEFWMTFEDLCR 332
Cdd:smart00230 230 AYSVTDVREVQGRR----------QELLRLRNPWGQVEWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLR 299
                          330
                   ....*....|....*....
gi 300798152   333 YFTDIIKCRLINTSYLSIH 351
Cdd:smart00230 300 HFDKVEICNLNPDSLEERS 318
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
16-341 1.26e-138

Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.


Pssm-ID: 238004  Cd Length: 315  Bit Score: 410.18  E-value: 1.26e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  16 LKRACLRRKVLFEDPNFPATDDSLYYK-----GSPGPTVRWKRPKDICED-----PRLFVDGISSHDLHQGQVGNCWFVA 85
Cdd:cd00044    2 LLQICLLSGVLFEDPDFPPNDSSLGFDdslsnGQPKKVIEWKRPSEIFADdgnsnPRLFVNGASPSDVCQGILGDCWFLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  86 ACSSLASRESLWQKVIPDWKEQEwdpekpNAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEK 165
Cdd:cd00044   82 ALAALAERPELLKRVIPPDQSFE------ENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFMHSRDRNELWVALLEK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 166 AYAKLAGCYQALDGGNTADALVDFTGGVSEPIDLTEGDFANDEakrNQLFERVLKVHSRGGLISASIKAVTAAdmEARLA 245
Cdd:cd00044  156 AYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADASSGD---NDLFALLLSFLQGGSLIGCSTGSRSEE--EARTA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 246 CGLVKGHAYAITDVRKvrlghgllafFKSEKLDMIRLRNPWGEREWNGPWSDTSEEWQkVSKSEREKLGVTVQDDGEFWM 325
Cdd:cd00044  231 NGLVKGHAYSVLDVRE----------VQEEGLRLLRLRNPWGVGEWWGGWSDDSSEWW-VIDAERKKLLLSGKDDGEFWM 299
                        330
                 ....*....|....*.
gi 300798152 326 TFEDLCRYFTDIIKCR 341
Cdd:cd00044  300 SFEDFLRNFDGLYVCN 315
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
515-638 1.35e-60

C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176011  Cd Length: 126  Bit Score: 199.81  E-value: 1.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 515 PQQVTQVHVLGAAGLK--DSPTGANSYVIIKCEGDKVRSAVQKGTSTPEYDVKGVFYRKKPSQPITVQIWNHRVLKDEFL 592
Cdd:cd04046    1 PQVVTQVHVHSAEGLSkqDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300798152 593 GQVHLKANADDLQALHTLHLRDRNSRQPSDLPGTVAVRVLSSASLT 638
Cdd:cd04046   81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
354-493 3.23e-57

Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.


Pssm-ID: 279416  Cd Length: 146  Bit Score: 191.22  E-value: 3.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  354 WEEARLRGAWTRHEdplqnRSGGCINHKDSFFQNPQYIFDVKKPED-------EVLISIQQRPKQSTRRDGKgENLAIGF 426
Cdd:pfam01067   1 WEESVFEGRWVRGS-----TAGGCRNYPDTFWTNPQYRITLTEPDDddddgecTVLVSLMQKNRRRLRREGL-DLLTIGF 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300798152  427 DIYKV--EENRQYRMHSLQHR---AASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPS 493
Cdd:pfam01067  75 AIYKVpkEQNRKLRRHFFLRNqpvARSSTFINLREVSLRFRLPPGEYVIVPSTFEPNEEGEFLLRIFSEKES 146
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
352-498 9.40e-55

Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.


Pssm-ID: 238132  Cd Length: 150  Bit Score: 184.42  E-value: 9.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 352 KTWEEARLRGAWTRHedplqNRSGGCINHKDSFFQNPQYIFDVKKPED-----EVLISIQQRPKQSTRRDGKgENLAIGF 426
Cdd:cd00214    1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEPDDdegkcTVLIALMQKNRRHLRKKGL-DLLTIGF 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798152 427 DIYKV-EENRQYRMHSLQH---RAASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPSSCREL 498
Cdd:cd00214   75 HVYKVpGENRHLRRDFFLHkapRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
calpain_III smart00720
calpain_III domain;
354-496 1.03e-49

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 170.24  E-value: 1.03e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   354 WEEARLRGAWTRHEdplqnRSGGCINHKDSFFQNPQYIFDVKKPEDE---VLISIQQRPKQSTRRDGKgENLAIGFDIYK 430
Cdd:smart00720   1 WHTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEPDDDdctVLIALMQKNRRRLRRKGA-DFLTIGFAVYK 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300798152   431 VEEN---RQYRMHSLQHRAASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPSSCR 496
Cdd:smart00720  75 VPKElhlRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
C2 pfam00168
C2 domain;
521-609 1.14e-08

C2 domain;


Pssm-ID: 278593  Cd Length: 104  Bit Score: 53.09  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  521 VHVLGAAGL--KDSPTGANSYVIIKCEGD--KVRSAVQKGTSTPEYDVKGVFYRKKP-SQPITVQIWNH-RVLKDEFLGQ 594
Cdd:pfam00168   5 VTVIEAKNLppKDLNGKSDPYVKVSLLDGkqKKKTKVVKNTLNPVWNETFTFSVPDPeNAVLEIEVYDYdRFGRDDFLGE 84
                          90
                  ....*....|....*
gi 300798152  595 VHLKANADDLQALHT 609
Cdd:pfam00168  85 VRIPLSELDLGEVLD 99
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
521-597 2.67e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577  Cd Length: 101  Bit Score: 52.10  E-value: 2.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   521 VHVLGAAGL--KDSPTGANSYVIIKCEGD---KVRSAVQKGTSTPEYDVKGVFYRKKP-SQPITVQIWNH-RVLKDEFLG 593
Cdd:smart00239   4 VKIISARNLppKDKGGKSDPYVKVSLDGDpkeKKKTKVVKNTLNPVWNETFEFEVPPPeLAELEIEVYDKdRFGRDDFIG 83

                   ....
gi 300798152   594 QVHL 597
Cdd:smart00239  84 QVTI 87
 
Name Accession Description Interval E-value
Peptidase_C2 pfam00648
Calpain family cysteine protease;
27-341 0e+00

Calpain family cysteine protease;


Pssm-ID: 279042  Cd Length: 292  Bit Score: 517.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   27 FEDPNFPATDDSLYYKGSPGPTVRWKRPKDICEDPRLFVDGISSHDLHQGQVGNCWFVAACSSLASRESLWQKVIPDwke 106
Cdd:pfam00648   1 FEDPEFPADDSSLGYSPKPPRKIEWKRPKEICSNPQFFVDGASRFDICQGELGDCWFLAALASLTLRPDLLKRVVPP--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  107 qewDPEKPNAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEKAYAKLAGCYQALDGGNTADAL 186
Cdd:pfam00648  78 ---DQSFEENYAGIFHFRFWRFGEWVDVVIDDRLPTINGRLLFVHSADKNEFWSALLEKAYAKLHGSYEALKGGSTSEAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  187 VDFTGGVSEPIDLTEgdfandeaKRNQLFERVLKVHSRGGLISASIKAvTAADMEARLACGLVKGHAYAITDVRKVRLgh 266
Cdd:pfam00648 155 EDFTGGVTESIDLKK--------APPDLWEILLKALKRGSLMGCSIDA-TPTEEEAVLPNGLVKGHAYSVTGVREVNY-- 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798152  267 gllaffKSEKLDMIRLRNPWGEREWNGPWSDTSEEWQKVSKSEREKLGVTVQDDGEFWMTFEDLCRYFTDIIKCR 341
Cdd:pfam00648 224 ------KGGKVRLVRLRNPWGEVEWNGAWSDGSPEWQSVSPEEKKKLGLTFADDGEFWMSFEDFLKNFTDLEICN 292
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
13-351 1.66e-175

Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).


Pssm-ID: 128526  Cd Length: 318  Bit Score: 504.55  E-value: 1.66e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152    13 YSALKRACLRRKVLFEDPNFPATDDSLYYKGSPGPTVRWKRPKDICEDPRLFVDGISSHDLHQGQVGNCWFVAACSSLAS 92
Cdd:smart00230   1 YEALRQYCKESGTLFEDPLFPANNGSLFFSQRQRKFVVWKRPHEIFENPPFIVGGASRTDICQGVLGDCWLLAALASLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152    93 RESLWQKVIPdwKEQEWDPekpnAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEKAYAKLAG 172
Cdd:smart00230  81 REKLLDRVIP--HDQEFSE----NYAGIFHFRFWRFGKWVDVVIDDRLPTYNGELVFMHSNSRNEFWSALLEKAYAKLNG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   173 CYQALDGGNTADALVDFTGGVSEPIDLTEGDFandeaKRNQLFERVLKVHSRGGLISASIKAVTAADMEARLACGLVKGH 252
Cdd:smart00230 155 CYEALKGGSTTEALEDLTGGVAESIDLKEASK-----DPDNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   253 AYAITDVRKVRLGHgllaffksekLDMIRLRNPWGEREWNGPWSDTSEEWQKVSKSEREKLGVTVQDDGEFWMTFEDLCR 332
Cdd:smart00230 230 AYSVTDVREVQGRR----------QELLRLRNPWGQVEWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLR 299
                          330
                   ....*....|....*....
gi 300798152   333 YFTDIIKCRLINTSYLSIH 351
Cdd:smart00230 300 HFDKVEICNLNPDSLEERS 318
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
16-341 1.26e-138

Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.


Pssm-ID: 238004  Cd Length: 315  Bit Score: 410.18  E-value: 1.26e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  16 LKRACLRRKVLFEDPNFPATDDSLYYK-----GSPGPTVRWKRPKDICED-----PRLFVDGISSHDLHQGQVGNCWFVA 85
Cdd:cd00044    2 LLQICLLSGVLFEDPDFPPNDSSLGFDdslsnGQPKKVIEWKRPSEIFADdgnsnPRLFVNGASPSDVCQGILGDCWFLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  86 ACSSLASRESLWQKVIPDWKEQEwdpekpNAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEK 165
Cdd:cd00044   82 ALAALAERPELLKRVIPPDQSFE------ENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFMHSRDRNELWVALLEK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 166 AYAKLAGCYQALDGGNTADALVDFTGGVSEPIDLTEGDFANDEakrNQLFERVLKVHSRGGLISASIKAVTAAdmEARLA 245
Cdd:cd00044  156 AYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADASSGD---NDLFALLLSFLQGGSLIGCSTGSRSEE--EARTA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 246 CGLVKGHAYAITDVRKvrlghgllafFKSEKLDMIRLRNPWGEREWNGPWSDTSEEWQkVSKSEREKLGVTVQDDGEFWM 325
Cdd:cd00044  231 NGLVKGHAYSVLDVRE----------VQEEGLRLLRLRNPWGVGEWWGGWSDDSSEWW-VIDAERKKLLLSGKDDGEFWM 299
                        330
                 ....*....|....*.
gi 300798152 326 TFEDLCRYFTDIIKCR 341
Cdd:cd00044  300 SFEDFLRNFDGLYVCN 315
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
515-638 1.35e-60

C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176011  Cd Length: 126  Bit Score: 199.81  E-value: 1.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 515 PQQVTQVHVLGAAGLK--DSPTGANSYVIIKCEGDKVRSAVQKGTSTPEYDVKGVFYRKKPSQPITVQIWNHRVLKDEFL 592
Cdd:cd04046    1 PQVVTQVHVHSAEGLSkqDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300798152 593 GQVHLKANADDLQALHTLHLRDRNSRQPSDLPGTVAVRVLSSASLT 638
Cdd:cd04046   81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
354-493 3.23e-57

Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.


Pssm-ID: 279416  Cd Length: 146  Bit Score: 191.22  E-value: 3.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  354 WEEARLRGAWTRHEdplqnRSGGCINHKDSFFQNPQYIFDVKKPED-------EVLISIQQRPKQSTRRDGKgENLAIGF 426
Cdd:pfam01067   1 WEESVFEGRWVRGS-----TAGGCRNYPDTFWTNPQYRITLTEPDDddddgecTVLVSLMQKNRRRLRREGL-DLLTIGF 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300798152  427 DIYKV--EENRQYRMHSLQHR---AASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPS 493
Cdd:pfam01067  75 AIYKVpkEQNRKLRRHFFLRNqpvARSSTFINLREVSLRFRLPPGEYVIVPSTFEPNEEGEFLLRIFSEKES 146
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
352-498 9.40e-55

Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.


Pssm-ID: 238132  Cd Length: 150  Bit Score: 184.42  E-value: 9.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 352 KTWEEARLRGAWTRHedplqNRSGGCINHKDSFFQNPQYIFDVKKPED-----EVLISIQQRPKQSTRRDGKgENLAIGF 426
Cdd:cd00214    1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEPDDdegkcTVLIALMQKNRRHLRKKGL-DLLTIGF 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798152 427 DIYKV-EENRQYRMHSLQH---RAASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPSSCREL 498
Cdd:cd00214   75 HVYKVpGENRHLRRDFFLHkapRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
calpain_III smart00720
calpain_III domain;
354-496 1.03e-49

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 170.24  E-value: 1.03e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   354 WEEARLRGAWTRHEdplqnRSGGCINHKDSFFQNPQYIFDVKKPEDE---VLISIQQRPKQSTRRDGKgENLAIGFDIYK 430
Cdd:smart00720   1 WHTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEPDDDdctVLIALMQKNRRRLRRKGA-DFLTIGFAVYK 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300798152   431 VEEN---RQYRMHSLQHRAASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPSSCR 496
Cdd:smart00720  75 VPKElhlRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
520-598 3.81e-09

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973  Cd Length: 102  Bit Score: 54.77  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 520 QVHVLGAAGL--KDSPTGANSYVIIKCEGD-KVRSAVQKGTSTPEYDVKGVF-YRKKPSQPITVQIWNH-RVLKDEFLGQ 594
Cdd:cd00030    2 RVTVIEARNLpaKDLNGKSDPYVKVSLGGKqKFKTKVVKNTLNPVWNETFEFpVLDPESDTLTVEVWDKdRFSKDDFLGE 81

                 ....
gi 300798152 595 VHLK 598
Cdd:cd00030   82 VEIP 85
C2 pfam00168
C2 domain;
521-609 1.14e-08

C2 domain;


Pssm-ID: 278593  Cd Length: 104  Bit Score: 53.09  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152  521 VHVLGAAGL--KDSPTGANSYVIIKCEGD--KVRSAVQKGTSTPEYDVKGVFYRKKP-SQPITVQIWNH-RVLKDEFLGQ 594
Cdd:pfam00168   5 VTVIEAKNLppKDLNGKSDPYVKVSLLDGkqKKKTKVVKNTLNPVWNETFTFSVPDPeNAVLEIEVYDYdRFGRDDFLGE 84
                          90
                  ....*....|....*
gi 300798152  595 VHLKANADDLQALHT 609
Cdd:pfam00168  85 VRIPLSELDLGEVLD 99
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
521-597 2.67e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577  Cd Length: 101  Bit Score: 52.10  E-value: 2.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152   521 VHVLGAAGL--KDSPTGANSYVIIKCEGD---KVRSAVQKGTSTPEYDVKGVFYRKKP-SQPITVQIWNH-RVLKDEFLG 593
Cdd:smart00239   4 VKIISARNLppKDKGGKSDPYVKVSLDGDpkeKKKTKVVKNTLNPVWNETFEFEVPPPeLAELEIEVYDKdRFGRDDFIG 83

                   ....
gi 300798152   594 QVHL 597
Cdd:smart00239  84 QVTI 87
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
520-615 1.78e-04

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176064  Cd Length: 126  Bit Score: 40.51  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 520 QVHVLGAAGLK-DSPTGAN-SYVIIKCEGDKVRSAVQKGTSTPEYDVKGVF-----YRKKPSQPITVQIWNHR--VLKDE 590
Cdd:cd08682    2 QVTVLQARGLLcKGKSGTNdAYVIIQLGKEKYSTSVKEKTTSPVWKEECSFelpglLSGNGNRATLQLTVMHRnlLGLDK 81
                         90       100
                 ....*....|....*....|....*
gi 300798152 591 FLGQVHLkanadDLQALHTLHLRDR 615
Cdd:cd08682   82 FLGQVSI-----PLNDLDEDKGRRR 101
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
518-608 1.86e-04

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009  Cd Length: 124  Bit Score: 40.62  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 518 VTQVHVLGAAGLKDSPTGANS---YVIIKCEGDKV--RSAVQKGTSTPEYDVKGVFYRKKPSQPITVQIWNHR-VLKDEF 591
Cdd:cd04044    3 VLAVTIKSARGLKGSDIIGGTvdpYVTFSISNRRElaRTKVKKDTSNPVWNETKYILVNSLTEPLNLTVYDFNdKRKDKL 82
                         90
                 ....*....|....*..
gi 300798152 592 LGQVHLkanadDLQALH 608
Cdd:cd04044   83 IGTAEF-----DLSSLL 94
C2D_MCTP_PRT_plant cd08379
C2 domain fourth repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
520-618 1.28e-03

C2 domain fourth repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fourth C2 repeat, C2D, and has a type-II topology.


Pssm-ID: 176025  Cd Length: 126  Bit Score: 37.77  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 520 QVHVLGAAGL-----KDSPTGANSYVIIKcEGDK-VRSAVQKGTSTPEYDVKGVFYRKKPSQPITVQIWNHRVL------ 587
Cdd:cd08379    3 EVGILGAQGLdvlraKDGRGSTDAYCVAK-YGPKwVRTRTVEDSSNPRWNEQYTWPVYDPCTVLTVGVFDNSQShwkeav 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 300798152 588 -KDEFLGQV--HLKANADDLQALHTLHLRDRNSR 618
Cdd:cd08379   82 qPDVLIGKVriRLSTLEDDRVYAHSYPLLSLNPS 115
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
533-634 1.77e-03

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 38.08  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 533 PTGANSYVIIKCEGDKVRSAVQKGTSTPEYDVKGVFYRKKPSQPITVQIWNH-RVLKDEFLGQVHLkanadDLQALHTLH 611
Cdd:cd04038   19 FTSSDPYVVLTLGNQKVKTRVIKKNLNPVWNEELTLSVPNPMAPLKLEVFDKdTFSKDDSMGEAEI-----DLEPLVEAA 93
                         90       100
                 ....*....|....*....|...
gi 300798152 612 LRDRNSRQPSdlpGTVAVRVLSS 634
Cdd:cd04038   94 KLDHLRDTPG---GTQIKKVLPS 113
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
520-624 3.40e-03

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 36.52  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 520 QVHVLGAAGL--KD---SPtgaNSYVIIKCEGDKVRS-AVQKGTSTP----EYDVKgvfyrKKPSQPITVQIWNHRVLK- 588
Cdd:cd08382    3 RLTVLCADGLakRDlfrLP---DPFAVITVDGGQTHStDVAKKTLDPkwneHFDLT-----VGPSSIITIQVFDQKKFKk 74
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 300798152 589 --DEFLGQVHLKANA-DDLQALHTLHLRDRNSRQPSDLP 624
Cdd:cd08382   75 kdQGFLGCVRIRANAvLPLKDTGYQRLDLRKLKKSDNLS 113
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
521-597 5.78e-03

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 36.16  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 521 VHVLGAAGL--KDSPTGANSYVIIKCEGDKVRSAVQKGTSTPEYDVKGVFYRKKPS----QPITVQIWNHR--VLKDEFL 592
Cdd:cd04022    4 VEVVDAQDLmpKDGQGSSSAYVELDFDGQKKRTRTKPKDLNPVWNEKLVFNVSDPSrlsnLVLEVYVYNDRrsGRRRSFL 83

                 ....*
gi 300798152 593 GQVHL 597
Cdd:cd04022   84 GRVRI 88
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
517-593 5.98e-03

C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175978  Cd Length: 111  Bit Score: 35.63  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 517 QVtQVHVLGAAGLKdsptGANS--YVIIKCEGDKVRSAVQKGTSTPEYDVKGVFYRKKP-----SQPITVQIWNHRVL-K 588
Cdd:cd04011    5 QV-RVRVIEARQLV----GGNIdpVVKVEVGGQKKYTSVKKGTNCPFYNEYFFFNFHESpdelfDKIIKISVYDSRSLrS 79

                 ....*
gi 300798152 589 DEFLG 593
Cdd:cd04011   80 DTLIG 84
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
520-598 8.75e-03

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-II topology.


Pssm-ID: 176014  Cd Length: 124  Bit Score: 35.39  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798152 520 QVHVLGAAGLKDS-PTGA-NSYVIIKCEGDKVRSAVQKGT-STPEYDVKGVFYRKKPSQP----ITVQIWNHRVL-KDEF 591
Cdd:cd04049    4 EVLLISAKGLQDTdFLGKiDPYVIIQCRTQERKSKVAKGDgRNPEWNEKFKFTVEYPGWGgdtkLILRIMDKDNFsDDDF 83

                 ....*....
gi 300798152 592 LGQ--VHLK 598
Cdd:cd04049   84 IGEatIHLK 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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