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Conserved domains on  [gi|19745190|ref|NP_604456|]
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calpain-5 [Rattus norvegicus]

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List of domain hits

Name Accession Description Interval E-value
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
16-341 1.94e-133

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: 396.70  E-value: 1.94e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190  16 LKRACLRRKVLFEDPHFPASDDSLYYK-----GTPGPTVRWKRPFDICDD-----PRLFVDGISSHDLHQGQVGNCWFVA 85
Cdd:cd00044   2 LLQICLLSGVLFEDPDFPPNDSSLGFDdslsnGQPKKVIEWKRPSEIFADdgnsnPRLFVNGASPSDVCQGILGDCWFLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190  86 ACSSLASRESLWQKVIPDWKEQEwnpekpDSYAGIFHFNFWRFGEWVDVVVDDRLPTVNNQLIYCHSNSKNEFWCAPVEK 165
Cdd:cd00044  82 ALAALAERPELLKRVIPPDQSFE------ENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFMHSRDRNELWVALLEK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 166 AYAKLAGCYQALDGGNTADALVDFTGGVSEPIDLTEGDLATDEakrSQLFERVLKVHSRGGLISASIKAMTAAdmETRLA 245
Cdd:cd00044 156 AYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADASSGD---NDLFALLLSFLQGGSLIGCSTGSRSEE--EARTA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 246 CGLVKGHAYAVTDVRKvrlghgllafFKSEKLDMIRLRNPWGERVWTGPWSDTSEEWQkVSKSEREKMGVTVQDDGEFWM 325
Cdd:cd00044 231 NGLVKGHAYSVLDVRE----------VQEEGLRLLRLRNPWGVGEWWGGWSDDSSEWW-VIDAERKKLLLSGKDDGEFWM 299
                       330
                ....*....|....*.
gi 19745190 326 TYEDMCRYFTDIIKCR 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 9.58e-58

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: 191.72  E-value: 9.58e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 515 PQQVTQVHVLGAAGLK--DSSTGANSYVIIKCEGEKVRSAVQRGTSTPEYNVKGIFYRKKLSQPITVQVWNNRVLKDEFL 592
Cdd:cd04046   1 PQVVTQVHVHSAEGLSkqDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19745190 593 GQVHLKTAPDDLQDLHSLHLQDRSGRQPSDLPGIVAVRVLCSASLT 638
Cdd:cd04046  81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
352-498 2.84e-56

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: 188.66  E-value: 2.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 352 KTWEEARLRGAWTRHedpqqNRSGGCINHKDTFFQNPQYIFEVKKPED-----EVLICIQQRPKRSTRREGKgENLAIGF 426
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEPDDdegkcTVLIALMQKNRRHLRKKGL-DLLTIGF 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19745190 427 DIYKV-EENRQYRMHSLQHK---AASSIYINSRSVFLRTELPEGRYVIIPTTFEPGHTGELLLRVFTDVPSNCREL 498
Cdd:cd00214  75 HVYKVpGENRHLRRDFFLHKaprARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
 
Name Accession Description Interval E-value
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
16-341 1.94e-133

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: 396.70  E-value: 1.94e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190  16 LKRACLRRKVLFEDPHFPASDDSLYYK-----GTPGPTVRWKRPFDICDD-----PRLFVDGISSHDLHQGQVGNCWFVA 85
Cdd:cd00044   2 LLQICLLSGVLFEDPDFPPNDSSLGFDdslsnGQPKKVIEWKRPSEIFADdgnsnPRLFVNGASPSDVCQGILGDCWFLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190  86 ACSSLASRESLWQKVIPDWKEQEwnpekpDSYAGIFHFNFWRFGEWVDVVVDDRLPTVNNQLIYCHSNSKNEFWCAPVEK 165
Cdd:cd00044  82 ALAALAERPELLKRVIPPDQSFE------ENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFMHSRDRNELWVALLEK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 166 AYAKLAGCYQALDGGNTADALVDFTGGVSEPIDLTEGDLATDEakrSQLFERVLKVHSRGGLISASIKAMTAAdmETRLA 245
Cdd:cd00044 156 AYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADASSGD---NDLFALLLSFLQGGSLIGCSTGSRSEE--EARTA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 246 CGLVKGHAYAVTDVRKvrlghgllafFKSEKLDMIRLRNPWGERVWTGPWSDTSEEWQkVSKSEREKMGVTVQDDGEFWM 325
Cdd:cd00044 231 NGLVKGHAYSVLDVRE----------VQEEGLRLLRLRNPWGVGEWWGGWSDDSSEWW-VIDAERKKLLLSGKDDGEFWM 299
                       330
                ....*....|....*.
gi 19745190 326 TYEDMCRYFTDIIKCR 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 9.58e-58

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: 191.72  E-value: 9.58e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 515 PQQVTQVHVLGAAGLK--DSSTGANSYVIIKCEGEKVRSAVQRGTSTPEYNVKGIFYRKKLSQPITVQVWNNRVLKDEFL 592
Cdd:cd04046   1 PQVVTQVHVHSAEGLSkqDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19745190 593 GQVHLKTAPDDLQDLHSLHLQDRSGRQPSDLPGIVAVRVLCSASLT 638
Cdd:cd04046  81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
352-498 2.84e-56

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: 188.66  E-value: 2.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 352 KTWEEARLRGAWTRHedpqqNRSGGCINHKDTFFQNPQYIFEVKKPED-----EVLICIQQRPKRSTRREGKgENLAIGF 426
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEPDDdegkcTVLIALMQKNRRHLRKKGL-DLLTIGF 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19745190 427 DIYKV-EENRQYRMHSLQHK---AASSIYINSRSVFLRTELPEGRYVIIPTTFEPGHTGELLLRVFTDVPSNCREL 498
Cdd:cd00214  75 HVYKVpGENRHLRRDFFLHKaprARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
13-351 1.46e-170

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: 492.23  E-value: 1.46e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190     13 YSALKRACLRRKVLFEDPHFPASDDSLYYKGTPGPTVRWKRPFDICDDPRLFVDGISSHDLHQGQVGNCWFVAACSSLAS 92
Cdd:smart00230   1 YEALRQYCKESGTLFEDPLFPANNGSLFFSQRQRKFVVWKRPHEIFENPPFIVGGASRTDICQGVLGDCWLLAALASLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190     93 RESLWQKVIPdwKEQEWNPekpdSYAGIFHFNFWRFGEWVDVVVDDRLPTVNNQLIYCHSNSKNEFWCAPVEKAYAKLAG 172
Cdd:smart00230  81 REKLLDRVIP--HDQEFSE----NYAGIFHFRFWRFGKWVDVVIDDRLPTYNGELVFMHSNSRNEFWSALLEKAYAKLNG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    173 CYQALDGGNTADALVDFTGGVSEPIDLTEGdlatdEAKRSQLFERVLKVHSRGGLISASIKAMTAADMETRLACGLVKGH 252
Cdd:smart00230 155 CYEALKGGSTTEALEDLTGGVAESIDLKEA-----SKDPDNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    253 AYAVTDVRKVRLGHgllaffksekLDMIRLRNPWGERVWTGPWSDTSEEWQKVSKSEREKMGVTVQDDGEFWMTYEDMCR 332
Cdd:smart00230 230 AYSVTDVREVQGRR----------QELLRLRNPWGQVEWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLR 299
                          330
                   ....*....|....*....
gi 19745190    333 YFTDIIKCRLINTSYLSIH 351
Cdd:smart00230 300 HFDKVEICNLNPDSLEERS 318
Peptidase_C2 pfam00648
Calpain family cysteine protease;
26-342 2.64e-118

Calpain family cysteine protease;


Pssm-ID: 250029  Cd Length: 303  Bit Score: 357.54  E-value: 2.64e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    26 LFEDPHFPASDDSLYYK-----GTPGPTVRWKRPFDICDDPRLFVDGISSHDLHQGQVGNCWFVAACSSLASRESLWQKV 100
Cdd:pfam00648   1 LFVDPSFPADPKSLGYKplgpySSKTRGIEWKRPHEICENPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEELLFRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   101 IPdwKEQEWNpekpDSYAGIFHFNFWRFGEWVDVVVDDRLPTVNNQLIYCHSNSKNEFWCAPVEKAYAKLAGCYQALDGG 180
Cdd:pfam00648  81 VP--HDQSFQ----ENYAGIFHFQFWQYGEWVDVVVDDRLPTKDGELVFVHSAERNEFWSALLEKAYAKLHGCYEALSGG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   181 NTADALVDFTGGVSEPIDLtegdlaTDEAKRSQLFERVLKVHSRGGLISASIKAMTAADMETRLACGLVKGHAYAVTDVR 260
Cdd:pfam00648 155 STTEAMEDFTGGVAEWYEL------KQAPSDLNLFKIIAKALERGSLMGCSIDITSPVDMEARTFKGLVKGHAYSVTGVK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   261 KVRlghgllafFKSEKLDMIRLRNPWGERVWTGPWSDTSEEWQKVSKSEREKMGVTVQDDGEFWMTYEDMCRYFTDIIKC 340
Cdd:pfam00648 229 EVN--------YRGEKQKLIRLRNPWGQVEWTGAWSDGSPEWRFIDPDERARLQLQFEEDGEFWMSFEDFLRHFSRLEIC 300

                  ..
gi 19745190   341 RL 342
Cdd:pfam00648 301 NL 302
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
353-494 2.32e-51

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: 250338  Cd Length: 142  Bit Score: 174.81  E-value: 2.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   353 TWEEARLRGAWTRHedpqqNRSGGCINHKDTFFQNPQYIFEVKKPEDE---VLICIQQRPKRSTRREGKgENLAIGFDIY 429
Cdd:pfam01067   1 KWKVTVYEGSWVRG-----STAGGCRNFPDTFWTNPQYRLSLTEPDDDdctVLVALMQKNRRKKRKEGA-DNLTIGFAIY 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19745190   430 KV----EENRQYRMHSlQHKAASSIYINSRSVFLRTELPEGRYVIIPTTFEPGHTGELLLRVFTDVPSN 494
Cdd:pfam01067  75 KVdpqkELPRKFFSQN-RSIARSSTYINLREVTERFRLPPGTYVIVPSTFEPGQEGEFLLRVFSEKPID 142
calpain_III smart00720
calpain_III domain;
354-496 4.23e-50

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 171.39  E-value: 4.23e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    354 WEEARLRGAWTRHEdpqqnRSGGCINHKDTFFQNPQYIFEVKKPEDE---VLICIQQRPKRSTRREGKgENLAIGFDIYK 430
Cdd:smart00720   1 WHTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEPDDDdctVLIALMQKNRRRLRRKGA-DFLTIGFAVYK 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19745190    431 VEEN---RQYRMHSLQHKAASSIYINSRSVFLRTELPEGRYVIIPTTFEPGHTGELLLRVFTDVPSNCR 496
Cdd:smart00720  75 VPKElhlRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
521-618 7.43e-09

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: 53.65  E-value: 7.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    521 VHVLGAAGL--KDSSTGANSYVIIKCEG---EKVRSAVQRGTSTPEYNVKGIFY-RKKLSQPITVQVWN-NRVLKDEFLG 593
Cdd:smart00239   4 VKIISARNLppKDKGGKSDPYVKVSLDGdpkEKKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVYDkDRFGRDDFIG 83
                           90       100
                   ....*....|....*....|....*
gi 19745190    594 QVHLktapddlqDLHSLHLQDRSGR 618
Cdd:smart00239  84 QVTI--------PLSDLLLGGRHEK 100
C2 pfam00168
C2 domain;
521-596 1.90e-08

C2 domain;


Pssm-ID: 249647  Cd Length: 85  Bit Score: 52.27  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   521 VHVLGAAGL--KDSSTGANSYVIIKCEGEKV---RSAVQRGTSTPEYNVKGIFY-RKKLSQPITVQVWN-NRVLKDEFLG 593
Cdd:pfam00168   3 VTVISAKNLppKDLNGKSDPYVKVSLGGQKKdtkKTKVVKNTLNPVWNETFTFEvVLPELAELRIEVYDyDRFGKDDFIG 82

                  ...
gi 19745190   594 QVH 596
Cdd:pfam00168  83 EVT 85
 
Name Accession Description Interval E-value
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
16-341 1.94e-133

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: 396.70  E-value: 1.94e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190  16 LKRACLRRKVLFEDPHFPASDDSLYYK-----GTPGPTVRWKRPFDICDD-----PRLFVDGISSHDLHQGQVGNCWFVA 85
Cdd:cd00044   2 LLQICLLSGVLFEDPDFPPNDSSLGFDdslsnGQPKKVIEWKRPSEIFADdgnsnPRLFVNGASPSDVCQGILGDCWFLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190  86 ACSSLASRESLWQKVIPDWKEQEwnpekpDSYAGIFHFNFWRFGEWVDVVVDDRLPTVNNQLIYCHSNSKNEFWCAPVEK 165
Cdd:cd00044  82 ALAALAERPELLKRVIPPDQSFE------ENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFMHSRDRNELWVALLEK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 166 AYAKLAGCYQALDGGNTADALVDFTGGVSEPIDLTEGDLATDEakrSQLFERVLKVHSRGGLISASIKAMTAAdmETRLA 245
Cdd:cd00044 156 AYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADASSGD---NDLFALLLSFLQGGSLIGCSTGSRSEE--EARTA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 246 CGLVKGHAYAVTDVRKvrlghgllafFKSEKLDMIRLRNPWGERVWTGPWSDTSEEWQkVSKSEREKMGVTVQDDGEFWM 325
Cdd:cd00044 231 NGLVKGHAYSVLDVRE----------VQEEGLRLLRLRNPWGVGEWWGGWSDDSSEWW-VIDAERKKLLLSGKDDGEFWM 299
                       330
                ....*....|....*.
gi 19745190 326 TYEDMCRYFTDIIKCR 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 9.58e-58

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: 191.72  E-value: 9.58e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 515 PQQVTQVHVLGAAGLK--DSSTGANSYVIIKCEGEKVRSAVQRGTSTPEYNVKGIFYRKKLSQPITVQVWNNRVLKDEFL 592
Cdd:cd04046   1 PQVVTQVHVHSAEGLSkqDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19745190 593 GQVHLKTAPDDLQDLHSLHLQDRSGRQPSDLPGIVAVRVLCSASLT 638
Cdd:cd04046  81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
352-498 2.84e-56

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: 188.66  E-value: 2.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 352 KTWEEARLRGAWTRHedpqqNRSGGCINHKDTFFQNPQYIFEVKKPED-----EVLICIQQRPKRSTRREGKgENLAIGF 426
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEPDDdegkcTVLIALMQKNRRHLRKKGL-DLLTIGF 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19745190 427 DIYKV-EENRQYRMHSLQHK---AASSIYINSRSVFLRTELPEGRYVIIPTTFEPGHTGELLLRVFTDVPSNCREL 498
Cdd:cd00214  75 HVYKVpGENRHLRRDFFLHKaprARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
13-351 1.46e-170

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: 492.23  E-value: 1.46e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190     13 YSALKRACLRRKVLFEDPHFPASDDSLYYKGTPGPTVRWKRPFDICDDPRLFVDGISSHDLHQGQVGNCWFVAACSSLAS 92
Cdd:smart00230   1 YEALRQYCKESGTLFEDPLFPANNGSLFFSQRQRKFVVWKRPHEIFENPPFIVGGASRTDICQGVLGDCWLLAALASLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190     93 RESLWQKVIPdwKEQEWNPekpdSYAGIFHFNFWRFGEWVDVVVDDRLPTVNNQLIYCHSNSKNEFWCAPVEKAYAKLAG 172
Cdd:smart00230  81 REKLLDRVIP--HDQEFSE----NYAGIFHFRFWRFGKWVDVVIDDRLPTYNGELVFMHSNSRNEFWSALLEKAYAKLNG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    173 CYQALDGGNTADALVDFTGGVSEPIDLTEGdlatdEAKRSQLFERVLKVHSRGGLISASIKAMTAADMETRLACGLVKGH 252
Cdd:smart00230 155 CYEALKGGSTTEALEDLTGGVAESIDLKEA-----SKDPDNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    253 AYAVTDVRKVRLGHgllaffksekLDMIRLRNPWGERVWTGPWSDTSEEWQKVSKSEREKMGVTVQDDGEFWMTYEDMCR 332
Cdd:smart00230 230 AYSVTDVREVQGRR----------QELLRLRNPWGQVEWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLR 299
                          330
                   ....*....|....*....
gi 19745190    333 YFTDIIKCRLINTSYLSIH 351
Cdd:smart00230 300 HFDKVEICNLNPDSLEERS 318
Peptidase_C2 pfam00648
Calpain family cysteine protease;
26-342 2.64e-118

Calpain family cysteine protease;


Pssm-ID: 250029  Cd Length: 303  Bit Score: 357.54  E-value: 2.64e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    26 LFEDPHFPASDDSLYYK-----GTPGPTVRWKRPFDICDDPRLFVDGISSHDLHQGQVGNCWFVAACSSLASRESLWQKV 100
Cdd:pfam00648   1 LFVDPSFPADPKSLGYKplgpySSKTRGIEWKRPHEICENPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEELLFRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   101 IPdwKEQEWNpekpDSYAGIFHFNFWRFGEWVDVVVDDRLPTVNNQLIYCHSNSKNEFWCAPVEKAYAKLAGCYQALDGG 180
Cdd:pfam00648  81 VP--HDQSFQ----ENYAGIFHFQFWQYGEWVDVVVDDRLPTKDGELVFVHSAERNEFWSALLEKAYAKLHGCYEALSGG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   181 NTADALVDFTGGVSEPIDLtegdlaTDEAKRSQLFERVLKVHSRGGLISASIKAMTAADMETRLACGLVKGHAYAVTDVR 260
Cdd:pfam00648 155 STTEAMEDFTGGVAEWYEL------KQAPSDLNLFKIIAKALERGSLMGCSIDITSPVDMEARTFKGLVKGHAYSVTGVK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   261 KVRlghgllafFKSEKLDMIRLRNPWGERVWTGPWSDTSEEWQKVSKSEREKMGVTVQDDGEFWMTYEDMCRYFTDIIKC 340
Cdd:pfam00648 229 EVN--------YRGEKQKLIRLRNPWGQVEWTGAWSDGSPEWRFIDPDERARLQLQFEEDGEFWMSFEDFLRHFSRLEIC 300

                  ..
gi 19745190   341 RL 342
Cdd:pfam00648 301 NL 302
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
353-494 2.32e-51

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: 250338  Cd Length: 142  Bit Score: 174.81  E-value: 2.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   353 TWEEARLRGAWTRHedpqqNRSGGCINHKDTFFQNPQYIFEVKKPEDE---VLICIQQRPKRSTRREGKgENLAIGFDIY 429
Cdd:pfam01067   1 KWKVTVYEGSWVRG-----STAGGCRNFPDTFWTNPQYRLSLTEPDDDdctVLVALMQKNRRKKRKEGA-DNLTIGFAIY 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19745190   430 KV----EENRQYRMHSlQHKAASSIYINSRSVFLRTELPEGRYVIIPTTFEPGHTGELLLRVFTDVPSN 494
Cdd:pfam01067  75 KVdpqkELPRKFFSQN-RSIARSSTYINLREVTERFRLPPGTYVIVPSTFEPGQEGEFLLRVFSEKPID 142
calpain_III smart00720
calpain_III domain;
354-496 4.23e-50

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 171.39  E-value: 4.23e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    354 WEEARLRGAWTRHEdpqqnRSGGCINHKDTFFQNPQYIFEVKKPEDE---VLICIQQRPKRSTRREGKgENLAIGFDIYK 430
Cdd:smart00720   1 WHTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEPDDDdctVLIALMQKNRRRLRRKGA-DFLTIGFAVYK 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19745190    431 VEEN---RQYRMHSLQHKAASSIYINSRSVFLRTELPEGRYVIIPTTFEPGHTGELLLRVFTDVPSNCR 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 1.84e-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: 55.54  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 520 QVHVLGAAGL--KDSSTGANSYVIIKCEGE-KVRSAVQRGTSTPEYNVKGIF-YRKKLSQPITVQVWN-NRVLKDEFLGQ 594
Cdd:cd00030   2 RVTVIEARNLpaKDLNGKSDPYVKVSLGGKqKFKTKVVKNTLNPVWNETFEFpVLDPESDTLTVEVWDkDRFSKDDFLGE 81

                ....
gi 19745190 595 VHLK 598
Cdd:cd00030  82 VEIP 85
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
521-618 7.43e-09

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: 53.65  E-value: 7.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190    521 VHVLGAAGL--KDSSTGANSYVIIKCEG---EKVRSAVQRGTSTPEYNVKGIFY-RKKLSQPITVQVWN-NRVLKDEFLG 593
Cdd:smart00239   4 VKIISARNLppKDKGGKSDPYVKVSLDGdpkEKKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVYDkDRFGRDDFIG 83
                           90       100
                   ....*....|....*....|....*
gi 19745190    594 QVHLktapddlqDLHSLHLQDRSGR 618
Cdd:smart00239  84 QVTI--------PLSDLLLGGRHEK 100
C2 pfam00168
C2 domain;
521-596 1.90e-08

C2 domain;


Pssm-ID: 249647  Cd Length: 85  Bit Score: 52.27  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190   521 VHVLGAAGL--KDSSTGANSYVIIKCEGEKV---RSAVQRGTSTPEYNVKGIFY-RKKLSQPITVQVWN-NRVLKDEFLG 593
Cdd:pfam00168   3 VTVISAKNLppKDLNGKSDPYVKVSLGGQKKdtkKTKVVKNTLNPVWNETFTFEvVLPELAELRIEVYDyDRFGKDDFIG 82

                  ...
gi 19745190   594 QVH 596
Cdd:pfam00168  83 EVT 85
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
518-614 6.85e-07

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: 47.93  E-value: 6.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 518 VTQVHVLGAAGLKDSSTGANS---YVIIKCEGEKV--RSAVQRGTSTPEYNVKGIFYRKKLSQPITVQVWN-NRVLKDEF 591
Cdd:cd04044   3 VLAVTIKSARGLKGSDIIGGTvdpYVTFSISNRRElaRTKVKKDTSNPVWNETKYILVNSLTEPLNLTVYDfNDKRKDKL 82
                        90       100
                ....*....|....*....|...
gi 19745190 592 LGQVHLktapdDLQDLHSLHLQD 614
Cdd:cd04044  83 IGTAEF-----DLSSLLQNPEQE 100
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
521-603 6.62e-05

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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 a type-I topology and do not bind Ca2+.


Pssm-ID: 175997  Cd Length: 125  Bit Score: 41.85  E-value: 6.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 521 VHVLGAAGL--KDSSTGANSYVIIK-----CEGEKVRSAVQRGTSTPEYN----VKGIFYRKKLSQPITVQVWNN-RVLK 588
Cdd:cd04031  20 VTVLQARDLppRDDGSLRNPYVKVYllpdrSEKSKRRTKTVKKTLNPEWNqtfeYSNVRRETLKERTLEVTVWDYdRDGE 99
                        90
                ....*....|....*..
gi 19745190 589 DEFLGQV--HLKTAPDD 603
Cdd:cd04031 100 NDFLGEVviDLADALLD 116
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
520-611 2.10e-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: 40.13  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 520 QVHVLGAAGL--KDSSTGANSYVIIKCEGEKVRSAVQRGTSTPEYNVKGIFYRKKLSQP------ITVQVWN-NRVLKDE 590
Cdd:cd08682   2 QVTVLQARGLlcKGKSGTNDAYVIIQLGKEKYSTSVKEKTTSPVWKEECSFELPGLLSGngnratLQLTVMHrNLLGLDK 81
                        90       100
                ....*....|....*....|.
gi 19745190 591 FLGQVHLktapdDLQDLHSLH 611
Cdd:cd08682  82 FLGQVSI-----PLNDLDEDK 97
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
534-636 9.40e-04

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  Cd Length: 145  Bit Score: 38.85  E-value: 9.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 534 TGANSYVIIKCEGEKVRSAVQRGTSTPEYNVKGIFYRKKLSQPITVQVWN-NRVLKDEFLGQVHLktapdDLQDLHSLHL 612
Cdd:cd04038  20 TSSDPYVVLTLGNQKVKTRVIKKNLNPVWNEELTLSVPNPMAPLKLEVFDkDTFSKDDSMGEAEI-----DLEPLVEAAK 94
                        90       100
                ....*....|....*....|....*.
gi 19745190 613 QD--RSGRQPSDLPGIVAVRVLCSAS 636
Cdd:cd04038  95 LDhlRDTPGGTQIKKVLPSVENCLAS 120
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
521-597 1.49e-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  Cd Length: 127  Bit Score: 37.70  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19745190 521 VHVLGAAGL--KDSSTGANSYVIIKCEGEKVRSAVQRGTSTPEYNVKGIFYRKKLS----QPITVQVWNNR--VLKDEFL 592
Cdd:cd04022   4 VEVVDAQDLmpKDGQGSSSAYVELDFDGQKKRTRTKPKDLNPVWNEKLVFNVSDPSrlsnLVLEVYVYNDRrsGRRRSFL 83

                ....*
gi 19745190 593 GQVHL 597
Cdd:cd04022  84 GRVRI 88
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
543-606 5.97e-03

C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. Little is known about the expression or localization of Slp3. The C2A domain of Slp3 is Ca2+ dependent. It has been demonstrated that Slp3 promotes dense-core vesicle exocytosis. 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-I topology.


Pssm-ID: 176038  Cd Length: 128  Bit Score: 35.96  E-value: 5.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19745190 543 KCEGEKVRSAVQRGTSTPEYN--VKGIFYRKKL-SQPITVQVWNNRVLKDE-FLGQVHLKTAPDDLQD 606
Cdd:cd08392  49 KSHNSKRKTAVKKGTVNPVFNetLKYVVEADLLsSRQLQVSVWHSRTLKRRvFLGEVLIPLADWDFED 116
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
520-568 9.62e-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: 9.62e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19745190 520 QVHVLGAAGLKDSSTGAN--SYVIIKCEGEKVRSAVQRGT-STPEYNVKGIF 568
Cdd:cd04049   4 EVLLISAKGLQDTDFLGKidPYVIIQCRTQERKSKVAKGDgRNPEWNEKFKF 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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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