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Conserved domains on  [gi|1039792666|ref|XP_017168761|]
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transmembrane protease serine 4 isoform X1 [Mus musculus]

Protein Classification

SRCR_2 and Tryp_SPc domain-containing protein( domain architecture ID 11636394)

SRCR_2 and Tryp_SPc domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
62-287 4.76e-99

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


:

Pssm-ID: 214473  Cd Length: 229  Bit Score: 289.96  E-value: 4.76e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666   62 RVVGGVEAPVDSWPWQVSIQYNK-QHVCGGSILDPHWILTAAHCFRKYlDVSSWKVRAGSNILGNSPSLPVAKIFIAEPN 140
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  141 PLYPKE---KDIALVKLQMPLTFSGSVRPICLPFSDEVLVPATPVWVIGWGFTEENGGKMSDMLLQASVQVIDSTRCNAE 217
Cdd:smart00020  80 PNYNPStydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  218 DAYEGEVTAEMLCAGTPQGGKDTCQGDSGGPLMYHSDKWQVVGIVSWGHGCGGPSTPGVYTKVTAYLNWI 287
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
SRCR_2 super family cl02509
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
1-55 4.87e-04

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


The actual alignment was detected with superfamily member pfam15494:

Pssm-ID: 470597  Cd Length: 99  Bit Score: 38.85  E-value: 4.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039792666   1 MGYDSQPAFRAVEIRPDQNLPV---AQVTGNSQELQVQN---GSRSCLSGSLVSLRCLDCG 55
Cdd:pfam15494  36 LGYLRLTHHKSVNLTDISSNSSqsfMKLNSSSLNTDLYEalqPRDSCSSGSVVSLRCSECG 96
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
62-287 4.76e-99

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 289.96  E-value: 4.76e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666   62 RVVGGVEAPVDSWPWQVSIQYNK-QHVCGGSILDPHWILTAAHCFRKYlDVSSWKVRAGSNILGNSPSLPVAKIFIAEPN 140
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  141 PLYPKE---KDIALVKLQMPLTFSGSVRPICLPFSDEVLVPATPVWVIGWGFTEENGGKMSDMLLQASVQVIDSTRCNAE 217
Cdd:smart00020  80 PNYNPStydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  218 DAYEGEVTAEMLCAGTPQGGKDTCQGDSGGPLMYHSDKWQVVGIVSWGHGCGGPSTPGVYTKVTAYLNWI 287
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
63-290 9.35e-95

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 279.55  E-value: 9.35e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  63 VVGGVEAPVDSWPWQVSIQYNK-QHVCGGSILDPHWILTAAHCFRKYlDVSSWKVRAGSNILGNSPS----LPVAKIFIa 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGggqvIKVKKVIV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 138 epNPLY---PKEKDIALVKLQMPLTFSGSVRPICLPFSDEVLVPATPVWVIGWGfTEENGGKMSDMLLQASVQVIDSTRC 214
Cdd:cd00190    79 --HPNYnpsTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792666 215 NAEDAYEGEVTAEMLCAGTPQGGKDTCQGDSGGPLMYHS-DKWQVVGIVSWGHGCGGPSTPGVYTKVTAYLNWIYNV 290
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDnGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
60-287 1.95e-76

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 1.95e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  60 TPRVVGGVEAPVDSWPWQVSIQYNK---QHVCGGSILDPHWILTAAHCFRKYlDVSSWKVRAGSNILGNSP--SLPVAKI 134
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGgtVVKVARI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 135 FIaepNPLY---PKEKDIALVKLQMPLTfsgSVRPICLPFSDEVLVPATPVWVIGWGFTEENGGKMSDMLLQASVQVIDS 211
Cdd:COG5640   107 VV---HPDYdpaTPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792666 212 TRCNAedaYEGEVTAEMLCAGTPQGGKDTCQGDSGGPLMYHSD-KWQVVGIVSWGHGCGGPSTPGVYTKVTAYLNWI 287
Cdd:COG5640   181 ATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGgGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
63-287 4.23e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.46  E-value: 4.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  63 VVGGVEAPVDSWPWQVSIQY-NKQHVCGGSILDPHWILTAAHCFRkylDVSSWKVRAGSNILGNS-PSLPVAKIFIAEPN 140
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLReGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 141 PLYP---KEKDIALVKLQMPLTFSGSVRPICLPFSDEVLVPATPVWVIGWGFTEENGgkMSDMLLQASVQVIDSTRCNAe 217
Cdd:pfam00089  78 PNYNpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 218 dAYEGEVTAEMLCAGTpqGGKDTCQGDSGGPLMYHSDKwqVVGIVSWGHGCGGPSTPGVYTKVTAYLNWI 287
Cdd:pfam00089 155 -AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE--LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
1-55 4.87e-04

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 38.85  E-value: 4.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039792666   1 MGYDSQPAFRAVEIRPDQNLPV---AQVTGNSQELQVQN---GSRSCLSGSLVSLRCLDCG 55
Cdd:pfam15494  36 LGYLRLTHHKSVNLTDISSNSSqsfMKLNSSSLNTDLYEalqPRDSCSSGSVVSLRCSECG 96
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
62-287 4.76e-99

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 289.96  E-value: 4.76e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666   62 RVVGGVEAPVDSWPWQVSIQYNK-QHVCGGSILDPHWILTAAHCFRKYlDVSSWKVRAGSNILGNSPSLPVAKIFIAEPN 140
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  141 PLYPKE---KDIALVKLQMPLTFSGSVRPICLPFSDEVLVPATPVWVIGWGFTEENGGKMSDMLLQASVQVIDSTRCNAE 217
Cdd:smart00020  80 PNYNPStydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  218 DAYEGEVTAEMLCAGTPQGGKDTCQGDSGGPLMYHSDKWQVVGIVSWGHGCGGPSTPGVYTKVTAYLNWI 287
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
63-290 9.35e-95

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 279.55  E-value: 9.35e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  63 VVGGVEAPVDSWPWQVSIQYNK-QHVCGGSILDPHWILTAAHCFRKYlDVSSWKVRAGSNILGNSPS----LPVAKIFIa 137
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGggqvIKVKKVIV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 138 epNPLY---PKEKDIALVKLQMPLTFSGSVRPICLPFSDEVLVPATPVWVIGWGfTEENGGKMSDMLLQASVQVIDSTRC 214
Cdd:cd00190    79 --HPNYnpsTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792666 215 NAEDAYEGEVTAEMLCAGTPQGGKDTCQGDSGGPLMYHS-DKWQVVGIVSWGHGCGGPSTPGVYTKVTAYLNWIYNV 290
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDnGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
60-287 1.95e-76

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 1.95e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  60 TPRVVGGVEAPVDSWPWQVSIQYNK---QHVCGGSILDPHWILTAAHCFRKYlDVSSWKVRAGSNILGNSP--SLPVAKI 134
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGgtVVKVARI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 135 FIaepNPLY---PKEKDIALVKLQMPLTfsgSVRPICLPFSDEVLVPATPVWVIGWGFTEENGGKMSDMLLQASVQVIDS 211
Cdd:COG5640   107 VV---HPDYdpaTPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792666 212 TRCNAedaYEGEVTAEMLCAGTPQGGKDTCQGDSGGPLMYHSD-KWQVVGIVSWGHGCGGPSTPGVYTKVTAYLNWI 287
Cdd:COG5640   181 ATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGgGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
63-287 4.23e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.46  E-value: 4.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  63 VVGGVEAPVDSWPWQVSIQY-NKQHVCGGSILDPHWILTAAHCFRkylDVSSWKVRAGSNILGNS-PSLPVAKIFIAEPN 140
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLReGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 141 PLYP---KEKDIALVKLQMPLTFSGSVRPICLPFSDEVLVPATPVWVIGWGFTEENGgkMSDMLLQASVQVIDSTRCNAe 217
Cdd:pfam00089  78 PNYNpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 218 dAYEGEVTAEMLCAGTpqGGKDTCQGDSGGPLMYHSDKwqVVGIVSWGHGCGGPSTPGVYTKVTAYLNWI 287
Cdd:pfam00089 155 -AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE--LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
86-289 2.09e-12

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 64.70  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  86 HVCGGSILDPHWILTAAHCFRKYLD---VSSWKVRAGSNilgNSP-------SLPVAKIFIAEPNPLYpkekDIALVKLQ 155
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYN---GGPygtatatRFRVPPGWVASGDAGY----DYALLRLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 156 MPLTfsGSVRPICLPFSDEVLVPaTPVWVIGWGfteenGGKMSDMLLQASvqvidstrCNAEDAYEGEVTaeMLCagtpq 235
Cdd:COG3591    85 EPLG--DTTGWLGLAFNDAPLAG-EPVTIIGYP-----GDRPKDLSLDCS--------GRVTGVQGNRLS--YDC----- 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039792666 236 ggkDTCQGDSGGPLMYHSD-KWQVVGIVSWGHgcGGPSTPGVYTkVTAYLNWIYN 289
Cdd:COG3591   142 ---DTTGGSSGSPVLDDSDgGGRVVGVHSAGG--ADRANTGVRL-TSAIVAALRA 190
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
90-261 1.09e-05

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 44.33  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  90 GSILDP-HWILTAAHCFRKYLDVSswkVRAGSNILGNSPSLPvAKIFIAEPnplypkEKDIALVKLQMPLTfsgSVRPic 168
Cdd:pfam13365   3 GFVVSSdGLVLTNAHVVDDAEEAA---VELVSVVLADGREYP-ATVVARDP------DLDLALLRVSGDGR---GLPP-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666 169 LPFSD-EVLVPATPVWVIGWGFTEENggkmsdmlLQASVQVIDSTRCNAEDAYEGEVtaeMLCAGTPQGgkdtcqGDSGG 247
Cdd:pfam13365  68 LPLGDsEPLVGGERVYAVGYPLGGEK--------LSLSEGIVSGVDEGRDGGDDGRV---IQTDAALSP------GSSGG 130
                         170
                  ....*....|....
gi 1039792666 248 PLMyhSDKWQVVGI 261
Cdd:pfam13365 131 PVF--DADGRVVGI 142
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
74-170 2.75e-05

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 42.53  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792666  74 WPWQVSIQYNKQHVCGGSILDPHWILTAAHCFRKY-LDVSSWKVRAGSNILGNSPSLPVAKIFIAEPNPLYPKEKdIALV 152
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTnLRHQYISVVLGGAKTLKSIEGPYEQIVRVDCRHDIPESE-ISLL 79
                          90
                  ....*....|....*...
gi 1039792666 153 KLQMPLTFSGSVRPICLP 170
Cdd:pfam09342  80 HLASPASFSNHVLPTFVP 97
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
1-55 4.87e-04

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 38.85  E-value: 4.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039792666   1 MGYDSQPAFRAVEIRPDQNLPV---AQVTGNSQELQVQN---GSRSCLSGSLVSLRCLDCG 55
Cdd:pfam15494  36 LGYLRLTHHKSVNLTDISSNSSqsfMKLNSSSLNTDLYEalqPRDSCSSGSVVSLRCSECG 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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