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Conserved domains on  [gi|2462526394|ref|XP_054225337|]
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transmembrane protease serine 4 isoform X7 [Homo sapiens]

Protein Classification

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 ...
197-422 9.14e-100

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: 297.28  E-value: 9.14e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  197 RVVGGEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRKHtDVFNWKVRAGSDKL---GSFPSLAVAKIIIi 272
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLssgEEGQVIKVSKVII- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  273 efNPMYPK---DNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRC 349
Cdd:smart00020  79 --HPNYNPstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462526394  350 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 422
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
SRCR_2 super family cl02509
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
106-190 1.62e-13

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: 66.20  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 106 KDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSRAVEIGpdqDLDVVEITENSQELRMR--------------N 171
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLTHHK---SVNLTDISSNSSQSFMKlnssslntdlyealQ 77
                          90
                  ....*....|....*....
gi 2462526394 172 SSGPCLSGSLVSLHCLACG 190
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECG 96
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
56-90 2.07e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 41.42  E-value: 2.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462526394  56 DKYYFLCGQPlHFIPRKQLCDGELDCPLGEDEEHC 90
Cdd:cd00112     2 PPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
197-422 9.14e-100

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: 297.28  E-value: 9.14e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  197 RVVGGEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRKHtDVFNWKVRAGSDKL---GSFPSLAVAKIIIi 272
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLssgEEGQVIKVSKVII- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  273 efNPMYPK---DNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRC 349
Cdd:smart00020  79 --HPNYNPstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462526394  350 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 422
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
198-425 1.22e-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: 286.87  E-value: 1.22e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 198 VVGGEEASVDSWPWQVSIQYDK-QHVCGGSILDPHWVLTAAHCFRKhTDVFNWKVRAGSDKLGSFPS----LAVAKIIIi 272
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGggqvIKVKKVIV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 273 efNPMY---PKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTkQNGGKMSDILLQASVQVIDSTRC 349
Cdd:cd00190    79 --HPNYnpsTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526394 350 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQS-DQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNV 425
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDnGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
188-422 2.87e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.01  E-value: 2.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 188 ACGKSLKTPRVVGGEEASVDSWPWQVSIQYDK---QHVCGGSILDPHWVLTAAHCFrKHTDVFNWKVRAGSDKLGSFP-- 262
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLSTSGgt 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 263 SLAVAKIIIiefNPMY---PKDNDIALMKLQFPLTfsgTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQA 339
Cdd:COG5640   100 VVKVARIVV---HPDYdpaTPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 340 SVQVIDSTRCNAddaYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSD-QWHVVGIVSWGYGCGGPSTPGVYTKVSAY 418
Cdd:COG5640   174 DVPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGgGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                  ....
gi 2462526394 419 LNWI 422
Cdd:COG5640   251 RDWI 254
Trypsin pfam00089
Trypsin;
198-422 2.15e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.24  E-value: 2.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 198 VVGGEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRkhtDVFNWKVRAGSDKLG-SFPSLAVAKIIIIEFN 275
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVlREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 276 PMYP---KDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGgkMSDILLQASVQVIDSTRCNAd 352
Cdd:pfam00089  78 PNYNpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 353 dAYQGEVTEKMMCAGipEGGVDTCQGDSGGPLMYqSDQwHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 422
Cdd:pfam00089 155 -AYGGTVTDTMICAG--AGGKDACQGDSGGPLVC-SDG-ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
106-190 1.62e-13

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: 66.20  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 106 KDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSRAVEIGpdqDLDVVEITENSQELRMR--------------N 171
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLTHHK---SVNLTDISSNSSQSFMKlnssslntdlyealQ 77
                          90
                  ....*....|....*....
gi 2462526394 172 SSGPCLSGSLVSLHCLACG 190
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECG 96
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
102-187 3.97e-09

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 53.89  E-value: 3.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  102 VRLSKDRS----TLQVLDSatGNWFSACFDNFTEALAETACRQMGYSRAVEI------GPDQD---LDVVEI--TENSQE 166
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHN--GQWGTVCDDGWDLRDANVVCRQLGFGGAVSAsgsayfGPGSGpiwLDNVRCsgTEASLS 78
                           90       100
                   ....*....|....*....|...
gi 2462526394  167 LRMRNSSG--PCLSGSLVSLHCL 187
Cdd:smart00202  79 DCPHSGWGshNCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
56-90 2.07e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 41.42  E-value: 2.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462526394  56 DKYYFLCGQPlHFIPRKQLCDGELDCPLGEDEEHC 90
Cdd:cd00112     2 PPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
69-90 1.69e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.07  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|..
gi 2462526394  69 IPRKQLCDGELDCPLGEDEEHC 90
Cdd:pfam00057  16 IPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
197-422 9.14e-100

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: 297.28  E-value: 9.14e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  197 RVVGGEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRKHtDVFNWKVRAGSDKL---GSFPSLAVAKIIIi 272
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLssgEEGQVIKVSKVII- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  273 efNPMYPK---DNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRC 349
Cdd:smart00020  79 --HPNYNPstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462526394  350 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 422
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
198-425 1.22e-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: 286.87  E-value: 1.22e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 198 VVGGEEASVDSWPWQVSIQYDK-QHVCGGSILDPHWVLTAAHCFRKhTDVFNWKVRAGSDKLGSFPS----LAVAKIIIi 272
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGggqvIKVKKVIV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 273 efNPMY---PKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTkQNGGKMSDILLQASVQVIDSTRC 349
Cdd:cd00190    79 --HPNYnpsTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462526394 350 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQS-DQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNV 425
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDnGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
188-422 2.87e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.01  E-value: 2.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 188 ACGKSLKTPRVVGGEEASVDSWPWQVSIQYDK---QHVCGGSILDPHWVLTAAHCFrKHTDVFNWKVRAGSDKLGSFP-- 262
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLSTSGgt 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 263 SLAVAKIIIiefNPMY---PKDNDIALMKLQFPLTfsgTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQA 339
Cdd:COG5640   100 VVKVARIVV---HPDYdpaTPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 340 SVQVIDSTRCNAddaYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSD-QWHVVGIVSWGYGCGGPSTPGVYTKVSAY 418
Cdd:COG5640   174 DVPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGgGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                  ....
gi 2462526394 419 LNWI 422
Cdd:COG5640   251 RDWI 254
Trypsin pfam00089
Trypsin;
198-422 2.15e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.24  E-value: 2.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 198 VVGGEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRkhtDVFNWKVRAGSDKLG-SFPSLAVAKIIIIEFN 275
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVlREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 276 PMYP---KDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGgkMSDILLQASVQVIDSTRCNAd 352
Cdd:pfam00089  78 PNYNpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 353 dAYQGEVTEKMMCAGipEGGVDTCQGDSGGPLMYqSDQwHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 422
Cdd:pfam00089 155 -AYGGTVTDTMICAG--AGGKDACQGDSGGPLVC-SDG-ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
221-424 4.14e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 70.48  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 221 HVCGGSILDPHWVLTAAHCF---RKHTDVFNWKVRAGSDKlGSFPSLAVAKIII-IEFNPMYPKDNDIALMKLQFPLTfs 296
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNG-GPYGTATATRFRVpPGWVASGDAGYDYALLRLDEPLG-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 297 GTVRPICLpFFDEELTPATPLWIIGWGftkqnGGKMSDILLQASvqvidstrCNADDAYQGEVTekMMCagipeggvDTC 376
Cdd:COG3591    89 DTTGWLGL-AFNDAPLAGEPVTIIGYP-----GDRPKDLSLDCS--------GRVTGVQGNRLS--YDC--------DTT 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462526394 377 QGDSGGPLMYQSD-QWHVVGIVSWGYgcGGPSTPGVYTkVSAYLNWIYN 424
Cdd:COG3591   145 GGSSGSPVLDDSDgGGRVVGVHSAGG--ADRANTGVRL-TSAIVAALRA 190
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
106-190 1.62e-13

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: 66.20  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 106 KDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSRAVEIGpdqDLDVVEITENSQELRMR--------------N 171
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLTHHK---SVNLTDISSNSSQSFMKlnssslntdlyealQ 77
                          90
                  ....*....|....*....
gi 2462526394 172 SSGPCLSGSLVSLHCLACG 190
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECG 96
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
102-187 3.97e-09

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 53.89  E-value: 3.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394  102 VRLSKDRS----TLQVLDSatGNWFSACFDNFTEALAETACRQMGYSRAVEI------GPDQD---LDVVEI--TENSQE 166
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHN--GQWGTVCDDGWDLRDANVVCRQLGFGGAVSAsgsayfGPGSGpiwLDNVRCsgTEASLS 78
                           90       100
                   ....*....|....*....|...
gi 2462526394  167 LRMRNSSG--PCLSGSLVSLHCL 187
Cdd:smart00202  79 DCPHSGWGshNCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
56-90 2.07e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 41.42  E-value: 2.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462526394  56 DKYYFLCGQPlHFIPRKQLCDGELDCPLGEDEEHC 90
Cdd:cd00112     2 PPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
357-421 2.06e-04

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 41.91  E-value: 2.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462526394 357 GEVTEKMMCAGIPEGGV------DTC--QGDSGGPLmYQSDQwhVVGIVSWGYG-CGGPSTPGVYTKVSAYLNW 421
Cdd:cd21112   116 GTVTAVNVTVNYPGGTVtgltrtNACaePGDSGGPV-FSGTQ--ALGITSGGSGnCGSGGGTSYFQPVNPVLSA 186
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
209-305 4.22e-04

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: 39.84  E-value: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 209 WPWQVSIQYDKQHVCGGSILDPHWVLTAAHCFR----KHTDVfnwKVRAGSDKLGSFPSLAVAKIIIIEFNPMYPKDNdI 284
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRdtnlRHQYI---SVVLGGAKTLKSIEGPYEQIVRVDCRHDIPESE-I 76
                          90       100
                  ....*....|....*....|.
gi 2462526394 285 ALMKLQFPLTFSGTVRPICLP 305
Cdd:pfam09342  77 SLLHLASPASFSNHVLPTFVP 97
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
69-90 1.69e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.07  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|..
gi 2462526394  69 IPRKQLCDGELDCPLGEDEEHC 90
Cdd:pfam00057  16 IPRSWVCDGDPDCGDGSDEENC 37
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
225-396 2.52e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 38.17  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 225 GSILDP-HWVLTAAHCFRKHTDVFNWKVRAGsdklgsFPSLAVAKIIIIEFNPmypkDNDIALmklqfpLTFSGTVRPI- 302
Cdd:pfam13365   3 GFVVSSdGLVLTNAHVVDDAEEAAVELVSVV------LADGREYPATVVARDP----DLDLAL------LRVSGDGRGLp 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526394 303 CLPFFD-EELTPATPLWIIGWGFTKQNggkmsdilLQASVQVIDSTRCNADDAYQGEVtekMMCAGIPEGgvdtcqGDSG 381
Cdd:pfam13365  67 PLPLGDsEPLVGGERVYAVGYPLGGEK--------LSLSEGIVSGVDEGRDGGDDGRV---IQTDAALSP------GSSG 129
                         170
                  ....*....|....*
gi 2462526394 382 GPLMyqSDQWHVVGI 396
Cdd:pfam13365 130 GPVF--DADGRVVGI 142
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
119-148 3.73e-03

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 36.59  E-value: 3.73e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462526394 119 GNWFSACFDNFTEALAETACRQMGYSRAVE 148
Cdd:pfam00530  15 GSWGTVCDDGWDLRDAHVVCRQLGCGGAVS 44
 
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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