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Conserved domains on  [gi|1890345345|ref|NP_001277023|]
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transmembrane protease serine 4 isoform 6 [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 ...
179-404 2.91e-97

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: 2.91e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  179 RVVGVEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRKHtDVFNWKVRAGSDKL---GSFPSLAVAKIIIi 254
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLssgEEGQVIKVSKVII- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  255 efNPMYPK---DNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRC 331
Cdd:smart00020  79 --HPNYNPstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890345345  332 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 404
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
SRCR_2 super family cl02509
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
83-172 3.68e-15

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: 70.82  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  83 KDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQ--------DLDVVEITENSQElrMRNS 154
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISsnssqsfmKLNSSSLNTDLYE--ALQP 78
                          90
                  ....*....|....*...
gi 1890345345 155 SGPCLSGSLVSLHCLACG 172
Cdd:pfam15494  79 RDSCSSGSVVSLRCSECG 96
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
33-67 1.95e-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: 1.95e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1890345345  33 DKYYFLCGQPlHFIPRKQLCDGELDCPLGEDEEHC 67
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 ...
179-404 2.91e-97

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: 2.91e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  179 RVVGVEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRKHtDVFNWKVRAGSDKL---GSFPSLAVAKIIIi 254
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLssgEEGQVIKVSKVII- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  255 efNPMYPK---DNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRC 331
Cdd:smart00020  79 --HPNYNPstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890345345  332 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 404
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
180-407 1.56e-93

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: 280.70  E-value: 1.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 180 VVGVEEASVDSWPWQVSIQYDK-QHVCGGSILDPHWVLTAAHCFRKhTDVFNWKVRAGSDKLGSFPS----LAVAKIIIi 254
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGggqvIKVKKVIV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 255 efNPMY---PKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTkQNGGKMSDILLQASVQVIDSTRC 331
Cdd:cd00190    79 --HPNYnpsTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890345345 332 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQS-DQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNV 407
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDnGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
170-404 1.02e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 231.08  E-value: 1.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 170 ACGKSLKTPRVVGVEEASVDSWPWQVSIQYDK---QHVCGGSILDPHWVLTAAHCFrKHTDVFNWKVRAGSDKLGSFP-- 244
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLSTSGgt 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 245 SLAVAKIIIiefNPMY---PKDNDIALMKLQFPLTfsgTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQA 321
Cdd:COG5640   100 VVKVARIVV---HPDYdpaTPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 322 SVQVIDSTRCNAddaYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSD-QWHVVGIVSWGYGCGGPSTPGVYTKVSAY 400
Cdd:COG5640   174 DVPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGgGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                  ....
gi 1890345345 401 LNWI 404
Cdd:COG5640   251 RDWI 254
Trypsin pfam00089
Trypsin;
180-404 1.22e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.24  E-value: 1.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 180 VVGVEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRkhtDVFNWKVRAGSDKLG-SFPSLAVAKIIIIEFN 257
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVlREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 258 PMYP---KDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGgkMSDILLQASVQVIDSTRCNAd 334
Cdd:pfam00089  78 PNYNpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 335 dAYQGEVTEKMMCAGipEGGVDTCQGDSGGPLMYqSDQwHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 404
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 ...
83-172 3.68e-15

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: 70.82  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  83 KDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQ--------DLDVVEITENSQElrMRNS 154
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISsnssqsfmKLNSSSLNTDLYE--ALQP 78
                          90
                  ....*....|....*...
gi 1890345345 155 SGPCLSGSLVSLHCLACG 172
Cdd:pfam15494  79 RDSCSSGSVVSLRCSECG 96
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
79-169 1.78e-08

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: 51.96  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345   79 VRLSKDRS----TLQVLDSatGNWFSACFDNFTEALAETACRQMGYSSKP-TFRAVEIGPDQD---LDVVEI--TENSQE 148
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHN--GQWGTVCDDGWDLRDANVVCRQLGFGGAVsASGSAYFGPGSGpiwLDNVRCsgTEASLS 78
                           90       100
                   ....*....|....*....|...
gi 1890345345  149 LRMRNSSG--PCLSGSLVSLHCL 169
Cdd:smart00202  79 DCPHSGWGshNCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
33-67 1.95e-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: 1.95e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1890345345  33 DKYYFLCGQPlHFIPRKQLCDGELDCPLGEDEEHC 67
Cdd:cd00112     2 PPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
46-67 1.62e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.07  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|..
gi 1890345345  46 IPRKQLCDGELDCPLGEDEEHC 67
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 ...
179-404 2.91e-97

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: 2.91e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  179 RVVGVEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRKHtDVFNWKVRAGSDKL---GSFPSLAVAKIIIi 254
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLssgEEGQVIKVSKVII- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  255 efNPMYPK---DNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRC 331
Cdd:smart00020  79 --HPNYNPstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890345345  332 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 404
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
180-407 1.56e-93

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: 280.70  E-value: 1.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 180 VVGVEEASVDSWPWQVSIQYDK-QHVCGGSILDPHWVLTAAHCFRKhTDVFNWKVRAGSDKLGSFPS----LAVAKIIIi 254
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGggqvIKVKKVIV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 255 efNPMY---PKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTkQNGGKMSDILLQASVQVIDSTRC 331
Cdd:cd00190    79 --HPNYnpsTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890345345 332 NADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQS-DQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNV 407
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDnGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
170-404 1.02e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 231.08  E-value: 1.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 170 ACGKSLKTPRVVGVEEASVDSWPWQVSIQYDK---QHVCGGSILDPHWVLTAAHCFrKHTDVFNWKVRAGSDKLGSFP-- 244
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLSTSGgt 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 245 SLAVAKIIIiefNPMY---PKDNDIALMKLQFPLTfsgTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQA 321
Cdd:COG5640   100 VVKVARIVV---HPDYdpaTPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 322 SVQVIDSTRCNAddaYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSD-QWHVVGIVSWGYGCGGPSTPGVYTKVSAY 400
Cdd:COG5640   174 DVPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGgGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                  ....
gi 1890345345 401 LNWI 404
Cdd:COG5640   251 RDWI 254
Trypsin pfam00089
Trypsin;
180-404 1.22e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.24  E-value: 1.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 180 VVGVEEASVDSWPWQVSIQY-DKQHVCGGSILDPHWVLTAAHCFRkhtDVFNWKVRAGSDKLG-SFPSLAVAKIIIIEFN 257
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVlREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 258 PMYP---KDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGgkMSDILLQASVQVIDSTRCNAd 334
Cdd:pfam00089  78 PNYNpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 335 dAYQGEVTEKMMCAGipEGGVDTCQGDSGGPLMYqSDQwHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWI 404
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 ...
83-172 3.68e-15

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: 70.82  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345  83 KDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQ--------DLDVVEITENSQElrMRNS 154
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISsnssqsfmKLNSSSLNTDLYE--ALQP 78
                          90
                  ....*....|....*...
gi 1890345345 155 SGPCLSGSLVSLHCLACG 172
Cdd:pfam15494  79 RDSCSSGSVVSLRCSECG 96
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
203-406 5.64e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 70.09  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 203 HVCGGSILDPHWVLTAAHCF---RKHTDVFNWKVRAGSDKlGSFPSLAVAKIII-IEFNPMYPKDNDIALMKLQFPLTfs 278
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNG-GPYGTATATRFRVpPGWVASGDAGYDYALLRLDEPLG-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 279 GTVRPICLpFFDEELTPATPLWIIGWGftkqnGGKMSDILLQASvqvidstrCNADDAYQGEVTekMMCagipeggvDTC 358
Cdd:COG3591    89 DTTGWLGL-AFNDAPLAGEPVTIIGYP-----GDRPKDLSLDCS--------GRVTGVQGNRLS--YDC--------DTT 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1890345345 359 QGDSGGPLMYQSD-QWHVVGIVSWGYgcGGPSTPGVYTkVSAYLNWIYN 406
Cdd:COG3591   145 GGSSGSPVLDDSDgGGRVVGVHSAGG--ADRANTGVRL-TSAIVAALRA 190
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
79-169 1.78e-08

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: 51.96  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345   79 VRLSKDRS----TLQVLDSatGNWFSACFDNFTEALAETACRQMGYSSKP-TFRAVEIGPDQD---LDVVEI--TENSQE 148
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHN--GQWGTVCDDGWDLRDANVVCRQLGFGGAVsASGSAYFGPGSGpiwLDNVRCsgTEASLS 78
                           90       100
                   ....*....|....*....|...
gi 1890345345  149 LRMRNSSG--PCLSGSLVSLHCL 169
Cdd:smart00202  79 DCPHSGWGshNCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
33-67 1.95e-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: 1.95e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1890345345  33 DKYYFLCGQPlHFIPRKQLCDGELDCPLGEDEEHC 67
Cdd:cd00112     2 PPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
339-403 3.63e-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: 41.14  E-value: 3.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890345345 339 GEVTEKMMCAGIPEGGV------DTC--QGDSGGPLmYQSDQwhVVGIVSWGYG-CGGPSTPGVYTKVSAYLNW 403
Cdd:cd21112   116 GTVTAVNVTVNYPGGTVtgltrtNACaePGDSGGPV-FSGTQ--ALGITSGGSGnCGSGGGTSYFQPVNPVLSA 186
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
191-287 4.30e-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: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 191 WPWQVSIQYDKQHVCGGSILDPHWVLTAAHCFR----KHTDVfnwKVRAGSDKLGSFPSLAVAKIIIIEFNPMYPKDNdI 266
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRdtnlRHQYI---SVVLGGAKTLKSIEGPYEQIVRVDCRHDIPESE-I 76
                          90       100
                  ....*....|....*....|.
gi 1890345345 267 ALMKLQFPLTFSGTVRPICLP 287
Cdd:pfam09342  77 SLLHLASPASFSNHVLPTFVP 97
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
46-67 1.62e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.07  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|..
gi 1890345345  46 IPRKQLCDGELDCPLGEDEEHC 67
Cdd:pfam00057  16 IPRSWVCDGDPDCGDGSDEENC 37
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
207-378 2.84e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.79  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 207 GSILDP-HWVLTAAHCFRKHTDVFNWKVRAGsdklgsFPSLAVAKIIIIEFNPmypkDNDIALmklqfpLTFSGTVRPI- 284
Cdd:pfam13365   3 GFVVSSdGLVLTNAHVVDDAEEAAVELVSVV------LADGREYPATVVARDP----DLDLAL------LRVSGDGRGLp 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890345345 285 CLPFFD-EELTPATPLWIIGWGFTKQNggkmsdilLQASVQVIDSTRCNADDAYQGEVtekMMCAGIPEGgvdtcqGDSG 363
Cdd:pfam13365  67 PLPLGDsEPLVGGERVYAVGYPLGGEK--------LSLSEGIVSGVDEGRDGGDDGRV---IQTDAALSP------GSSG 129
                         170
                  ....*....|....*
gi 1890345345 364 GPLMyqSDQWHVVGI 378
Cdd:pfam13365 130 GPVF--DADGRVVGI 142
 
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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