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Conserved domains on  [gi|554851642|ref|XP_005936065|]
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transmembrane protease serine 2 [Haplochromis burtoni]

Protein Classification

SRCR_2 and Tryp_SPc domain-containing protein (domain architecture ID 11258211)

protein containing domains LDLa, SRCR_2, and Tryp_SPc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
272-499 1.14e-101

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  Cd Length: 232  Bit Score: 304.58  E-value: 1.14e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 272 IVGGTEAVNGAWPWQVSLQVS-GRHSCGGSIISRYWILSAAHCFkYSSSPSLWRVYYGDVNLENMFNS----RVQKIIKH 346
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGgqviKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 347 KDFDTRTNNYDIALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQAWITGWGALQSTGPTPKIMNQAKVTIYSRATCNAPE 426
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554851642 427 VLNGEVTKAMFCAGSLEGGVDSCQGDSGGPLVVKEGDRWWLAGATSYGYGCALKNKPGVYANVPFFIDWIYEN 499
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
168-265 3.69e-23

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: 406055  Cd Length: 99  Bit Score: 93.56  E-value: 3.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  168 GANSMLESYSSSSQTWMPVCADNWDDNYGRTVCRQIGYSRDDYFAYSQTSAGSLA-SNGYMRLeSGSNSGSLIQSQLTHS 246
Cdd:pfam15494   1 GPNFLLQVYSRARASWLPVCSDGWNPSYGKAACQQLGYSRLTYHKSVNLTDISSNsSQGFMKL-SSSTSGTDLYESLQPS 79
                          90       100
                  ....*....|....*....|
gi 554851642  247 LLCFS-KAVTLQCIECGKSS 265
Cdd:pfam15494  80 SSCSSgSVVSLRCSECGLRT 99
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
128-160 5.54e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. 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. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


:

Pssm-ID: 197566  Cd Length: 33  Bit Score: 43.01  E-value: 5.54e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 554851642   128 QCLLGKSCGKGGMCLSHTRWCDGTIDCPDGEDE 160
Cdd:smart00192   1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
272-499 1.14e-101

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  Cd Length: 232  Bit Score: 304.58  E-value: 1.14e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 272 IVGGTEAVNGAWPWQVSLQVS-GRHSCGGSIISRYWILSAAHCFkYSSSPSLWRVYYGDVNLENMFNS----RVQKIIKH 346
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGgqviKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 347 KDFDTRTNNYDIALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQAWITGWGALQSTGPTPKIMNQAKVTIYSRATCNAPE 426
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554851642 427 VLNGEVTKAMFCAGSLEGGVDSCQGDSGGPLVVKEGDRWWLAGATSYGYGCALKNKPGVYANVPFFIDWIYEN 499
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
271-496 1.25e-98

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: 296.51  E-value: 1.25e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642   271 RIVGGTEAVNGAWPWQVSLQVSG-RHSCGGSIISRYWILSAAHCFkYSSSPSLWRVYYGDVNL---ENMFNSRVQKIIKH 346
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLssgEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642   347 KDFDTRTNNYDIALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQAWITGWGALQ-STGPTPKIMNQAKVTIYSRATCNAP 425
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554851642   426 EVLNGEVTKAMFCAGSLEGGVDSCQGDSGGPLVVKeGDRWWLAGATSYGYGCALKNKPGVYANVPFFIDWI 496
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
272-496 1.37e-70

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 224.24  E-value: 1.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  272 IVGGTEAVNGAWPWQVSLQV-SGRHSCGGSIISRYWILSAAHCFKYSSSpslWRVYYGDVNLENMFNSR----VQKIIKH 346
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEqkfdVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  347 KDFDTRTNNYDIALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQAWITGWGALQSTGPtPKIMNQAKVTIYSRATCNapE 426
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR--S 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  427 VLNGEVTKAMFCAGSleGGVDSCQGDSGGPLVVKEGDrwwLAGATSYGYGCALKNKPGVYANVPFFIDWI 496
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
269-496 4.01e-28

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 116.13  E-value: 4.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 269 SSRIVGGTEAVNGAWPWQVSLQVSGRHS-----CGGSIISRYWILSAAHCFKYSS--SPSLWRVYYGDVNLENMFNSRVQ 341
Cdd:COG5640   30 SSRIIGGSNANAGEYPSLVALVDRISDYvsgtfCGGSKLGGRYVLTAAHCADASSpiSSDVNRVVVDLNDSSQAERGHVR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 342 KIIKHKDFDTRTNNYDIALLKLDTPL-TFNNKVRPVCLPNVDLN-LSANRQAWITGWGA-LQSTGP--TPK--IMNQAKV 414
Cdd:COG5640  110 TIYVHEFYSPGNLGNDIAVLELARAAsLPRVKITSFDASDTFLNsVTTVSPMTNGTFGVtTPSDVPrsSPKgtILHEVAV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 415 TIYSRATCNA----PEVLNGEVTKAMFCAGSLegGVDSCQGDSGGPLVVKEGDRWWLAGATSYGYG-CALKNKPGVYANV 489
Cdd:COG5640  190 LFVPLSTCAQykgcANASDGATGLTGFCAGRP--PKDACQGDSGGPIFHKGEEGRVQRGVVSWGDGgCGGTLIPGVYTNV 267

                 ....*..
gi 554851642 490 PFFIDWI 496
Cdd:COG5640  268 SNYQDWI 274
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
168-265 3.69e-23

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: 406055  Cd Length: 99  Bit Score: 93.56  E-value: 3.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  168 GANSMLESYSSSSQTWMPVCADNWDDNYGRTVCRQIGYSRDDYFAYSQTSAGSLA-SNGYMRLeSGSNSGSLIQSQLTHS 246
Cdd:pfam15494   1 GPNFLLQVYSRARASWLPVCSDGWNPSYGKAACQQLGYSRLTYHKSVNLTDISSNsSQGFMKL-SSSTSGTDLYESLQPS 79
                          90       100
                  ....*....|....*....|
gi 554851642  247 LLCFS-KAVTLQCIECGKSS 265
Cdd:pfam15494  80 SSCSSgSVVSLRCSECGLRT 99
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
128-160 5.54e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. 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. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 43.01  E-value: 5.54e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 554851642   128 QCLLGKSCGKGGMCLSHTRWCDGTIDCPDGEDE 160
Cdd:smart00192   1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
137-163 9.85e-06

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: 42.19  E-value: 9.85e-06
                         10        20
                 ....*....|....*....|....*..
gi 554851642 137 KGGMCLSHTRWCDGTIDCPDGEDESQC 163
Cdd:cd00112    9 ANGRCIPSSWVCDGEDDCGDGSDEENC 35
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
182-207 1.04e-05

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  Cd Length: 101  Bit Score: 44.26  E-value: 1.04e-05
                           10        20
                   ....*....|....*....|....*.
gi 554851642   182 TWMPVCADNWDDNYGRTVCRQIGYSR 207
Cdd:smart00202  21 QWGTVCDDGWDLRDANVVCRQLGFGG 46
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
272-499 1.14e-101

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  Cd Length: 232  Bit Score: 304.58  E-value: 1.14e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 272 IVGGTEAVNGAWPWQVSLQVS-GRHSCGGSIISRYWILSAAHCFkYSSSPSLWRVYYGDVNLENMFNS----RVQKIIKH 346
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGgqviKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 347 KDFDTRTNNYDIALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQAWITGWGALQSTGPTPKIMNQAKVTIYSRATCNAPE 426
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554851642 427 VLNGEVTKAMFCAGSLEGGVDSCQGDSGGPLVVKEGDRWWLAGATSYGYGCALKNKPGVYANVPFFIDWIYEN 499
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
271-496 1.25e-98

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: 296.51  E-value: 1.25e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642   271 RIVGGTEAVNGAWPWQVSLQVSG-RHSCGGSIISRYWILSAAHCFkYSSSPSLWRVYYGDVNL---ENMFNSRVQKIIKH 346
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLssgEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642   347 KDFDTRTNNYDIALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQAWITGWGALQ-STGPTPKIMNQAKVTIYSRATCNAP 425
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554851642   426 EVLNGEVTKAMFCAGSLEGGVDSCQGDSGGPLVVKeGDRWWLAGATSYGYGCALKNKPGVYANVPFFIDWI 496
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
272-496 1.37e-70

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 224.24  E-value: 1.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  272 IVGGTEAVNGAWPWQVSLQV-SGRHSCGGSIISRYWILSAAHCFKYSSSpslWRVYYGDVNLENMFNSR----VQKIIKH 346
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEqkfdVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  347 KDFDTRTNNYDIALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQAWITGWGALQSTGPtPKIMNQAKVTIYSRATCNapE 426
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR--S 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  427 VLNGEVTKAMFCAGSleGGVDSCQGDSGGPLVVKEGDrwwLAGATSYGYGCALKNKPGVYANVPFFIDWI 496
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
269-496 4.01e-28

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 116.13  E-value: 4.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 269 SSRIVGGTEAVNGAWPWQVSLQVSGRHS-----CGGSIISRYWILSAAHCFKYSS--SPSLWRVYYGDVNLENMFNSRVQ 341
Cdd:COG5640   30 SSRIIGGSNANAGEYPSLVALVDRISDYvsgtfCGGSKLGGRYVLTAAHCADASSpiSSDVNRVVVDLNDSSQAERGHVR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 342 KIIKHKDFDTRTNNYDIALLKLDTPL-TFNNKVRPVCLPNVDLN-LSANRQAWITGWGA-LQSTGP--TPK--IMNQAKV 414
Cdd:COG5640  110 TIYVHEFYSPGNLGNDIAVLELARAAsLPRVKITSFDASDTFLNsVTTVSPMTNGTFGVtTPSDVPrsSPKgtILHEVAV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642 415 TIYSRATCNA----PEVLNGEVTKAMFCAGSLegGVDSCQGDSGGPLVVKEGDRWWLAGATSYGYG-CALKNKPGVYANV 489
Cdd:COG5640  190 LFVPLSTCAQykgcANASDGATGLTGFCAGRP--PKDACQGDSGGPIFHKGEEGRVQRGVVSWGDGgCGGTLIPGVYTNV 267

                 ....*..
gi 554851642 490 PFFIDWI 496
Cdd:COG5640  268 SNYQDWI 274
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
168-265 3.69e-23

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: 406055  Cd Length: 99  Bit Score: 93.56  E-value: 3.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  168 GANSMLESYSSSSQTWMPVCADNWDDNYGRTVCRQIGYSRDDYFAYSQTSAGSLA-SNGYMRLeSGSNSGSLIQSQLTHS 246
Cdd:pfam15494   1 GPNFLLQVYSRARASWLPVCSDGWNPSYGKAACQQLGYSRLTYHKSVNLTDISSNsSQGFMKL-SSSTSGTDLYESLQPS 79
                          90       100
                  ....*....|....*....|
gi 554851642  247 LLCFS-KAVTLQCIECGKSS 265
Cdd:pfam15494  80 SSCSSgSVVSLRCSECGLRT 99
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
128-160 5.54e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. 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. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 43.01  E-value: 5.54e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 554851642   128 QCLLGKSCGKGGMCLSHTRWCDGTIDCPDGEDE 160
Cdd:smart00192   1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
137-163 9.85e-06

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: 42.19  E-value: 9.85e-06
                         10        20
                 ....*....|....*....|....*..
gi 554851642 137 KGGMCLSHTRWCDGTIDCPDGEDESQC 163
Cdd:cd00112    9 ANGRCIPSSWVCDGEDDCGDGSDEENC 35
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
182-207 1.04e-05

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  Cd Length: 101  Bit Score: 44.26  E-value: 1.04e-05
                           10        20
                   ....*....|....*....|....*.
gi 554851642   182 TWMPVCADNWDDNYGRTVCRQIGYSR 207
Cdd:smart00202  21 QWGTVCDDGWDLRDANVVCRQLGFGG 46
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
283-390 3.10e-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: 40.22  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  283 WPWQVSLQVSGRHSCGGSIISRYWILSAAHCfkyssspsLWrvyygDVNLENMFNSRVqkIIKHKDFDTRTNNYD----- 357
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC--------LR-----DTNLRHQYISVV--LGGAKTLKSIEGPYEqivrv 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 554851642  358 ----------IALLKLDTPLTFNNKVRPVCLPNVDLNLSANRQ 390
Cdd:pfam09342  66 dcrhdipeseISLLHLASPASFSNHVLPTFVPETRNENEKDNE 108
Hepsin-SRCR pfam09272
Hepsin, SRCR; Members of this family form an extracellular domain of the serine protease ...
169-263 3.76e-04

Hepsin, SRCR; Members of this family form an extracellular domain of the serine protease hepsin. They are formed primarily by three elements of regular secondary structure: a 12-residue alpha helix, a twisted five-stranded antiparallel beta sheet, and a second, two-stranded, antiparallel sheet. The two beta-sheets lie at roughly right angles to each other, with the helix nestled between the two, adopting an SRCR fold. The exact function of this domain has not been identified, though it probably may serve to orient the protease domain or place it in the vicinity of its substrate.


Pssm-ID: 401275  Cd Length: 110  Bit Score: 40.11  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554851642  169 ANSMLESYSSSSQTWMPVCADNWDDNYGRTVCRQIGYSRDdyFAYSQTSAGSLASNGymrlesGSNSGSLIQSQLTH--S 246
Cdd:pfam09272  10 ADSRLTVFDESEGRWRLVCSSSSNALVATLSCEEMGFVRS--LSHSELHVRSAGGNG------TSGFFCVDESRLPYakK 81
                          90       100
                  ....*....|....*....|....*
gi 554851642  247 LLCFS--------KAVTLQCIECGK 263
Cdd:pfam09272  82 LKEVLtvcdcpsgRFLAVLCQDCGR 106
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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