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Conserved domains on  [gi|14602457|ref|NP_115781|]
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transmembrane protease serine 3 isoform 3 [Homo sapiens]

Protein Classification

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 ...
217-337 2.82e-34

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: 125.85  E-value: 2.82e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457 217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPS--HLVEKIVYH 293
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGqvIKVKKVIVH 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 14602457 294 SKYKPKRLGNDIALMKLAGPLTFNGTSGSLCgsaaLPLFQEDLQ 337
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPIC----LPSSGYNLP 119
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
112-210 2.19e-31

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: 113.96  E-value: 2.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457   112 GQNAVLQVFTAA--SWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSidhLLPDDKVTALHHSVY 189
Cdd:pfam15494   1 GENFLLQVYSSArpSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSNSSQSFMK---LNSSSLNTDLYEALQ 77
                          90       100
                  ....*....|....*....|.
gi 14602457   190 VREGCASGHVVTLQCTACGHR 210
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECGLR 98
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
74-107 1.78e-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: 44.12  E-value: 1.78e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 14602457  74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:cd00112   3 PNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
217-337 2.82e-34

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: 125.85  E-value: 2.82e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457 217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPS--HLVEKIVYH 293
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGqvIKVKKVIVH 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 14602457 294 SKYKPKRLGNDIALMKLAGPLTFNGTSGSLCgsaaLPLFQEDLQ 337
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPIC----LPSSGYNLP 119
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
216-324 1.57e-33

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: 123.56  E-value: 1.57e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457    216 RIVGGNMSLLSQWPWQASLQFQG-YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLL-DNPAPSHLVEKIVYH 293
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSsGEEGQVIKVSKVIIH 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 14602457    294 SKYKPKRLGNDIALMKLAGPLTFNGTSGSLC 324
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPIC 110
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
112-210 2.19e-31

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: 113.96  E-value: 2.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457   112 GQNAVLQVFTAA--SWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSidhLLPDDKVTALHHSVY 189
Cdd:pfam15494   1 GENFLLQVYSSArpSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSNSSQSFMK---LNSSSLNTDLYEALQ 77
                          90       100
                  ....*....|....*....|.
gi 14602457   190 VREGCASGHVVTLQCTACGHR 210
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECGLR 98
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
214-315 3.86e-27

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 107.43  E-value: 3.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457 214 SSRIVGGNMSLLSQWPWQASLQFQG---YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPSHLVEKI 290
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVVKVARI 106
                        90       100
                ....*....|....*....|....*
gi 14602457 291 VYHSKYKPKRLGNDIALMKLAGPLT 315
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVP 131
Trypsin pfam00089
Trypsin;
217-334 8.57e-26

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 102.91  E-value: 8.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457   217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlylPKSWTIQVG--LVSLLDNPAPSHLVEKIVYH 293
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGahNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 14602457   294 SKYKPKRLGNDIALMKLAGPLTFNGTSGSLCGSAALPLFQE 334
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV 118
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
74-107 1.78e-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: 44.12  E-value: 1.78e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 14602457  74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:cd00112   3 PNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
74-104 2.15e-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: 43.78  E-value: 2.15e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 14602457     74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDE 104
Cdd:smart00192   4 PGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
108-149 3.10e-06

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: 45.03  E-value: 3.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 14602457    108 VR-VGGQNA---VLQVFTAASWKTMCSDDWKGHYANVACAQLGFPS 149
Cdd:smart00202   1 VRlVGGGSPcegRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGG 46
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
74-107 1.50e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 14602457    74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:pfam00057   5 PNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
217-337 2.82e-34

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: 125.85  E-value: 2.82e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457 217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPS--HLVEKIVYH 293
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGqvIKVKKVIVH 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 14602457 294 SKYKPKRLGNDIALMKLAGPLTFNGTSGSLCgsaaLPLFQEDLQ 337
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPIC----LPSSGYNLP 119
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
216-324 1.57e-33

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: 123.56  E-value: 1.57e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457    216 RIVGGNMSLLSQWPWQASLQFQG-YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLL-DNPAPSHLVEKIVYH 293
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSsGEEGQVIKVSKVIIH 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 14602457    294 SKYKPKRLGNDIALMKLAGPLTFNGTSGSLC 324
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPIC 110
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
112-210 2.19e-31

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: 113.96  E-value: 2.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457   112 GQNAVLQVFTAA--SWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSidhLLPDDKVTALHHSVY 189
Cdd:pfam15494   1 GENFLLQVYSSArpSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSNSSQSFMK---LNSSSLNTDLYEALQ 77
                          90       100
                  ....*....|....*....|.
gi 14602457   190 VREGCASGHVVTLQCTACGHR 210
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECGLR 98
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
214-315 3.86e-27

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 107.43  E-value: 3.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457 214 SSRIVGGNMSLLSQWPWQASLQFQG---YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPSHLVEKI 290
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVVKVARI 106
                        90       100
                ....*....|....*....|....*
gi 14602457 291 VYHSKYKPKRLGNDIALMKLAGPLT 315
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVP 131
Trypsin pfam00089
Trypsin;
217-334 8.57e-26

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 102.91  E-value: 8.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457   217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlylPKSWTIQVG--LVSLLDNPAPSHLVEKIVYH 293
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGahNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 14602457   294 SKYKPKRLGNDIALMKLAGPLTFNGTSGSLCGSAALPLFQE 334
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV 118
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
238-315 2.35e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.45  E-value: 2.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457 238 GYHLCGGSVITPLWIITAAHCVYDLY---LPKSWTIQVGlvsLLDNPAPSHLVEKIVYHSKYKPK-RLGNDIALMKLAGP 313
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVYDGAgggWATNIVFVPG---YNGGPYGTATATRFRVPPGWVASgDAGYDYALLRLDEP 86

                ..
gi 14602457 314 LT 315
Cdd:COG3591  87 LG 88
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
74-107 1.78e-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: 44.12  E-value: 1.78e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 14602457  74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:cd00112   3 PNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
74-104 2.15e-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: 43.78  E-value: 2.15e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 14602457     74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDE 104
Cdd:smart00192   4 PGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
108-149 3.10e-06

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: 45.03  E-value: 3.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 14602457    108 VR-VGGQNA---VLQVFTAASWKTMCSDDWKGHYANVACAQLGFPS 149
Cdd:smart00202   1 VRlVGGGSPcegRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGG 46
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
74-107 1.50e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 14602457    74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:pfam00057   5 PNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEENC 37
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
117-153 2.17e-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: 36.97  E-value: 2.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 14602457   117 LQVFTAASWKTMCSDDWKGHYANVACAQLGFPSYVSS 153
Cdd:pfam00530   9 VEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSA 45
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
228-316 8.44e-03

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: 35.60  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14602457   228 WPWQASLQFQGYHLCGGSVITPLWIITAAHCVYDLYLPKSWTIQV--GLVSLLDNPAPSHLVEKI-VYHSKYKPKrlgnd 304
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlgGAKTLKSIEGPYEQIVRVdCRHDIPESE----- 75
                          90
                  ....*....|..
gi 14602457   305 IALMKLAGPLTF 316
Cdd:pfam09342  76 ISLLHLASPASF 87
 
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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