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Conserved domains on  [gi|186910296|ref|NP_001119574|]
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haptoglobin isoform 2 preproprotein [Homo sapiens]

Protein Classification

haptoglobin( domain architecture ID 10034116)

haptoglobin binds to free hemoglobin released from erythrocytes with high affinity and thereby inhibits its deleterious oxidative activity

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 ...
103-343 3.51e-63

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: 200.58  E-value: 3.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 103 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 181
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 182 NYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGRNA-NFKFTDHLKYVMLPVADQDQCIRHYE 255
Cdd:cd00190   81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 256 GstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleEDTWYATGILSFDKSCAVAEY-GVYVKVT 334
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 186910296 335 SIQDWVQKT 343
Cdd:cd00190  224 SYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
33-87 2.21e-03

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 35.90  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186910296  33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNNEKQWINkavgdKLPECE 87
Cdd:cd00033    1 CPPPPVPENGTVTGSkgsysygstVTYSCNEGYTLV--GSSTITCTENGGWSP-----PPPTCE 57
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
103-343 3.51e-63

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: 200.58  E-value: 3.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 103 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 181
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 182 NYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGRNA-NFKFTDHLKYVMLPVADQDQCIRHYE 255
Cdd:cd00190   81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 256 GstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleEDTWYATGILSFDKSCAVAEY-GVYVKVT 334
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 186910296 335 SIQDWVQKT 343
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
102-340 1.25e-58

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: 189.04  E-value: 1.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296   102 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 172
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296   173 EIEKVVLHPNYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGR--NANFKFTDHLKYVMLPVA 245
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRtsEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296   246 DQDQCIRHYEGstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleeDTWYATGILSFDKSCAVA 325
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 186910296   326 EY-GVYVKVTSIQDWV 340
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
103-340 5.20e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 171.47  E-value: 5.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  103 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 181
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  182 NYSQV----DIGLIKLKQKVSVNERVMPICLPSK-DYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEG 256
Cdd:pfam00089  79 NYNPDtldnDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  257 StvpekktpkspvgvqpiLNEHTFCAGMskYQEDTCYGDAGSAFAVHDLeedtwYATGILSFDKSCAVAEY-GVYVKVTS 335
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 186910296  336 IQDWV 340
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
96-347 1.55e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 116.67  E-value: 1.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  96 PANPVQRILGGHLDAKGSFPWQAKMVS---HHNLTTGATLINEQWLLTTAknlflnHsenATAKDIAPTLTLYVG----- 167
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAA------H---CVDGDGPSDLRVVIGstdls 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 168 --KKQLVEIEKVVLHPNYSQV----DIGLIKLKQKVSvneRVMPICLP-SKDYAEVGRVGYVSGWGRNANF--KFTDHLK 238
Cdd:COG5640   95 tsGGTVVKVARIVVHPDYDPAtpgnDIALLKLATPVP---GVAPAPLAtSADAAAPGTPATVAGWGRTSEGpgSQSGTLR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 239 YVMLPVADQDQCiRHYEGstvpekktpkspvgvqpILNEHTFCAGMSKYQEDTCYGDAGS-AFAVHDleeDTWYATGILS 317
Cdd:COG5640  172 KADVPVVSDATC-AAYGG-----------------FDGGTMLCAGYPEGGKDACQGDSGGpLVVKDG---GGWVLVGVVS 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 186910296 318 F-DKSCAVAEYGVYVKVTSIQDWVQKTIAEN 347
Cdd:COG5640  231 WgGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
33-87 2.21e-03

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 35.90  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186910296  33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNNEKQWINkavgdKLPECE 87
Cdd:cd00033    1 CPPPPVPENGTVTGSkgsysygstVTYSCNEGYTLV--GSSTITCTENGGWSP-----PPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
33-86 7.68e-03

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 34.42  E-value: 7.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186910296    33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLrtEGDGVYTLNNEKQWINKAvgdklPEC 86
Cdd:smart00032   1 CPPPPDIENGTVTSSsgtysygdtVTYSCDPGYTL--IGSSTITCLENGTWSPPP-----PTC 56
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
103-343 3.51e-63

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: 200.58  E-value: 3.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 103 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 181
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 182 NYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGRNA-NFKFTDHLKYVMLPVADQDQCIRHYE 255
Cdd:cd00190   81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 256 GstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleEDTWYATGILSFDKSCAVAEY-GVYVKVT 334
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 186910296 335 SIQDWVQKT 343
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
102-340 1.25e-58

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: 189.04  E-value: 1.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296   102 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 172
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296   173 EIEKVVLHPNYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGR--NANFKFTDHLKYVMLPVA 245
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRtsEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296   246 DQDQCIRHYEGstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleeDTWYATGILSFDKSCAVA 325
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 186910296   326 EY-GVYVKVTSIQDWV 340
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
103-340 5.20e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 171.47  E-value: 5.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  103 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 181
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  182 NYSQV----DIGLIKLKQKVSVNERVMPICLPSK-DYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEG 256
Cdd:pfam00089  79 NYNPDtldnDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  257 StvpekktpkspvgvqpiLNEHTFCAGMskYQEDTCYGDAGSAFAVHDLeedtwYATGILSFDKSCAVAEY-GVYVKVTS 335
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 186910296  336 IQDWV 340
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
96-347 1.55e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 116.67  E-value: 1.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296  96 PANPVQRILGGHLDAKGSFPWQAKMVS---HHNLTTGATLINEQWLLTTAknlflnHsenATAKDIAPTLTLYVG----- 167
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAA------H---CVDGDGPSDLRVVIGstdls 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 168 --KKQLVEIEKVVLHPNYSQV----DIGLIKLKQKVSvneRVMPICLP-SKDYAEVGRVGYVSGWGRNANF--KFTDHLK 238
Cdd:COG5640   95 tsGGTVVKVARIVVHPDYDPAtpgnDIALLKLATPVP---GVAPAPLAtSADAAAPGTPATVAGWGRTSEGpgSQSGTLR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186910296 239 YVMLPVADQDQCiRHYEGstvpekktpkspvgvqpILNEHTFCAGMSKYQEDTCYGDAGS-AFAVHDleeDTWYATGILS 317
Cdd:COG5640  172 KADVPVVSDATC-AAYGG-----------------FDGGTMLCAGYPEGGKDACQGDSGGpLVVKDG---GGWVLVGVVS 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 186910296 318 F-DKSCAVAEYGVYVKVTSIQDWVQKTIAEN 347
Cdd:COG5640  231 WgGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
33-87 2.21e-03

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 35.90  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186910296  33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNNEKQWINkavgdKLPECE 87
Cdd:cd00033    1 CPPPPVPENGTVTGSkgsysygstVTYSCNEGYTLV--GSSTITCTENGGWSP-----PPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
33-86 7.68e-03

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 34.42  E-value: 7.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186910296    33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLrtEGDGVYTLNNEKQWINKAvgdklPEC 86
Cdd:smart00032   1 CPPPPDIENGTVTSSsgtysygdtVTYSCDPGYTL--IGSSTITCLENGTWSPPP-----PTC 56
 
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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