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Conserved domains on  [gi|4826762|ref|NP_005134|]
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haptoglobin isoform 1 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 ...
162-402 2.31e-62

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: 2.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  162 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 240
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  241 NYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGRNA-NFKFTDHLKYVMLPVADQDQCIRHYE 314
Cdd:cd00190  81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  315 GstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleEDTWYATGILSFDKSCAVAEY-GVYVKVT 393
Cdd:cd00190 161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                ....*....
gi 4826762  394 SIQDWVQKT 402
Cdd:cd00190 224 SYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
33-87 2.71e-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: 2.71e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826762   33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNDKKQWINkavgdKLPECE 87
Cdd:cd00033   1 CPPPPVPENGTVTGSkgsysygstVTYSCNEGYTLV--GSSTITCTENGGWSP-----PPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
92-146 4.75e-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: 35.13  E-value: 4.75e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826762   92 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNNEKQWINkavgdKLPECE 146
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 ...
162-402 2.31e-62

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: 2.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  162 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 240
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  241 NYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGRNA-NFKFTDHLKYVMLPVADQDQCIRHYE 314
Cdd:cd00190  81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  315 GstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleEDTWYATGILSFDKSCAVAEY-GVYVKVT 393
Cdd:cd00190 161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                ....*....
gi 4826762  394 SIQDWVQKT 402
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
161-399 8.72e-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: 188.66  E-value: 8.72e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762     161 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 231
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762     232 EIEKVVLHPNYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGR--NANFKFTDHLKYVMLPVA 304
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRtsEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762     305 DQDQCIRHYEGstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleeDTWYATGILSFDKSCAVA 384
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 4826762     385 EY-GVYVKVTSIQDWV 399
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
162-399 1.99e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 171.86  E-value: 1.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762    162 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 240
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762    241 NYSQV----DIGLIKLKQKVSVNERVMPICLPSK-DYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEG 315
Cdd:pfam00089  79 NYNPDtldnDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762    316 StvpekktpkspvgvqpiLNEHTFCAGMskYQEDTCYGDAGSAFAVHDLeedtwYATGILSFDKSCAVAEY-GVYVKVTS 394
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 4826762    395 IQDWV 399
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
155-406 1.67e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 117.83  E-value: 1.67e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  155 PANPVQRILGGHLDAKGSFPWQAKMVS---HHNLTTGATLINEQWLLTTAknlflnHsenATAKDIAPTLTLYVG----- 226
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAA------H---CVDGDGPSDLRVVIGstdls 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  227 --KKQLVEIEKVVLHPNYSQV----DIGLIKLKQKVSvneRVMPICLP-SKDYAEVGRVGYVSGWGRNANF--KFTDHLK 297
Cdd:COG5640  95 tsGGTVVKVARIVVHPDYDPAtpgnDIALLKLATPVP---GVAPAPLAtSADAAAPGTPATVAGWGRTSEGpgSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  298 YVMLPVADQDQCiRHYEGstvpekktpkspvgvqpILNEHTFCAGMSKYQEDTCYGDAGS-AFAVHDleeDTWYATGILS 376
Cdd:COG5640 172 KADVPVVSDATC-AAYGG-----------------FDGGTMLCAGYPEGGKDACQGDSGGpLVVKDG---GGWVLVGVVS 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 4826762  377 F-DKSCAVAEYGVYVKVTSIQDWVQKTIAEN 406
Cdd:COG5640 231 WgGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
33-87 2.71e-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: 2.71e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826762   33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNDKKQWINkavgdKLPECE 87
Cdd:cd00033   1 CPPPPVPENGTVTGSkgsysygstVTYSCNEGYTLV--GSSTITCTENGGWSP-----PPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
92-146 4.75e-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: 35.13  E-value: 4.75e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826762   92 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNNEKQWINkavgdKLPECE 146
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 ...
162-402 2.31e-62

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: 2.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  162 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 240
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  241 NYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGRNA-NFKFTDHLKYVMLPVADQDQCIRHYE 314
Cdd:cd00190  81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  315 GstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleEDTWYATGILSFDKSCAVAEY-GVYVKVT 393
Cdd:cd00190 161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                ....*....
gi 4826762  394 SIQDWVQKT 402
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
161-399 8.72e-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: 188.66  E-value: 8.72e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762     161 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 231
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762     232 EIEKVVLHPNYSQV----DIGLIKLKQKVSVNERVMPICLPSKDY-AEVGRVGYVSGWGR--NANFKFTDHLKYVMLPVA 304
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRtsEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762     305 DQDQCIRHYEGstvpekktpkspvgvQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDleeDTWYATGILSFDKSCAVA 384
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 4826762     385 EY-GVYVKVTSIQDWV 399
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
162-399 1.99e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 171.86  E-value: 1.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762    162 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 240
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762    241 NYSQV----DIGLIKLKQKVSVNERVMPICLPSK-DYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEG 315
Cdd:pfam00089  79 NYNPDtldnDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762    316 StvpekktpkspvgvqpiLNEHTFCAGMskYQEDTCYGDAGSAFAVHDLeedtwYATGILSFDKSCAVAEY-GVYVKVTS 394
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 4826762    395 IQDWV 399
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
155-406 1.67e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 117.83  E-value: 1.67e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  155 PANPVQRILGGHLDAKGSFPWQAKMVS---HHNLTTGATLINEQWLLTTAknlflnHsenATAKDIAPTLTLYVG----- 226
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAA------H---CVDGDGPSDLRVVIGstdls 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  227 --KKQLVEIEKVVLHPNYSQV----DIGLIKLKQKVSvneRVMPICLP-SKDYAEVGRVGYVSGWGRNANF--KFTDHLK 297
Cdd:COG5640  95 tsGGTVVKVARIVVHPDYDPAtpgnDIALLKLATPVP---GVAPAPLAtSADAAAPGTPATVAGWGRTSEGpgSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826762  298 YVMLPVADQDQCiRHYEGstvpekktpkspvgvqpILNEHTFCAGMSKYQEDTCYGDAGS-AFAVHDleeDTWYATGILS 376
Cdd:COG5640 172 KADVPVVSDATC-AAYGG-----------------FDGGTMLCAGYPEGGKDACQGDSGGpLVVKDG---GGWVLVGVVS 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 4826762  377 F-DKSCAVAEYGVYVKVTSIQDWVQKTIAEN 406
Cdd:COG5640 231 WgGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
33-87 2.71e-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: 2.71e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826762   33 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNDKKQWINkavgdKLPECE 87
Cdd:cd00033   1 CPPPPVPENGTVTGSkgsysygstVTYSCNEGYTLV--GSSTITCTENGGWSP-----PPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
92-146 4.75e-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: 35.13  E-value: 4.75e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826762   92 CPKPPEIAHGYVEHS---------VRYQCKNYYKLRteGDGVYTLNNEKQWINkavgdKLPECE 146
Cdd:cd00033   1 CPPPPVPENGTVTGSkgsysygstVTYSCNEGYTLV--GSSTITCTENGGWSP-----PPPTCE 57
 
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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