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Conserved domains on  [gi|585398|sp|P28175|]
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RecName: Full=Clotting factor C; Short=FC; AltName: Full=Limulus factor C; Contains: RecName: Full=Clotting factor C heavy chain; Contains: RecName: Full=Clotting factor C light chain; Contains: RecName: Full=Clotting factor C chain A; Contains: RecName: Full=Clotting factor C chain B; Flags: Precursor

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 ...
 763-1017 2.60e-80

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: 261.06  E-value: 2.60e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    763 IWNGNSTEIGQWPWQAGISRwladhNMWFLQCGGSLLNEKWIVTAAHCVTYSAtaeiidPSQFKIYLGKYYRDDSRDDDy 842
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY-----TGGRHFCGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSNEGGG- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    843 vQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPtdiTTREHLKEGTLAVVTGWGLNENN-TYSEMIQQ 921
Cdd:cd00190   69 -QVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP---SSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    922 AVLPVVAASTCEEGYKEADlplTVTENMFCAGYKKGRYDACSGDSGGPLVFADDsrteRRWVLEGIVSWGspSGCGKANQ 1001
Cdd:cd00190  145 VNVPIVSNAECKRAYSYGG---TITDNMLCAGGLEGGKDACQGDSGGPLVCNDN----GRGVLVGIVSWG--SGCARPNY 215

                        250
                 ....*....|....*.
gi 585398   1002 YGGFTKVNVFLSWIRQ 1017
Cdd:cd00190  216 PGVYTRVSSYLDWIQK 231
LCCL smart00603
LCCL domain;
327-412 8.08e-37

LCCL domain;


:

Pssm-ID: 128866  Cd Length: 85  Bit Score: 133.29  E-value: 8.08e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       327 REVDCDSKAVDFLDDVGEPvRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSDL 406
Cdd:smart00603    1 QAVTCDTRGLDLCKPVTDN-RVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDA 79


                    ....*.
gi 585398       407 NGIKSE 412
Cdd:smart00603   80 NGIQSE 85
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 436-564 3.88e-18

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 81.49  E-value: 3.88e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGLTTT-WIGLHRLDAEKPFVWelMD 514
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYyWIGLSDPDSNGSWQW--SD 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 585398       515 RSNVVlndNLTFWASGEPGNET-NCVYLDIRDQLqpvWKTKSCFQPSSFAC 564
Cdd:smart00034   79 GSGPV---SYSNWAPGEPNNSSgDCVVLSTSGGK---WNDVSCTSKLPFVC 123
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 199-255 1.72e-12

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: 62.87  E-value: 1.72e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 585398    199 CAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQCK 255
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 163-321 1.88e-11

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 65.83  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     163 TIDYSCSPGFKLKGVARI--SCLPNGqWSSFPPKCIRECAKVSSPEHGKVNApsGNMIEGATLRFSCDSPYYLIGQETLT 240
Cdd:PHA02927   49 TIEYLCLPGYRKQKMGPIyaKCTGTG-WTLFNQCIKRRCPSPRDIDNGQLDI--GGVDFGSSITYSCNSGYQLIGESKSY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     241 CQ----GNGQWSGQIPQCKKlVFCPDLDPVNHAEHQvkiGVEQKYgqfPQGTEVTYTCSGNYFLMGFNTLKCNpDGSWSg 316
Cdd:PHA02927  126 CElgstGSMVWNPEAPICES-VKCQSPPSISNGRHN---GYEDFY---TDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS- 196


                  ....*
gi 585398     317 SQPSC 321
Cdd:PHA02927  197 DPPTC 201
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 576-635 6.98e-11

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: 58.63  E-value: 6.98e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    576 CDDPGPLENGHATLhgqSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRCI 635
Cdd:cd00033    1 CPPPPVPENGTVTG---SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 702-749 4.18e-06

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: 44.76  E-value: 4.18e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 585398    702 KVKLPEGHYRVGSRAIYTCESrYYELLGSQGRRCDSNGNWSGRPASCI 749
Cdd:cd00033   11 TVTGSKGSYSYGSTVTYSCNE-GYTLVGSSTITCTENGGWSPPPPTCE 57
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 112-136 1.22e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


:

Pssm-ID: 400365  Cd Length: 26  Bit Score: 36.94  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|....*
gi 585398      112 CKNGGICDQRTGACTCRDRYEGAHC 136
Cdd:pfam07974    2 CSGRGTCVNQCGKCVCDSGYQGATC 26
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 763-1017 2.60e-80

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: 261.06  E-value: 2.60e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    763 IWNGNSTEIGQWPWQAGISRwladhNMWFLQCGGSLLNEKWIVTAAHCVTYSAtaeiidPSQFKIYLGKYYRDDSRDDDy 842
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY-----TGGRHFCGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSNEGGG- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    843 vQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPtdiTTREHLKEGTLAVVTGWGLNENN-TYSEMIQQ 921
Cdd:cd00190   69 -QVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP---SSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    922 AVLPVVAASTCEEGYKEADlplTVTENMFCAGYKKGRYDACSGDSGGPLVFADDsrteRRWVLEGIVSWGspSGCGKANQ 1001
Cdd:cd00190  145 VNVPIVSNAECKRAYSYGG---TITDNMLCAGGLEGGKDACQGDSGGPLVCNDN----GRGVLVGIVSWG--SGCARPNY 215

                        250
                 ....*....|....*.
gi 585398   1002 YGGFTKVNVFLSWIRQ 1017
Cdd:cd00190  216 PGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 763-1015 1.03e-77

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: 253.75  E-value: 1.03e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       763 IWNGNSTEIGQWPWQAGISRWLADHnmwflQCGGSLLNEKWIVTAAHCVTYSataeiiDPSQFKIYLGKYYRDDSRDDdy 842
Cdd:smart00020    2 IVGGSEANIGSFPWQVSLQYGGGRH-----FCGGSLISPRWVLTAAHCVRGS------DPSNIRVRLGSHDLSSGEEG-- 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       843 vQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPtdiTTREHLKEGTLAVVTGWGLNENN--TYSEMIQ 920
Cdd:smart00020   69 -QVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLP---SSNYNVPAGTTCTVSGWGRTSEGagSLPDTLQ 144

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       921 QAVLPVVAASTCEEGYKEadlPLTVTENMFCAGYKKGRYDACSGDSGGPLVFADdsrteRRWVLEGIVSWGspSGCGKAN 1000
Cdd:smart00020  145 EVNVPIVSNATCRRAYSG---GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND-----GRWVLVGIVSWG--SGCARPG 214

                           250
                    ....*....|....*
gi 585398      1001 QYGGFTKVNVFLSWI 1015
Cdd:smart00020  215 KPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
763-1015 6.76e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 201.52  E-value: 6.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      763 IWNGNSTEIGQWPWQAGISRwlaDHNMWFlqCGGSLLNEKWIVTAAHCVTysataeiiDPSQFKIYLGKYYRDDSRDDdy 842
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQL---SSGKHF--CGGSLISENWVLTAAHCVS--------GASDVKVVLGAHNIVLREGG-- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      843 VQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPtdiTTREHLKEGTLAVVTGWGLNENNTYSEMIQQA 922
Cdd:pfam00089   66 EQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLP---DASSDLPVGTTCTVSGWGNTKTLGPSDTLQEV 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      923 VLPVVAASTCEEGYkeadlPLTVTENMFCAGYkkGRYDACSGDSGGPLVFADDsrterrwVLEGIVSWGspSGCGKANQY 1002
Cdd:pfam00089  143 TVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-------ELIGIVSWG--YGCASGNYP 206

                          250
                   ....*....|...
gi 585398     1003 GGFTKVNVFLSWI 1015
Cdd:pfam00089  207 GVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 746-1017 6.23e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 200.26  E-value: 6.23e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    746 ASCIPVCGRSDSPRSPFIWNGNSTEIGQWPWQAGISRWLADHNMWflqCGGSLLNEKWIVTAAHCVtysataEIIDPSQF 825
Cdd:COG5640   14 ALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCV------DGDGPSDL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    826 KIYLGKYYRDDSRDddyvQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTlttRVQPICLPTditTREHLKEGTLAVVT 905
Cdd:COG5640   85 RVVIGSTDLSTSGG----TVVKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLAT---SADAAAPGTPATVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    906 GWGLNENN--TYSEMIQQAVLPVVAASTCeegykeADLPLTVTENMFCAGYKKGRYDACSGDSGGPLVFADDSrterRWV 983
Cdd:COG5640  155 GWGRTSEGpgSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGG----GWV 224

                        250       260       270
                 ....*....|....*....|....*....|....
gi 585398    984 LEGIVSWGSpSGCGkANQYGGFTKVNVFLSWIRQ 1017
Cdd:COG5640  225 LVGVVSWGG-GPCA-AGYPGVYTRVSAYRDWIKS 256
LCCL smart00603
LCCL domain;
327-412 8.08e-37

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 133.29  E-value: 8.08e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       327 REVDCDSKAVDFLDDVGEPvRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSDL 406
Cdd:smart00603    1 QAVTCDTRGLDLCKPVTDN-RVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDA 79


                    ....*.
gi 585398       407 NGIKSE 412
Cdd:smart00603   80 NGIQSE 85
LCCL pfam03815
LCCL domain;
329-421 1.65e-23

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 95.81  E-value: 1.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      329 VDCDSKAVD---FLDDVGEPVRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSD 405
Cdd:pfam03815    1 LSCSTTLLDicnFCPFTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                           90
                   ....*....|....*.
gi 585398      406 LNGIKSEELKSLARSF 421
Cdd:pfam03815   81 QNGIESLSLSSWSKSF 96
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 436-564 3.88e-18

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 81.49  E-value: 3.88e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGLTTT-WIGLHRLDAEKPFVWelMD 514
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYyWIGLSDPDSNGSWQW--SD 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 585398       515 RSNVVlndNLTFWASGEPGNET-NCVYLDIRDQLqpvWKTKSCFQPSSFAC 564
Cdd:smart00034   79 GSGPV---SYSNWAPGEPNNSSgDCVVLSTSGGK---WNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 446-566 6.19e-14

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 69.19  E-value: 6.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    446 NCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGLTTTWIGLHRLDAEKPFVWelMDRSNVVlndNLT 525
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKW--SDGSPLV---DYT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 585398    526 FWASGEP--GNETNCVYLDIRDQLQpvWKTKSCFQPSSFACMM 566
Cdd:cd00037   76 NWAPGEPnpGGSEDCVVLSSSSDGK--WNDVSCSSKLPFICEK 116
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 199-255 1.72e-12

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: 62.87  E-value: 1.72e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 585398    199 CAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQCK 255
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 199-254 2.09e-12

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: 62.93  E-value: 2.09e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 585398       199 CAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQC 254
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 163-321 1.88e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 65.83  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     163 TIDYSCSPGFKLKGVARI--SCLPNGqWSSFPPKCIRECAKVSSPEHGKVNApsGNMIEGATLRFSCDSPYYLIGQETLT 240
Cdd:PHA02927   49 TIEYLCLPGYRKQKMGPIyaKCTGTG-WTLFNQCIKRRCPSPRDIDNGQLDI--GGVDFGSSITYSCNSGYQLIGESKSY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     241 CQ----GNGQWSGQIPQCKKlVFCPDLDPVNHAEHQvkiGVEQKYgqfPQGTEVTYTCSGNYFLMGFNTLKCNpDGSWSg 316
Cdd:PHA02927  126 CElgstGSMVWNPEAPICES-VKCQSPPSISNGRHN---GYEDFY---TDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS- 196


                  ....*
gi 585398     317 SQPSC 321
Cdd:PHA02927  197 DPPTC 201
Sushi pfam00084
Sushi repeat (SCR repeat);
199-254 6.07e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 58.66  E-value: 6.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 585398      199 CAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQC 254
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 576-635 6.98e-11

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: 58.63  E-value: 6.98e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    576 CDDPGPLENGHATLhgqSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRCI 635
Cdd:cd00033    1 CPPPPVPENGTVTG---SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 576-634 1.80e-10

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: 57.15  E-value: 1.80e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 585398       576 CDDPGPLENGHATLHGqsiDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRC 634
Cdd:smart00032    1 CPPPPDIENGTVTSSS---GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
576-634 1.34e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.81  E-value: 1.34e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 585398      576 CDDPGPLENGHATlhgQSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRC 634
Cdd:pfam00084    1 CPPPPDIPNGKVS---ATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 260-321 3.13e-09

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: 53.68  E-value: 3.13e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585398       260 CPDLDPVNHAEhqvkigVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSC 321
Cdd:smart00032    1 CPPPPDIENGT------VTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 260-322 3.78e-09

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: 53.62  E-value: 3.78e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585398    260 CPDLDPVNHAEhqvkigVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSCV 322
Cdd:cd00033    1 CPPPPVPENGT------VTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 454-566 6.63e-09

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 54.41  E-value: 6.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      454 QRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGlTTTWIGLHRLDAEKPFVWElmdRSNVVLNDNLTFWASGEPG 533
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTWKWV---DGSPVNYTNWAPEPNNNGE 76

                           90       100       110
                   ....*....|....*....|....*....|...
gi 585398      534 NEtNCVYLDIRDQLqpvWKTKSCFQPSSFACMM 566
Cdd:pfam00059   77 NE-DCVELSSSSGK---WNDENCNSKNPFVCEK 105
Sushi pfam00084
Sushi repeat (SCR repeat);
260-321 1.43e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 1.43e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585398      260 CPDLDPVNHAEhqvkigVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSC 321
Cdd:pfam00084    1 CPPPPDIPNGK------VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 702-749 4.18e-06

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: 44.76  E-value: 4.18e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 585398    702 KVKLPEGHYRVGSRAIYTCESrYYELLGSQGRRCDSNGNWSGRPASCI 749
Cdd:cd00033   11 TVTGSKGSYSYGSTVTYSCNE-GYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 702-748 6.46e-05

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: 41.36  E-value: 6.46e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 585398       702 KVKLPEGHYRVGSRAIYTCESRYYeLLGSQGRRCDSNGNWSGRPASC 748
Cdd:smart00032   11 TVTSSSGTYSYGDTVTYSCDPGYT-LIGSSTITCLENGTWSPPPPTC 56
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 436-544 6.51e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.49  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDlipSSLTETLRGKGLTTTWIGLHRLDAEKPFVWelmdr 515
Cdd:PHA02642   88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETE---EELNFLKRYKDSSDHWIGLNRESSNHPWKW----- 159

                          90       100       110
                  ....*....|....*....|....*....|
gi 585398     516 snvvlNDNLTFWASGEPGNETNCVYL-DIR 544
Cdd:PHA02642  160 -----ADNSNYNASFVITGTGECAYLnDIR 184
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 573-752 8.06e-04

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 42.33  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     573 KAKCDDPGPLENGHAtlhgqSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGT----WSAPKPRCiKVITCQNPPVPSY 648
Cdd:PHA02927   83 KRRCPSPRDIDNGQL-----DIGGVDFGSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPEAPIC-ESVKCQSPPSISN 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     649 GsveikppsRTNSIsrvgspflrlprlplplaraakpppkprssqpstvdlaskvklpEGHYRVGSRAIYTCESRyYELL 728
Cdd:PHA02927  157 G--------RHNGY--------------------------------------------EDFYTDGSVVTYSCNSG-YSLI 183

                         170       180
                  ....*....|....*....|....
gi 585398     729 GSQGRRCdSNGNWSGRPASCIPVC 752
Cdd:PHA02927  184 GNSGVLC-SGGEWSDPPTCQIVKC 206
PHA02639 PHA02639
EEV host range protein; Provisional
 543-643 9.76e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 42.34  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     543 IRDQLQPVWKTKSCFqpssfaCMMDlsdrnkaKCDDPGPLENGHATlhgQSIDGFYAGSSIRYSCE----VLHYLSGTET 618
Cdd:PHA02639   65 IKDKNNAIWSNKAPF------CMLK-------ECNDPPSIINGKIY---NKREMYKVGDEIYYVCNehkgVQYSLVGNEK 128

                          90       100
                  ....*....|....*....|....*
gi 585398     619 VTCTTNGTWSAPKPRCiKVITCQNP 643
Cdd:PHA02639  129 ITCIQDKSWKPDPPIC-KMINCRFP 152
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 112-136 1.22e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 36.94  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|....*
gi 585398      112 CKNGGICDQRTGACTCRDRYEGAHC 136
Cdd:pfam07974    2 CSGRGTCVNQCGKCVCDSGYQGATC 26
Sushi pfam00084
Sushi repeat (SCR repeat);
702-748 3.80e-03

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 36.71  E-value: 3.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 585398      702 KVKLPEGHYRVGSRAIYTCESRYYeLLGSQGRRCDSNGNWSGRPASC 748
Cdd:pfam00084   11 KVSATKNEYNYGASVSYECDPGYR-LVGSPTITCQEDGTWSPPFPEC 56
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 110-137 4.86e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 36.18  E-value: 4.86e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 585398    110 CQCKNGG----ICDQRTGACTCRDRYEGAHCE 137
Cdd:cd00055    2 CDCNGHGslsgQCDPGTGQCECKPNTTGRRCD 33
PHA02817 PHA02817
EEV Host range protein; Provisional
 172-256 6.42e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 39.54  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     172 FKLKGVARISCLPNGQWSSFPPKCIRECAKVSSPEHGKVNA--PSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSG 249
Cdd:PHA02817   61 YTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNGFVNGipDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIP 140


                  ....*..
gi 585398     250 QIPQCKK 256
Cdd:PHA02817  141 KVPICSR 147
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 763-1017 2.60e-80

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: 261.06  E-value: 2.60e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    763 IWNGNSTEIGQWPWQAGISRwladhNMWFLQCGGSLLNEKWIVTAAHCVTYSAtaeiidPSQFKIYLGKYYRDDSRDDDy 842
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY-----TGGRHFCGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSNEGGG- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    843 vQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPtdiTTREHLKEGTLAVVTGWGLNENN-TYSEMIQQ 921
Cdd:cd00190   69 -QVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP---SSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    922 AVLPVVAASTCEEGYKEADlplTVTENMFCAGYKKGRYDACSGDSGGPLVFADDsrteRRWVLEGIVSWGspSGCGKANQ 1001
Cdd:cd00190  145 VNVPIVSNAECKRAYSYGG---TITDNMLCAGGLEGGKDACQGDSGGPLVCNDN----GRGVLVGIVSWG--SGCARPNY 215

                        250
                 ....*....|....*.
gi 585398   1002 YGGFTKVNVFLSWIRQ 1017
Cdd:cd00190  216 PGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 763-1015 1.03e-77

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: 253.75  E-value: 1.03e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       763 IWNGNSTEIGQWPWQAGISRWLADHnmwflQCGGSLLNEKWIVTAAHCVTYSataeiiDPSQFKIYLGKYYRDDSRDDdy 842
Cdd:smart00020    2 IVGGSEANIGSFPWQVSLQYGGGRH-----FCGGSLISPRWVLTAAHCVRGS------DPSNIRVRLGSHDLSSGEEG-- 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       843 vQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPtdiTTREHLKEGTLAVVTGWGLNENN--TYSEMIQ 920
Cdd:smart00020   69 -QVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLP---SSNYNVPAGTTCTVSGWGRTSEGagSLPDTLQ 144

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       921 QAVLPVVAASTCEEGYKEadlPLTVTENMFCAGYKKGRYDACSGDSGGPLVFADdsrteRRWVLEGIVSWGspSGCGKAN 1000
Cdd:smart00020  145 EVNVPIVSNATCRRAYSG---GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND-----GRWVLVGIVSWG--SGCARPG 214

                           250
                    ....*....|....*
gi 585398      1001 QYGGFTKVNVFLSWI 1015
Cdd:smart00020  215 KPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
763-1015 6.76e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 201.52  E-value: 6.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      763 IWNGNSTEIGQWPWQAGISRwlaDHNMWFlqCGGSLLNEKWIVTAAHCVTysataeiiDPSQFKIYLGKYYRDDSRDDdy 842
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQL---SSGKHF--CGGSLISENWVLTAAHCVS--------GASDVKVVLGAHNIVLREGG-- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      843 VQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPtdiTTREHLKEGTLAVVTGWGLNENNTYSEMIQQA 922
Cdd:pfam00089   66 EQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLP---DASSDLPVGTTCTVSGWGNTKTLGPSDTLQEV 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      923 VLPVVAASTCEEGYkeadlPLTVTENMFCAGYkkGRYDACSGDSGGPLVFADDsrterrwVLEGIVSWGspSGCGKANQY 1002
Cdd:pfam00089  143 TVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-------ELIGIVSWG--YGCASGNYP 206

                          250
                   ....*....|...
gi 585398     1003 GGFTKVNVFLSWI 1015
Cdd:pfam00089  207 GVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 746-1017 6.23e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 200.26  E-value: 6.23e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    746 ASCIPVCGRSDSPRSPFIWNGNSTEIGQWPWQAGISRWLADHNMWflqCGGSLLNEKWIVTAAHCVtysataEIIDPSQF 825
Cdd:COG5640   14 ALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCV------DGDGPSDL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    826 KIYLGKYYRDDSRDddyvQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTlttRVQPICLPTditTREHLKEGTLAVVT 905
Cdd:COG5640   85 RVVIGSTDLSTSGG----TVVKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLAT---SADAAAPGTPATVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    906 GWGLNENN--TYSEMIQQAVLPVVAASTCeegykeADLPLTVTENMFCAGYKKGRYDACSGDSGGPLVFADDSrterRWV 983
Cdd:COG5640  155 GWGRTSEGpgSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGG----GWV 224

                        250       260       270
                 ....*....|....*....|....*....|....
gi 585398    984 LEGIVSWGSpSGCGkANQYGGFTKVNVFLSWIRQ 1017
Cdd:COG5640  225 LVGVVSWGG-GPCA-AGYPGVYTRVSAYRDWIKS 256
LCCL smart00603
LCCL domain;
327-412 8.08e-37

LCCL domain;


Pssm-ID: 128866  Cd Length: 85  Bit Score: 133.29  E-value: 8.08e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       327 REVDCDSKAVDFLDDVGEPvRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSDL 406
Cdd:smart00603    1 QAVTCDTRGLDLCKPVTDN-RVLCPAGCLLEKAKVFGTIVYASLSSICRAAVHAGVISNSGGAVDVVRVGGRENYISSDA 79


                    ....*.
gi 585398       407 NGIKSE 412
Cdd:smart00603   80 NGIQSE 85
LCCL pfam03815
LCCL domain;
329-421 1.65e-23

LCCL domain;


Pssm-ID: 427521  Cd Length: 96  Bit Score: 95.81  E-value: 1.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      329 VDCDSKAVD---FLDDVGEPVRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSD 405
Cdd:pfam03815    1 LSCSTTLLDicnFCPFTGTCFLVRCPANCADEKASVYGTDVYSSDSSICKAAIHAGVIDNSGGLVVVRIVGGQNEYTGST 80

                           90
                   ....*....|....*.
gi 585398      406 LNGIKSEELKSLARSF 421
Cdd:pfam03815   81 QNGIESLSLSSWSKSF 96
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 436-564 3.88e-18

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 81.49  E-value: 3.88e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398       436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGLTTT-WIGLHRLDAEKPFVWelMD 514
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYyWIGLSDPDSNGSWQW--SD 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 585398       515 RSNVVlndNLTFWASGEPGNET-NCVYLDIRDQLqpvWKTKSCFQPSSFAC 564
Cdd:smart00034   79 GSGPV---SYSNWAPGEPNNSSgDCVVLSTSGGK---WNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 446-566 6.19e-14

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 69.19  E-value: 6.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    446 NCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGLTTTWIGLHRLDAEKPFVWelMDRSNVVlndNLT 525
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKW--SDGSPLV---DYT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 585398    526 FWASGEP--GNETNCVYLDIRDQLQpvWKTKSCFQPSSFACMM 566
Cdd:cd00037   76 NWAPGEPnpGGSEDCVVLSSSSDGK--WNDVSCSSKLPFICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 436-566 9.07e-13

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 66.17  E-value: 9.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGltTTWIGLHRLDAEKPFVWelMDr 515
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNR--SYWIGLSDEETEGEWKW--VD- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 585398    516 sNVVLNDNLTFWASGEP----GNETNCVYLDIRDQLqpvWKTKSCFQPSSFACMM 566
Cdd:cd03590   76 -GTPLNSSKTFWHPGEPnnwgGGGEDCAELVYDSGG---WNDVPCNLEYRWICEK 126
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 199-255 1.72e-12

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: 62.87  E-value: 1.72e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 585398    199 CAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQCK 255
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 199-254 2.09e-12

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: 62.93  E-value: 2.09e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 585398       199 CAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQC 254
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 163-321 1.88e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 65.83  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     163 TIDYSCSPGFKLKGVARI--SCLPNGqWSSFPPKCIRECAKVSSPEHGKVNApsGNMIEGATLRFSCDSPYYLIGQETLT 240
Cdd:PHA02927   49 TIEYLCLPGYRKQKMGPIyaKCTGTG-WTLFNQCIKRRCPSPRDIDNGQLDI--GGVDFGSSITYSCNSGYQLIGESKSY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     241 CQ----GNGQWSGQIPQCKKlVFCPDLDPVNHAEHQvkiGVEQKYgqfPQGTEVTYTCSGNYFLMGFNTLKCNpDGSWSg 316
Cdd:PHA02927  126 CElgstGSMVWNPEAPICES-VKCQSPPSISNGRHN---GYEDFY---TDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS- 196


                  ....*
gi 585398     317 SQPSC 321
Cdd:PHA02927  197 DPPTC 201
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 163-323 2.06e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 65.44  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     163 TIDYSCSPGFKLKGVARISCLPNGQ----WSSFPPKCirECAKVSSP---EHGKVNAPSGNMIEGATLRFSCDSPYYLIG 235
Cdd:PHA02927  107 SITYSCNSGYQLIGESKSYCELGSTgsmvWNPEAPIC--ESVKCQSPpsiSNGRHNGYEDFYTDGSVVTYSCNSGYSLIG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     236 QETLTCQGnGQWSGQiPQCKkLVFCPDLDPVNHaehQVKIGVEQKYGQfpqGTEVTYTCSGNYFLMGFNTLKCNPDGSWS 315
Cdd:PHA02927  185 NSGVLCSG-GEWSDP-PTCQ-IVKCPHPTISNG---YLSSGFKRSYSY---NDNVDFKCKYGYKLSGSSSSTCSPGNTWQ 255


                  ....*...
gi 585398     316 GSQPSCVK 323
Cdd:PHA02927  256 PELPKCVR 263
Sushi pfam00084
Sushi repeat (SCR repeat);
199-254 6.07e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 58.66  E-value: 6.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 585398      199 CAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQC 254
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 576-635 6.98e-11

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: 58.63  E-value: 6.98e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    576 CDDPGPLENGHATLhgqSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRCI 635
Cdd:cd00033    1 CPPPPVPENGTVTG---SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 576-634 1.80e-10

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: 57.15  E-value: 1.80e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 585398       576 CDDPGPLENGHATLHGqsiDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRC 634
Cdd:smart00032    1 CPPPPDIENGTVTSSS---GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
576-634 1.34e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.81  E-value: 1.34e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 585398      576 CDDPGPLENGHATlhgQSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRC 634
Cdd:pfam00084    1 CPPPPDIPNGKVS---ATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 260-321 3.13e-09

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: 53.68  E-value: 3.13e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585398       260 CPDLDPVNHAEhqvkigVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSC 321
Cdd:smart00032    1 CPPPPDIENGT------VTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 260-322 3.78e-09

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: 53.62  E-value: 3.78e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585398    260 CPDLDPVNHAEhqvkigVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSCV 322
Cdd:cd00033    1 CPPPPVPENGT------VTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 142-196 5.48e-09

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: 53.24  E-value: 5.48e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 585398    142 CPLLPSDS--QVQEVRNPPDNPQTIDYSCSPGFKLKGVARISCLPNGQWSSFPPKCI 196
Cdd:cd00033    1 CPPPPVPEngTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 454-566 6.63e-09

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 54.41  E-value: 6.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398      454 QRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGlTTTWIGLHRLDAEKPFVWElmdRSNVVLNDNLTFWASGEPG 533
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTWKWV---DGSPVNYTNWAPEPNNNGE 76

                           90       100       110
                   ....*....|....*....|....*....|...
gi 585398      534 NEtNCVYLDIRDQLqpvWKTKSCFQPSSFACMM 566
Cdd:pfam00059   77 NE-DCVELSSSSGK---WNDENCNSKNPFVCEK 105
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 142-195 7.56e-08

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: 49.83  E-value: 7.56e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 585398       142 CPLLPS--DSQVQEVRNPPDNPQTIDYSCSPGFKLKGVARISCLPNGQWSSFPPKC 195
Cdd:smart00032    1 CPPPPDieNGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 162-323 1.16e-07

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 54.67  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     162 QTIDYSCSPGFKLKGVARISCLP---NGQWSSFPPKC-IRECAKVSSPEHGKVNAPSGNMIEGATLRFSCDS----PYYL 233
Cdd:PHA02639   44 KLIEYTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCmLKECNDPPSIINGKIYNKREMYKVGDEIYYVCNEhkgvQYSL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     234 IGQETLTCQGNGQWSGQIPQCKkLVFCPDldPVNHAEHQVKIGVEQKygqFPQGTEVTYTCSGNYFLMGFNTLKCNPDGS 313
Cdd:PHA02639  124 VGNEKITCIQDKSWKPDPPICK-MINCRF--PALQNGYINGIPSNKK---FYYKTRVGFSCKSGFDLVGEKYSTCNINAT 197

                         170
                  ....*....|
gi 585398     314 WSGSQPSCVK 323
Cdd:PHA02639  198 WFPSIPTCVR 207
Sushi pfam00084
Sushi repeat (SCR repeat);
260-321 1.43e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 1.43e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585398      260 CPDLDPVNHAEhqvkigVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSC 321
Cdd:pfam00084    1 CPPPPDIPNGK------VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 436-541 4.04e-07

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 49.64  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDK----DLIPSSLTETLRgkgltttWIGLHRLDAEKPFVWE 511
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDeeelEFLQSQIGSSSY-------WIGLSREKSEKPWKWI 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 585398    512 lmDRSnvVLNDNLTFwaSGEPGNEtNCVYL 541
Cdd:cd03593   74 --DGS--PLNNLFNI--RGSTKSG-NCAYL 96
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 794-994 5.18e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.22  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    794 CGGSLLNEKWIVTAAHCVTYSATAEIidPSQFKIYLGKYYRDDSRDDdyvqvreALEIHVNPNYDP-GNLNFDIALIQLK 872
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAGGGW--ATNIVFVPGYNGGPYGTAT-------ATRFRVPPGWVAsGDAGYDYALLRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    873 TPVTLTTRVQPICLPTDITTrehlkeGTLAVVTGWGLNENNTYSemiQQAVLPVVAastceegykeadlpltVTENMFca 952
Cdd:COG3591   85 EPLGDTTGWLGLAFNDAPLA------GEPVTIIGYPGDRPKDLS---LDCSGRVTG----------------VQGNRL-- 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 585398    953 gykkgRY--DACSGDSGGPlVFADDSrteRRWVLEGIVSWGSPS 994
Cdd:COG3591  138 -----SYdcDTTGGSSGSP-VLDDSD---GGGRVVGVHSAGGAD 172
Sushi pfam00084
Sushi repeat (SCR repeat);
163-195 3.11e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 45.18  E-value: 3.11e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 585398      163 TIDYSCSPGFKLKGVARISCLPNGQWSSFPPKC 195
Cdd:pfam00084   24 SVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 702-749 4.18e-06

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: 44.76  E-value: 4.18e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 585398    702 KVKLPEGHYRVGSRAIYTCESrYYELLGSQGRRCDSNGNWSGRPASCI 749
Cdd:cd00033   11 TVTGSKGSYSYGSTVTYSCNE-GYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02817 PHA02817
EEV Host range protein; Provisional
 220-323 4.11e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 46.09  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     220 GATLRFSCDS-----PYYLIGQETLTCQGNGQWSGQIPQCkKLVFC--PDLDP--VNHAEHQVKIGVEQkygqfpqgtEV 290
Cdd:PHA02817   45 GSNVTFFCGNntrgvRYTLVGEKNIICEKDGKWNKEFPVC-KIIRCrfPALQNgfVNGIPDSKKFYYES---------EV 114

                          90       100       110
                  ....*....|....*....|....*....|...
gi 585398     291 TYTCSGNYFLMGFNTLKCNPDGSWSGSQPSCVK 323
Cdd:PHA02817  115 SFSCKPGFVLIGTKYSVCGINSSWIPKVPICSR 147
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 702-748 6.46e-05

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: 41.36  E-value: 6.46e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 585398       702 KVKLPEGHYRVGSRAIYTCESRYYeLLGSQGRRCDSNGNWSGRPASC 748
Cdd:smart00032   11 TVTSSSGTYSYGDTVTYSCDPGYT-LIGSSTITCLENGTWSPPPPTC 56
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 436-544 6.51e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.49  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDlipSSLTETLRGKGLTTTWIGLHRLDAEKPFVWelmdr 515
Cdd:PHA02642   88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETE---EELNFLKRYKDSSDHWIGLNRESSNHPWKW----- 159

                          90       100       110
                  ....*....|....*....|....*....|
gi 585398     516 snvvlNDNLTFWASGEPGNETNCVYL-DIR 544
Cdd:PHA02642  160 -----ADNSNYNASFVITGTGECAYLnDIR 184
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 436-541 7.36e-05

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.


Pssm-ID: 153067  Cd Length: 129  Bit Score: 43.34  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    436 CPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDK----DLIPSSLTETLRGKGLTTTWIGLHRLDAEKpFVWE 511
Cdd:cd03597    1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTqkkvEFVLKELQKHQMTKQKLTPWVGLRKINVSY-WCWE 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 585398    512 LMDR-SNVVLNdnltfWASGEPGNETNCVYL 541
Cdd:cd03597   80 DMSPfTNTTLQ-----WLPGEPSDAGFCGYL 105
PHA02831 PHA02831
EEV host range protein; Provisional
 153-341 8.36e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 45.37  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     153 EVRNPPDNpQTIDYSCSPGFKlkgVARISClPNGQWSSfPPKCI--RECAKVSSPEHGKVNAPSGNMIEGATLRFSCD-- 228
Cdd:PHA02831   36 ENKVYEEN-ENLEYKCNNNFD---KVFVTC-NNGSWST-KNMCIgkRNCKDPVTILNGYIKNKKDQYSFGDSVTYACKvn 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     229 --SPYYLIGQETLTCQgNGQWSGQIPQCKkLVFC--PDLdpvnhaEHQVKIGVEQKygqFPQGTEVTYTCSGNYFLMGFN 304
Cdd:PHA02831  110 klEKYSIVGNETVKCI-NKQWVPKYPVCK-LIRCkyPAL------QNGFLNVFEKK---FYYGDIVNFKCKKGFILLGSS 178

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 585398     305 TLKCNPDGSWSGSQPSCVKVADREVDCDSKAVDFLDD 341
Cdd:PHA02831  179 VSTCDINSIWYPGIPKCVKDKVHNEIQPNYLFDDLDE 215
PHA02639 PHA02639
EEV host range protein; Provisional
 220-321 2.64e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 44.27  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     220 GATLRFSCDSPYYLIGQETLTC---QGNGQWSGQIPQCKklvfcpdLDPVNHAEHQVKIGVEQKYGQFPQGTEVTYTCSG 296
Cdd:PHA02639   43 GKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCM-------LKECNDPPSIINGKIYNKREMYKVGDEIYYVCNE 115

                          90       100
                  ....*....|....*....|....*....
gi 585398     297 N----YFLMGFNTLKCNPDGSWSGSQPSC 321
Cdd:PHA02639  116 HkgvqYSLVGNEKITCIQDKSWKPDPPIC 144
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 457-565 2.78e-04

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 41.21  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    457 WERAQGVCTNMAARLAVLDKDLIPSSLTETLRGkGLTTTWIGLHRLdaekpfVWELMDRSNvvlnDNLTF--WASGEPGN 534
Cdd:cd03602   12 WSEAQQYCRENYTDLATVQNQEDNALLSNLSRV-SNSAAWIGLYRD------VDSWRWSDG----SESSFrnWNTFQPFG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 585398    535 ETNCVYLDIRdqlqPVWKTKSCFQPSSFACM 565
Cdd:cd03602   81 QGDCATMYSS----GRWYAALCSALKPFICY 107
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 482-566 5.27e-04

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 41.19  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    482 SLTETLRGKGLTT-TWIGLHRLDAEKPFVWElmDRSNVvlndNLTFWASGEP---GNETNCVYLDIRDQLQPVWKTKSCF 557
Cdd:cd03589   55 DLFESSRGPDTPYgLWIGLHDRTSEGPFEWT--DGSPV----DFTKWAGGQPdnyGGNEDCVQMWRRGDAGQSWNDMPCD 128


                 ....*....
gi 585398    558 QPSSFACMM 566
Cdd:cd03589  129 AVFPYICKM 137
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 573-752 8.06e-04

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 42.33  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     573 KAKCDDPGPLENGHAtlhgqSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGT----WSAPKPRCiKVITCQNPPVPSY 648
Cdd:PHA02927   83 KRRCPSPRDIDNGQL-----DIGGVDFGSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPEAPIC-ESVKCQSPPSISN 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     649 GsveikppsRTNSIsrvgspflrlprlplplaraakpppkprssqpstvdlaskvklpEGHYRVGSRAIYTCESRyYELL 728
Cdd:PHA02927  157 G--------RHNGY--------------------------------------------EDFYTDGSVVTYSCNSG-YSLI 183

                         170       180
                  ....*....|....*....|....
gi 585398     729 GSQGRRCdSNGNWSGRPASCIPVC 752
Cdd:PHA02927  184 GNSGVLC-SGGEWSDPPTCQIVKC 206
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 436-516 8.32e-04

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 40.43  E-value: 8.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398    436 CPDGWFEVEENCVYVTSKQRAWERAQGVC------TNMAARLAVLDKDLIPSSLTETLRGKGltTTWIGLHRLdaEKPFV 509
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkygpgAHLASIHSPAEAAAIASLISSYQKAYQ--PVWIGLHDP--QQSRG 76


                 ....*..
gi 585398    510 WELMDRS 516
Cdd:cd03594   77 WEWSDGS 83
PHA02639 PHA02639
EEV host range protein; Provisional
 543-643 9.76e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 42.34  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     543 IRDQLQPVWKTKSCFqpssfaCMMDlsdrnkaKCDDPGPLENGHATlhgQSIDGFYAGSSIRYSCE----VLHYLSGTET 618
Cdd:PHA02639   65 IKDKNNAIWSNKAPF------CMLK-------ECNDPPSIINGKIY---NKREMYKVGDEIYYVCNehkgVQYSLVGNEK 128

                          90       100
                  ....*....|....*....|....*
gi 585398     619 VTCTTNGTWSAPKPRCiKVITCQNP 643
Cdd:PHA02639  129 ITCIQDKSWKPDPPIC-KMINCRFP 152
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 112-136 1.22e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 36.94  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|....*
gi 585398      112 CKNGGICDQRTGACTCRDRYEGAHC 136
Cdd:pfam07974    2 CSGRGTCVNQCGKCVCDSGYQGATC 26
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 106-267 3.53e-03

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 40.84  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     106 CSGE-----CQCKNGGICDQRTGACTcrdryeGAHCEilkgcPLLPSDSQVQEVRNPPDNPQTIDYSCSPGFKLKGVARI 180
Cdd:PHA02954  101 CKDEtkyfrCEEKNGNTSWNDTVTCP------NAECQ-----PLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYI 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     181 SCLPNgQWSSFpPKCIRECaKVSSPEHGKVNAPSGNMieGATLRFSCDSPYYLIGQETLTCQgNGQWSGQIPQCKKLvfC 260
Cdd:PHA02954  170 SCTAN-SWNVI-PSCQQKC-DIPSLSNGLISGSTFSI--GGVIHLSCKSGFTLTGSPSSTCI-DGKWNPVLPICVRS--N 241


                  ....*..
gi 585398     261 PDLDPVN 267
Cdd:PHA02954  242 EEFDPVD 248
Sushi pfam00084
Sushi repeat (SCR repeat);
702-748 3.80e-03

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 36.71  E-value: 3.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 585398      702 KVKLPEGHYRVGSRAIYTCESRYYeLLGSQGRRCDSNGNWSGRPASC 748
Cdd:pfam00084   11 KVSATKNEYNYGASVSYECDPGYR-LVGSPTITCQEDGTWSPPFPEC 56
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 110-137 4.86e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 36.18  E-value: 4.86e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 585398    110 CQCKNGG----ICDQRTGACTCRDRYEGAHCE 137
Cdd:cd00055    2 CDCNGHGslsgQCDPGTGQCECKPNTTGRRCD 33
PHA02817 PHA02817
EEV Host range protein; Provisional
 172-256 6.42e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 39.54  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585398     172 FKLKGVARISCLPNGQWSSFPPKCIRECAKVSSPEHGKVNA--PSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSG 249
Cdd:PHA02817   61 YTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNGFVNGipDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIP 140


                  ....*..
gi 585398     250 QIPQCKK 256
Cdd:PHA02817  141 KVPICSR 147
 
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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