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Conserved domains on  [gi|442616393|ref|NP_001259562|]
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uncharacterized protein Dmel_CG9095, isoform C [Drosophila melanogaster]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 12867611)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sad1_UNC super family cl23730
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 94-242 2.21e-60

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


The actual alignment was detected with superfamily member smart00607:

Pssm-ID: 474037  Cd Length: 151  Bit Score: 202.40  E-value: 2.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393    94 LNVAAGKAPMQISTDGAGAP-----QKAIDGSTSAFFTPETCSLTKAERSPWWYVNLLEPYMVQLVRLDFGKSCCGNKPA 168
Cdd:smart00607   1 QENVAGRGPATQSTYGRGAPpglshASAAIDGNRASFTPEGSCSHTEKRSNPWWRVDLLQYMTIHSVTITNRGDCCGERI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616393   169 TIVVRVGNNRPDLGTNPICNRFTGLLEAGQPLFLPCNPPMPGAFVSVHLENStPNPLSICEAFVytDQALPIER 242
Cdd:smart00607  81 TGARILIGNSLENGGINNPNCSTGGLMAGGETKTFCCPPPMIGRYVTVYLPK-PNESLILCEVE--VNALFPER 151
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 256-375 3.73e-23

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: 95.74  E-value: 3.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393   256 SYNGKCYIFYNrQPLNFLDALSFCRSRGGTLISESNPALQGFIsWELWRrhRSDVSSQYWMGAVRDGSDrSSWKWVNGDE 335
Cdd:smart00034   7 SYGGKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFV-ASLLK--NSGSSDYYWIGLSDPDSN-GSWQWSDGSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 442616393   336 LTVSFWSHPG----GDEDCARFDGSKGwLWSDTNCNTLLNFICQ 375
Cdd:smart00034  82 PVSYSNWAPGepnnSSGDCVVLSTSGG-KWNDVSCTSKLPFVCE 124
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 368-557 1.77e-20

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 92.41  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 368 TLLNficQHQPKTCGRPEQPPNSTMvALNGFEVGAQIKYSCDANHLLVGPATRTClETGF-----YNEFPPVCKYIECGL 442
Cdd:PHA02927  76 TLFN---QCIKRRCPSPRDIDNGQL-DIGGVDFGSSITYSCNSGYQLIGESKSYC-ELGStgsmvWNPEAPICESVKCQS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 443 PASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDErWNGPPPrCEIVEC--DTLPGNYYSTiiNAPNGTYY 520
Cdd:PHA02927 151 PPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSGGE-WSDPPT-CQIVKCphPTISNGYLSS--GFKRSYSY 226

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 442616393 521 GSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRCIK 557
Cdd:PHA02927 227 NDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKCVR 263
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 37-93 3.17e-10

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: 56.70  E-value: 3.17e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442616393  37 CSFPGSPAHSSVVFSNANLTQGTVASYSCERGFELLGPARRVC-DKGQWVPEgIPFCV 93
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCtENGGWSPP-PPTCE 57
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 527-725 1.31e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  527 SCPPGYRMEGP-RVLTCLASGQWSSALPRCIKLEPSTQPTAASTIPVPSSVATPPPFRPkvVSSTTSRTPYRPAVSTASS 605
Cdd:PHA03247 2769 PAPPAAPAAGPpRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPTAPPPPPGPP 2846

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  606 GIGGSSTSTV---GTYPSLSPTQveingeseseeeiNVPPVPGTvreefPPRRTVRPVLIPKKPNST-PAALPPTTHQVP 681
Cdd:PHA03247 2847 PPSLPLGGSVapgGDVRRRPPSR-------------SPAAKPAA-----PARPPVRRLARPAVSRSTeSFALPPDQPERP 2908

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 442616393  682 PQPPS----TYAPTPPRSSRPSGAPNSAGEVETTTRNTQQIIANSHPQ 725
Cdd:PHA03247 2909 PQPQAppppQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
 
Name Accession Description Interval E-value
FTP smart00607
eel-Fucolectin Tachylectin-4 Pentaxrin-1 Domain;
94-242 2.21e-60

eel-Fucolectin Tachylectin-4 Pentaxrin-1 Domain;


Pssm-ID: 128870  Cd Length: 151  Bit Score: 202.40  E-value: 2.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393    94 LNVAAGKAPMQISTDGAGAP-----QKAIDGSTSAFFTPETCSLTKAERSPWWYVNLLEPYMVQLVRLDFGKSCCGNKPA 168
Cdd:smart00607   1 QENVAGRGPATQSTYGRGAPpglshASAAIDGNRASFTPEGSCSHTEKRSNPWWRVDLLQYMTIHSVTITNRGDCCGERI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616393   169 TIVVRVGNNRPDLGTNPICNRFTGLLEAGQPLFLPCNPPMPGAFVSVHLENStPNPLSICEAFVytDQALPIER 242
Cdd:smart00607  81 TGARILIGNSLENGGINNPNCSTGGLMAGGETKTFCCPPPMIGRYVTVYLPK-PNESLILCEVE--VNALFPER 151
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 256-375 3.73e-23

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: 95.74  E-value: 3.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393   256 SYNGKCYIFYNrQPLNFLDALSFCRSRGGTLISESNPALQGFIsWELWRrhRSDVSSQYWMGAVRDGSDrSSWKWVNGDE 335
Cdd:smart00034   7 SYGGKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFV-ASLLK--NSGSSDYYWIGLSDPDSN-GSWQWSDGSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 442616393   336 LTVSFWSHPG----GDEDCARFDGSKGwLWSDTNCNTLLNFICQ 375
Cdd:smart00034  82 PVSYSNWAPGepnnSSGDCVVLSTSGG-KWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 260-376 6.34e-23

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: 94.61  E-value: 6.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 260 KCYIFYNrQPLNFLDALSFCRSRGGTLISESNPALQGFIswelWRRHRSDVSSQYWMGAVRDGSDRSsWKWVNGDE-LTV 338
Cdd:cd00037    1 SCYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFL----ASLLKKSSSSDVWIGLNDLSSEGT-WKWSDGSPlVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 442616393 339 SFWS----HPGGDEDCARFDGSKGWLWSDTNCNTLLNFICQH 376
Cdd:cd00037   75 TNWApgepNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 368-557 1.77e-20

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 92.41  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 368 TLLNficQHQPKTCGRPEQPPNSTMvALNGFEVGAQIKYSCDANHLLVGPATRTClETGF-----YNEFPPVCKYIECGL 442
Cdd:PHA02927  76 TLFN---QCIKRRCPSPRDIDNGQL-DIGGVDFGSSITYSCNSGYQLIGESKSYC-ELGStgsmvWNPEAPICESVKCQS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 443 PASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDErWNGPPPrCEIVEC--DTLPGNYYSTiiNAPNGTYY 520
Cdd:PHA02927 151 PPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSGGE-WSDPPT-CQIVKCphPTISNGYLSS--GFKRSYSY 226

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 442616393 521 GSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRCIK 557
Cdd:PHA02927 227 NDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKCVR 263
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 269-376 1.49e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 75.98  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  269 PLNFLDALSFCRSRGGTLISESNPALQGFISWELWRRhrsdvSSQYWMGAVRDGSDrSSWKWVNGDELTVSFW----SHP 344
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS-----NKYFWIGLTDRKNE-GTWKWVDGSPVNYTNWapepNNN 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 442616393  345 GGDEDCARFdGSKGWLWSDTNCNTLLNFICQH 376
Cdd:pfam00059  75 GENEDCVEL-SSSSGKWNDENCNSKNPFVCEK 105
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 500-556 1.86e-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: 60.17  E-value: 1.86e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393 500 CDTLPGNYYSTIINAPNGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRCI 556
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 500-555 3.47e-11

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: 59.08  E-value: 3.47e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393   500 CDTLPGNYYSTIINAPNGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRC 555
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 37-93 3.17e-10

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: 56.70  E-value: 3.17e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442616393  37 CSFPGSPAHSSVVFSNANLTQGTVASYSCERGFELLGPARRVC-DKGQWVPEgIPFCV 93
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCtENGGWSPP-PPTCE 57
Sushi pfam00084
Sushi repeat (SCR repeat);
516-555 9.01e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.20  E-value: 9.01e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 442616393  516 NGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRC 555
Cdd:pfam00084  17 NEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 37-92 1.57e-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: 54.45  E-value: 1.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393    37 CSFPGSPAHSSVVFSNANLTQGTVASYSCERGFELLGPARRVCDK-GQWVPEgIPFC 92
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLEnGTWSPP-PPTC 56
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 106-229 4.61e-06

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 46.67  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  106 STDGAGAPQKAIDGSTSAFFTPETCSltkaeRSPWWYVNLLEPYMVQLVRLDFGKSCCGNKPATIVVRVGNNrpdlGTN- 184
Cdd:pfam00754   7 SYSGEGPAAAALDGDPNTAWSAWSGD-----DPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEYSLD----GENw 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 442616393  185 --PICNRFTGLLEAGQPLFLPCNPPMPGAFVSVHL--ENSTPNPLSICE 229
Cdd:pfam00754  78 ttVKDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPtsWNGGNGIALRAE 126
Sushi pfam00084
Sushi repeat (SCR repeat);
37-92 4.02e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 42.10  E-value: 4.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393   37 CSFPGSPAHSSVVFSNANLTQGTVASYSCERGFELLGPARRVCDK-GQWVPEgIPFC 92
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEdGTWSPP-FPEC 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
 527-725 1.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  527 SCPPGYRMEGP-RVLTCLASGQWSSALPRCIKLEPSTQPTAASTIPVPSSVATPPPFRPkvVSSTTSRTPYRPAVSTASS 605
Cdd:PHA03247 2769 PAPPAAPAAGPpRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPTAPPPPPGPP 2846

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  606 GIGGSSTSTV---GTYPSLSPTQveingeseseeeiNVPPVPGTvreefPPRRTVRPVLIPKKPNST-PAALPPTTHQVP 681
Cdd:PHA03247 2847 PPSLPLGGSVapgGDVRRRPPSR-------------SPAAKPAA-----PARPPVRRLARPAVSRSTeSFALPPDQPERP 2908

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 442616393  682 PQPPS----TYAPTPPRSSRPSGAPNSAGEVETTTRNTQQIIANSHPQ 725
Cdd:PHA03247 2909 PQPQAppppQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
 
Name Accession Description Interval E-value
FTP smart00607
eel-Fucolectin Tachylectin-4 Pentaxrin-1 Domain;
94-242 2.21e-60

eel-Fucolectin Tachylectin-4 Pentaxrin-1 Domain;


Pssm-ID: 128870  Cd Length: 151  Bit Score: 202.40  E-value: 2.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393    94 LNVAAGKAPMQISTDGAGAP-----QKAIDGSTSAFFTPETCSLTKAERSPWWYVNLLEPYMVQLVRLDFGKSCCGNKPA 168
Cdd:smart00607   1 QENVAGRGPATQSTYGRGAPpglshASAAIDGNRASFTPEGSCSHTEKRSNPWWRVDLLQYMTIHSVTITNRGDCCGERI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616393   169 TIVVRVGNNRPDLGTNPICNRFTGLLEAGQPLFLPCNPPMPGAFVSVHLENStPNPLSICEAFVytDQALPIER 242
Cdd:smart00607  81 TGARILIGNSLENGGINNPNCSTGGLMAGGETKTFCCPPPMIGRYVTVYLPK-PNESLILCEVE--VNALFPER 151
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 256-375 3.73e-23

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: 95.74  E-value: 3.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393   256 SYNGKCYIFYNrQPLNFLDALSFCRSRGGTLISESNPALQGFIsWELWRrhRSDVSSQYWMGAVRDGSDrSSWKWVNGDE 335
Cdd:smart00034   7 SYGGKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFV-ASLLK--NSGSSDYYWIGLSDPDSN-GSWQWSDGSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 442616393   336 LTVSFWSHPG----GDEDCARFDGSKGwLWSDTNCNTLLNFICQ 375
Cdd:smart00034  82 PVSYSNWAPGepnnSSGDCVVLSTSGG-KWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 260-376 6.34e-23

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: 94.61  E-value: 6.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 260 KCYIFYNrQPLNFLDALSFCRSRGGTLISESNPALQGFIswelWRRHRSDVSSQYWMGAVRDGSDRSsWKWVNGDE-LTV 338
Cdd:cd00037    1 SCYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFL----ASLLKKSSSSDVWIGLNDLSSEGT-WKWSDGSPlVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 442616393 339 SFWS----HPGGDEDCARFDGSKGWLWSDTNCNTLLNFICQH 376
Cdd:cd00037   75 TNWApgepNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 368-557 1.77e-20

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 92.41  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 368 TLLNficQHQPKTCGRPEQPPNSTMvALNGFEVGAQIKYSCDANHLLVGPATRTClETGF-----YNEFPPVCKYIECGL 442
Cdd:PHA02927  76 TLFN---QCIKRRCPSPRDIDNGQL-DIGGVDFGSSITYSCNSGYQLIGESKSYC-ELGStgsmvWNPEAPICESVKCQS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 443 PASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDErWNGPPPrCEIVEC--DTLPGNYYSTiiNAPNGTYY 520
Cdd:PHA02927 151 PPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSGGE-WSDPPT-CQIVKCphPTISNGYLSS--GFKRSYSY 226

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 442616393 521 GSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRCIK 557
Cdd:PHA02927 227 NDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKCVR 263
PHA02639 PHA02639
EEV host range protein; Provisional
 381-560 8.72e-19

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 88.18  E-value: 8.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 381 CGRPEQPPNSTMVAL-NGFEVGAQIKYSCDANHLLVGPATRTCLE---TGFYNEFPPVCKYIECGLPASIAHGSYALLNN 456
Cdd:PHA02639  22 CDKPDDISNGFITELmEKYEIGKLIEYTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKECNDPPSIINGKIYNKRE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 457 TVGYLSLVKYSCEE----GYEMIGRALLTCDFDERWNGPPPRCEIVECdTLPG--NYYSTIINAPNGTYYGSKAEISCPP 530
Cdd:PHA02639 102 MYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICKMINC-RFPAlqNGYINGIPSNKKFYYKTRVGFSCKS 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 442616393 531 GYRMEGPRVLTCLASGQWSSALPRCIKLEP 560
Cdd:PHA02639 181 GFDLVGEKYSTCNINATWFPSIPTCVRNKP 210
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 256-375 1.10e-17

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: 80.04  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 256 SYNGKCYiFYNRQPLNFLDALSFCRSRGGTLISESNPALQGFISwelwrrHRSDVSSQYWMGaVRDGSDRSSWKWVNGDE 335
Cdd:cd03590    7 SFQSSCY-FFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS------KILSGNRSYWIG-LSDEETEGEWKWVDGTP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 442616393 336 L--TVSFW------SHPGGDEDCARFDGSKgWLWSDTNCNTLLNFICQ 375
Cdd:cd03590   79 LnsSKTFWhpgepnNWGGGGEDCAELVYDS-GGWNDVPCNLEYRWICE 125
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 269-376 1.49e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 75.98  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  269 PLNFLDALSFCRSRGGTLISESNPALQGFISWELWRRhrsdvSSQYWMGAVRDGSDrSSWKWVNGDELTVSFW----SHP 344
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS-----NKYFWIGLTDRKNE-GTWKWVDGSPVNYTNWapepNNN 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 442616393  345 GGDEDCARFdGSKGWLWSDTNCNTLLNFICQH 376
Cdd:pfam00059  75 GENEDCVEL-SSSSGKWNDENCNSKNPFVCEK 105
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 250-375 2.77e-13

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: 67.40  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 250 PPGALAsYNGKCYIFYnRQPLNFLDALSFCRSR--GGTLISESNPALQGFISWELWRRHRSDvsSQYWMGaVRDGSDRSS 327
Cdd:cd03594    2 PKGWLP-YKGNCYGYF-RQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAY--QPVWIG-LHDPQQSRG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442616393 328 WKWVNGDELTVSFW----SHPGGdEDCARFDGSKGWL-WSDTNCNTLLNFICQ 375
Cdd:cd03594   77 WEWSDGSKLDYRSWdrnpPYARG-GYCAELSRSTGFLkWNDANCEERNPFICK 128
PHA02817 PHA02817
EEV Host range protein; Provisional
 435-557 1.79e-11

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 64.96  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 435 CKYIECGLPASIAHGSYALLNNTVGYLSLVKYSCEEG-----YEMIGRALLTCDFDERWNGPPPRCEIVECdTLPG--NY 507
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRC-RFPAlqNG 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 442616393 508 YSTIINAPNGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRCIK 557
Cdd:PHA02817  98 FVNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPICSR 147
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 500-556 1.86e-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: 60.17  E-value: 1.86e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393 500 CDTLPGNYYSTIINAPNGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRCI 556
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 500-555 3.47e-11

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: 59.08  E-value: 3.47e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393   500 CDTLPGNYYSTIINAPNGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRC 555
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 440-496 1.29e-10

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: 57.47  E-value: 1.29e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393 440 CGLPASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDERWNGPPPRCE 496
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 37-93 3.17e-10

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: 56.70  E-value: 3.17e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442616393  37 CSFPGSPAHSSVVFSNANLTQGTVASYSCERGFELLGPARRVC-DKGQWVPEgIPFCV 93
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCtENGGWSPP-PPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 440-495 6.03e-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: 55.61  E-value: 6.03e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393   440 CGLPASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDERWNGPPPRC 495
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 262-374 7.56e-10

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: 57.00  E-value: 7.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 262 YIFYNrQPLNFLDALSFCRSRGGTLISesnpaLQGFISWELWRRHRSDVSSQYWMGAVRDgsdRSSWKWVNGDELTVSFW 341
Cdd:cd03602    3 FYLVN-ESKTWSEAQQYCRENYTDLAT-----VQNQEDNALLSNLSRVSNSAAWIGLYRD---VDSWRWSDGSESSFRNW 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442616393 342 S--HPGGDEDCA--RFDGSkgwlWSDTNCNTLLNFIC 374
Cdd:cd03602   74 NtfQPFGQGDCAtmYSSGR----WYAALCSALKPFIC 106
Sushi pfam00084
Sushi repeat (SCR repeat);
516-555 9.01e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.20  E-value: 9.01e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 442616393  516 NGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRC 555
Cdd:pfam00084  17 NEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 263-375 1.04e-09

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 56.92  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 263 IFY-NRQPLNFLDALSFCRSRGGTLIS----ESNPALQGFISWELWRRHrsdvssqywMGaVRDGSDRSSWKWVNGDELT 337
Cdd:cd03591    3 IFVtNGEEKNFDDAQKLCSEAGGTLAMprnaAENAAIASYVKKGNTYAF---------IG-ITDLETEGQFVYLDGGPLT 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442616393 338 VSFW-----SHPGGDEDCARF--DGskgwLWSDTNCNTLLNFICQ 375
Cdd:cd03591   73 YTNWkpgepNNAGGGEDCVEMytSG----KWNDVACNLTRLFVCE 113
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 257-376 1.31e-09

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: 56.57  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 257 YNGKCYIFYNrQPLNFLDALSFCRSRGGTLISESNPALQGFISwelwrrhRSDVSSQYWMGAVRDGSDRSsWKWVNGDEL 336
Cdd:cd03593    8 YGNKCYYFSM-EKKTWNESKEACSSKNSSLLKIDDEEELEFLQ-------SQIGSSSYWIGLSREKSEKP-WKWIDGSPL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442616393 337 TVSFWSHPGGDED-CARFDGSKGwlwSDTNCNTLLNFICQH 376
Cdd:cd03593   79 NNLFNIRGSTKSGnCAYLSSTGI---YSEDCSTKKRWICEK 116
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 37-92 1.57e-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: 54.45  E-value: 1.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393    37 CSFPGSPAHSSVVFSNANLTQGTVASYSCERGFELLGPARRVCDK-GQWVPEgIPFC 92
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLEnGTWSPP-PPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
440-495 1.18e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 52.12  E-value: 1.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393  440 CGLPASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDERWNGPPPRC 495
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 381-436 1.57e-08

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: 51.69  E-value: 1.57e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393 381 CGRPEQPPNSTMV-ALNGFEVGAQIKYSCDANHLLVGPATRTCLETGFYNEFPPVCK 436
Cdd:cd00033    1 CPPPPVPENGTVTgSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 263-375 3.18e-08

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 52.76  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 263 IFYNRQPLNFLDALSFCRSRGGTLI----SESNPALQGFIswelwrrhRSDVSSQYWMgavrDGSDRSS-WKWV--NGDE 335
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVaiqnAEENALLNGFA--------LKYNLGYYWI----DGNDINNeGTWVdtDKKE 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442616393 336 LTVSFWsHPG-----GDEDCARFDGSKGWLWSDTNCNTLLNFICQ 375
Cdd:cd03592   71 LEYKNW-APGepnngRNENCLEIYIKDNGKWNDEPCSKKKSAICY 114
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 243-376 3.89e-08

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: 53.13  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 243 CPTFrdqppgaLASYNGKCYIFYNRQpLNFLDALSFCRS-----RGGTLISESNPALQGFIsWELWR-RHRSDVSSQYWM 316
Cdd:cd03589    1 CPTF-------WTAFGGYCYRFFGDR-LTWEEAELRCRSfsipgLIAHLVSIHSQEENDFV-YDLFEsSRGPDTPYGLWI 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 317 GA---VRDGSdrssWKWVNGDELTVSFW--SHP---GGDEDCARF--DGSKGWLWSDTNCNTLLNFICQH 376
Cdd:cd03589   72 GLhdrTSEGP----FEWTDGSPVDFTKWagGQPdnyGGNEDCVQMwrRGDAGQSWNDMPCDAVFPYICKM 137
Sushi pfam00084
Sushi repeat (SCR repeat);
381-435 4.06e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 4.06e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393  381 CGRPEQPPN-STMVALNGFEVGAQIKYSCDANHLLVGPATRTCLETGFYNEFPPVC 435
Cdd:pfam00084   1 CPPPPDIPNgKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 259-376 7.29e-08

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 51.68  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 259 GKCYIFyNRQPLNFLDALSFCRS-RGGTLISESNPAlqgfISWELWRRHRSDVSSQYWMGAVRDGSDRSS-WKWVNGDEL 336
Cdd:cd03598    1 GRCYRF-VKSPRTFRDAQVICRRcYRGNLASIHSFA----FNYRVQRLVSTLNQAQVWIGGIITGKGRCRrFSWVDGSVW 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 442616393 337 TVSFWS--HPG-GDEDCARFDGSKGWlWSDTNCNTLLNFICQH 376
Cdd:cd03598   76 NYAYWApgQPGnRRGHCVELCTRGGH-WRRAHCKLRRPFICSY 117
PHA02831 PHA02831
EEV host range protein; Provisional
 398-495 2.60e-07

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 53.07  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 398 FEVGAQIKYSCDANHL----LVGPATRTCLETGFYNEFPpVCKYIECGLPAsIAHGSYALLNNTVGYLSLVKYSCEEGYE 473
Cdd:PHA02831  96 YSFGDSVTYACKVNKLekysIVGNETVKCINKQWVPKYP-VCKLIRCKYPA-LQNGFLNVFEKKFYYGDIVNFKCKKGFI 173

                         90       100
                 ....*....|....*....|..
gi 442616393 474 MIGRALLTCDFDERWNGPPPRC 495
Cdd:PHA02831 174 LLGSSVSTCDINSIWYPGIPKC 195
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 381-435 2.97e-07

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: 47.91  E-value: 2.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393   381 CGRPEQPPNSTMVALNG-FEVGAQIKYSCDANHLLVGPATRTCLETGFYNEFPPVC 435
Cdd:smart00032   1 CPPPPDIENGTVTSSSGtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 259-375 5.61e-07

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 49.69  E-value: 5.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 259 GKCYIFYNrQPLNFLDALSFCRSRGGTLI----SESNPALQGFIswelwrRHRSDVSSQYWMGaVRDGSDRSSWKWVNGD 334
Cdd:cd03596    9 KKCYLVSE-ETKHYHEASEDCIARGGTLAtprdSDENDALRDYV------KASVPGNWEVWLG-INDMVAEGKWVDVNGS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 442616393 335 ELTVSFW-----SHPGGD--EDCARFDGSKGWLWSDTNCNTLLNFICQ 375
Cdd:cd03596   81 PISYFNWereitAQPDGGkrENCVALSSSAQGKWFDEDCRREKPYVCE 128
PHA02817 PHA02817
EEV Host range protein; Provisional
 398-527 3.93e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 49.17  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 398 FEVGAQIKYSCDAN-----HLLVGPATRTCLETGFYNEFPPVCKYIECGLPAsIAHGSYALL--NNTVGYLSLVKYSCEE 470
Cdd:PHA02817  42 YNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPA-LQNGFVNGIpdSKKFYYESEVSFSCKP 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393 471 GYEMIGRALLTCDFDERWNGPPPRCE---------IVECDTLPGNYYSTIINApNGTYYGSKAEIS 527
Cdd:PHA02817 121 GFVLIGTKYSVCGINSSWIPKVPICSrdnitynkiYINKVNIDDNFFNQINNS-NTYYFDKILQIN 185
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 106-229 4.61e-06

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 46.67  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  106 STDGAGAPQKAIDGSTSAFFTPETCSltkaeRSPWWYVNLLEPYMVQLVRLDFGKSCCGNKPATIVVRVGNNrpdlGTN- 184
Cdd:pfam00754   7 SYSGEGPAAAALDGDPNTAWSAWSGD-----DPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEYSLD----GENw 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 442616393  185 --PICNRFTGLLEAGQPLFLPCNPPMPGAFVSVHL--ENSTPNPLSICE 229
Cdd:pfam00754  78 ttVKDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPtsWNGGNGIALRAE 126
PHA02831 PHA02831
EEV host range protein; Provisional
 440-557 5.70e-06

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 49.22  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 440 CGLPASIAHGSYALLNNTVGYLSLVKYSCE----EGYEMIGRALLTCdFDERWNGPPPRCEIVECdTLPGNYYSTIINAP 515
Cdd:PHA02831  78 CKDPVTILNGYIKNKKDQYSFGDSVTYACKvnklEKYSIVGNETVKC-INKQWVPKYPVCKLIRC-KYPALQNGFLNVFE 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 442616393 516 NGTYYGSKAEISCPPGYRMEGPRVLTCLASGQWSSALPRCIK 557
Cdd:PHA02831 156 KKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKCVK 197
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 257-375 6.28e-06

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 46.42  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 257 YNGKCY-IFYNRQplNFLDALSFCRSRGGTLISESNPALQGFISwelwrRHRSDVSsqyWMGaVRDGSDRSSWKWVNGDE 335
Cdd:cd03588    8 FQGHCYrHFPDRE--TWEDAERRCREQQGHLSSIVTPEEQEFVN-----NNAQDYQ---WIG-LNDRTIEGDFRWSDGHP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 442616393 336 LTVSFWSHPGGD------EDCARFDGSKGWLWSDTNCNTLLNFICQ 375
Cdd:cd03588   77 LQFENWRPNQPDnffatgEDCVVMIWHEEGEWNDVPCNYHLPFTCK 122
Sushi pfam00084
Sushi repeat (SCR repeat);
37-92 4.02e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 42.10  E-value: 4.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393   37 CSFPGSPAHSSVVFSNANLTQGTVASYSCERGFELLGPARRVCDK-GQWVPEgIPFC 92
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEdGTWSPP-FPEC 56
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 261-376 6.82e-05

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 44.11  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 261 CY-IFY---NRQPLNFLDALSFCRSRGGTLISESNPALQGFIS-------------W-ELWRR-----HRSDVSSQY-WM 316
Cdd:cd03595   12 CYkIAYfqdSRRRLNFEEARQACREDGGELLSIESENEQKLIErfiqtlrasdgdfWiGLRRSsqynvTSSACSSLYyWL 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442616393 317 gavrDGSDRSSWKWVN-----GDELTVSFWSHPGGDedcARFDGSKGWLWSDTNCNTLLNFICQH 376
Cdd:cd03595   92 ----DGSISTFRNWYVdepscGSEVCVVMYHQPSAP---AGQGGPYLFQWNDDNCNMKNNFICKY 149
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 435-564 6.84e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 46.23  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 435 CKYIECGlPASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDErWNgPPPRCEiVECDtlpgnyystIINA 514
Cdd:PHA02954 125 CPNAECQ-PLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN-VIPSCQ-QKCD---------IPSL 191

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393 515 PNGTYYGSKAEI------SCPPGYRMEGPRVLTCLaSGQWSSALPRCIKLEPSTQP 564
Cdd:PHA02954 192 SNGLISGSTFSIggvihlSCKSGFTLTGSPSSTCI-DGKWNPVLPICVRSNEEFDP 246
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 274-365 7.66e-05

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial 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. Bacterial CTLDs within this group are functionally uncharacterized. 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: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 43.18  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 274 DALSFCRSRGGTLISESNPALQGFIsWELwrrhrSDVSSQYWMGAvRDGSDRSSWKWVNGDELTVSFW------SHPGGD 347
Cdd:cd03603   14 AAQTLAESLGGHLVTINSAEENDWL-LSN-----FGGYGASWIGA-SDAATEGTWKWSDGEESTYTNWgsgephNNGGGN 86

                         90       100
                 ....*....|....*....|
gi 442616393 348 EDCARFDGSKGWL--WSDTN 365
Cdd:cd03603   87 EDYAAINHFPGISgkWNDLA 106
PHA03247 PHA03247
large tegument protein UL36; Provisional
 527-725 1.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  527 SCPPGYRMEGP-RVLTCLASGQWSSALPRCIKLEPSTQPTAASTIPVPSSVATPPPFRPkvVSSTTSRTPYRPAVSTASS 605
Cdd:PHA03247 2769 PAPPAAPAAGPpRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPTAPPPPPGPP 2846

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  606 GIGGSSTSTV---GTYPSLSPTQveingeseseeeiNVPPVPGTvreefPPRRTVRPVLIPKKPNST-PAALPPTTHQVP 681
Cdd:PHA03247 2847 PPSLPLGGSVapgGDVRRRPPSR-------------SPAAKPAA-----PARPPVRRLARPAVSRSTeSFALPPDQPERP 2908

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 442616393  682 PQPPS----TYAPTPPRSSRPSGAPNSAGEVETTTRNTQQIIANSHPQ 725
Cdd:PHA03247 2909 PQPQAppppQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
PHA03247 PHA03247
large tegument protein UL36; Provisional
 559-715 4.98e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  559 EPSTQPTAASTIPVPSSVATPPPFRPKVVSSTTS-------------RTPYRPAVSTASSGIGGSSTSTvgTYPSLSPTQ 625
Cdd:PHA03247 2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapggdvrrRPPSRSPAAKPAAPARPPVRRL--ARPAVSRST 2895

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  626 VEINGESESEEEINVPPVPGTVREEFPPRRTVRPVLIPKKPNSTPAALPPTTHQVPPQPPSTYAPTP------------P 693
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlgalvpgrvavP 2975

                         170       180
                  ....*....|....*....|..
gi 442616393  694 RSSRPSGAPNSAGEVETTTRNT 715
Cdd:PHA03247 2976 RFRVPQPAPSREAPASSTPPLT 2997
PHA02639 PHA02639
EEV host range protein; Provisional
 436-571 7.12e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 42.73  E-value: 7.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 436 KYIECGLPASIAHGSYALLNNTVGYLSLVKYSCEEGYEMIGRALLTCDFDER---WNGPPPRCEIVECDTLPGNYYSTII 512
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDKNnaiWSNKAPFCMLKECNDPPSIINGKIY 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442616393 513 NAPNGTYYGSKAEISCPP----GYRMEGPRVLTCLASGQWSSALPRCIKLE---PSTQPTAASTIP 571
Cdd:PHA02639  98 NKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICKMINcrfPALQNGYINGIP 163
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
543-707 7.16e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 543 LASGQWSSALPRCIKLEPSTQPTAAstiPVPSSVATPPPFRPKVVSSTTSRTPYRPAVSTASSGIGGSSTSTV-GTYPSL 621
Cdd:PRK12323 433 LAAARQASARGPGGAPAPAPAPAAA---PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELpPEFASP 509

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 622 SPTQVEINGESESEEEINVPpvpgTVREEFPPRRTvrpvlipKKPNSTPAALPPTTHQVPPQPPstyaPTPPRSSRPSGA 701
Cdd:PRK12323 510 APAQPDAAPAGWVAESIPDP----ATADPDDAFET-------LAPAPAAAPAPRAAAATEPVVA----PRPPRASASGLP 574


                 ....*.
gi 442616393 702 PNSAGE 707
Cdd:PRK12323 575 DMFDGD 580
PHA03247 PHA03247
large tegument protein UL36; Provisional
 560-706 1.08e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  560 PSTQPTAASTIPVPSSVATPPPFRPKVVSSTTSRTPYRPAVSTASSGIGGSSTSTvGTYPSLSPTQVEINGESEseeein 639
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR-PRRRAARPTVGSLTSLAD------ 2700

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442616393  640 vPPVPGTVREEfPPRRTVRPVLIPKKPNSTPAALPPTTHQVPPQPPSTYAPTPPRSSRPSGAPNSAG 706
Cdd:PHA03247 2701 -PPPPPPTPEP-APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 263-375 1.42e-03

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 39.44  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393 263 IFYNRQPLNFLDALSFCRSRGGTLISESNPAL---QGFISWELWRRHrsdvssQYWMGAvrDGSDRSSWK--WVNGDELT 337
Cdd:cd03601    3 ILCSDETMNYAKAGAFCRSRGMRLASLAMRDSemrDAILAFTLVKGH------GYWVGA--DNLQDGEYDflWNDGVSLP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442616393 338 VSF--W-----SHPGGDEDCARFDGSKGwLWSDTNCNTLLNFICQ 375
Cdd:cd03601   75 TDSdlWapnepSNPQSRQLCVQLWSKYN-LLDDEYCGRAKRVICE 118
PHA03247 PHA03247
large tegument protein UL36; Provisional
 543-732 2.31e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  543 LASGQWSSALPRciklEPSTQPTAASTIP--VPSSVATPPPFRPKVVSSTTSRTPYRPAVSTASSGIGGSSTSTVGTYPS 620
Cdd:PHA03247 2762 TTAGPPAPAPPA----APAAGPPRRLTRPavASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT 2837

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  621 LSPTQVEINGESESEEEINVPPvpGTVREEFPPRRTVRPVLIPKKPNSTPAALPPTTHQVPPQPPSTYAPTPPRSSRPSG 700
Cdd:PHA03247 2838 APPPPPGPPPPSLPLGGSVAPG--GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP 2915

                         170       180       190
                  ....*....|....*....|....*....|..
gi 442616393  701 APNSAGEVETTTRNTQQIIANSHPQDNEIPDS 732
Cdd:PHA03247 2916 PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTT 2947
PHA03377 PHA03377
EBNA-3C; Provisional
 617-701 6.60e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.42  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  617 TYPsLSPTQVEINGES-ESEEEINVPPVPGTVREefpPRRTVRPvlipkkPNSTPAALPPT-THQVPPQPPS-TYAPTPP 693
Cdd:PHA03377  426 THP-VKRTLVKTSGRSdEAEQAQSTPERPGPSDQ---PSVPVEP------AHLTPVEHTTViLHQPPQSPPTvAIKPAPP 495


                  ....*...
gi 442616393  694 RSSRPSGA 701
Cdd:PHA03377  496 PSRRRRGA 503
PHA03247 PHA03247
large tegument protein UL36; Provisional
 641-770 7.35e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 7.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  641 PPVPG-TVREEFP--PRRTVRPVLIPKKPNSTPAALPPTthqvpPQPPSTYAPTPPRSSrPSGAPNSAGEVETTTRNTQQ 717
Cdd:PHA03247 2577 PSEPAvTSRARRPdaPPQSARPRAPVDDRGDPRGPAPPS-----PLPPDTHAPDPPPPS-PSPAANEPDPHPPPTVPPPE 2650

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442616393  718 iiansHPQDNEIPDSVNIQQNQSPNVNVPFAVDNPDRKETKEAKLNLGAIVAL 770
Cdd:PHA03247 2651 -----RPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
PHA03247 PHA03247
large tegument protein UL36; Provisional
 529-714 8.06e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  529 PPGYRMEGPRVLTCLASGQWSSALPRCIKlEPSTQPTAASTipvpSSVATPPPFRPKVVSSTTSRTPYRPAVSTASSGIG 608
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASSPPQRPR-RRAARPTVGSL----TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQ 2730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616393  609 GSSTSTVGTYPSLSPtqveingeseseeeiNVPPVPGTvreefpPRRTVRPVLIPKKPNSTPAALPPTTHQVPPQPPSTY 688
Cdd:PHA03247 2731 ASPALPAAPAPPAVP---------------AGPATPGG------PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789

                         170       180
                  ....*....|....*....|....*.
gi 442616393  689 APTPPRSSRPSGAPNSAGEVETTTRN 714
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPA 2815
 
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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