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Conserved domains on  [gi|24661363|ref|NP_729451|]
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tequila, isoform D [Drosophila melanogaster]

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 ...
1205-1442 5.16e-92

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: 297.27  E-value: 5.16e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1205 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENW 1284
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG----GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1285 YLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPaQVLGSAELPILADHV 1364
Cdd:cd00190   77 IVHPNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAE 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24661363 1365 CKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEK 1442
Cdd:cd00190  155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
1040-1138 1.83e-41

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 147.49  E-value: 1.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    1040 RLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNI-FGNSNGPIWLDQVMCFGNETSIDQCN 1118
Cdd:smart00202    2 RLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAyFGPGSGPIWLDNVRCSGTEASLSDCP 81
                            90       100
                    ....*....|....*....|
gi 24661363    1119 HWNWGEHNCNHTEDVALHCS 1138
Cdd:smart00202   82 HSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
887-989 2.52e-37

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 135.93  E-value: 2.52e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363     887 VRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFyapPNQDFNYLMDEVECHGNETKL 966
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYF---GPGSGPIWLDNVRCSGTEASL 77
                            90       100
                    ....*....|....*....|...
gi 24661363     967 GQCAFKGWGVHNCGVDEVAGVTC 989
Cdd:smart00202   78 SDCPHSGWGSHNCSHGEDAGVVC 100
ChtBD2 smart00494
Chitin-binding domain type 2;
136-184 4.08e-13

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 64.77  E-value: 4.08e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 24661363     136 PKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHK 184
Cdd:smart00494    1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
65-115 1.61e-12

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 63.20  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24661363     65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVV 115
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
995-1028 7.83e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


:

Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.86  E-value: 7.83e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 24661363     995 KCPNNYWLCHTSKeCIPPAFVCDNTPDCADKSDE 1028
Cdd:smart00192    1 TCPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
851-880 1.30e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 1.30e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 24661363  851 FDCGNGQCLKKEEICDGKKNCPNGKDEANC 880
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
PHA03247 super family cl33720
large tegument protein UL36; Provisional
245-564 3.71e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   245 RPSGVGVEQNPHHhhhgynPGWSGQETSyvQRGPTQSTLYVEGSLQPNrNYPTNKTPLAPMAPT--------NTGGVYYG 316
Cdd:PHA03247 2576 RPSEPAVTSRARR------PDAPPQSAR--PRAPVDDRGDPRGPAPPS-PLPPDTHAPDPPPPSpspaanepDPHPPPTV 2646
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   317 QPVEDKQNVPS--RQNYSRRI-------DYGSPGNGWKPMPPLDPLGgqqPLNLDYSPHSPGaKEPQsqdslPGQKPINL 387
Cdd:PHA03247 2647 PPPERPRDDPApgRVSRPRRArrlgraaQASSPPQRPRRRAARPTVG---SLTSLADPPPPP-PTPE-----PAPHALVS 2717
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   388 DYDEEPIPQYLHNGLPPYPGSPPrfyPDQLPSGSKPIGRQQPVESSPDASGYPDQQKPLDPDNGlhgskvPPRHSPNPGY 467
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPA---PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG------PPRRLTRPAV 2788
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   468 PLYNESnLYGGLLPPKPDSPVNTTPTPTPNPSSSQAPTPQLANRLHTFPIYPPvdnktsLRNPIQPHYSPSYAGIAH--- 544
Cdd:PHA03247 2789 ASLSES-RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP------PPPGPPPPSLPLGGSVAPggd 2861
                         330       340
                  ....*....|....*....|.
gi 24661363   545 -SRDAPWAKVPVTSTTPAQDP 564
Cdd:PHA03247 2862 vRRRPPSRSPAAKPAAPARPP 2882
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
399-750 9.71e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   399 HNGLPPYPGSPPrfYPDQLPSGSKpiGRQQPVESSPDASGYPDQQKPLDPDNGLHGSKVPP--RHSPN--------PGYP 468
Cdd:PTZ00449  507 HDEPPEGPEASG--LPPKAPGDKE--GEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPakEHKPSkiptlskkPEFP 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   469 LYNESnlyggllpPKPDSPVNTTPTPTPNPSSSQAPTPQLANRLHTFPIYPPVDNKTSLRNPIQPHYSPSyagiahSRDA 548
Cdd:PTZ00449  583 KDPKH--------PKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSS------PERP 648
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   549 PWAKVPVTSTTPAQDPDPFNPELDEPFYDDVDFLTTTVRNVLVPPPFDHKFyspqstnPSINRNQSASGPNSQAAIKEAL 628
Cdd:PTZ00449  649 EGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESF-------ESILKETLPETPGTPFTTPRPL 721
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   629 --KLMLRPYFNHSGNAQEQLAQQAESAIVSviskpSTTTTTTPRPTSKTPKTDPDFDAELIKAGEQESLDSVDDDyvfPD 706
Cdd:PTZ00449  722 ppKLPRDEEFPFEPIGDPDAEQPDDIEFFT-----PPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDE---AM 793
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 24661363   707 ARETSRTEQTLDPSTTYASTnfqrSTRRAELDPDTLTATTMKTN 750
Cdd:PTZ00449  794 KRPDSPSEHEDKPPGDHPSL----PKKRHRLDGLALSTTDLESD 833
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1205-1442 5.16e-92

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: 297.27  E-value: 5.16e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1205 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENW 1284
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG----GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1285 YLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPaQVLGSAELPILADHV 1364
Cdd:cd00190   77 IVHPNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAE 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24661363 1365 CKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEK 1442
Cdd:cd00190  155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1204-1439 6.20e-89

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: 288.42  E-value: 6.20e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    1204 RVVRGNVAQRGRHPWQATIRTRGRggisSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIEN 1283
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGG----RHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIKVSKV 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    1284 wYLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 1363
Cdd:smart00020   77 -IIHPNYNPST-YDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24661363    1364 VCKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGeTLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 1439
Cdd:smart00020  155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW-VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1205-1439 9.24e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 9.24e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   1205 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPkgAYFVRVGDHYANIAESSEVDSFIENW 1284
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSS----GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   1285 YLHENFRKGTHmNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVstPAQVLGSAELPILADHV 1364
Cdd:pfam00089   75 IVHPNYNPDTL-DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRET 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24661363   1365 CKQSnvYGSAMSEGMFCAGSmdESVDACEGDSGGPLVCSDddgETLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 1439
Cdd:pfam00089  152 CRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSD---GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1204-1445 6.14e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.03  E-value: 6.14e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1204 RVVRGNVAQRGRHPWQATIRTRGrgGISSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHyaNIAESSEVDSFIEN 1283
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSN--GPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGST--DLSTSGGTVVKVAR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1284 WYLHENFRKGThMNNDIALVVLKTPLkfsDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 1363
Cdd:COG5640  106 IVVHPDYDPAT-PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1364 VCkqsNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEKI 1443
Cdd:COG5640  182 TC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                 ..
gi 24661363 1444 NE 1445
Cdd:COG5640  259 GG 260
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
1040-1138 1.83e-41

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 147.49  E-value: 1.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    1040 RLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNI-FGNSNGPIWLDQVMCFGNETSIDQCN 1118
Cdd:smart00202    2 RLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAyFGPGSGPIWLDNVRCSGTEASLSDCP 81
                            90       100
                    ....*....|....*....|
gi 24661363    1119 HWNWGEHNCNHTEDVALHCS 1138
Cdd:smart00202   82 HSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
887-989 2.52e-37

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 135.93  E-value: 2.52e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363     887 VRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFyapPNQDFNYLMDEVECHGNETKL 966
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYF---GPGSGPIWLDNVRCSGTEASL 77
                            90       100
                    ....*....|....*....|...
gi 24661363     967 GQCAFKGWGVHNCGVDEVAGVTC 989
Cdd:smart00202   78 SDCPHSGWGSHNCSHGEDAGVVC 100
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
892-990 6.72e-36

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 131.73  E-value: 6.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    892 GESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSfYAPPNQDFNYLMDEVECHGNETKLGQCAF 971
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGCS-YFGPGSTGPIWLDDVRCSGNETSLWQCPH 79
                           90
                   ....*....|....*....
gi 24661363    972 KGWGVHNCGVDEVAGVTCK 990
Cdd:pfam00530   80 RPWGNHNCSHSEDAGVICS 98
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
1044-1138 4.25e-35

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 129.42  E-value: 4.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   1044 GRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKI---EKNIFGNSNGPIWLDQVMCFGNETSIDQCNHW 1120
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSApsgCSYFGPGSTGPIWLDDVRCSGNETSLWQCPHR 80
                           90
                   ....*....|....*...
gi 24661363   1121 NWGEHNCNHTEDVALHCS 1138
Cdd:pfam00530   81 PWGNHNCSHSEDAGVICS 98
ChtBD2 smart00494
Chitin-binding domain type 2;
136-184 4.08e-13

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 64.77  E-value: 4.08e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 24661363     136 PKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHK 184
Cdd:smart00494    1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
138-189 7.23e-13

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 64.36  E-value: 7.23e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24661363    138 CQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHKD-LAKC 189
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDnVVDC 53
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
65-115 1.61e-12

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 63.20  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24661363     65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVV 115
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
65-111 9.40e-10

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 55.53  E-value: 9.40e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 24661363      65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHP 111
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
995-1028 7.83e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.86  E-value: 7.83e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 24661363     995 KCPNNYWLCHTSKeCIPPAFVCDNTPDCADKSDE 1028
Cdd:smart00192    1 TCPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
851-880 1.30e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 1.30e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 24661363  851 FDCGNGQCLKKEEICDGKKNCPNGKDEANC 880
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
996-1028 1.34e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 1.34e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 24661363  996 CPNNYWLCHtSKECIPPAFVCDNTPDCADKSDE 1028
Cdd:cd00112    1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDE 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
245-564 3.71e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   245 RPSGVGVEQNPHHhhhgynPGWSGQETSyvQRGPTQSTLYVEGSLQPNrNYPTNKTPLAPMAPT--------NTGGVYYG 316
Cdd:PHA03247 2576 RPSEPAVTSRARR------PDAPPQSAR--PRAPVDDRGDPRGPAPPS-PLPPDTHAPDPPPPSpspaanepDPHPPPTV 2646
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   317 QPVEDKQNVPS--RQNYSRRI-------DYGSPGNGWKPMPPLDPLGgqqPLNLDYSPHSPGaKEPQsqdslPGQKPINL 387
Cdd:PHA03247 2647 PPPERPRDDPApgRVSRPRRArrlgraaQASSPPQRPRRRAARPTVG---SLTSLADPPPPP-PTPE-----PAPHALVS 2717
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   388 DYDEEPIPQYLHNGLPPYPGSPPrfyPDQLPSGSKPIGRQQPVESSPDASGYPDQQKPLDPDNGlhgskvPPRHSPNPGY 467
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPA---PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG------PPRRLTRPAV 2788
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   468 PLYNESnLYGGLLPPKPDSPVNTTPTPTPNPSSSQAPTPQLANRLHTFPIYPPvdnktsLRNPIQPHYSPSYAGIAH--- 544
Cdd:PHA03247 2789 ASLSES-RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP------PPPGPPPPSLPLGGSVAPggd 2861
                         330       340
                  ....*....|....*....|.
gi 24661363   545 -SRDAPWAKVPVTSTTPAQDP 564
Cdd:PHA03247 2862 vRRRPPSRSPAAKPAAPARPP 2882
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
851-877 1.11e-04

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 40.69  E-value: 1.11e-04
                            10        20
                    ....*....|....*....|....*..
gi 24661363     851 FDCGNGQCLKKEEICDGKKNCPNGKDE 877
Cdd:smart00192    7 FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
995-1028 1.93e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.23  E-value: 1.93e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 24661363    995 KCPNNYWLCHTSkECIPPAFVCDNTPDCADKSDE 1028
Cdd:pfam00057    2 TCSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDE 34
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
399-750 9.71e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   399 HNGLPPYPGSPPrfYPDQLPSGSKpiGRQQPVESSPDASGYPDQQKPLDPDNGLHGSKVPP--RHSPN--------PGYP 468
Cdd:PTZ00449  507 HDEPPEGPEASG--LPPKAPGDKE--GEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPakEHKPSkiptlskkPEFP 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   469 LYNESnlyggllpPKPDSPVNTTPTPTPNPSSSQAPTPQLANRLHTFPIYPPVDNKTSLRNPIQPHYSPSyagiahSRDA 548
Cdd:PTZ00449  583 KDPKH--------PKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSS------PERP 648
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   549 PWAKVPVTSTTPAQDPDPFNPELDEPFYDDVDFLTTTVRNVLVPPPFDHKFyspqstnPSINRNQSASGPNSQAAIKEAL 628
Cdd:PTZ00449  649 EGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESF-------ESILKETLPETPGTPFTTPRPL 721
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   629 --KLMLRPYFNHSGNAQEQLAQQAESAIVSviskpSTTTTTTPRPTSKTPKTDPDFDAELIKAGEQESLDSVDDDyvfPD 706
Cdd:PTZ00449  722 ppKLPRDEEFPFEPIGDPDAEQPDDIEFFT-----PPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDE---AM 793
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 24661363   707 ARETSRTEQTLDPSTTYASTnfqrSTRRAELDPDTLTATTMKTN 750
Cdd:PTZ00449  794 KRPDSPSEHEDKPPGDHPSL----PKKRHRLDGLALSTTDLESD 833
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1205-1442 5.16e-92

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: 297.27  E-value: 5.16e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1205 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENW 1284
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG----GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1285 YLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPaQVLGSAELPILADHV 1364
Cdd:cd00190   77 IVHPNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAE 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24661363 1365 CKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEK 1442
Cdd:cd00190  155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1204-1439 6.20e-89

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: 288.42  E-value: 6.20e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    1204 RVVRGNVAQRGRHPWQATIRTRGRggisSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIEN 1283
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGG----RHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIKVSKV 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    1284 wYLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 1363
Cdd:smart00020   77 -IIHPNYNPST-YDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24661363    1364 VCKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGeTLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 1439
Cdd:smart00020  155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW-VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1205-1439 9.24e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 9.24e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   1205 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPkgAYFVRVGDHYANIAESSEVDSFIENW 1284
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSS----GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   1285 YLHENFRKGTHmNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVstPAQVLGSAELPILADHV 1364
Cdd:pfam00089   75 IVHPNYNPDTL-DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRET 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24661363   1365 CKQSnvYGSAMSEGMFCAGSmdESVDACEGDSGGPLVCSDddgETLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 1439
Cdd:pfam00089  152 CRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSD---GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1204-1445 6.14e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.03  E-value: 6.14e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1204 RVVRGNVAQRGRHPWQATIRTRGrgGISSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHyaNIAESSEVDSFIEN 1283
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSN--GPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGST--DLSTSGGTVVKVAR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1284 WYLHENFRKGThMNNDIALVVLKTPLkfsDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 1363
Cdd:COG5640  106 IVVHPDYDPAT-PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1364 VCkqsNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEKI 1443
Cdd:COG5640  182 TC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                 ..
gi 24661363 1444 NE 1445
Cdd:COG5640  259 GG 260
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
1040-1138 1.83e-41

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 147.49  E-value: 1.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    1040 RLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNI-FGNSNGPIWLDQVMCFGNETSIDQCN 1118
Cdd:smart00202    2 RLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAyFGPGSGPIWLDNVRCSGTEASLSDCP 81
                            90       100
                    ....*....|....*....|
gi 24661363    1119 HWNWGEHNCNHTEDVALHCS 1138
Cdd:smart00202   82 HSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
887-989 2.52e-37

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 135.93  E-value: 2.52e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363     887 VRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFyapPNQDFNYLMDEVECHGNETKL 966
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYF---GPGSGPIWLDNVRCSGTEASL 77
                            90       100
                    ....*....|....*....|...
gi 24661363     967 GQCAFKGWGVHNCGVDEVAGVTC 989
Cdd:smart00202   78 SDCPHSGWGSHNCSHGEDAGVVC 100
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
892-990 6.72e-36

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 131.73  E-value: 6.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363    892 GESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSfYAPPNQDFNYLMDEVECHGNETKLGQCAF 971
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGCS-YFGPGSTGPIWLDDVRCSGNETSLWQCPH 79
                           90
                   ....*....|....*....
gi 24661363    972 KGWGVHNCGVDEVAGVTCK 990
Cdd:pfam00530   80 RPWGNHNCSHSEDAGVICS 98
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
1044-1138 4.25e-35

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 129.42  E-value: 4.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   1044 GRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKI---EKNIFGNSNGPIWLDQVMCFGNETSIDQCNHW 1120
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSApsgCSYFGPGSTGPIWLDDVRCSGNETSLWQCPHR 80
                           90
                   ....*....|....*...
gi 24661363   1121 NWGEHNCNHTEDVALHCS 1138
Cdd:pfam00530   81 PWGNHNCSHSEDAGVICS 98
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
1231-1445 1.24e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 71.25  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1231 SSHWCGAVVISKRHLLTAAHCLYGSPKGAYF--VRVGDHYANIAESSEVdsfIENWYLHENFRKGTHMNNDIALVVLKTP 1308
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWAtnIVFVPGYNGGPYGTAT---ATRFRVPPGWVASGDAGYDYALLRLDEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363 1309 LkfSDYVQPICLpDKNAELVEDRKCTISGWGSIKSGVSTpaqvlgsaelpilADHVCKQSNVYGSAMSegMFCagsmdes 1388
Cdd:COG3591   87 L--GDTTGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDLS-------------LDCSGRVTGVQGNRLS--YDC------- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24661363 1389 vDACEGDSGGPLVCSDDDGETLYGLISWGqHCGFKNRpGVYVRvNHYIDWIYEKINE 1445
Cdd:COG3591  142 -DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVRLT-SAIVAALRAWASA 194
ChtBD2 smart00494
Chitin-binding domain type 2;
136-184 4.08e-13

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 64.77  E-value: 4.08e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 24661363     136 PKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHK 184
Cdd:smart00494    1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
138-189 7.23e-13

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 64.36  E-value: 7.23e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24661363    138 CQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHKD-LAKC 189
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDnVVDC 53
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
65-115 1.61e-12

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 63.20  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24661363     65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVV 115
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
65-111 9.40e-10

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 55.53  E-value: 9.40e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 24661363      65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHP 111
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
995-1028 7.83e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.86  E-value: 7.83e-07
                            10        20        30
                    ....*....|....*....|....*....|....
gi 24661363     995 KCPNNYWLCHTSKeCIPPAFVCDNTPDCADKSDE 1028
Cdd:smart00192    1 TCPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
851-880 1.30e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 1.30e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 24661363  851 FDCGNGQCLKKEEICDGKKNCPNGKDEANC 880
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
996-1028 1.34e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 1.34e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 24661363  996 CPNNYWLCHtSKECIPPAFVCDNTPDCADKSDE 1028
Cdd:cd00112    1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDE 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
245-564 3.71e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   245 RPSGVGVEQNPHHhhhgynPGWSGQETSyvQRGPTQSTLYVEGSLQPNrNYPTNKTPLAPMAPT--------NTGGVYYG 316
Cdd:PHA03247 2576 RPSEPAVTSRARR------PDAPPQSAR--PRAPVDDRGDPRGPAPPS-PLPPDTHAPDPPPPSpspaanepDPHPPPTV 2646
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   317 QPVEDKQNVPS--RQNYSRRI-------DYGSPGNGWKPMPPLDPLGgqqPLNLDYSPHSPGaKEPQsqdslPGQKPINL 387
Cdd:PHA03247 2647 PPPERPRDDPApgRVSRPRRArrlgraaQASSPPQRPRRRAARPTVG---SLTSLADPPPPP-PTPE-----PAPHALVS 2717
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   388 DYDEEPIPQYLHNGLPPYPGSPPrfyPDQLPSGSKPIGRQQPVESSPDASGYPDQQKPLDPDNGlhgskvPPRHSPNPGY 467
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPA---PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG------PPRRLTRPAV 2788
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   468 PLYNESnLYGGLLPPKPDSPVNTTPTPTPNPSSSQAPTPQLANRLHTFPIYPPvdnktsLRNPIQPHYSPSYAGIAH--- 544
Cdd:PHA03247 2789 ASLSES-RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP------PPPGPPPPSLPLGGSVAPggd 2861
                         330       340
                  ....*....|....*....|.
gi 24661363   545 -SRDAPWAKVPVTSTTPAQDP 564
Cdd:PHA03247 2862 vRRRPPSRSPAAKPAAPARPP 2882
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
851-877 1.11e-04

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 40.69  E-value: 1.11e-04
                            10        20
                    ....*....|....*....|....*..
gi 24661363     851 FDCGNGQCLKKEEICDGKKNCPNGKDE 877
Cdd:smart00192    7 FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
291-640 9.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   291 PNRNYPTNKTPLAPMAPTNTGgvyygQPVedkqnvpsrqnysrridygSPGNGWKPMPPLDPLGGQQPLNLDYSPHSPgA 370
Cdd:PHA03247 2814 PAAALPPAASPAGPLPPPTSA-----QPT-------------------APPPPPGPPPPSLPLGGSVAPGGDVRRRPP-S 2868
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   371 KEPQSQDSLPGQKPINLDYDEEPIPQYLHNGLPPYPGSPPRFYPDQLPSGSKPIGRQQPVES-SPDASGYPDQQKPLDPD 449
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQpPPPPPPRPQPPLAPTTD 2948
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   450 NGLHGSKVPPRHSPNPGYPLYNESNLYGGLLPPKPDSPVNTTPTPTPNPSSSQAPTPQLANR--LHTFPIYPPVDNKTSL 527
Cdd:PHA03247 2949 PAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSlaLHEETDPPPVSLKQTL 3028
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   528 RNPIQPHYSpsyagiahSRDAPWAKVPVTSTTPAQDPDPfnPELDEPFYDDVDFLTTTVRNVLVP-----PPfdhkfysP 602
Cdd:PHA03247 3029 WPPDDTEDS--------DADSLFDSDSERSDLEALDPLP--PEPHDPFAHEPDPATPEAGARESPssqfgPP-------P 3091
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 24661363   603 QSTNPSINRNQSASGPNSQAA--------IKEALKLMLRPYFNHSG 640
Cdd:PHA03247 3092 LSANAALSRRYVRSTGRSALAvlieacrrIRRQLRRTRHALLDRSG 3137
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
995-1028 1.93e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.23  E-value: 1.93e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 24661363    995 KCPNNYWLCHTSkECIPPAFVCDNTPDCADKSDE 1028
Cdd:pfam00057    2 TCSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDE 34
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
399-750 9.71e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   399 HNGLPPYPGSPPrfYPDQLPSGSKpiGRQQPVESSPDASGYPDQQKPLDPDNGLHGSKVPP--RHSPN--------PGYP 468
Cdd:PTZ00449  507 HDEPPEGPEASG--LPPKAPGDKE--GEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPakEHKPSkiptlskkPEFP 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   469 LYNESnlyggllpPKPDSPVNTTPTPTPNPSSSQAPTPQLANRLHTFPIYPPVDNKTSLRNPIQPHYSPSyagiahSRDA 548
Cdd:PTZ00449  583 KDPKH--------PKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSS------PERP 648
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   549 PWAKVPVTSTTPAQDPDPFNPELDEPFYDDVDFLTTTVRNVLVPPPFDHKFyspqstnPSINRNQSASGPNSQAAIKEAL 628
Cdd:PTZ00449  649 EGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESF-------ESILKETLPETPGTPFTTPRPL 721
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661363   629 --KLMLRPYFNHSGNAQEQLAQQAESAIVSviskpSTTTTTTPRPTSKTPKTDPDFDAELIKAGEQESLDSVDDDyvfPD 706
Cdd:PTZ00449  722 ppKLPRDEEFPFEPIGDPDAEQPDDIEFFT-----PPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDE---AM 793
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 24661363   707 ARETSRTEQTLDPSTTYASTnfqrSTRRAELDPDTLTATTMKTN 750
Cdd:PTZ00449  794 KRPDSPSEHEDKPPGDHPSL----PKKRHRLDGLALSTTDLESD 833
 
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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