|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1850-2107 |
4.68e-107 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 343.24 E-value: 4.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1850 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1929
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1930 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2009
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2010 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2089
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 767998705 2090 ADSSLLQTNIALQLMEKS 2107
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.48e-102 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 327.78 E-value: 5.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 767998705 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.04e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 767998705 282 VTRRYYYSIKDISIGG 297
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2291-2419 |
2.44e-43 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 155.34 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2291 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2361
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 2362 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2419
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1521-1655 |
1.48e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1521 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1598
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998705 1599 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1655
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1517-1644 |
9.22e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1517 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1596
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998705 1597 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1644
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3161-3312 |
5.11e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 132.16 E-value: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3161 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3239
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998705 3240 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3312
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3184-3313 |
3.39e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3184 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3261
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 3262 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3313
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3189-3314 |
9.98e-30 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 115.98 E-value: 9.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3189 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3268
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767998705 3269 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3314
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2997-3137 |
4.18e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2997 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3074
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998705 3075 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3137
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3014-3139 |
7.41e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3014 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3090
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 3091 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3139
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2605-2745 |
2.40e-25 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 104.42 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2605 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2681
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 2682 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2745
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2624-2745 |
2.37e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2624 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2700
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998705 2701 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2745
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3021-3139 |
1.19e-21 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 92.87 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3021 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3097
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767998705 3098 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3139
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2772-2904 |
1.20e-20 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 90.94 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2772 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2848
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998705 2849 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2904
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2797-2906 |
4.85e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2797 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2872
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767998705 2873 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2906
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1269-1317 |
7.45e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.93 E-value: 7.45e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 1269 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1317
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2631-2745 |
5.38e-15 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 73.99 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2631 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2709
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767998705 2710 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2745
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1268-1310 |
2.72e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.31 E-value: 2.72e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 1268 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1310
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1841-2344 |
3.07e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 79.29 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1902
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1903 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1972
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1973 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2048
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2049 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2128
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2129 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2207
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2208 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2281
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2282 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2342
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 767998705 2343 NK 2344
Cdd:TIGR04523 738 NK 739
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1269-1310 |
1.15e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.15e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998705 1269 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1310
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1359-1410 |
4.69e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 4.69e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 1359 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1410
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
5.56e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 5.56e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
7.67e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1359-1404 |
8.30e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 8.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 1359 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1404
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1359-1405 |
1.73e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 1359 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1405
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1407-1457 |
1.83e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1407 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1457
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2438-2573 |
2.09e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2438 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2511
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998705 2512 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2573
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1689-1735 |
2.25e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.25e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1689 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1735
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
491-538 |
3.21e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1832-2166 |
6.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1832 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1910
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1911 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1982
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1983 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2051
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2052 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2125
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767998705 2126 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2166
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1737-1787 |
7.02e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 7.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1737 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1787
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2393-2571 |
8.40e-11 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 62.82 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2393 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2472
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2473 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2546
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 767998705 2547 PPDFKLPSRLSFPPYKGCIELDDLN 2571
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1408-1456 |
1.12e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 1408 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1456
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
536-583 |
1.39e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.39e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998705 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 583
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.59e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.59e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-531 |
2.56e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.56e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998705 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
5.72e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.72e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 491 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 533
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1736-1788 |
6.25e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 6.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767998705 1736 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1788
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
1.11e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.11e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 426 CSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPF 466
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1690-1737 |
1.29e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1690 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1737
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1408-1450 |
1.87e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 1408 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1450
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1737-1780 |
2.10e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.10e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 1737 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1780
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
4.62e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFC 467
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2800-2904 |
7.37e-09 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 56.27 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2800 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2874
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767998705 2875 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2904
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.38e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1690-1732 |
2.43e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 1690 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1732
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
4.68e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.68e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767998705 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
631-681 |
4.70e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 4.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1859-2355 |
8.10e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1859 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1937
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1938 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2017
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2018 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2097
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2098 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2153
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2154 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2233
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2234 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2313
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 767998705 2314 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2355
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
4.94e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.89 E-value: 4.94e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998705 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.06e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2060-2378 |
1.41e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 54.19 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2060 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2139
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2140 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2219
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2220 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2296
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2297 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2372
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 767998705 2373 MDRIRE 2378
Cdd:COG5185 529 FMRARG 534
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1974-2246 |
4.95e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.34 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1974 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2049
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2050 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2118
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2119 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2190
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998705 2191 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2246
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
6.65e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.42 E-value: 6.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.09e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.42 E-value: 7.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.08e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.08e-05
10 20 30
....*....|....*....|....*....|....*....
gi 767998705 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1859-2390 |
2.13e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1859 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1938
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1939 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2018
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2019 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2082
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2083 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2155
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2156 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2217
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2218 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2290
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2291 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2358
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 767998705 2359 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2390
Cdd:TIGR01612 1336 khnsdINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEI 1374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1841-2378 |
2.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1910
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1911 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1989
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1990 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2061
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2062 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2132
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2133 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2211
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2212 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2289
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2290 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2369
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 767998705 2370 SDNMDRIRE 2378
Cdd:PRK02224 697 RERREALEN 705
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2095-2259 |
4.33e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 46.55 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2095 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2172
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2173 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2247
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 767998705 2248 LNNLQQTLNIVT 2259
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.10e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 5.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998705 355 ACNCHGHAS---NCYYdpdverqqaslntqgiyaGGGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDP------------------GTGQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2440-2566 |
5.69e-05 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 45.10 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2440 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2515
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 2516 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2566
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.05e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998705 356 CNCH--GHASN-CYYDpdverqqaslntqgiyagGGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPD------------------TGQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
684-722 |
3.35e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.35e-04
10 20 30
....*....|....*....|....*....|....*....
gi 767998705 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
6.51e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.03 E-value: 6.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998705 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
6.90e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 6.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998705 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.31e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1668-1791 |
2.31e-03 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 41.52 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1668 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1743
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998705 1744 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1791
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1861-2179 |
6.16e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1861 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1937
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1938 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2004
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2005 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2076
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2077 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2150
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767998705 2151 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2179
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2094-2190 |
6.36e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2094 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2167
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 767998705 2168 GDELvrcavdaATAYENILNAIK 2190
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1850-2107 |
4.68e-107 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 343.24 E-value: 4.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1850 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1929
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1930 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2009
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2010 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2089
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 767998705 2090 ADSSLLQTNIALQLMEKS 2107
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.48e-102 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 327.78 E-value: 5.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 767998705 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.04e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 767998705 282 VTRRYYYSIKDISIGG 297
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2291-2419 |
2.44e-43 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 155.34 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2291 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2361
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 2362 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2419
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1521-1655 |
1.48e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1521 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1598
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998705 1599 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1655
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1517-1644 |
9.22e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1517 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1596
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998705 1597 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1644
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3161-3312 |
5.11e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 132.16 E-value: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3161 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3239
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998705 3240 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3312
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3184-3313 |
3.39e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3184 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3261
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 3262 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3313
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3189-3314 |
9.98e-30 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 115.98 E-value: 9.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3189 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3268
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767998705 3269 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3314
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2997-3137 |
4.18e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2997 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3074
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998705 3075 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3137
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3014-3139 |
7.41e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3014 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3090
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 3091 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3139
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2605-2745 |
2.40e-25 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 104.42 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2605 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2681
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 2682 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2745
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2624-2745 |
2.37e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2624 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2700
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998705 2701 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2745
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3021-3139 |
1.19e-21 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 92.87 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3021 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3097
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767998705 3098 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3139
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2772-2904 |
1.20e-20 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 90.94 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2772 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2848
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998705 2849 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2904
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3021-3141 |
3.49e-18 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 83.14 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3021 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 3096
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998705 3097 LPGNSTISIRAPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPL 3141
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
2797-2906 |
4.85e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2797 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2872
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767998705 2873 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2906
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1269-1317 |
7.45e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.93 E-value: 7.45e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 1269 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1317
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2631-2745 |
5.38e-15 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 73.99 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2631 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2709
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767998705 2710 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2745
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1268-1310 |
2.72e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.31 E-value: 2.72e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 1268 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1310
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1841-2344 |
3.07e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 79.29 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1902
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1903 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1972
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1973 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2048
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2049 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2128
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2129 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2207
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2208 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2281
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2282 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2342
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 767998705 2343 NK 2344
Cdd:TIGR04523 738 NK 739
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3189-3316 |
3.25e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 71.96 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3189 IRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSVAVTIKQHILHLELD------ 3261
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDgearpt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998705 3262 -TDSSYTAGQIPFPpastqEPLHLGGAPANLTTLRI-PVWKSFFGCLRNIHVNHIPV 3316
Cdd:pfam00054 79 gESPLGATTDLDVD-----GPLYVGGLPSLGVKKRRlAISPSFDGCIRDVIVNGKPL 130
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1838-2289 |
3.39e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1838 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEF-ETLQEKAQVns 1916
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQF-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1917 rkaqtlnnnvnraTQSAKELDVKIKNVIRNVHILLKQISgTDGEGNNvpsgdfsREWAE-------AQRMMRELRNRNFG 1989
Cdd:pfam15921 369 -------------SQESGNLDDQLQKLLADLHKREKELS-LEKEQNK-------RLWDRdtgnsitIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1990 KHLREA--EADKRESQLLLNRirtWQKTHQGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAAQAKQANGL 2058
Cdd:pfam15921 428 VQRLEAllKAMKSECQGQMER---QMAAIQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2059 NQENERALGAIQRQVKEINS---LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRS 2135
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2136 AG-----KTSLVEEAEKHARSLQEL--------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKA 2191
Cdd:pfam15921 585 AGamqveKAQLEKEINDRRLELQEFkilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2192 aedaanraasaSESALQTvIKEDLPRKAKTLSSNSDkllnEAKMTQKKLKQEVSPALNNLQQTLNIVTvQKEVIDTNLTT 2271
Cdd:pfam15921 665 -----------SRNELNS-LSEDYEVLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMK 727
|
490 500
....*....|....*....|.
gi 767998705 2272 LRDGLHG---IQRGDIDAMIS 2289
Cdd:pfam15921 728 VAMGMQKqitAKRGQIDALQS 748
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1269-1310 |
1.15e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.15e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998705 1269 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1310
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1359-1410 |
4.69e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 4.69e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 1359 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1410
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
5.56e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 5.56e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
7.67e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1359-1404 |
8.30e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 8.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 1359 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1404
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1839-2381 |
1.41e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.43 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1839 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqEKAQVNSRK 1918
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1919 AQTLNNNVNRatqSAKELDVKIKNVIRN-VHI--LLKQISGTDGEGNNVpSGDFSREWAEAQRMMRELRNRNFGKHLREA 1995
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLeVELnkLEKQKKENKKNIDKF-LTEIKKKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1996 EADKRESQLllnrirtwqktHQGENNglANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKE 2075
Cdd:TIGR04523 174 ELNLLEKEK-----------LNIQKN--IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2076 INSLQSDF----TKYLTTADSsllQTNIALQLMEKsQKEYEK-------LAASLNEARQELSD----KVRELSRsagktS 2140
Cdd:TIGR04523 241 INEKTTEIsntqTQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQLNQLKSEISDlnnqKEQDWNK-----E 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2141 LVEEAEKHARSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKaaedaANRAASASE-SALQTVIKEDLpRKA 2219
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLK-----KELTNSESEnSEKQRELEEKQ-NEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2220 KTLSSNSDKLLNEAkmtqKKLKQEVspalNNLQQTLNIVTVQKEVIDTNLTTLRdglhgIQRGDIDAMISSAKSMVRKAN 2299
Cdd:TIGR04523 373 EKLKKENQSYKQEI----KNLESQI----NDLESKIQNQEKLNQQKDEQIKKLQ-----QEKELLEKEIERLKETIIKNN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2300 DITDEVLDGLNPIQTDVERIKDTygrtqNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPL--------GNISD 2371
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneekkeleEKVKD 514
|
570
....*....|
gi 767998705 2372 NMDRIRELIQ 2381
Cdd:TIGR04523 515 LTKKISSLKE 524
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1359-1405 |
1.73e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 1359 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1405
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1407-1457 |
1.83e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1407 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1457
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2438-2573 |
2.09e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2438 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2511
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998705 2512 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2573
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1689-1735 |
2.25e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.25e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1689 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1735
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1874-2162 |
2.87e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1874 RNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK---AQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHIL 1950
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1951 LKQISGTDGEgnnvpsgdfsrewAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIrtwqkthqgenNGLANSIRDS 2030
Cdd:TIGR02168 749 IAQLSKELTE-------------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------KEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2031 LNEYEAKLSDLRARLQEAAAQAKQA-----------NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2099
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLerriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998705 2100 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSagKTSLVEEAEKHARSLQELAKQLEEI 2162
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
491-538 |
3.21e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1834-2390 |
3.44e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 69.28 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1834 NDLATMGEQLRLVKSQLQglsasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSKIE---GLERELTDLNQEFETLQE 1910
Cdd:TIGR04523 162 NDLKKQKEELENELNLLE---------KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1911 KAQVNSRKAQTLNNNVNRATQ----------------SAKELDV-KIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREW 1973
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTqlnqlkdeqnkikkqlSEKQKELeQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1974 AEaqrmmrELRNRNfgKHLREAEADKRESQLLLNR-------IRTWQKTHQGENNglanSIRDSLNEYEAKLSDLrarlq 2046
Cdd:TIGR04523 313 KS------ELKNQE--KKLEEIQNQISQNNKIISQlneqisqLKKELTNSESENS----EKQRELEEKQNEIEKL----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2047 eaaaqakqanglNQENERALGAIQRQVKEINSLQSDFTKYltTADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQE 2124
Cdd:TIGR04523 376 ------------KKENQSYKQEIKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2125 LSDKVRElsrsagKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASE 2204
Cdd:TIGR04523 442 IKDLTNQ------DSVKELIIKNLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2205 SALQTVIKE---------DLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV--IDTNLTTLR 2273
Cdd:TIGR04523 496 KELKKLNEEkkeleekvkDLTKKISSLKEKIEKLESEKKEKESKISDLED-ELNKDDFELKKENLEKEIdeKNKEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2274 DglhgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIkdtygrtqnEDFKKALTDADNSVNKLTNKLPDLW 2353
Cdd:TIGR04523 575 Q--------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI---------SSLEKELEKAKKENEKLSSIIKNIK 637
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 767998705 2354 RKIESINQQllpLGNISDNMDRIR----ELIQQARDAASKV 2390
Cdd:TIGR04523 638 SKKNKLKQE---VKQIKETIKEIRnkwpEIIKKIKESKTKI 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1832-2166 |
6.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1832 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1910
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1911 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1982
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1983 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2051
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2052 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2125
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767998705 2126 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2166
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1737-1787 |
7.02e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 7.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1737 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1787
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2393-2571 |
8.40e-11 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 62.82 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2393 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2472
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2473 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2546
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 767998705 2547 PPDFKLPSRLSFPPYKGCIELDDLN 2571
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1408-1456 |
1.12e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998705 1408 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1456
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
536-583 |
1.39e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.39e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998705 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 583
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.59e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.59e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-531 |
2.56e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.56e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998705 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
5.72e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.72e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 491 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 533
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1736-1788 |
6.25e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 6.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767998705 1736 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1788
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
1.11e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.11e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 426 CSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPF 466
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1690-1737 |
1.29e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1690 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1737
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1832-2379 |
1.44e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1832 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHmETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK 1911
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1912 AQVNSRKAQTLNNNVNRATQ---SAKELDVKIKNVIRNVHILLK---QISGTDG---EGNNVPSGdFSR--EWAEAQRM- 1979
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKnqsGLSGILGvlsELISVDEG-YEAaiEAALGGRLq 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1980 MRELRNRNFGK----HLREAEADKReSQLLLNRIR--------TWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQE 2047
Cdd:TIGR02168 549 AVVVENLNAAKkaiaFLKQNELGRV-TFLPLDSIKgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2048 AAAQAKQANGLNQENERAL------------GAIQRQ-VKEINSLQS------DFTKYLTTADSSLLQTNIALQLMEKSQ 2108
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRivtldgdlvrpgGVITGGsAKTNSSILErrreieELEEKIEELEEKIAELEKALAELRKEL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2109 KEYEKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAA 2179
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLAR--LEAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIE 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2180 TAYENILNAIKAAedaanraaSASESALQTVIKE--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ-------------EV 2244
Cdd:TIGR02168 786 ELEAQIEQLKEEL--------KALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedieSL 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2245 SPALNNLQQT-------LNIVTVQKEVIDTNLTTLRDglhgiQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVE 2317
Cdd:TIGR02168 858 AAEIEELEELieeleseLEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998705 2318 RIKDTYGRTQ---NEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2379
Cdd:TIGR02168 933 GLEVRIDNLQerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1408-1450 |
1.87e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998705 1408 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1450
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1737-1780 |
2.10e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.10e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 1737 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1780
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1841-2188 |
3.30e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1920
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1921 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEgnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEAD-K 1999
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----------LEELEEELEEAEEELEEAEAELAEAEEAlL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2000 RESQLLLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLQEAAAqakqangLNQENERALGAIQRQVKEINSL 2079
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLER-------LEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2080 QSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSdkvRELSRSAGKTSLVEEAEKHARSLQELAKQL 2159
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA---EAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340
....*....|....*....|....*....
gi 767998705 2160 EEIKRNASGDELVRCAVDAATAYENILNA 2188
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
4.62e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFC 467
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2800-2904 |
7.37e-09 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 56.27 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2800 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2874
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767998705 2875 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2904
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1859-2157 |
1.49e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1859 LLEQMRHMETQAKDLRNQLlnyrSAISNHgskIEGLERELTDLNQEFETLQEK-AQVNSRKAQTLNNNVNRATQSAKELD 1937
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL----ASLEEE---LEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1938 VKIKNVIRNVHILLKQISGTDGEGNNVPSgDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQL--LLNRIRTWQKT 2015
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2016 HQgennglanSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL- 2094
Cdd:TIGR02169 380 FA--------ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIk 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 2095 -----LQTNIALqlMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 2157
Cdd:TIGR02169 452 kqewkLEQLAAD--LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1856-2385 |
1.52e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.96 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1856 SAGLLEQMRHMETQAKDLRNQLLNYRSAIS-------NHGSKIEGLERELTDLNQEFETLQ-EKAQVNSRKAQtLNNNVN 1927
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQklqlekvTTEAKIKKLEEDILLLEDQNSKLSkERKLLEERISE-FTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1928 RATQSAKELDvKIKN----VIRNVHILLKQISGT-----------DGEgnnvpSGDFSREWAEAQRMMRELRnrnfgkhl 1992
Cdd:pfam01576 170 EEEEKAKSLS-KLKNkheaMISDLEERLKKEEKGrqelekakrklEGE-----STDLQEQIAELQAQIAELR-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1993 reAEADKRESQL--LLNRIrtwqKTHQGENNGLANSIRdslnEYEAKLSDLRARLqeaaaqakqanglnqENERALGAIQ 2070
Cdd:pfam01576 236 --AQLAKKEEELqaALARL----EEETAQKNNALKKIR----ELEAQISELQEDL---------------ESERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2071 RQVK-----EINSLQsdfTKYLTTADSsllqTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktslveea 2145
Cdd:pfam01576 291 EKQRrdlgeELEALK---TELEDTLDT----TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMR------------ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2146 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDAANRAASASESALQTV---------IKEDL 2215
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQDSEHKRKKLEGQLQELqarlseserQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2216 PRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LNIVTVQKEVIDTNLTTLRDGLHGIQrgdidamis 2289
Cdd:pfam01576 432 AEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETRQKLNLSTRLRQLEDERNSLQ--------- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2290 saksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2369
Cdd:pfam01576 503 --------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
570
....*....|....*.
gi 767998705 2370 SDNMDRIRELIQQARD 2385
Cdd:pfam01576 568 YDKLEKTKNRLQQELD 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1971-2392 |
1.68e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1971 REWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaa 2050
Cdd:COG4717 88 EEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERL----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2051 qakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2130
Cdd:COG4717 156 ---------EELRELEEELEELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2131 ELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAED 2194
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2195 AANRAASASESALQTVIKEDLPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnltt 2271
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE-------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2272 LRDGLHGIQRGDIDAMISSAK------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKL 2345
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 767998705 2346 TNKLpdlwRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAV 2392
Cdd:COG4717 452 REEL----AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.38e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767998705 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1690-1732 |
2.43e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 1690 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1732
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
4.68e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.68e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767998705 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
631-681 |
4.70e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 4.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2629-2745 |
5.39e-08 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 54.25 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2629 IQTTVDRGLLFFAE--NGDRFISLNIEDGKLMVRYKLNSELPKERGvGDAINNGRDHSI---------QIKIGKLQKRMW 2697
Cdd:pfam00054 1 FRTTEPSGLLLYNGtqTERDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVelerngrsgTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767998705 2698 INVDVQNTIIDGEvfdfSTYYLGGIPIAI--RERFNISTPaFRGCMKNLK 2745
Cdd:pfam00054 80 ESPLGATTDLDVD----GPLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1859-2355 |
8.10e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1859 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1937
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1938 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2017
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2018 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2097
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2098 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2153
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2154 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2233
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2234 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2313
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 767998705 2314 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2355
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1841-2357 |
1.07e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSASAG-LLEQMRHMETQAKDLrnQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1919
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDrILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1920 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnNVPSGDFSREWAEAQR----MMRElRNRNFGKHLREA 1995
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG-------YFPNKKQLEDWLHSKSkeinQTRD-RLAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1996 EADKresqlllNRIRTWQKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAAQAKQANG-----------LNQEN 2062
Cdd:TIGR00606 604 EQNK-------NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDEN 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2063 ERALGAIQRQVK---EINSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT 2139
Cdd:TIGR00606 677 QSCCPVCQRVFQteaELQEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2140 -SLVEEAEKHARSLQELAKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRK 2218
Cdd:TIGR00606 754 qKVNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2219 AKTLSSNSDKLLNEAKMTQkKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTtlrdglhgiQRGDID----AMISSAKSM 2294
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ---------RRQQFEeqlvELSTEVQSL 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998705 2295 VRKANDITDEVLDGLNPIQTDVERiKDTYGRTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 2357
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1844-2183 |
1.75e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1844 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN 1923
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1924 NNVNRATQSAKELDvkiknvirnvhillKQISGTDGEGNNVPSgdfSREWAEAQR-MMRELRNRNFGKhLREAEADKRES 2002
Cdd:PRK02224 377 EAVEDRREEIEELE--------------EEIEELRERFGDAPV---DLGNAEDFLeELREERDELRER-EAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2003 QlllNRIRtwqkthqgENNGL--------------ANSIRDSLNEYEAKLSDLRARLqeaAAQAKQANGLNQENERA--L 2066
Cdd:PRK02224 439 R---ERVE--------EAEALleagkcpecgqpveGSPHVETIEEDRERVEELEAEL---EDLEEEVEEVEERLERAedL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2067 GAIQRQVKEINSLQSDFTKYLTTADSSllqtnialqLMEKSQKeyeklAASLNEARQELSDKVRELSRSAgkTSLVEEAE 2146
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRET---------IEEKRER-----AEELRERAAELEAEAEEKREAA--AEAEEEAE 568
|
330 340 350
....*....|....*....|....*....|....*..
gi 767998705 2147 KHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYE 2183
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1841-2177 |
2.41e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.06 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEkaqvnsrKAQ 1920
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1921 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVpsgdfsreWAEAQRMMRELRNRNFGKHLREAEADKR 2000
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL--------EQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2001 ESQL--LLNRIRTWQKTHQGENNGLANSIRDSLnEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINS 2078
Cdd:COG4372 156 EEQLesLQEELAALEQELQALSEAEAEQALDEL-LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2079 LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQ 2158
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330
....*....|....*....
gi 767998705 2159 LEEIKRNASGDELVRCAVD 2177
Cdd:COG4372 315 DALLAALLELAKKLELALA 333
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1841-2168 |
4.34e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSAS-AGLLEQMRHMEtqakdlrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1919
Cdd:TIGR02169 674 AELQRLRERLEGLKRElSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1920 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQIsgtdgegnNVPSGDFSRE-WAEAQRMMREL---RNRNFG------ 1989
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--------NDLEARLSHSrIPEIQAELSKLeeeVSRIEArlreie 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1990 -----KHLREAEADKrESQLLLNRIRTWQ------KTHQGENNGLANSIRDSLNEYEAKLSDLRARLQeaaaqakqanGL 2058
Cdd:TIGR02169 819 qklnrLTLEKEYLEK-EIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLG----------DL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2059 NQENERA---LGAIQRQVKEINSlqsdftkYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-------- 2127
Cdd:TIGR02169 888 KKERDELeaqLRELERKIEELEA-------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqael 960
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767998705 2128 -KVRELSRSAGKTSL--VEEAEKHARSLQELAKQLEEIKRNASG 2168
Cdd:TIGR02169 961 qRVEEEIRALEPVNMlaIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1841-2161 |
4.74e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNhgskiegLERELTDLNQEFETLQEKAQvnsrKAQ 1920
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-------IEKRLSRLEEEINGIEERIK----ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1921 TLNNNVNRATQSAKELDVKIkNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNfgKHLRE------ 1994
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEeiskit 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1995 ---AEADKRESQLLLNRI-------------RTWQKTHQGEnnglansirdSLNEYEAKLSDLRARLQEAaaqakqangl 2058
Cdd:PRK03918 412 ariGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKE----------LLEEYTAELKRIEKELKEI---------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2059 nQENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLNEARQELSDKVREL 2132
Cdd:PRK03918 472 -EEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350
....*....|....*....|....*....|...
gi 767998705 2133 SRSAG----KTSLVEEAEKHARSLQELAKQLEE 2161
Cdd:PRK03918 549 EKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
4.94e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.89 E-value: 4.94e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998705 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1951-2164 |
5.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1951 LKQISGTDgegnnvpsgDFSREWAEAQRMMRELRNRnfgkhlREAEAD--KRESQLLlNRIRTwQKTHQGENNGLANSIR 2028
Cdd:PRK03918 151 VRQILGLD---------DYENAYKNLGEVIKEIKRR------IERLEKfiKRTENIE-ELIKE-KEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2029 DSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKylTTADSSLLQTNIA-LQLMEKS 2107
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKeLKELKEK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998705 2108 QKEYEKLAASLNEARQELSDKVRELSR----SAGKTSLVEEAEKHARSLQELAKQLEEIKR 2164
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRleeeINGIEERIKELEEKEERLEELKKKLKELEK 352
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.06e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998705 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
3003-3141 |
1.18e-06 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 50.85 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3003 KLPQELLkPRSQFAVDM-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 3076
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998705 3077 GHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 3141
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2060-2378 |
1.41e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 54.19 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2060 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2139
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2140 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2219
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2220 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2296
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2297 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2372
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 767998705 2373 MDRIRE 2378
Cdd:COG5185 529 FMRARG 534
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1802-2256 |
2.53e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1802 HPLTGDCINQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSA----SAGLLEQMRHMET--QAKDLRN 1875
Cdd:TIGR00618 279 LEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkqQSSIEEQRRLLQTlhSQEIHIR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1876 QLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA-TQSAKELDVKIKNVIRNVHILLKQI 1954
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRDLQGQLAHAKKQQELQQR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1955 SGTDGE--GNNVPSGDFSREwAEAQRMMRELRNRNFGK------HLREAEADKRESQLLLNrirtwqktHQGENNGLANS 2026
Cdd:TIGR00618 439 YAELCAaaITCTAQCEKLEK-IHLQESAQSLKEREQQLqtkeqiHLQETRKKAVVLARLLE--------LQEEPCPLCGS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2027 IRdslnEYEAKLSDL-----RARLQEAAAQAKQANGLNQENERALG-AIQRQVK----EINSLQSDFTKYLTTADSSLLQ 2096
Cdd:TIGR00618 510 CI----HPNPARQDIdnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRAslkeQMQEIQQSFSILTQCDNRSKED 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2097 TNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE----LV 2172
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehAL 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2173 RCAVDAATAYENILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQ 2252
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
....
gi 767998705 2253 QTLN 2256
Cdd:TIGR00618 743 QSLK 746
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1974-2246 |
4.95e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.34 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1974 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2049
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2050 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2118
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2119 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2190
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998705 2191 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2246
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1840-2245 |
6.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1840 GEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRnQLLNYRSAISnhgSKIEGLERELTDLNQEFETLQEKAQvnsrkA 1919
Cdd:COG4717 63 GRKPELNLKELKELE------EELKEAEEKEEEYA-ELQEELEELE---EELEELEAELEELREELEKLEKLLQ-----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1920 QTLNNNVNRATQSAKELDVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEADK 1999
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-------LEERL----------------EELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2000 RESQLLLNRIRTWQKTHQgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER--------ALGAIQR 2071
Cdd:COG4717 185 QLSLATEEELQDLAEELE-ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2072 QVKEINSLQSDFTKYLTTAdSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-KVRELSRSAG-----KTSLVEEA 2145
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLV-LGLLALLFLLLAREKASLGKEAEELQALPALEELEEeELEELLAALGlppdlSPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2146 EKHARSLQELAKQLEEIKR------------------NASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESAL 2207
Cdd:COG4717 343 LDRIEELQELLREAEELEEelqleeleqeiaallaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767998705 2208 QTVIKEDLPRKAKTLSSNSDKL---LNEAKMTQKKLKQEVS 2245
Cdd:COG4717 423 EALDEEELEEELEELEEELEELeeeLEELREELAELEAELE 463
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
6.65e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.42 E-value: 6.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.09e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.42 E-value: 7.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.08e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.08e-05
10 20 30
....*....|....*....|....*....|....*....
gi 767998705 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1861-2171 |
1.32e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1861 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTD-------LNQEFETLQEKAQVNSRKAQTLNNNVNRATQSA 1933
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrdeLNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1934 KELDVKIKNVIRNVHILLKQISGTDGEGNNVPS--------------GDFSREW-----AEAQRMMRELRNRnfgKHLRE 1994
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqqtEVLSPEEekelvEKIKELEKELEKA---KKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1995 AEADKREsqlLLNRIRTWQKthqgenngLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEneralgaIQRQVK 2074
Cdd:COG1340 158 KNEKLKE---LRAELKELRK--------EAEEIHKKIKELAEEAQELHEEMIE----------LYKE-------ADELRK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2075 EINSLQSDFTKYLTTADssllqtnialqlMEKsqKEYEKLAASLNEARQELsDKVRELSRSAGKTSLVEEAEKHARSLqe 2154
Cdd:COG1340 210 EADELHKEIVEAQEKAD------------ELH--EEIIELQKELRELRKEL-KKLRKKQRALKREKEKEELEEKAEEI-- 272
|
330
....*....|....*....
gi 767998705 2155 lakqLEEIKRNA--SGDEL 2171
Cdd:COG1340 273 ----FEKLKKGEklTTEEL 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1912-2279 |
1.45e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1912 AQVNSRKAQTLNNnVNRATQSAKELDVKIKNVIRNVHILLKQisgtdgegnnvpsgdfsREWAEA-QRMMRELRNRNFGK 1990
Cdd:TIGR02169 166 AEFDRKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRRE-----------------REKAERyQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1991 HLREAEADKRESQLLLNRIrtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQakqangLNQENER--ALGA 2068
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL---------------ASLEEELEKLTEEISELEKRLEEIEQL------LEELNKKikDLGE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2069 iqrqvKEINSLQSDFTKylTTADSSLLQTNIAL--QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-KTSLVEE- 2144
Cdd:TIGR02169 287 -----EEQLRVKEKIGE--LEAEIASLERSIAEkeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrRDKLTEEy 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2145 -----------------AEKHARSLQELAK----------QLEEIKRNAS--GDELVRcavdAATAYENILNAIKAAEDA 2195
Cdd:TIGR02169 360 aelkeeledlraeleevDKEFAETRDELKDyrekleklkrEINELKRELDrlQEELQR----LSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2196 ANRAASASESAlQTVIKEDlPRKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQQTLNIVTVQKEVIDT-------N 2268
Cdd:TIGR02169 436 INELEEEKEDK-ALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEErvrggraV 512
|
410
....*....|.
gi 767998705 2269 LTTLRDGLHGI 2279
Cdd:TIGR02169 513 EEVLKASIQGV 523
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1860-2391 |
1.48e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 50.79 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1860 LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK 1939
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1940 IKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNR---IRTWQKTH 2016
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLAlalLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2017 QGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINslQSDFTKYLTTadssllq 2096
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDV------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2097 tnialqlmeKSQKEYEKLAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcav 2176
Cdd:COG0840 232 ---------DSKDEIGQLADAFNRMIENLRELVGQVRESA--EQVASASEELAASAEELAAGAEEQAASLE--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2177 DAATAYENILNAIKaaedaanraaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQKKLK---QEVSPALNNL-- 2251
Cdd:COG0840 292 ETAAAMEELSATVQ----------EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGIEEIResvEETAETIEELge 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2252 --QQTLNIVTVQKEVID-TNLTTL-------RDGLHGiqRG--------------------DIDAMISSAKSMVRKANDI 2301
Cdd:COG0840 359 ssQEIGEIVDVIDDIAEqTNLLALnaaieaaRAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2302 TDEVLDGlnpIQTDVERIKDTygrtqnedfKKALTDADNSVNKLTNKLpdlwRKI-ESINQQLLPLGNISDNMDRIRELI 2380
Cdd:COG0840 437 MEEGSEE---VEEGVELVEEA---------GEALEEIVEAVEEVSDLI----QEIaAASEEQSAGTEEVNQAIEQIAAAA 500
|
570
....*....|.
gi 767998705 2381 QQARDAASKVA 2391
Cdd:COG0840 501 QENAASVEEVA 511
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1859-2390 |
2.13e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1859 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1938
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1939 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2018
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2019 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2082
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2083 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2155
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2156 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2217
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2218 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2290
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2291 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2358
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 767998705 2359 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2390
Cdd:TIGR01612 1336 khnsdINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEI 1374
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2065-2351 |
2.45e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 48.95 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2065 ALGAIQRQVKEINSLQSDFTKYLTtadSSLLQTNIALQLMEKSQKEYEklaaSLNEARQELSDKVRELSRSAGK------ 2138
Cdd:pfam06008 6 SLTGALPAPYKINYNLENLTKQLQ---EYLSPENAHKIQIEILEKELS----SLAQETEELQKKATQTLAKAQQvnaese 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2139 ------TSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcavdaATAYENILNAIKAAEDAANRAASASESALQTVIK 2212
Cdd:pfam06008 79 rtlghaKELAEAIKNLIDNIKEINEKVATLGENDF-----------ALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2213 EDLpRKAKtlssnsdKLLNEAKMTQKKLKQEVSPALNNLQQTLNivtvqkeviDTNlttlrDGLHgiqrgDIDAMISSAK 2292
Cdd:pfam06008 148 AEL-KAAQ-------DLLSRIQTWFQSPQEENKALANALRDSLA---------EYE-----AKLS-----DLRELLREAA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998705 2293 SMVRKANDITDEVLDGLNPIQTDVERIkdtygRTQNEDFKKALTDADNSV---NKLTNKLPD 2351
Cdd:pfam06008 201 AKTRDANRLNLANQANLREFQRKKEEV-----SEQKNQLEETLKTARDSLdaaNLLLQEIDD 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1841-2378 |
2.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1910
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1911 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1989
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1990 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2061
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2062 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2132
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2133 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2211
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2212 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2289
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2290 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2369
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 767998705 2370 SDNMDRIRE 2378
Cdd:PRK02224 697 RERREALEN 705
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1843-2173 |
2.58e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1843 LRLVKSQLQG-----LSASAGL---LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 1914
Cdd:pfam15921 435 LKAMKSECQGqmerqMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1915 NSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDgegnnvpsgdfsrEWAEAQRMMRELRNRNFGKH 1991
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKD-------------KVIEILRQQIENMTQLVGQH 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1992 LREAEADKRESQLLLNRIRTwQKTHQGENNGLANSIRDSLNEYEAKLSDL---RARLQEAAAQA-KQANGLNQENERALG 2067
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEIND-RRLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSERlRAVKDIKQERDQLLN 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2068 AIQRQVKEINSLQSDF---------------------TKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLneaRQELS 2126
Cdd:pfam15921 661 EVKTSRNELNSLSEDYevlkrnfrnkseemetttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM---QKQIT 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767998705 2127 DKVRELSRSAGKTSLVEEA------EKH------ARSLQELAKQLEEIKRNASGDELVR 2173
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAmtnankEKHflkeekNKLSQELSTVATEKNKMAGELEVLR 796
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1811-2079 |
3.16e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1811 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGlsasaglLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1890
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-------AEDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1891 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDGEGNNVPSg 1967
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKlaeLKERIESLERIRTLLAAIADAEDEIER- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1968 dfSREWAEAQRMMRELRnrnfgkhlREAEADKREsqlllnRIRTWQKTHQGENNGLANSIRDSLNEY----EAKLSDLRA 2043
Cdd:PRK02224 611 --LREKREALAELNDER--------RERLAEKRE------RKRELEAEFDEARIEEAREDKERAEEYleqvEEKLDELRE 674
|
250 260 270
....*....|....*....|....*....|....*.
gi 767998705 2044 RlqeaaaqakqanglNQENERALGAIQRQVKEINSL 2079
Cdd:PRK02224 675 E--------------RDDLQAEIGAVENELEELEEL 696
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1974-2190 |
3.25e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1974 AEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRtwqkthqgENNGL------ANSIRDSLNEYEAKLSDLRARLQE 2047
Cdd:COG3206 171 EEARKALEFLEEQ-----LPELRKELEEAEAALEEFR--------QKNGLvdlseeAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2048 AAAQAKQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLT--TADSSL---LQTNIAlQLMEKSQKEYEKLAA 2116
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSAryTPNHPDviaLRAQIA-ALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998705 2117 SLNEARQELSDKVRELSRSagktslVEEAEKHARSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 2190
Cdd:COG3206 317 SLEAELEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1976-2305 |
3.94e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1976 AQRMmRELRNRnfgkhLREAEADkresqLLLNRIRtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQA 2055
Cdd:TIGR02168 212 AERY-KELKAE-----LRELELA-----LLVLRLE--------ELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2056 NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL--LQTNIA-----LQLMEKSQKEYEKLAASLNEARQELSDK 2128
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2129 VrelsrsagkTSLVEEAEKHARSLQELAKQLEEIKRNAsgdELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQ 2208
Cdd:TIGR02168 353 L---------ESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2209 TVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQrgdidAMI 2288
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQ-----ARL 491
|
330
....*....|....*..
gi 767998705 2289 SSAKSMVRKANDITDEV 2305
Cdd:TIGR02168 492 DSLERLQENLEGFSEGV 508
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2095-2259 |
4.33e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 46.55 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2095 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2172
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2173 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2247
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 767998705 2248 LNNLQQTLNIVT 2259
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1992-2310 |
4.84e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1992 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQR 2071
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEEL----------EELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2072 QVKEINSLQSDFTKY------LTTADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEA 2145
Cdd:COG4372 99 AQEELESLQEEAEELqeeleeLQKERQDLEQQRKQL---EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2146 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSN 2225
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2226 SDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEV 2305
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
....*
gi 767998705 2306 LDGLN 2310
Cdd:COG4372 336 LAELA 340
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1811-1941 |
5.01e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1811 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1890
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 1891 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIK 1941
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.10e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 5.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998705 355 ACNCHGHAS---NCYYdpdverqqaslntqgiyaGGGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDP------------------GTGQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2440-2566 |
5.69e-05 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 45.10 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2440 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2515
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767998705 2516 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2566
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1828-2141 |
5.92e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1828 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFE 1906
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1907 TLQEKaqvnsrkaqtlnnnVNRATQSAKELDVKIKNVIRNvhillkqisgtdgegnnvpsgdfsrewaeAQRMMRE---- 1982
Cdd:COG4942 87 ELEKE--------------IAELRAELEAQKEELAELLRA-----------------------------LYRLGRQppla 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1983 --LRNRNFGKHLREAEADKRESQLLLNRIRTWQKThqgennglansiRDSLNEYEAKLSDLRARLqeaaaqakqanglnq 2060
Cdd:COG4942 124 llLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------LAELAALRAELEAERAEL--------------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2061 enERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2140
Cdd:COG4942 177 --EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 767998705 2141 L 2141
Cdd:COG4942 255 L 255
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1872-2393 |
7.31e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1872 DLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN---NNVNRATQSAKELDVKIK------- 1941
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKtaesdls 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1942 ----------------------------NVIRNVHILLKQI-------SGTDGEGNNVPSG--------DFSREWAEAQR 1978
Cdd:PRK01156 267 meleknnyykeleerhmkiindpvyknrNYINDYFKYKNDIenkkqilSNIDAEINKYHAIikklsvlqKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1979 MMRELRN-------------------RNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLS 2039
Cdd:PRK01156 347 RYDDLNNqilelegyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2040 DLRARLQEAAAQAK----QANGLNQENERALGAIQRQVKEINSLQSDFTKylttaDSSLLQTNIalqlmeksqKEYEKLA 2115
Cdd:PRK01156 427 SLNQRIRALRENLDelsrNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE-----KKSRLEEKI---------REIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2116 ASLNEARQELsdkVRELSRSAGKTslVEEAEKHARSLQELAKQLEEIKrnasgDELVRCAvDAATAYENILNAIKAAEDA 2195
Cdd:PRK01156 493 KDIDEKIVDL---KKRKEYLESEE--INKSINEYNKIESARADLEDIK-----IKINELK-DKHDKYEEIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2196 ANRAASASESALQTVI-----------KEDLPRKAKTLSSNSDKLLNE----AKMTQKKLKqEVSPALNNLQQTLNIVTV 2260
Cdd:PRK01156 562 DLDSKRTSWLNALAVIslidietnrsrSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIR-EIENEANNLNNKYNEIQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2261 QKEVIDTNLTTLRDglHGIQRGDIDAMISSAKSMVRKANDITDEvldgLNPIQTDVERIKDTYGRtqnedfKKALTDADN 2340
Cdd:PRK01156 641 NKILIEKLRGKIDN--YKKQIAEIDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRAR------LESTIEILR 708
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 767998705 2341 S-VNKLTNKLPDLWRKIESINQQLLPLGNIsdnmDRIREliqqardAASKVAVP 2393
Cdd:PRK01156 709 TrINELSDRINDINETLESMKKIKKAIGDL----KRLRE-------AFDKSGVP 751
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1836-2181 |
1.07e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1836 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN----- 1902
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1903 --QEFETLQEKAQVNSRKAQTLNNNVN--RATQSAKE------------------------------LDVKiknvIRNVH 1948
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVDalRLRLEEKEsflnkktkqlqdlteekstlageirdlkdmLDVK----ERKIN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1949 ILLKQISgtdgegnnvpsgDFSREWAEAQRMMRELRNRNFGKH------------LREAEADK------------RESQL 2004
Cdd:pfam10174 398 VLQKKIE------------NLQEQLRDKDKQLAGLKERVKSLQtdssntdtalttLEEALSEKeriierlkeqreREDRE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2005 LLNRIRTWQKthqgENNGL---ANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENEralGAIQRQVKEINSLQS 2081
Cdd:pfam10174 466 RLEELESLKK----ENKDLkekVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE---IAVEQKKEECSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2082 DFTKYLTTADSSLLQTNIA--LQLME-----------KSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL-VEEAEK 2147
Cdd:pfam10174 539 QLKKAHNAEEAVRTNPEINdrIRLLEqevarykeesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRqMKEQNK 618
|
410 420 430
....*....|....*....|....*....|....
gi 767998705 2148 HARSLQelAKQLEEIKRNASGDELVRCAVDAATA 2181
Cdd:pfam10174 619 KVANIK--HGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1862-2093 |
1.67e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1862 QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQsakeldvKIK 1941
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1942 NVIRNVhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFGKHLREAEADKRESQLLLNRIRTWQK 2014
Cdd:COG3883 90 ERARAL-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767998705 2015 THQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSS 2093
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1835-2159 |
1.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1835 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE 1910
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1911 KAQVNSRkaQTLNNNVNRATQSAKELDVKiknvirnvHILLKQISGTDGEGNnvpsgdfsREWAEAQRMMRELRNR--NF 1988
Cdd:COG4913 742 LARLELR--ALLEERFAAALGDAVERELR--------ENLEERIDALRARLN--------RAEEELERAMRAFNREwpAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1989 GKHLREAEADKRESQLLLNRIrtwqkthqgENNGLAnsirdslnEYEAKLSDLRARLQEAAAQakqanGLNQENERALGA 2068
Cdd:COG4913 804 TADLDADLESLPEYLALLDRL---------EEDGLP--------EYEERFKELLNENSIEFVA-----DLLSKLRRAIRE 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2069 IQRQVKEIN-SL-QSDFtkyltTADSSllqtniaLQLmeksqkEYEKlaaSLNEARQELSDKVRELSRSAGKTSLvEEAE 2146
Cdd:COG4913 862 IKERIDPLNdSLkRIPF-----GPGRY-------LRL------EARP---RPDPEVREFRQELRAVTSGASLFDE-ELSE 919
|
330
....*....|...
gi 767998705 2147 KHARSLQELAKQL 2159
Cdd:COG4913 920 ARFAALKRLIERL 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1886-2396 |
2.15e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1886 NHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNvirnvHILLKQISGTDGEGNNVP 1965
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA-----RDSLIQSLATRLELDGFE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1966 SGDFS-REWAEAQRMMRELRN---RNFGKHLREAEADKRESQLLLNRIRTwqkthqgENNGLANSIRDSLNEYEAKLSDL 2041
Cdd:TIGR00606 384 RGPFSeRQIKNFHTLVIERQEdeaKTAAQLCADLQSKERLKQEQADEIRD-------EKKGLGRTIELKKEILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2042 RARLqeaaaqakqanglnQENERALGAIQRQVKeinsLQSDFTKYLttADSSLLQTNIALQLMEKSQKEYEKLAASLNEA 2121
Cdd:TIGR00606 457 KFVI--------------KELQQLEGSSDRILE----LDQELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2122 RQELSDKVRELSRSagKTSLvEEAEKHARSLQELAKQLEEIKRNASgDELVRCA---------VDAATAYENILNAIKAA 2192
Cdd:TIGR00606 517 LRKLDQEMEQLNHH--TTTR-TQMEMLTKDKMDKDEQIRKIKSRHS-DELTSLLgyfpnkkqlEDWLHSKSKEINQTRDR 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2193 EDAANRAASASESaLQTVIKEDLPRKAKTLSSNSDKLLN-------EAKMtqKKLKQEVSPAlnnlQQTLNIVTVQKEVI 2265
Cdd:TIGR00606 593 LAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDvcgsqdeESDL--ERLKEEIEKS----SKQRAMLAGATAVY 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2266 DTNLTTLRDGLHG----IQR-----GDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEdfkkalt 2336
Cdd:TIGR00606 666 SQFITQLTDENQSccpvCQRvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI------- 738
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998705 2337 dadnsVNKLTNKLPDLWRKIESINQQLLPL-GNISDN---MDRIRELIQQARDAASKVAVPMRF 2396
Cdd:TIGR00606 739 -----IDLKEKEIPELRNKLQKVNRDIQRLkNDIEEQetlLGTIMPEEESAKVCLTDVTIMERF 797
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.05e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998705 356 CNCH--GHASN-CYYDpdverqqaslntqgiyagGGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPD------------------TGQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
684-722 |
3.35e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.35e-04
10 20 30
....*....|....*....|....*....|....*....
gi 767998705 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1841-2134 |
3.40e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1841 EQLRLVKSQLQGLSASAGLLEQMRH--------METQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA 1912
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1913 QVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQI----SGTDGEGNnvpsgdfSREWAEAQRMMRELRNRNF 1988
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleSELEALLN-------ERASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1989 GKHLREAEADKRESQLLLNRIRTwqkthqgennglansirdSLNEYEAKLSDLRARLQEAAAQakqangLNQENERALGA 2068
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELRE------------------KLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEE 955
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998705 2069 IQRQVKEINSLQS---DFTKYLTTADSSLLQTNI-ALQLMEKSQKEYEKLAA---SLNEARQELSDKVRELSR 2134
Cdd:TIGR02168 956 AEALENKIEDDEEearRRLKRLENKIKELGPVNLaAIEEYEELKERYDFLTAqkeDLTEAKETLEEAIEEIDR 1028
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1867-2140 |
3.70e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1867 ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRN 1946
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1947 VhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFgkhLREAEADKREsqlllnrirtwqkthqge 2019
Cdd:COG3883 95 L-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADL---LEELKADKAE------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2020 nnglansirdsLNEYEAKLSDLRARLQEaaaqakqangLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2099
Cdd:COG3883 145 -----------LEAKKAELEAKLAELEA----------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767998705 2100 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2140
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1697-1789 |
6.51e-04 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 42.77 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1697 NQCQDGSGICVNCQHNTAGEhCERCQEGYYGNAV-HGSCRacPCPHTNSFATGCVVNG----GDVRCSCKAGYT------ 1765
Cdd:cd13406 16 HECPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVnYEPCK--PCTQCNQRSGSEEKQKctktSDTVCRCRPGTQpldsyk 92
|
90 100
....*....|....*....|....*
gi 767998705 1766 -GTQCERCAPGYFGNPQkfGGSCQP 1789
Cdd:cd13406 93 pGVDCVPCPPGHFSRGD--NQACKP 115
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
6.51e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.03 E-value: 6.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998705 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
6.90e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 6.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998705 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1890-2167 |
7.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1890 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAK----ELDVK-IKNVIRNVHILLKQISGTdgegnnv 1964
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdEIDVAsAEREIAELEAELERLDAS------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1965 pSGDFS---REWAEAQRMMRELRnrnfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYeakLSDL 2041
Cdd:COG4913 684 -SDDLAaleEQLEELEAELEELE-----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2042 RARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFtKYLTTADSSLLQTNIAlqLMEKSQKEYEKLAAS-LNE 2120
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDADLE--SLPEYLALLDRLEEDgLPE 831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767998705 2121 ARQELSDKVRELSRsAGKTSLVEEAEKHARSLQElakQLEEIkrNAS 2167
Cdd:COG4913 832 YEERFKELLNENSI-EFVADLLSKLRRAIREIKE---RIDPL--NDS 872
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2056-2256 |
1.30e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2056 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 2131
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2132 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 2188
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998705 2189 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 2256
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEELKEKLT 317
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.31e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998705 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1832-2124 |
1.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1832 LLNDLAT--MGEQLRLVKSQLQglSASAGLLEQMRHMETQAKDLRNQLLNYRSA--ISNHGSKIEGLERELTDLNQEFET 1907
Cdd:COG3206 153 VANALAEayLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1908 LQEKAQVNSRKAQTLNNNVNRATQSAKEL--DVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRN 1985
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQ-------LRAQL-------------------AELEAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1986 RNFGKHLREAEADKRESQLllnrirtwqkthqgeNNGLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEnera 2065
Cdd:COG3206 285 RYTPNHPDVIALRAQIAAL---------------RAQLQQEAQRILASLEAELEALQAREAS----------LQAQ---- 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767998705 2066 LGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEKSQKEYEKLAASLNEARQE 2124
Cdd:COG3206 336 LAQLEARLAELPELEAELRR---------LEREV-----EVARELYESLLQRLEEARLA 380
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1884-2371 |
1.81e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1884 ISNHGSKIEGLERELTDLN---QEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE 1960
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIeliKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEEL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1961 GNNVPSG--DFSREWAEAQRMMRELRNRNFGKHLREAEAD-----------------KRESQLLLNRIR----------- 2010
Cdd:PTZ00440 604 INEALFNkeKFINEKNDLQEKVKYILNKFYKGDLQELLDElshflddhkylyheaksKEDLQTLLNTSKneyeklefmks 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2011 ------------------TWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQR 2071
Cdd:PTZ00440 684 dnidniiknlkkelqnllSLKENIIKKQlNNIEQDISNSLNQYTIKYNDLKSSI--------------EEYKEEEEKLEV 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2072 QVKEINSLQSDFTKYLTTADSSLLQ-TNIALQLMEK----SQKEyEKLAASLNEARQELSDKVRELSRSAGKTSLVE-EA 2145
Cdd:PTZ00440 750 YKHQIINRKNEFILHLYENDKDLPDgKNTYEEFLQYkdtiLNKE-NKISNDINILKENKKNNQDLLNSYNILIQKLEaHT 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2146 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAAS------ASESALQTV--------- 2210
Cdd:PTZ00440 829 EKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTlniainRSNSNKQLVehllnnkid 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2211 IKEDLPRKAKTLSSN-----SDK--LLNEAKMTQKKLKQEVSPA-LNNL----QQTLNIVTVQKEVIDTNLTTLRDGLHG 2278
Cdd:PTZ00440 909 LKNKLEQHMKIINTDniiqkNEKlnLLNNLNKEKEKIEKQLSDTkINNLkmqiEKTLEYYDKSKENINGNDGTHLEKLDK 988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2279 IQ------RGDIDAMISSAKSMVRKANDIT----DEVLDGLNPIQTD---------------VERIKDTYG-RTQNEDFK 2332
Cdd:PTZ00440 989 EKdewehfKSEIDKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEkgkeieekvdqyislLEKMKTKLSsFHFNIDIK 1068
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767998705 2333 KALTDA-DNSVNKLTNKLPDLWRKIESINQQLLPLGNISD 2371
Cdd:PTZ00440 1069 KYKNPKiKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSH 1108
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2057-2336 |
2.14e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2057 GLNQENERALGAIQRQVKEIN-SLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYE-----------KLAASLNEARQE 2124
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtgiqnltaeieQGQESLTENLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2125 LSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA--SGDELVRCAVDAATAYENILNAIKAAEDAANRAASA 2202
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2203 SESALQTVIKEdLPRKAKTLSSNSDKLLNEAkmtQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRG 2282
Cdd:COG5185 439 VSKLLNELISE-LNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998705 2283 DIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDT-----------YGRTQNEDFKKALT 2336
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASnaktdgqaanlRTAVIDELTQYLST 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1819-1998 |
2.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1819 AEECDDCDSCVMTLlnDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHG--------S 1889
Cdd:COG4913 268 RERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1890 KIEGLERELTDLNQEFETLQEKAQV--------------NSRKAQ----TLNNNVNRATQSAKELDVKIKNVIRNVHILL 1951
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAAlglplpasaeefaaLRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767998705 1952 KQISGTDGEGNNVPsgdfsrewAEAQRMMRELRnrnfgKHLREAEAD 1998
Cdd:COG4913 426 AEIASLERRKSNIP--------ARLLALRDALA-----EALGLDEAE 459
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1668-1791 |
2.31e-03 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 41.52 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1668 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1743
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998705 1744 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1791
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1835-2428 |
2.90e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1835 DLATMGEQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA-- 1912
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD-IETAAADQ-EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIke 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1913 ------------QVNSRKA----------------QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE---- 1960
Cdd:pfam12128 387 qnnrdiagikdkLAKIREArdrqlavaeddlqaleSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllql 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1961 GNNVPSGDFSREWAE--------AQRMMRELRNR--NFGKHLREAEA---------DKRESQL------LLNRIRT---- 2011
Cdd:pfam12128 467 ENFDERIERAREEQEaanaeverLQSELRQARKRrdQASEALRQASRrleerqsalDELELQLfpqagtLLHFLRKeapd 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2012 -----------------------WQKTHQGENN--GLANSI-RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERA 2065
Cdd:pfam12128 547 weqsigkvispellhrtdldpevWDGSVGGELNlyGVKLDLkRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2066 LGAIQRQVKEINSLQSDFTKYLTTADSSLLQ-----TNIALQLME-------KSQKEYEKLAASLN-------------- 2119
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRlfdekQSEKDKKNKalaerkdSANERLNSLEAQLKqldkkhqawleeqk 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2120 ----EARQELSDKVREL--SRSAGKTSLVEEAEKHARSLQELAKQLEE------IKRNASGDELVRCAVDAATAYENILN 2187
Cdd:pfam12128 707 eqkrEARTEKQAYWQVVegALDAQLALLKAAIAARRSGAKAELKALETwykrdlASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2188 AIKAAEDAANRAASASESALQtvikeDLPRKAKTLSSNSDKLLnEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDT 2267
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQ-----RRPRLATQLSNIERAIS-ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2268 NLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERikdtygrtQNEDFKKALTDADNSvnkltn 2347
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK--------YVEHFKNVIADHSGS------ 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2348 klpDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVrLPNDLEDLkgYTSLSLFLQRPN 2427
Cdd:pfam12128 927 ---GLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSI-LGVDLTEF--YDVLADFDRRIA 1000
|
.
gi 767998705 2428 S 2428
Cdd:pfam12128 1001 S 1001
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1861-2389 |
3.61e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1861 EQMRHMETQAKDLRNQLLNyrsaISNHGSKIEGLERELTDLNQEFETLQE--KAQVNSRKaqTLNNNVNRATQSAKELDV 1938
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLE----IDDEIIYINKLKLELKEKIKNISDKNEyiKKAIDLKK--IIENNNAYIDELAKISPY 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1939 KIKNVIRNVHILLKQISGtdgEGNNVPSGDFSREWAEAQRMMRE----------------------------LRNRNFGK 1990
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKS---ELSKIYEDDIDALYNELSSIVKEnaidntedkaklddlkskidkeydkiqnMETATVEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1991 HLREAEADKREsqlLLNRIRTWQKTHQGENNG---------------LANSI------RDSLNEYEAKLSDLRARLqeaA 2049
Cdd:TIGR01612 723 HLSNIENKKNE---LLDIIVEIKKHIHGEINKdlnkiledfknkekeLSNKIndyakeKDELNKYKSKISEIKNHY---N 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2050 AQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLT----TADSSLLQTNIALQL----MEKSQKEYEKLAASLNEA 2121
Cdd:TIGR01612 797 DQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINemkfMKDDFLNKVDKFINFenncKEKIDSEHEQFAELTNKI 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2122 RQELSDKvrELSRSAGK----TSLVEEA----EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNA-IKAA 2192
Cdd:TIGR01612 877 KAEISDD--KLNDYEKKfndsKSLINEInksiEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKnIDTI 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2193 EDAANRAASASESALQTVI--KEDLPRKAKTLS-----SNSDKLL---NEAKMTQKKLKQ--------EVSPALNNLQQt 2254
Cdd:TIGR01612 955 KESNLIEKSYKDKFDNTLIdkINELDKAFKDASlndyeAKNNELIkyfNDLKANLGKNKEnmlyhqfdEKEKATNDIEQ- 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2255 lNIVTVQKEV------IDTNLTTLRDglhgiqrgDIDAMISSAKSMVRKanditdEVLDGLNPIQTDVERIKDTYGRTQN 2328
Cdd:TIGR01612 1034 -KIEDANKNIpnieiaIHTSIYNIID--------EIEKEIGKNIELLNK------EILEEAEINITNFNEIKEKLKHYNF 1098
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998705 2329 EDF-KKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDN-MDRIRELIQQARDAASK 2389
Cdd:TIGR01612 1099 DDFgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENyIDEIKAQINDLEDVADK 1161
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1972-2159 |
3.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1972 EWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS----LNEYEAKLSDLRARLqe 2047
Cdd:COG4913 282 RLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLEREL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2048 aaaqakqanglnQENERALGAIQRQVKEI----NSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQ 2123
Cdd:COG4913 355 ------------EERERRRARLEALLAALglplPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRR 419
|
170 180 190
....*....|....*....|....*....|....*.
gi 767998705 2124 ELSDKVRELSRSAGKTSLVEEAEKHARslQELAKQL 2159
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALR--DALAEAL 453
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2058-2153 |
3.67e-03 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 40.55 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2058 LNQENERA-LGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRsa 2136
Cdd:pfam06009 24 QNLENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ----LEVNSSSLSDNISRIKE-- 97
|
90
....*....|....*..
gi 767998705 2137 gktsLVEEAEKHARSLQ 2153
Cdd:pfam06009 98 ----LIAQARKAANSIK 110
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1968-2173 |
3.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1968 DFSREWAEAQRMMRELRNRnFGKHLREAEADKRESQLLlnrirtwQKTHQgennglanSIRDSLN-------------EY 2034
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDL-------EQDYQ--------AASDHLNlvqtalrqqekieRY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2035 EAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQK----- 2109
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglp 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998705 2110 --EYEKLAASLNEAR---QELSDKVRELSRsagKTSLVEEA-EKHARSLQELAKQLEEIKRNASGD---ELVR 2173
Cdd:PRK04863 434 dlTADNAEDWLEEFQakeQEATEELLSLEQ---KLSVAQAAhSQFEQAYQLVRKIAGEVSRSEAWDvarELLR 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1837-2119 |
5.32e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1837 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVN 1915
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1916 SRKAQTLNNNvnratqsaKELDvkiknvirnvhILLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRnrnfgKHLREA 1995
Cdd:COG1579 79 EEQLGNVRNN--------KEYE-----------ALQKEI-------------------ESLKRRISDLE-----DEILEL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1996 EaDKREsqlllnrirtwqkthqgennglanSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQrqvKE 2075
Cdd:COG1579 116 M-ERIE------------------------ELEEELAELEAELAELEAEL----------EEKKAELDEELAELE---AE 157
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767998705 2076 INSLQSDFTKYLTTADSSLLqtnialqlmeksqKEYEKLAASLN 2119
Cdd:COG1579 158 LEELEAEREELAAKIPPELL-------------ALYERIRKRKN 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1861-2179 |
6.16e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1861 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1937
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1938 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2004
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2005 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2076
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2077 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2150
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767998705 2151 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2179
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2094-2190 |
6.36e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2094 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2167
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 767998705 2168 GDELvrcavdaATAYENILNAIK 2190
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3175-3311 |
6.60e-03 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 40.42 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 3175 HSVLLGPEFKLVFSIRPR-SLTGILIHI-GSQPGKHLCVYLEAGKVTAS-MDSGAGGTSTSVT-PKQSLCDGQWHSVAVT 3250
Cdd:smart00210 46 FPSGLPEDFSLLTTFRQTpKSRGVLFAIyDAQNVRQFGLEVDGRANTLLlRYQGVDGKQHTVSfRNLPLADGQWHKLALS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998705 3251 IKQHILHLELDTDSsytAGQIPFPPAStQEPLHLGGapANLTTLRIPVWKSFFGCLRNIHV 3311
Cdd:smart00210 126 VSGSSATLYVDCNE---IDSRPLDRPG-QPPIDTDG--IEVRGAQAADRKPFQGDLQQLKI 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1992-2170 |
8.50e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 1992 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQE---NERALGA 2068
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRI----------RALEQElaaLEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998705 2069 IQRQV----KEINSLQSDFTKYLTTA--------------DSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2130
Cdd:COG4942 88 LEKEIaelrAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767998705 2131 ELSR-SAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE 2170
Cdd:COG4942 168 ELEAeRAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| |
