|
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 ... |
1853-2110 |
4.69e-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: 4.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1853 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1932
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1933 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2012
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2013 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2092
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 767998703 2093 ADSSLLQTNIALQLMEKS 2110
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.65e-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: 5.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 767998703 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.06e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 767998703 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 ... |
2294-2422 |
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 767998703 2294 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2364
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 2365 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2422
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1524-1658 |
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 767998703 1524 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1601
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998703 1602 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1658
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1520-1647 |
9.23e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1520 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1599
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998703 1600 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1647
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3164-3315 |
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 767998703 3164 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3242
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998703 3243 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3315
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3187-3316 |
3.40e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 3187 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3264
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998703 3265 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3316
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3192-3317 |
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 767998703 3192 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3271
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767998703 3272 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3317
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3000-3140 |
4.19e-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: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 3000 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3077
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998703 3078 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3140
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3017-3142 |
7.42e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 3017 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3093
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998703 3094 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3142
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2608-2748 |
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 767998703 2608 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2684
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 2685 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2748
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2627-2748 |
2.38e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2627 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2703
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998703 2704 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2748
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3024-3142 |
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 767998703 3024 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3100
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767998703 3101 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3142
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2775-2907 |
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 767998703 2775 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2851
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998703 2852 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2907
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2800-2909 |
4.86e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2800 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2875
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767998703 2876 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2909
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1272-1320 |
7.32e-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: 7.32e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998703 1272 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1320
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2634-2748 |
5.39e-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: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2634 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2712
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767998703 2713 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2748
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1271-1313 |
2.67e-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: 2.67e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 1271 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1313
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1844-2347 |
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 767998703 1844 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1905
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1906 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1975
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1976 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2051
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2052 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2131
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2132 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2210
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2211 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2284
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2285 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2345
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 767998703 2346 NK 2347
Cdd:TIGR04523 738 NK 739
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1272-1313 |
1.17e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.17e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998703 1272 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1313
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1362-1413 |
4.64e-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: 4.64e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767998703 1362 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1413
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
5.51e-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: 5.51e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
7.68e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.68e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998703 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1362-1407 |
8.22e-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: 8.22e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998703 1362 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1407
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1362-1408 |
1.74e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998703 1362 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1408
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1410-1460 |
1.82e-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: 1.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1410 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1460
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2441-2576 |
2.10e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2441 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2514
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998703 2515 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2576
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1692-1738 |
2.23e-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: 2.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1692 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1738
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 |
3.18e-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: 3.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998703 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1835-2169 |
6.71e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1835 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1913
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1914 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1985
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1986 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2054
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2055 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2128
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767998703 2129 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2169
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1740-1790 |
6.82e-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: 6.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1740 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1790
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2396-2574 |
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 767998703 2396 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2475
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2476 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2549
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 767998703 2550 PPDFKLPSRLSFPPYKGCIELDDLN 2574
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1411-1459 |
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 767998703 1411 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1459
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 |
1.38e-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: 1.38e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998703 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 |
1.57e-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: 1.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 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 |
2.52e-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: 2.52e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998703 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 767998703 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 ... |
1739-1791 |
6.13e-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: 6.13e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767998703 1739 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1791
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 767998703 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. |
1693-1740 |
1.27e-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: 1.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1693 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1740
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1411-1453 |
1.89e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.89e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 1411 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1453
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1740-1783 |
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 767998703 1740 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1783
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 |
4.58e-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: 4.58e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998703 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 ... |
2803-2907 |
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 767998703 2803 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2877
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767998703 2878 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2907
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 767998703 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1693-1735 |
2.40e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998703 1693 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1735
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
631-681 |
4.57e-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: 4.57e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
4.73e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.73e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767998703 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1862-2358 |
8.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1862 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1940
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1941 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2020
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2021 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2100
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2101 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2156
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2157 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2236
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2237 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2316
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 767998703 2317 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2358
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 |
4.90e-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: 4.90e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998703 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 767998703 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2063-2381 |
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 767998703 2063 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2142
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2143 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2222
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2223 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2299
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2300 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2375
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 767998703 2376 MDRIRE 2381
Cdd:COG5185 529 FMRARG 534
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1977-2249 |
5.00e-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: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1977 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2052
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2053 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2121
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2122 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2193
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998703 2194 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2249
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 |
6.46e-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: 6.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 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 767998703 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.09e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.09e-05
10 20 30
....*....|....*....|....*....|....*....
gi 767998703 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1862-2393 |
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 767998703 1862 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1941
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1942 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2021
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2022 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2085
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2086 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2158
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2159 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2220
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2221 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2293
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2294 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2361
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 767998703 2362 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2393
Cdd:TIGR01612 1336 khnsdINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEI 1374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1844-2381 |
2.50e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1844 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1913
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1914 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1992
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1993 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2064
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2065 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2135
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2136 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2214
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2215 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2292
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2293 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2372
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 767998703 2373 SDNMDRIRE 2381
Cdd:PRK02224 697 RERREALEN 705
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2098-2262 |
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 767998703 2098 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2175
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2176 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2250
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 767998703 2251 LNNLQQTLNIVT 2262
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.11e-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: 5.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998703 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 ... |
2443-2569 |
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 767998703 2443 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2518
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 2519 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2569
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
2.99e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998703 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 767998703 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 |
6.39e-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: 6.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998703 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
6.97e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 6.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998703 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 767998703 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 ... |
1671-1794 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1671 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1746
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998703 1747 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1794
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1864-2182 |
6.17e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1864 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1940
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1941 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2007
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2008 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2079
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2080 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2153
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767998703 2154 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2182
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2097-2193 |
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 767998703 2097 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2170
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 767998703 2171 GDELvrcavdaATAYENILNAIK 2193
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 ... |
1853-2110 |
4.69e-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: 4.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1853 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1932
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1933 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2012
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2013 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2092
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 767998703 2093 ADSSLLQTNIALQLMEKS 2110
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.65e-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: 5.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 767998703 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.06e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 767998703 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 ... |
2294-2422 |
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 767998703 2294 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2364
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 2365 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2422
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1524-1658 |
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 767998703 1524 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1601
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998703 1602 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1658
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1520-1647 |
9.23e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1520 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1599
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998703 1600 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1647
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3164-3315 |
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 767998703 3164 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3242
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998703 3243 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3315
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3187-3316 |
3.40e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 3187 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3264
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998703 3265 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3316
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3192-3317 |
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 767998703 3192 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3271
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767998703 3272 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3317
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3000-3140 |
4.19e-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: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 3000 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3077
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998703 3078 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3140
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3017-3142 |
7.42e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 3017 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3093
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767998703 3094 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3142
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2608-2748 |
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 767998703 2608 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2684
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 2685 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2748
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2627-2748 |
2.38e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2627 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2703
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998703 2704 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2748
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3024-3142 |
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 767998703 3024 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3100
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767998703 3101 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3142
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2775-2907 |
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 767998703 2775 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2851
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998703 2852 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2907
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3024-3144 |
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 767998703 3024 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 3099
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998703 3100 LPGNSTISIRAPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPL 3144
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
2800-2909 |
4.86e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2800 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2875
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767998703 2876 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2909
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1272-1320 |
7.32e-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: 7.32e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998703 1272 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1320
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2634-2748 |
5.39e-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: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2634 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2712
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767998703 2713 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2748
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1271-1313 |
2.67e-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: 2.67e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 1271 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1313
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1844-2347 |
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 767998703 1844 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1905
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1906 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1975
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1976 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2051
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2052 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2131
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2132 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2210
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2211 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2284
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2285 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2345
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 767998703 2346 NK 2347
Cdd:TIGR04523 738 NK 739
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3192-3319 |
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 767998703 3192 IRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSVAVTIKQHILHLELD------ 3264
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDgearpt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998703 3265 -TDSSYTAGQIPFPpastqEPLHLGGAPANLTTLRI-PVWKSFFGCLRNIHVNHIPV 3319
Cdd:pfam00054 79 gESPLGATTDLDVD-----GPLYVGGLPSLGVKKRRlAISPSFDGCIRDVIVNGKPL 130
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1841-2292 |
3.40e-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: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1841 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEF-ETLQEKAQVns 1919
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQF-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1920 rkaqtlnnnvnraTQSAKELDVKIKNVIRNVHILLKQISgTDGEGNNvpsgdfsREWAE-------AQRMMRELRNRNFG 1992
Cdd:pfam15921 369 -------------SQESGNLDDQLQKLLADLHKREKELS-LEKEQNK-------RLWDRdtgnsitIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1993 KHLREA--EADKRESQLLLNRirtWQKTHQGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAAQAKQANGL 2061
Cdd:pfam15921 428 VQRLEAllKAMKSECQGQMER---QMAAIQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2062 NQENERALGAIQRQVKEINS---LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRS 2138
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2139 AG-----KTSLVEEAEKHARSLQEL--------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKA 2194
Cdd:pfam15921 585 AGamqveKAQLEKEINDRRLELQEFkilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2195 aedaanraasaSESALQTvIKEDLPRKAKTLSSNSDkllnEAKMTQKKLKQEVSPALNNLQQTLNIVTvQKEVIDTNLTT 2274
Cdd:pfam15921 665 -----------SRNELNS-LSEDYEVLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMK 727
|
490 500
....*....|....*....|.
gi 767998703 2275 LRDGLHG---IQRGDIDAMIS 2292
Cdd:pfam15921 728 VAMGMQKqitAKRGQIDALQS 748
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1272-1313 |
1.17e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.17e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998703 1272 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1313
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1362-1413 |
4.64e-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: 4.64e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767998703 1362 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1413
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
5.51e-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: 5.51e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
7.68e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.68e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998703 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1362-1407 |
8.22e-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: 8.22e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998703 1362 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1407
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1842-2384 |
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 767998703 1842 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqEKAQVNSRK 1921
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1922 AQTLNNNVNRatqSAKELDVKIKNVIRN-VHI--LLKQISGTDGEGNNVpSGDFSREWAEAQRMMRELRNRNFGKHLREA 1998
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLeVELnkLEKQKKENKKNIDKF-LTEIKKKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1999 EADKRESQLllnrirtwqktHQGENNglANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKE 2078
Cdd:TIGR04523 174 ELNLLEKEK-----------LNIQKN--IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2079 INSLQSDF----TKYLTTADSsllQTNIALQLMEKsQKEYEK-------LAASLNEARQELSD----KVRELSRsagktS 2143
Cdd:TIGR04523 241 INEKTTEIsntqTQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQLNQLKSEISDlnnqKEQDWNK-----E 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2144 LVEEAEKHARSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKaaedaANRAASASE-SALQTVIKEDLpRKA 2222
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLK-----KELTNSESEnSEKQRELEEKQ-NEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2223 KTLSSNSDKLLNEAkmtqKKLKQEVspalNNLQQTLNIVTVQKEVIDTNLTTLRdglhgIQRGDIDAMISSAKSMVRKAN 2302
Cdd:TIGR04523 373 EKLKKENQSYKQEI----KNLESQI----NDLESKIQNQEKLNQQKDEQIKKLQ-----QEKELLEKEIERLKETIIKNN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2303 DITDEVLDGLNPIQTDVERIKDTygrtqNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPL--------GNISD 2374
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneekkeleEKVKD 514
|
570
....*....|
gi 767998703 2375 NMDRIRELIQ 2384
Cdd:TIGR04523 515 LTKKISSLKE 524
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1362-1408 |
1.74e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998703 1362 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1408
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1410-1460 |
1.82e-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: 1.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1410 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1460
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2441-2576 |
2.10e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2441 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2514
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998703 2515 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2576
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1692-1738 |
2.23e-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: 2.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1692 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1738
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1877-2165 |
2.88e-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: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1877 RNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK---AQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHIL 1953
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1954 LKQISGTDGEgnnvpsgdfsrewAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIrtwqkthqgenNGLANSIRDS 2033
Cdd:TIGR02168 749 IAQLSKELTE-------------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------KEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2034 LNEYEAKLSDLRARLQEAAAQAKQA-----------NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2102
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLerriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998703 2103 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSagKTSLVEEAEKHARSLQELAKQLEEI 2165
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 |
3.18e-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: 3.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767998703 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 ... |
1837-2393 |
3.47e-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: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1837 NDLATMGEQLRLVKSQLQglsasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSKIE---GLERELTDLNQEFETLQE 1913
Cdd:TIGR04523 162 NDLKKQKEELENELNLLE---------KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1914 KAQVNSRKAQTLNNNVNRATQ----------------SAKELDV-KIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREW 1976
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTqlnqlkdeqnkikkqlSEKQKELeQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1977 AEaqrmmrELRNRNfgKHLREAEADKRESQLLLNR-------IRTWQKTHQGENNglanSIRDSLNEYEAKLSDLrarlq 2049
Cdd:TIGR04523 313 KS------ELKNQE--KKLEEIQNQISQNNKIISQlneqisqLKKELTNSESENS----EKQRELEEKQNEIEKL----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2050 eaaaqakqanglNQENERALGAIQRQVKEINSLQSDFTKYltTADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQE 2127
Cdd:TIGR04523 376 ------------KKENQSYKQEIKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2128 LSDKVRElsrsagKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASE 2207
Cdd:TIGR04523 442 IKDLTNQ------DSVKELIIKNLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2208 SALQTVIKE---------DLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV--IDTNLTTLR 2276
Cdd:TIGR04523 496 KELKKLNEEkkeleekvkDLTKKISSLKEKIEKLESEKKEKESKISDLED-ELNKDDFELKKENLEKEIdeKNKEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2277 DglhgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIkdtygrtqnEDFKKALTDADNSVNKLTNKLPDLW 2356
Cdd:TIGR04523 575 Q--------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI---------SSLEKELEKAKKENEKLSSIIKNIK 637
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 767998703 2357 RKIESINQQllpLGNISDNMDRIR----ELIQQARDAASKV 2393
Cdd:TIGR04523 638 SKKNKLKQE---VKQIKETIKEIRnkwpEIIKKIKESKTKI 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1835-2169 |
6.71e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1835 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1913
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1914 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1985
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1986 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2054
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2055 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2128
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767998703 2129 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2169
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1740-1790 |
6.82e-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: 6.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1740 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1790
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2396-2574 |
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 767998703 2396 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2475
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2476 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2549
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 767998703 2550 PPDFKLPSRLSFPPYKGCIELDDLN 2574
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1411-1459 |
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 767998703 1411 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1459
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 |
1.38e-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: 1.38e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998703 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 |
1.57e-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: 1.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 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 |
2.52e-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: 2.52e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767998703 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 767998703 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 ... |
1739-1791 |
6.13e-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: 6.13e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767998703 1739 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1791
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 767998703 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. |
1693-1740 |
1.27e-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: 1.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1693 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1740
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1835-2382 |
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 767998703 1835 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHmETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK 1914
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1915 AQVNSRKAQTLNNNVNRATQ---SAKELDVKIKNVIRNVHILLK---QISGTDG---EGNNVPSGdFSR--EWAEAQRM- 1982
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKnqsGLSGILGvlsELISVDEG-YEAaiEAALGGRLq 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1983 MRELRNRNFGK----HLREAEADKReSQLLLNRIR--------TWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQE 2050
Cdd:TIGR02168 549 AVVVENLNAAKkaiaFLKQNELGRV-TFLPLDSIKgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2051 AAAQAKQANGLNQENERAL------------GAIQRQ-VKEINSLQS------DFTKYLTTADSSLLQTNIALQLMEKSQ 2111
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRivtldgdlvrpgGVITGGsAKTNSSILErrreieELEEKIEELEEKIAELEKALAELRKEL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2112 KEYEKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAA 2182
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLAR--LEAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIE 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2183 TAYENILNAIKAAedaanraaSASESALQTVIKE--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ-------------EV 2247
Cdd:TIGR02168 786 ELEAQIEQLKEEL--------KALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedieSL 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2248 SPALNNLQQT-------LNIVTVQKEVIDTNLTTLRDglhgiQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVE 2320
Cdd:TIGR02168 858 AAEIEELEELieeleseLEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998703 2321 RIKDTYGRTQ---NEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2382
Cdd:TIGR02168 933 GLEVRIDNLQerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1411-1453 |
1.89e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.89e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767998703 1411 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1453
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1740-1783 |
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 767998703 1740 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1783
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1844-2191 |
3.33e-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: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1844 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1923
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1924 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEgnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEAD-K 2002
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----------LEELEEELEEAEEELEEAEAELAEAEEAlL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2003 RESQLLLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLQEAAAqakqangLNQENERALGAIQRQVKEINSL 2082
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLER-------LEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2083 QSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSdkvRELSRSAGKTSLVEEAEKHARSLQELAKQL 2162
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA---EAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340
....*....|....*....|....*....
gi 767998703 2163 EEIKRNASGDELVRCAVDAATAYENILNA 2191
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 |
4.58e-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: 4.58e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767998703 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 ... |
2803-2907 |
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 767998703 2803 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2877
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767998703 2878 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2907
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1862-2160 |
1.50e-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: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1862 LLEQMRHMETQAKDLRNQLlnyrSAISNHgskIEGLERELTDLNQEFETLQEK-AQVNSRKAQTLNNNVNRATQSAKELD 1940
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL----ASLEEE---LEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1941 VKIKNVIRNVHILLKQISGTDGEGNNVPSgDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQL--LLNRIRTWQKT 2018
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2019 HQgennglanSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL- 2097
Cdd:TIGR02169 380 FA--------ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIk 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 2098 -----LQTNIALqlMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 2160
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 ... |
1859-2388 |
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 767998703 1859 SAGLLEQMRHMETQAKDLRNQLLNYRSAIS-------NHGSKIEGLERELTDLNQEFETLQ-EKAQVNSRKAQtLNNNVN 1930
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQklqlekvTTEAKIKKLEEDILLLEDQNSKLSkERKLLEERISE-FTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1931 RATQSAKELDvKIKN----VIRNVHILLKQISGT-----------DGEgnnvpSGDFSREWAEAQRMMRELRnrnfgkhl 1995
Cdd:pfam01576 170 EEEEKAKSLS-KLKNkheaMISDLEERLKKEEKGrqelekakrklEGE-----STDLQEQIAELQAQIAELR-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1996 reAEADKRESQL--LLNRIrtwqKTHQGENNGLANSIRdslnEYEAKLSDLRARLqeaaaqakqanglnqENERALGAIQ 2073
Cdd:pfam01576 236 --AQLAKKEEELqaALARL----EEETAQKNNALKKIR----ELEAQISELQEDL---------------ESERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2074 RQVK-----EINSLQsdfTKYLTTADSsllqTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktslveea 2148
Cdd:pfam01576 291 EKQRrdlgeELEALK---TELEDTLDT----TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMR------------ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2149 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDAANRAASASESALQTV---------IKEDL 2218
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQDSEHKRKKLEGQLQELqarlseserQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2219 PRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LNIVTVQKEVIDTNLTTLRDGLHGIQrgdidamis 2292
Cdd:pfam01576 432 AEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETRQKLNLSTRLRQLEDERNSLQ--------- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2293 saksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2372
Cdd:pfam01576 503 --------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
570
....*....|....*.
gi 767998703 2373 SDNMDRIRELIQQARD 2388
Cdd:pfam01576 568 YDKLEKTKNRLQQELD 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1974-2395 |
1.69e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1974 REWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaa 2053
Cdd:COG4717 88 EEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERL----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2054 qakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2133
Cdd:COG4717 156 ---------EELRELEEELEELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2134 ELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAED 2197
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2198 AANRAASASESALQTVIKEDLPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnltt 2274
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE-------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2275 LRDGLHGIQRGDIDAMISSAK------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKL 2348
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 767998703 2349 TNKLpdlwRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAV 2395
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 767998703 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1693-1735 |
2.40e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767998703 1693 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1735
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
631-681 |
4.57e-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: 4.57e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
4.73e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.73e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767998703 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2632-2748 |
5.40e-08 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 54.25 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2632 IQTTVDRGLLFFAE--NGDRFISLNIEDGKLMVRYKLNSELPKERGvGDAINNGRDHSI---------QIKIGKLQKRMW 2700
Cdd:pfam00054 1 FRTTEPSGLLLYNGtqTERDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVelerngrsgTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767998703 2701 INVDVQNTIIDGEvfdfSTYYLGGIPIAI--RERFNISTPaFRGCMKNLK 2748
Cdd:pfam00054 80 ESPLGATTDLDVD----GPLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1862-2358 |
8.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1862 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1940
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1941 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2020
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2021 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2100
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2101 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2156
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2157 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2236
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2237 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2316
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 767998703 2317 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2358
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1844-2360 |
1.08e-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: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1844 EQLRLVKSQLQGLSASAG-LLEQMRHMETQAKDLrnQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1922
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDrILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1923 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnNVPSGDFSREWAEAQR----MMRElRNRNFGKHLREA 1998
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG-------YFPNKKQLEDWLHSKSkeinQTRD-RLAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1999 EADKresqlllNRIRTWQKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAAQAKQANG-----------LNQEN 2065
Cdd:TIGR00606 604 EQNK-------NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDEN 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2066 ERALGAIQRQVK---EINSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT 2142
Cdd:TIGR00606 677 QSCCPVCQRVFQteaELQEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2143 -SLVEEAEKHARSLQELAKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRK 2221
Cdd:TIGR00606 754 qKVNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2222 AKTLSSNSDKLLNEAKMTQkKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTtlrdglhgiQRGDID----AMISSAKSM 2297
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ---------RRQQFEeqlvELSTEVQSL 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998703 2298 VRKANDITDEVLDGLNPIQTDVERiKDTYGRTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 2360
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1847-2186 |
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 767998703 1847 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN 1926
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1927 NNVNRATQSAKELDvkiknvirnvhillKQISGTDGEGNNVPSgdfSREWAEAQR-MMRELRNRNFGKhLREAEADKRES 2005
Cdd:PRK02224 377 EAVEDRREEIEELE--------------EEIEELRERFGDAPV---DLGNAEDFLeELREERDELRER-EAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2006 QlllNRIRtwqkthqgENNGL--------------ANSIRDSLNEYEAKLSDLRARLqeaAAQAKQANGLNQENERA--L 2069
Cdd:PRK02224 439 R---ERVE--------EAEALleagkcpecgqpveGSPHVETIEEDRERVEELEAEL---EDLEEEVEEVEERLERAedL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2070 GAIQRQVKEINSLQSDFTKYLTTADSSllqtnialqLMEKSQKeyeklAASLNEARQELSDKVRELSRSAgkTSLVEEAE 2149
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRET---------IEEKRER-----AEELRERAAELEAEAEEKREAA--AEAEEEAE 568
|
330 340 350
....*....|....*....|....*....|....*..
gi 767998703 2150 KHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYE 2186
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1844-2180 |
2.43e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.06 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1844 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEkaqvnsrKAQ 1923
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1924 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVpsgdfsreWAEAQRMMRELRNRNFGKHLREAEADKR 2003
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL--------EQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2004 ESQL--LLNRIRTWQKTHQGENNGLANSIRDSLnEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINS 2081
Cdd:COG4372 156 EEQLesLQEELAALEQELQALSEAEAEQALDEL-LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2082 LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQ 2161
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330
....*....|....*....
gi 767998703 2162 LEEIKRNASGDELVRCAVD 2180
Cdd:COG4372 315 DALLAALLELAKKLELALA 333
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1844-2171 |
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 767998703 1844 EQLRLVKSQLQGLSAS-AGLLEQMRHMEtqakdlrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1922
Cdd:TIGR02169 674 AELQRLRERLEGLKRElSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1923 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQIsgtdgegnNVPSGDFSRE-WAEAQRMMREL---RNRNFG------ 1992
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--------NDLEARLSHSrIPEIQAELSKLeeeVSRIEArlreie 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1993 -----KHLREAEADKrESQLLLNRIRTWQ------KTHQGENNGLANSIRDSLNEYEAKLSDLRARLQeaaaqakqanGL 2061
Cdd:TIGR02169 819 qklnrLTLEKEYLEK-EIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLG----------DL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2062 NQENERA---LGAIQRQVKEINSlqsdftkYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-------- 2130
Cdd:TIGR02169 888 KKERDELeaqLRELERKIEELEA-------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqael 960
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767998703 2131 -KVRELSRSAGKTSL--VEEAEKHARSLQELAKQLEEIKRNASG 2171
Cdd:TIGR02169 961 qRVEEEIRALEPVNMlaIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1844-2164 |
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 767998703 1844 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNhgskiegLERELTDLNQEFETLQEKAQvnsrKAQ 1923
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-------IEKRLSRLEEEINGIEERIK----ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1924 TLNNNVNRATQSAKELDVKIkNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNfgKHLRE------ 1997
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEeiskit 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1998 ---AEADKRESQLLLNRI-------------RTWQKTHQGEnnglansirdSLNEYEAKLSDLRARLQEAaaqakqangl 2061
Cdd:PRK03918 412 ariGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKE----------LLEEYTAELKRIEKELKEI---------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2062 nQENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLNEARQELSDKVREL 2135
Cdd:PRK03918 472 -EEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350
....*....|....*....|....*....|...
gi 767998703 2136 SRSAG----KTSLVEEAEKHARSLQELAKQLEE 2164
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 |
4.90e-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: 4.90e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767998703 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1954-2167 |
5.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1954 LKQISGTDgegnnvpsgDFSREWAEAQRMMRELRNRnfgkhlREAEAD--KRESQLLlNRIRTwQKTHQGENNGLANSIR 2031
Cdd:PRK03918 151 VRQILGLD---------DYENAYKNLGEVIKEIKRR------IERLEKfiKRTENIE-ELIKE-KEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2032 DSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKylTTADSSLLQTNIA-LQLMEKS 2110
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKeLKELKEK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998703 2111 QKEYEKLAASLNEARQELSDKVRELSR----SAGKTSLVEEAEKHARSLQELAKQLEEIKR 2167
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 767998703 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 ... |
3006-3144 |
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 767998703 3006 KLPQELLkPRSQFAVDM-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 3079
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998703 3080 GHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 3144
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2063-2381 |
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 767998703 2063 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2142
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2143 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2222
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2223 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2299
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2300 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2375
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 767998703 2376 MDRIRE 2381
Cdd:COG5185 529 FMRARG 534
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1805-2259 |
2.55e-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: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1805 HPLTGDCINQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSA----SAGLLEQMRHMET--QAKDLRN 1878
Cdd:TIGR00618 279 LEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkqQSSIEEQRRLLQTlhSQEIHIR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1879 QLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA-TQSAKELDVKIKNVIRNVHILLKQI 1957
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRDLQGQLAHAKKQQELQQR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1958 SGTDGE--GNNVPSGDFSREwAEAQRMMRELRNRNFGK------HLREAEADKRESQLLLNrirtwqktHQGENNGLANS 2029
Cdd:TIGR00618 439 YAELCAaaITCTAQCEKLEK-IHLQESAQSLKEREQQLqtkeqiHLQETRKKAVVLARLLE--------LQEEPCPLCGS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2030 IRdslnEYEAKLSDL-----RARLQEAAAQAKQANGLNQENERALG-AIQRQVK----EINSLQSDFTKYLTTADSSLLQ 2099
Cdd:TIGR00618 510 CI----HPNPARQDIdnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRAslkeQMQEIQQSFSILTQCDNRSKED 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2100 TNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE----LV 2175
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehAL 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2176 RCAVDAATAYENILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQ 2255
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
....
gi 767998703 2256 QTLN 2259
Cdd:TIGR00618 743 QSLK 746
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1977-2249 |
5.00e-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: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1977 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2052
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2053 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2121
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2122 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2193
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767998703 2194 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2249
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 |
6.46e-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: 6.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1843-2248 |
6.80e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1843 GEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRnQLLNYRSAISnhgSKIEGLERELTDLNQEFETLQEKAQvnsrkA 1922
Cdd:COG4717 63 GRKPELNLKELKELE------EELKEAEEKEEEYA-ELQEELEELE---EELEELEAELEELREELEKLEKLLQ-----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1923 QTLNNNVNRATQSAKELDVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEADK 2002
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-------LEERL----------------EELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2003 RESQLLLNRIRTWQKTHQgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER--------ALGAIQR 2074
Cdd:COG4717 185 QLSLATEEELQDLAEELE-ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2075 QVKEINSLQSDFTKYLTTAdSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-KVRELSRSAG-----KTSLVEEA 2148
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLV-LGLLALLFLLLAREKASLGKEAEELQALPALEELEEeELEELLAALGlppdlSPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2149 EKHARSLQELAKQLEEIKR------------------NASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESAL 2210
Cdd:COG4717 343 LDRIEELQELLREAEELEEelqleeleqeiaallaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 767998703 2211 QTVIKEDLPRKAKTLSSNSDKL---LNEAKMTQKKLKQEVS 2248
Cdd:COG4717 423 EALDEEELEEELEELEEELEELeeeLEELREELAELEAELE 463
|
|
| 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 767998703 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.09e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.09e-05
10 20 30
....*....|....*....|....*....|....*....
gi 767998703 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1864-2174 |
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 767998703 1864 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTD-------LNQEFETLQEKAQVNSRKAQTLNNNVNRATQSA 1936
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrdeLNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1937 KELDVKIKNVIRNVHILLKQISGTDGEGNNVPS--------------GDFSREW-----AEAQRMMRELRNRnfgKHLRE 1997
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqqtEVLSPEEekelvEKIKELEKELEKA---KKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1998 AEADKREsqlLLNRIRTWQKthqgenngLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEneralgaIQRQVK 2077
Cdd:COG1340 158 KNEKLKE---LRAELKELRK--------EAEEIHKKIKELAEEAQELHEEMIE----------LYKE-------ADELRK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2078 EINSLQSDFTKYLTTADssllqtnialqlMEKsqKEYEKLAASLNEARQELsDKVRELSRSAGKTSLVEEAEKHARSLqe 2157
Cdd:COG1340 210 EADELHKEIVEAQEKAD------------ELH--EEIIELQKELRELRKEL-KKLRKKQRALKREKEKEELEEKAEEI-- 272
|
330
....*....|....*....
gi 767998703 2158 lakqLEEIKRNA--SGDEL 2174
Cdd:COG1340 273 ----FEKLKKGEklTTEEL 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1915-2282 |
1.47e-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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1915 AQVNSRKAQTLNNnVNRATQSAKELDVKIKNVIRNVHILLKQisgtdgegnnvpsgdfsREWAEA-QRMMRELRNRNFGK 1993
Cdd:TIGR02169 166 AEFDRKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRRE-----------------REKAERyQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1994 HLREAEADKRESQLLLNRIrtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQakqangLNQENER--ALGA 2071
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL---------------ASLEEELEKLTEEISELEKRLEEIEQL------LEELNKKikDLGE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2072 iqrqvKEINSLQSDFTKylTTADSSLLQTNIAL--QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-KTSLVEE- 2147
Cdd:TIGR02169 287 -----EEQLRVKEKIGE--LEAEIASLERSIAEkeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrRDKLTEEy 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2148 -----------------AEKHARSLQELAK----------QLEEIKRNAS--GDELVRcavdAATAYENILNAIKAAEDA 2198
Cdd:TIGR02169 360 aelkeeledlraeleevDKEFAETRDELKDyrekleklkrEINELKRELDrlQEELQR----LSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2199 ANRAASASESAlQTVIKEDlPRKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQQTLNIVTVQKEVIDT-------N 2271
Cdd:TIGR02169 436 INELEEEKEDK-ALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEErvrggraV 512
|
410
....*....|.
gi 767998703 2272 LTTLRDGLHGI 2282
Cdd:TIGR02169 513 EEVLKASIQGV 523
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1863-2394 |
1.49e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 50.79 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1863 LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK 1942
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1943 IKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNR---IRTWQKTH 2019
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLAlalLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2020 QGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINslQSDFTKYLTTadssllq 2099
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDV------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2100 tnialqlmeKSQKEYEKLAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcav 2179
Cdd:COG0840 232 ---------DSKDEIGQLADAFNRMIENLRELVGQVRESA--EQVASASEELAASAEELAAGAEEQAASLE--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2180 DAATAYENILNAIKaaedaanraaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQKKLK---QEVSPALNNL-- 2254
Cdd:COG0840 292 ETAAAMEELSATVQ----------EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGIEEIResvEETAETIEELge 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2255 --QQTLNIVTVQKEVID-TNLTTL-------RDGLHGiqRG--------------------DIDAMISSAKSMVRKANDI 2304
Cdd:COG0840 359 ssQEIGEIVDVIDDIAEqTNLLALnaaieaaRAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2305 TDEVLDGlnpIQTDVERIKDTygrtqnedfKKALTDADNSVNKLTNKLpdlwRKI-ESINQQLLPLGNISDNMDRIRELI 2383
Cdd:COG0840 437 MEEGSEE---VEEGVELVEEA---------GEALEEIVEAVEEVSDLI----QEIaAASEEQSAGTEEVNQAIEQIAAAA 500
|
570
....*....|.
gi 767998703 2384 QQARDAASKVA 2394
Cdd:COG0840 501 QENAASVEEVA 511
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1862-2393 |
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 767998703 1862 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1941
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1942 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2021
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2022 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2085
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2086 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2158
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2159 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2220
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2221 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2293
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2294 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2361
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 767998703 2362 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2393
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 ... |
2068-2354 |
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 767998703 2068 ALGAIQRQVKEINSLQSDFTKYLTtadSSLLQTNIALQLMEKSQKEYEklaaSLNEARQELSDKVRELSRSAGK------ 2141
Cdd:pfam06008 6 SLTGALPAPYKINYNLENLTKQLQ---EYLSPENAHKIQIEILEKELS----SLAQETEELQKKATQTLAKAQQvnaese 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2142 ------TSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcavdaATAYENILNAIKAAEDAANRAASASESALQTVIK 2215
Cdd:pfam06008 79 rtlghaKELAEAIKNLIDNIKEINEKVATLGENDF-----------ALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2216 EDLpRKAKtlssnsdKLLNEAKMTQKKLKQEVSPALNNLQQTLNivtvqkeviDTNlttlrDGLHgiqrgDIDAMISSAK 2295
Cdd:pfam06008 148 AEL-KAAQ-------DLLSRIQTWFQSPQEENKALANALRDSLA---------EYE-----AKLS-----DLRELLREAA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998703 2296 SMVRKANDITDEVLDGLNPIQTDVERIkdtygRTQNEDFKKALTDADNSV---NKLTNKLPD 2354
Cdd:pfam06008 201 AKTRDANRLNLANQANLREFQRKKEEV-----SEQKNQLEETLKTARDSLdaaNLLLQEIDD 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1844-2381 |
2.50e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1844 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1913
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1914 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1992
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1993 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2064
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2065 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2135
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2136 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2214
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2215 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2292
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2293 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2372
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 767998703 2373 SDNMDRIRE 2381
Cdd:PRK02224 697 RERREALEN 705
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1846-2176 |
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 767998703 1846 LRLVKSQLQG-----LSASAGL---LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 1917
Cdd:pfam15921 435 LKAMKSECQGqmerqMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1918 NSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDgegnnvpsgdfsrEWAEAQRMMRELRNRNFGKH 1994
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKD-------------KVIEILRQQIENMTQLVGQH 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1995 LREAEADKRESQLLLNRIRTwQKTHQGENNGLANSIRDSLNEYEAKLSDL---RARLQEAAAQA-KQANGLNQENERALG 2070
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEIND-RRLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSERlRAVKDIKQERDQLLN 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2071 AIQRQVKEINSLQSDF---------------------TKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLneaRQELS 2129
Cdd:pfam15921 661 EVKTSRNELNSLSEDYevlkrnfrnkseemetttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM---QKQIT 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767998703 2130 DKVRELSRSAGKTSLVEEA------EKH------ARSLQELAKQLEEIKRNASGDELVR 2176
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAmtnankEKHflkeekNKLSQELSTVATEKNKMAGELEVLR 796
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1814-2082 |
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 767998703 1814 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGlsasaglLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1893
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-------AEDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1894 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDGEGNNVPSg 1970
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKlaeLKERIESLERIRTLLAAIADAEDEIER- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1971 dfSREWAEAQRMMRELRnrnfgkhlREAEADKREsqlllnRIRTWQKTHQGENNGLANSIRDSLNEY----EAKLSDLRA 2046
Cdd:PRK02224 611 --LREKREALAELNDER--------RERLAEKRE------RKRELEAEFDEARIEEAREDKERAEEYleqvEEKLDELRE 674
|
250 260 270
....*....|....*....|....*....|....*.
gi 767998703 2047 RlqeaaaqakqanglNQENERALGAIQRQVKEINSL 2082
Cdd:PRK02224 675 E--------------RDDLQAEIGAVENELEELEEL 696
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1977-2193 |
3.31e-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: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1977 AEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRtwqkthqgENNGL------ANSIRDSLNEYEAKLSDLRARLQE 2050
Cdd:COG3206 171 EEARKALEFLEEQ-----LPELRKELEEAEAALEEFR--------QKNGLvdlseeAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2051 AAAQAKQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLT--TADSSL---LQTNIAlQLMEKSQKEYEKLAA 2119
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSAryTPNHPDviaLRAQIA-ALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998703 2120 SLNEARQELSDKVRELSRSagktslVEEAEKHARSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 2193
Cdd:COG3206 317 SLEAELEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1979-2308 |
4.04e-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: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1979 AQRMmRELRNRnfgkhLREAEADkresqLLLNRIRtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQA 2058
Cdd:TIGR02168 212 AERY-KELKAE-----LRELELA-----LLVLRLE--------ELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2059 NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL--LQTNIA-----LQLMEKSQKEYEKLAASLNEARQELSDK 2131
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2132 VrelsrsagkTSLVEEAEKHARSLQELAKQLEEIKRNAsgdELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQ 2211
Cdd:TIGR02168 353 L---------ESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2212 TVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQrgdidAMI 2291
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQ-----ARL 491
|
330
....*....|....*..
gi 767998703 2292 SSAKSMVRKANDITDEV 2308
Cdd:TIGR02168 492 DSLERLQENLEGFSEGV 508
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2098-2262 |
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 767998703 2098 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2175
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2176 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2250
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 767998703 2251 LNNLQQTLNIVT 2262
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1995-2313 |
4.89e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1995 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQR 2074
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEEL----------EELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2075 QVKEINSLQSDFTKY------LTTADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEA 2148
Cdd:COG4372 99 AQEELESLQEEAEELqeeleeLQKERQDLEQQRKQL---EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2149 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSN 2228
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2229 SDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEV 2308
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
....*
gi 767998703 2309 LDGLN 2313
Cdd:COG4372 336 LAELA 340
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1814-1944 |
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 767998703 1814 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1893
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 1894 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIK 1944
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.11e-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: 5.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767998703 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 ... |
2443-2569 |
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 767998703 2443 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2518
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767998703 2519 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2569
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1831-2144 |
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 767998703 1831 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFE 1909
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1910 TLQEKaqvnsrkaqtlnnnVNRATQSAKELDVKIKNVIRNvhillkqisgtdgegnnvpsgdfsrewaeAQRMMRE---- 1985
Cdd:COG4942 87 ELEKE--------------IAELRAELEAQKEELAELLRA-----------------------------LYRLGRQppla 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1986 --LRNRNFGKHLREAEADKRESQLLLNRIRTWQKThqgennglansiRDSLNEYEAKLSDLRARLqeaaaqakqanglnq 2063
Cdd:COG4942 124 llLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------LAELAALRAELEAERAEL--------------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2064 enERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2143
Cdd:COG4942 177 --EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 767998703 2144 L 2144
Cdd:COG4942 255 L 255
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1875-2396 |
7.26e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1875 DLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN---NNVNRATQSAKELDVKIK------- 1944
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKtaesdls 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1945 ----------------------------NVIRNVHILLKQI-------SGTDGEGNNVPSG--------DFSREWAEAQR 1981
Cdd:PRK01156 267 meleknnyykeleerhmkiindpvyknrNYINDYFKYKNDIenkkqilSNIDAEINKYHAIikklsvlqKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1982 MMRELRN-------------------RNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLS 2042
Cdd:PRK01156 347 RYDDLNNqilelegyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2043 DLRARLQEAAAQAKQ----ANGLNQENERALGAIQRQVKEINSLQSDFTKylttaDSSLLQTNIalqlmeksqKEYEKLA 2118
Cdd:PRK01156 427 SLNQRIRALRENLDElsrnMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE-----KKSRLEEKI---------REIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2119 ASLNEARQELsdkVRELSRSAGKTslVEEAEKHARSLQELAKQLEEIKrnasgDELVRCAvDAATAYENILNAIKAAEDA 2198
Cdd:PRK01156 493 KDIDEKIVDL---KKRKEYLESEE--INKSINEYNKIESARADLEDIK-----IKINELK-DKHDKYEEIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2199 ANRAASASESALQTVI-----------KEDLPRKAKTLSSNSDKLLNE----AKMTQKKLKqEVSPALNNLQQTLNIVTV 2263
Cdd:PRK01156 562 DLDSKRTSWLNALAVIslidietnrsrSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIR-EIENEANNLNNKYNEIQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2264 QKEVIDTNLTTLRDglHGIQRGDIDAMISSAKSMVRKANDITDEvldgLNPIQTDVERIKDTYGRtqnedfKKALTDADN 2343
Cdd:PRK01156 641 NKILIEKLRGKIDN--YKKQIAEIDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRAR------LESTIEILR 708
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 767998703 2344 S-VNKLTNKLPDLWRKIESINQQLLPLGNIsdnmDRIREliqqardAASKVAVP 2396
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 ... |
1839-2184 |
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 767998703 1839 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN----- 1905
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1906 --QEFETLQEKAQVNSRKAQTLNNNVN--RATQSAKE------------------------------LDVKiknvIRNVH 1951
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVDalRLRLEEKEsflnkktkqlqdlteekstlageirdlkdmLDVK----ERKIN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1952 ILLKQISgtdgegnnvpsgDFSREWAEAQRMMRELRNRNFGKH------------LREAEADK------------RESQL 2007
Cdd:pfam10174 398 VLQKKIE------------NLQEQLRDKDKQLAGLKERVKSLQtdssntdtalttLEEALSEKeriierlkeqreREDRE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2008 LLNRIRTWQKthqgENNGL---ANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENEralGAIQRQVKEINSLQS 2084
Cdd:pfam10174 466 RLEELESLKK----ENKDLkekVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE---IAVEQKKEECSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2085 DFTKYLTTADSSLLQTNIA--LQLME-----------KSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL-VEEAEK 2150
Cdd:pfam10174 539 QLKKAHNAEEAVRTNPEINdrIRLLEqevarykeesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRqMKEQNK 618
|
410 420 430
....*....|....*....|....*....|....
gi 767998703 2151 HARSLQelAKQLEEIKRNASGDELVRCAVDAATA 2184
Cdd:pfam10174 619 KVANIK--HGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1865-2096 |
1.68e-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: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1865 QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQsakeldvKIK 1944
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1945 NVIRNVhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFGKHLREAEADKRESQLLLNRIRTWQK 2017
Cdd:COG3883 90 ERARAL-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767998703 2018 THQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSS 2096
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1838-2162 |
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 767998703 1838 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE 1913
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1914 KAQVNSRkaQTLNNNVNRATQSAKELDVKiknvirnvHILLKQISGTDGEGNnvpsgdfsREWAEAQRMMRELRNR--NF 1991
Cdd:COG4913 742 LARLELR--ALLEERFAAALGDAVERELR--------ENLEERIDALRARLN--------RAEEELERAMRAFNREwpAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1992 GKHLREAEADKRESQLLLNRIrtwqkthqgENNGLAnsirdslnEYEAKLSDLRARLQEAAAQakqanGLNQENERALGA 2071
Cdd:COG4913 804 TADLDADLESLPEYLALLDRL---------EEDGLP--------EYEERFKELLNENSIEFVA-----DLLSKLRRAIRE 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2072 IQRQVKEIN-SL-QSDFtkyltTADSSllqtniaLQLmeksqkEYEKlaaSLNEARQELSDKVRELSRSAGKTSLvEEAE 2149
Cdd:COG4913 862 IKERIDPLNdSLkRIPF-----GPGRY-------LRL------EARP---RPDPEVREFRQELRAVTSGASLFDE-ELSE 919
|
330
....*....|...
gi 767998703 2150 KHARSLQELAKQL 2162
Cdd:COG4913 920 ARFAALKRLIERL 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1889-2399 |
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 767998703 1889 NHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNvirnvHILLKQISGTDGEGNNVP 1968
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA-----RDSLIQSLATRLELDGFE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1969 SGDFS-REWAEAQRMMRELRN---RNFGKHLREAEADKRESQLLLNRIRTwqkthqgENNGLANSIRDSLNEYEAKLSDL 2044
Cdd:TIGR00606 384 RGPFSeRQIKNFHTLVIERQEdeaKTAAQLCADLQSKERLKQEQADEIRD-------EKKGLGRTIELKKEILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2045 RARLqeaaaqakqanglnQENERALGAIQRQVKeinsLQSDFTKYLttADSSLLQTNIALQLMEKSQKEYEKLAASLNEA 2124
Cdd:TIGR00606 457 KFVI--------------KELQQLEGSSDRILE----LDQELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2125 RQELSDKVRELSRSagKTSLvEEAEKHARSLQELAKQLEEIKRNASgDELVRCA---------VDAATAYENILNAIKAA 2195
Cdd:TIGR00606 517 LRKLDQEMEQLNHH--TTTR-TQMEMLTKDKMDKDEQIRKIKSRHS-DELTSLLgyfpnkkqlEDWLHSKSKEINQTRDR 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2196 EDAANRAASASESaLQTVIKEDLPRKAKTLSSNSDKLLN-------EAKMtqKKLKQEVSPAlnnlQQTLNIVTVQKEVI 2268
Cdd:TIGR00606 593 LAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDvcgsqdeESDL--ERLKEEIEKS----SKQRAMLAGATAVY 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2269 DTNLTTLRDGLHG----IQR-----GDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEdfkkalt 2339
Cdd:TIGR00606 666 SQFITQLTDENQSccpvCQRvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI------- 738
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998703 2340 dadnsVNKLTNKLPDLWRKIESINQQLLPL-GNISDN---MDRIRELIQQARDAASKVAVPMRF 2399
Cdd:TIGR00606 739 -----IDLKEKEIPELRNKLQKVNRDIQRLkNDIEEQetlLGTIMPEEESAKVCLTDVTIMERF 797
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
2.99e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998703 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 767998703 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1844-2137 |
3.41e-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: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1844 EQLRLVKSQLQGLSASAGLLEQMRH--------METQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA 1915
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1916 QVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQI----SGTDGEGNnvpsgdfSREWAEAQRMMRELRNRNF 1991
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleSELEALLN-------ERASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1992 GKHLREAEADKRESQLLLNRIRTwqkthqgennglansirdSLNEYEAKLSDLRARLQEAAAQakqangLNQENERALGA 2071
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELRE------------------KLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEE 955
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998703 2072 IQRQVKEINSLQS---DFTKYLTTADSSLLQTNI-ALQLMEKSQKEYEKLAA---SLNEARQELSDKVRELSR 2137
Cdd:TIGR02168 956 AEALENKIEDDEEearRRLKRLENKIKELGPVNLaAIEEYEELKERYDFLTAqkeDLTEAKETLEEAIEEIDR 1028
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1870-2143 |
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 767998703 1870 ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRN 1949
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1950 VhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFgkhLREAEADKREsqlllnrirtwqkthqge 2022
Cdd:COG3883 95 L-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADL---LEELKADKAE------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2023 nnglansirdsLNEYEAKLSDLRARLQEaaaqakqangLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2102
Cdd:COG3883 145 -----------LEAKKAELEAKLAELEA----------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767998703 2103 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2143
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1700-1792 |
6.39e-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: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1700 NQCQDGSGICVNCQHNTAGEhCERCQEGYYGNAV-HGSCRacPCPHTNSFATGCVVNG----GDVRCSCKAGYT------ 1768
Cdd:cd13406 16 HECPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVnYEPCK--PCTQCNQRSGSEEKQKctktSDTVCRCRPGTQpldsyk 92
|
90 100
....*....|....*....|....*
gi 767998703 1769 -GTQCERCAPGYFGNPQkfGGSCQP 1792
Cdd:cd13406 93 pGVDCVPCPPGHFSRGD--NQACKP 115
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
6.39e-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: 6.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998703 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
6.97e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 6.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 767998703 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1893-2170 |
7.14e-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: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1893 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAK----ELDVK-IKNVIRNVHILLKQISGTdgegnnv 1967
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdEIDVAsAEREIAELEAELERLDAS------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1968 pSGDFS---REWAEAQRMMRELRnrnfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYeakLSDL 2044
Cdd:COG4913 684 -SDDLAaleEQLEELEAELEELE-----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2045 RARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFtKYLTTADSSLLQTNIAlqLMEKSQKEYEKLAAS-LNE 2123
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDADLE--SLPEYLALLDRLEEDgLPE 831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767998703 2124 ARQELSDKVRELSRsAGKTSLVEEAEKHARSLQElakQLEEIkrNAS 2170
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 ... |
2059-2259 |
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 767998703 2059 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 2134
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2135 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 2191
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767998703 2192 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 2259
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 767998703 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1835-2127 |
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 767998703 1835 LLNDLAT--MGEQLRLVKSQLQglSASAGLLEQMRHMETQAKDLRNQLLNYRSA--ISNHGSKIEGLERELTDLNQEFET 1910
Cdd:COG3206 153 VANALAEayLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1911 LQEKAQVNSRKAQTLNNNVNRATQSAKEL--DVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRN 1988
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQ-------LRAQL-------------------AELEAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1989 RNFGKHLREAEADKRESQLllnrirtwqkthqgeNNGLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEnera 2068
Cdd:COG3206 285 RYTPNHPDVIALRAQIAAL---------------RAQLQQEAQRILASLEAELEALQAREAS----------LQAQ---- 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767998703 2069 LGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEKSQKEYEKLAASLNEARQE 2127
Cdd:COG3206 336 LAQLEARLAELPELEAELRR---------LEREV-----EVARELYESLLQRLEEARLA 380
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1887-2374 |
1.83e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1887 ISNHGSKIEGLERELTDLN---QEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE 1963
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIeliKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEEL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1964 GNNVPSG--DFSREWAEAQRMMRELRNRNFGKHLREAEAD-----------------KRESQLLLNRIR----------- 2013
Cdd:PTZ00440 604 INEALFNkeKFINEKNDLQEKVKYILNKFYKGDLQELLDElshflddhkylyheaksKEDLQTLLNTSKneyeklefmks 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2014 ------------------TWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQR 2074
Cdd:PTZ00440 684 dnidniiknlkkelqnllSLKENIIKKQlNNIEQDISNSLNQYTIKYNDLKSSI--------------EEYKEEEEKLEV 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2075 QVKEINSLQSDFTKYLTTADSSLLQ-TNIALQLMEK----SQKEyEKLAASLNEARQELSDKVRELSRSAGKTSLVE-EA 2148
Cdd:PTZ00440 750 YKHQIINRKNEFILHLYENDKDLPDgKNTYEEFLQYkdtiLNKE-NKISNDINILKENKKNNQDLLNSYNILIQKLEaHT 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2149 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAAS------ASESALQTV--------- 2213
Cdd:PTZ00440 829 EKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTlniainRSNSNKQLVehllnnkid 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2214 IKEDLPRKAKTLSSN-----SDK--LLNEAKMTQKKLKQEVSPA-LNNL----QQTLNIVTVQKEVIDTNLTTLRDGLHG 2281
Cdd:PTZ00440 909 LKNKLEQHMKIINTDniiqkNEKlnLLNNLNKEKEKIEKQLSDTkINNLkmqiEKTLEYYDKSKENINGNDGTHLEKLDK 988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2282 IQ------RGDIDAMISSAKSMVRKANDIT----DEVLDGLNPIQTD---------------VERIKDTYG-RTQNEDFK 2335
Cdd:PTZ00440 989 EKdewehfKSEIDKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEkgkeieekvdqyislLEKMKTKLSsFHFNIDIK 1068
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767998703 2336 KALTDA-DNSVNKLTNKLPDLWRKIESINQQLLPLGNISD 2374
Cdd:PTZ00440 1069 KYKNPKiKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSH 1108
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2060-2339 |
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 767998703 2060 GLNQENERALGAIQRQVKEIN-SLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYE-----------KLAASLNEARQE 2127
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtgiqnltaeieQGQESLTENLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2128 LSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA--SGDELVRCAVDAATAYENILNAIKAAEDAANRAASA 2205
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2206 SESALQTVIKEdLPRKAKTLSSNSDKLLNEAkmtQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRG 2285
Cdd:COG5185 439 VSKLLNELISE-LNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998703 2286 DIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDT-----------YGRTQNEDFKKALT 2339
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASnaktdgqaanlRTAVIDELTQYLST 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1822-2001 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1822 AEECDDCDSCVMTLlnDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHG--------S 1892
Cdd:COG4913 268 RERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1893 KIEGLERELTDLNQEFETLQEKAQV--------------NSRKAQ----TLNNNVNRATQSAKELDVKIKNVIRNVHILL 1954
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAAlglplpasaeefaaLRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767998703 1955 KQISGTDGEGNNVPsgdfsrewAEAQRMMRELRnrnfgKHLREAEAD 2001
Cdd:COG4913 426 AEIASLERRKSNIP--------ARLLALRDALA-----EALGLDEAE 459
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1671-1794 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1671 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1746
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767998703 1747 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1794
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1838-2431 |
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 767998703 1838 DLATMGEQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA-- 1915
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD-IETAAADQ-EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIke 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1916 ------------QVNSRKA----------------QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE---- 1963
Cdd:pfam12128 387 qnnrdiagikdkLAKIREArdrqlavaeddlqaleSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllql 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1964 GNNVPSGDFSREWAE--------AQRMMRELRNR--NFGKHLREAEA---------DKRESQL------LLNRIRT---- 2014
Cdd:pfam12128 467 ENFDERIERAREEQEaanaeverLQSELRQARKRrdQASEALRQASRrleerqsalDELELQLfpqagtLLHFLRKeapd 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2015 -----------------------WQKTHQGENN--GLANSI-RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERA 2068
Cdd:pfam12128 547 weqsigkvispellhrtdldpevWDGSVGGELNlyGVKLDLkRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2069 LGAIQRQVKEINSLQSDFTKYLTTADSSLLQ-----TNIALQLME-------KSQKEYEKLAASLN-------------- 2122
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRlfdekQSEKDKKNKalaerkdSANERLNSLEAQLKqldkkhqawleeqk 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2123 ----EARQELSDKVREL--SRSAGKTSLVEEAEKHARSLQELAKQLEE------IKRNASGDELVRCAVDAATAYENILN 2190
Cdd:pfam12128 707 eqkrEARTEKQAYWQVVegALDAQLALLKAAIAARRSGAKAELKALETwykrdlASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2191 AIKAAEDAANRAASASESALQtvikeDLPRKAKTLSSNSDKLLnEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDT 2270
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQ-----RRPRLATQLSNIERAIS-ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2271 NLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERikdtygrtQNEDFKKALTDADNSvnkltn 2350
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK--------YVEHFKNVIADHSGS------ 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2351 klpDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVrLPNDLEDLkgYTSLSLFLQRPN 2430
Cdd:pfam12128 927 ---GLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSI-LGVDLTEF--YDVLADFDRRIA 1000
|
.
gi 767998703 2431 S 2431
Cdd:pfam12128 1001 S 1001
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1975-2162 |
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 767998703 1975 EWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS----LNEYEAKLSDLRARLqe 2050
Cdd:COG4913 282 RLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLEREL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2051 aaaqakqanglnQENERALGAIQRQVKEI----NSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQ 2126
Cdd:COG4913 355 ------------EERERRRARLEALLAALglplPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRR 419
|
170 180 190
....*....|....*....|....*....|....*.
gi 767998703 2127 ELSDKVRELSRSAGKTSLVEEAEKHARslQELAKQL 2162
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 ... |
2061-2156 |
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 767998703 2061 LNQENERA-LGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRsa 2139
Cdd:pfam06009 24 QNLENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ----LEVNSSSLSDNISRIKE-- 97
|
90
....*....|....*..
gi 767998703 2140 gktsLVEEAEKHARSLQ 2156
Cdd:pfam06009 98 ----LIAQARKAANSIK 110
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1864-2392 |
3.67e-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: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1864 EQMRHMETQAKDLRNQLLNyrsaISNHGSKIEGLERELTDLNQEFETLQE--KAQVNSRKaqTLNNNVNRATQSAKELDV 1941
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLE----IDDEIIYINKLKLELKEKIKNISDKNEyiKKAIDLKK--IIENNNAYIDELAKISPY 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1942 KIKNVIRNVHILLKQISGtdgEGNNVPSGDFSREWAEAQRMMRE----------------------------LRNRNFGK 1993
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKS---ELSKIYEDDIDALYNELSSIVKEnaidntedkaklddlkskidkeydkiqnMETATVEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1994 HLREAEADKREsqlLLNRIRTWQKTHQGENNG---------------LANSI------RDSLNEYEAKLSDLRARLqeaA 2052
Cdd:TIGR01612 723 HLSNIENKKNE---LLDIIVEIKKHIHGEINKdlnkiledfknkekeLSNKIndyakeKDELNKYKSKISEIKNHY---N 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2053 AQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLT----TADSSLLQTNIALQL----MEKSQKEYEKLAASLNEA 2124
Cdd:TIGR01612 797 DQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINemkfMKDDFLNKVDKFINFenncKEKIDSEHEQFAELTNKI 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2125 RQELSDKvrELSRSAGK----TSLVEEA----EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNA-IKAA 2195
Cdd:TIGR01612 877 KAEISDD--KLNDYEKKfndsKSLINEInksiEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKnIDTI 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2196 EDAANRAASASESALQTVI--KEDLPRKAKTLS-----SNSDKLL---NEAKMTQKKLKQ--------EVSPALNNLQQt 2257
Cdd:TIGR01612 955 KESNLIEKSYKDKFDNTLIdkINELDKAFKDASlndyeAKNNELIkyfNDLKANLGKNKEnmlyhqfdEKEKATNDIEQ- 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2258 lNIVTVQKEV------IDTNLTTLRDglhgiqrgDIDAMISSAKSMVRKanditdEVLDGLNPIQTDVERIKDTYGRTQN 2331
Cdd:TIGR01612 1034 -KIEDANKNIpnieiaIHTSIYNIID--------EIEKEIGKNIELLNK------EILEEAEINITNFNEIKEKLKHYNF 1098
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998703 2332 EDF-KKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDN-MDRIRELIQQARDAASK 2392
Cdd:TIGR01612 1099 DDFgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENyIDEIKAQINDLEDVADK 1161
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1971-2176 |
4.02e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1971 DFSREWAEAQRMMRELRNRnFGKHLREAEADKRESQLLlnrirtwQKTHQgennglanSIRDSLN-------------EY 2037
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDL-------EQDYQ--------AASDHLNlvqtalrqqekieRY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2038 EAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQK----- 2112
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglp 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998703 2113 --EYEKLAASLNEAR---QELSDKVRELSRsagKTSLVEEA-EKHARSLQELAKQLEEIKRNASGD---ELVR 2176
Cdd:PRK04863 434 dlTADNAEDWLEEFQakeQEATEELLSLEQ---KLSVAQAAhSQFEQAYQLVRKIAGEVSRSEAWDvarELLR 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1840-2122 |
5.33e-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: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1840 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVN 1918
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1919 SRKAQTLNNNvnratqsaKELDvkiknvirnvhILLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRnrnfgKHLREA 1998
Cdd:COG1579 79 EEQLGNVRNN--------KEYE-----------ALQKEI-------------------ESLKRRISDLE-----DEILEL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1999 EaDKREsqlllnrirtwqkthqgennglanSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQrqvKE 2078
Cdd:COG1579 116 M-ERIE------------------------ELEEELAELEAELAELEAEL----------EEKKAELDEELAELE---AE 157
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767998703 2079 INSLQSDFTKYLTTADSSLLqtnialqlmeksqKEYEKLAASLN 2122
Cdd:COG1579 158 LEELEAEREELAAKIPPELL-------------ALYERIRKRKN 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1864-2182 |
6.17e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1864 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1940
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1941 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2007
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2008 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2079
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2080 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2153
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767998703 2154 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2182
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2097-2193 |
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 767998703 2097 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2170
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 767998703 2171 GDELvrcavdaATAYENILNAIK 2193
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3178-3314 |
6.61e-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: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 3178 HSVLLGPEFKLVFSIRPR-SLTGILIHI-GSQPGKHLCVYLEAGKVTAS-MDSGAGGTSTSVT-PKQSLCDGQWHSVAVT 3253
Cdd:smart00210 46 FPSGLPEDFSLLTTFRQTpKSRGVLFAIyDAQNVRQFGLEVDGRANTLLlRYQGVDGKQHTVSfRNLPLADGQWHKLALS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998703 3254 IKQHILHLELDTDSsytAGQIPFPPAStQEPLHLGGapANLTTLRIPVWKSFFGCLRNIHV 3314
Cdd:smart00210 126 VSGSSATLYVDCNE---IDSRPLDRPG-QPPIDTDG--IEVRGAQAADRKPFQGDLQQLKI 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1995-2173 |
8.51e-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: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 1995 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQE---NERALGA 2071
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRI----------RALEQElaaLEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998703 2072 IQRQV----KEINSLQSDFTKYLTTA--------------DSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2133
Cdd:COG4942 88 LEKEIaelrAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767998703 2134 ELSR-SAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE 2173
Cdd:COG4942 168 ELEAeRAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| |
