|
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 ... |
1849-2106 |
4.68e-107 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 343.24 E-value: 4.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1849 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1928
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1929 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2008
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2009 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2088
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 167887604 2089 ADSSLLQTNIALQLMEKS 2106
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
6.04e-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: 327.39 E-value: 6.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 167887604 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.25e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 167887604 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 ... |
2290-2418 |
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 167887604 2290 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2360
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 2361 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2418
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1520-1654 |
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 167887604 1520 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1597
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167887604 1598 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1654
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1516-1643 |
9.22e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1516 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1595
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 167887604 1596 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1643
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3160-3311 |
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 167887604 3160 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3238
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887604 3239 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3311
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3183-3312 |
3.39e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 3183 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3260
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 167887604 3261 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3312
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3188-3313 |
9.97e-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: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 3188 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3267
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 167887604 3268 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3313
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2996-3136 |
4.18e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2996 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3073
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887604 3074 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3136
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3013-3138 |
7.41e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 3013 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3089
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 167887604 3090 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3138
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2604-2744 |
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 167887604 2604 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2680
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 2681 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2744
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2623-2744 |
2.37e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2623 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2699
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 167887604 2700 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2744
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3020-3138 |
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 167887604 3020 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3096
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 167887604 3097 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3138
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2771-2903 |
6.83e-21 |
|
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: 91.71 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2771 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSD-SGSPIFKSPQTYMD 2847
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLgSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887604 2848 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2903
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1268-1316 |
7.45e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.93 E-value: 7.45e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167887604 1268 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1316
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2796-2905 |
2.67e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.07 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2796 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGSPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2871
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 167887604 2872 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2905
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2630-2744 |
5.38e-15 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 73.99 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2630 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2708
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 167887604 2709 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2744
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1267-1309 |
2.71e-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: 2.71e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 1267 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1309
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1840-2343 |
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 167887604 1840 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1901
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1902 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1971
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1972 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2047
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2048 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2127
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2128 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2206
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2207 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2280
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2281 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2341
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 167887604 2342 NK 2343
Cdd:TIGR04523 738 NK 739
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1268-1309 |
1.16e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.16e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167887604 1268 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1309
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1358-1409 |
4.68e-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: 4.68e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 167887604 1358 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1409
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
537-579 |
5.56e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 5.56e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 537 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 579
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
538-581 |
7.67e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 538 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 581
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1358-1403 |
8.30e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 8.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 1358 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1403
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1358-1404 |
1.73e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167887604 1358 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1404
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1406-1456 |
1.83e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1406 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1456
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2437-2572 |
2.09e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2437 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2510
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887604 2511 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2572
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1688-1734 |
2.25e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.25e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1688 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1734
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. |
493-540 |
3.21e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167887604 493 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 540
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1831-2165 |
6.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1831 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1909
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1910 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1981
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1982 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2050
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2051 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2124
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 167887604 2125 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2165
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1736-1786 |
7.02e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 7.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1736 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1786
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2392-2570 |
8.39e-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: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2392 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2471
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2472 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2545
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 167887604 2546 PPDFKLPSRLSFPPYKGCIELDDLN 2570
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1407-1455 |
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 167887604 1407 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1455
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
538-585 |
1.39e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.39e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 167887604 538 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 585
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.59e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.59e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
493-533 |
2.56e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.56e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167887604 493 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 533
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
493-535 |
5.71e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.71e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 493 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 535
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1735-1787 |
6.24e-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: 6.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 167887604 1735 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1787
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 167887604 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. |
1689-1736 |
1.29e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1689 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1736
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1407-1449 |
1.87e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 1407 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1449
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1736-1779 |
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 167887604 1736 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1779
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
4.62e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167887604 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 ... |
2799-2903 |
2.16e-08 |
|
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: 55.12 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2799 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGSP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2873
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 167887604 2874 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2903
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
633-684 |
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 167887604 633 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 684
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1689-1731 |
2.43e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 1689 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1731
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
633-673 |
4.67e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.67e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 167887604 633 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 673
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
633-683 |
4.70e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 4.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 633 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 683
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1858-2354 |
8.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1858 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1936
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1937 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2016
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2017 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2096
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2097 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2152
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2153 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2232
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2233 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2312
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 167887604 2313 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2354
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
587-630 |
4.94e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.89 E-value: 4.94e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 167887604 587 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 630
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 167887604 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2059-2377 |
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 167887604 2059 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2138
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2139 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2218
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2219 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2295
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2296 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2371
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 167887604 2372 MDRIRE 2377
Cdd:COG5185 529 FMRARG 534
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1973-2245 |
4.99e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.34 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1973 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2048
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2049 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2117
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2118 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2189
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 167887604 2190 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2245
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
6.65e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.42 E-value: 6.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 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 ... |
686-729 |
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 167887604 686 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 729
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
686-724 |
1.08e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.08e-05
10 20 30
....*....|....*....|....*....|....*....
gi 167887604 686 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 724
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1858-2389 |
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 167887604 1858 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1937
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1938 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2017
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2018 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2081
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2082 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2154
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2155 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2216
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2217 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2289
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2290 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2357
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 167887604 2358 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2389
Cdd:TIGR01612 1336 khnsdINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEI 1374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1840-2377 |
2.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1840 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1909
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1910 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1988
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1989 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2060
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2061 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2131
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2132 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2210
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2211 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2288
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2289 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2368
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 167887604 2369 SDNMDRIRE 2377
Cdd:PRK02224 697 RERREALEN 705
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2094-2258 |
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 167887604 2094 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2171
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2172 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2246
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 167887604 2247 LNNLQQTLNIVT 2258
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.10e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 5.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887604 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 ... |
2439-2565 |
5.68e-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: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2439 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2514
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 2515 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2565
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.05e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887604 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. |
686-724 |
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 167887604 686 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 724
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
588-630 |
6.51e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.03 E-value: 6.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167887604 588 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 630
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
588-630 |
6.89e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 6.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167887604 588 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 630
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.32e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167887604 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 ... |
1667-1790 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1667 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1742
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 167887604 1743 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1790
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1860-2178 |
6.16e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1860 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1936
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1937 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2003
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2004 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2075
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2076 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2149
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 167887604 2150 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2178
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2093-2189 |
6.35e-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: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2093 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2166
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 167887604 2167 GDELvrcavdaATAYENILNAIK 2189
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 ... |
1849-2106 |
4.68e-107 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 343.24 E-value: 4.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1849 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1928
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1929 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2008
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2009 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2088
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 167887604 2089 ADSSLLQTNIALQLMEKS 2106
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
6.04e-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: 327.39 E-value: 6.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 167887604 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.25e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 167887604 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 ... |
2290-2418 |
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 167887604 2290 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2360
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 2361 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2418
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1520-1654 |
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 167887604 1520 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1597
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167887604 1598 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1654
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1516-1643 |
9.22e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1516 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1595
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 167887604 1596 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1643
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3160-3311 |
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 167887604 3160 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3238
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887604 3239 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3311
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3183-3312 |
3.39e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 3183 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3260
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 167887604 3261 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3312
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3188-3313 |
9.97e-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: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 3188 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3267
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 167887604 3268 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3313
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2996-3136 |
4.18e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2996 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3073
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887604 3074 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3136
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3013-3138 |
7.41e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 3013 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3089
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 167887604 3090 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3138
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2604-2744 |
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 167887604 2604 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2680
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 2681 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2744
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2623-2744 |
2.37e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2623 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2699
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 167887604 2700 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2744
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3020-3138 |
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 167887604 3020 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3096
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 167887604 3097 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3138
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2771-2903 |
6.83e-21 |
|
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: 91.71 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2771 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSD-SGSPIFKSPQTYMD 2847
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLgSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887604 2848 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2903
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3020-3140 |
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 167887604 3020 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 3095
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 167887604 3096 LPGNSTISIRAPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPL 3140
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPL 130
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1268-1316 |
7.45e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.93 E-value: 7.45e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167887604 1268 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1316
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2796-2905 |
2.67e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.07 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2796 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGSPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2871
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 167887604 2872 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2905
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2630-2744 |
5.38e-15 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 73.99 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2630 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2708
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 167887604 2709 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2744
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1267-1309 |
2.71e-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: 2.71e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 1267 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1309
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1840-2343 |
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 167887604 1840 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1901
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1902 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1971
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1972 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2047
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2048 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2127
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2128 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2206
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2207 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2280
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2281 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2341
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 167887604 2342 NK 2343
Cdd:TIGR04523 738 NK 739
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3188-3315 |
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 167887604 3188 IRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSVAVTIKQHILHLELD------ 3260
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDgearpt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167887604 3261 -TDSSYTAGQIPFPpastqEPLHLGGAPANLTTLRI-PVWKSFFGCLRNIHVNHIPV 3315
Cdd:pfam00054 79 gESPLGATTDLDVD-----GPLYVGGLPSLGVKKRRlAISPSFDGCIRDVIVNGKPL 130
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1837-2288 |
3.39e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1837 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEF-ETLQEKAQVns 1915
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQF-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1916 rkaqtlnnnvnraTQSAKELDVKIKNVIRNVHILLKQISgTDGEGNNvpsgdfsREWAE-------AQRMMRELRNRNFG 1988
Cdd:pfam15921 369 -------------SQESGNLDDQLQKLLADLHKREKELS-LEKEQNK-------RLWDRdtgnsitIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1989 KHLREA--EADKRESQLLLNRirtWQKTHQGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAAQAKQANGL 2057
Cdd:pfam15921 428 VQRLEAllKAMKSECQGQMER---QMAAIQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2058 NQENERALGAIQRQVKEINS---LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRS 2134
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2135 AG-----KTSLVEEAEKHARSLQEL--------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKA 2190
Cdd:pfam15921 585 AGamqveKAQLEKEINDRRLELQEFkilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2191 aedaanraasaSESALQTvIKEDLPRKAKTLSSNSDkllnEAKMTQKKLKQEVSPALNNLQQTLNIVTvQKEVIDTNLTT 2270
Cdd:pfam15921 665 -----------SRNELNS-LSEDYEVLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMK 727
|
490 500
....*....|....*....|.
gi 167887604 2271 LRDGLHG---IQRGDIDAMIS 2288
Cdd:pfam15921 728 VAMGMQKqitAKRGQIDALQS 748
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1268-1309 |
1.16e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.16e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167887604 1268 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1309
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1358-1409 |
4.68e-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: 4.68e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 167887604 1358 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1409
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
537-579 |
5.56e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 5.56e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 537 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 579
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
538-581 |
7.67e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 538 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 581
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1358-1403 |
8.30e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 8.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 1358 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1403
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1838-2380 |
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 167887604 1838 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqEKAQVNSRK 1917
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1918 AQTLNNNVNRatqSAKELDVKIKNVIRN-VHI--LLKQISGTDGEGNNVpSGDFSREWAEAQRMMRELRNRNFGKHLREA 1994
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLeVELnkLEKQKKENKKNIDKF-LTEIKKKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1995 EADKRESQLllnrirtwqktHQGENNglANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKE 2074
Cdd:TIGR04523 174 ELNLLEKEK-----------LNIQKN--IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2075 INSLQSDF----TKYLTTADSsllQTNIALQLMEKsQKEYEK-------LAASLNEARQELSD----KVRELSRsagktS 2139
Cdd:TIGR04523 241 INEKTTEIsntqTQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQLNQLKSEISDlnnqKEQDWNK-----E 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2140 LVEEAEKHARSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKaaedaANRAASASE-SALQTVIKEDLpRKA 2218
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLK-----KELTNSESEnSEKQRELEEKQ-NEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2219 KTLSSNSDKLLNEAkmtqKKLKQEVspalNNLQQTLNIVTVQKEVIDTNLTTLRdglhgIQRGDIDAMISSAKSMVRKAN 2298
Cdd:TIGR04523 373 EKLKKENQSYKQEI----KNLESQI----NDLESKIQNQEKLNQQKDEQIKKLQ-----QEKELLEKEIERLKETIIKNN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2299 DITDEVLDGLNPIQTDVERIKDTygrtqNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPL--------GNISD 2370
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneekkeleEKVKD 514
|
570
....*....|
gi 167887604 2371 NMDRIRELIQ 2380
Cdd:TIGR04523 515 LTKKISSLKE 524
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1358-1404 |
1.73e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167887604 1358 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1404
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1406-1456 |
1.83e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1406 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1456
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2437-2572 |
2.09e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2437 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2510
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887604 2511 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2572
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1688-1734 |
2.25e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.25e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1688 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1734
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1873-2161 |
2.87e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1873 RNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK---AQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHIL 1949
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1950 LKQISGTDGEgnnvpsgdfsrewAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIrtwqkthqgenNGLANSIRDS 2029
Cdd:TIGR02168 749 IAQLSKELTE-------------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------KEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2030 LNEYEAKLSDLRARLQEAAAQAKQA-----------NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2098
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLerriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887604 2099 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSagKTSLVEEAEKHARSLQELAKQLEEI 2161
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. |
493-540 |
3.21e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167887604 493 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 540
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1833-2389 |
3.44e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 69.28 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1833 NDLATMGEQLRLVKSQLQglsasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSKIE---GLERELTDLNQEFETLQE 1909
Cdd:TIGR04523 162 NDLKKQKEELENELNLLE---------KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1910 KAQVNSRKAQTLNNNVNRATQ----------------SAKELDV-KIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREW 1972
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTqlnqlkdeqnkikkqlSEKQKELeQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1973 AEaqrmmrELRNRNfgKHLREAEADKRESQLLLNR-------IRTWQKTHQGENNglanSIRDSLNEYEAKLSDLrarlq 2045
Cdd:TIGR04523 313 KS------ELKNQE--KKLEEIQNQISQNNKIISQlneqisqLKKELTNSESENS----EKQRELEEKQNEIEKL----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2046 eaaaqakqanglNQENERALGAIQRQVKEINSLQSDFTKYltTADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQE 2123
Cdd:TIGR04523 376 ------------KKENQSYKQEIKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2124 LSDKVRElsrsagKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASE 2203
Cdd:TIGR04523 442 IKDLTNQ------DSVKELIIKNLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2204 SALQTVIKE---------DLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV--IDTNLTTLR 2272
Cdd:TIGR04523 496 KELKKLNEEkkeleekvkDLTKKISSLKEKIEKLESEKKEKESKISDLED-ELNKDDFELKKENLEKEIdeKNKEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2273 DglhgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIkdtygrtqnEDFKKALTDADNSVNKLTNKLPDLW 2352
Cdd:TIGR04523 575 Q--------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI---------SSLEKELEKAKKENEKLSSIIKNIK 637
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 167887604 2353 RKIESINQQllpLGNISDNMDRIR----ELIQQARDAASKV 2389
Cdd:TIGR04523 638 SKKNKLKQE---VKQIKETIKEIRnkwpEIIKKIKESKTKI 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1831-2165 |
6.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1831 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1909
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1910 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1981
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1982 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2050
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2051 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2124
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 167887604 2125 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2165
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1736-1786 |
7.02e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 7.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1736 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1786
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2392-2570 |
8.39e-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: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2392 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2471
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2472 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2545
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 167887604 2546 PPDFKLPSRLSFPPYKGCIELDDLN 2570
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1407-1455 |
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 167887604 1407 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1455
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
538-585 |
1.39e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.39e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 167887604 538 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 585
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.59e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.59e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
493-533 |
2.56e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.56e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167887604 493 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 533
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
493-535 |
5.71e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.71e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 493 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 535
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1735-1787 |
6.24e-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: 6.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 167887604 1735 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1787
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 167887604 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. |
1689-1736 |
1.29e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1689 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1736
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1831-2378 |
1.43e-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: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1831 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHmETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK 1910
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1911 AQVNSRKAQTLNNNVNRATQ---SAKELDVKIKNVIRNVHILLK---QISGTDG---EGNNVPSGdFSR--EWAEAQRM- 1978
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKnqsGLSGILGvlsELISVDEG-YEAaiEAALGGRLq 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1979 MRELRNRNFGK----HLREAEADKReSQLLLNRIR--------TWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQE 2046
Cdd:TIGR02168 549 AVVVENLNAAKkaiaFLKQNELGRV-TFLPLDSIKgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2047 AAAQAKQANGLNQENERAL------------GAIQRQ-VKEINSLQS------DFTKYLTTADSSLLQTNIALQLMEKSQ 2107
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRivtldgdlvrpgGVITGGsAKTNSSILErrreieELEEKIEELEEKIAELEKALAELRKEL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2108 KEYEKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAA 2178
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLAR--LEAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIE 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2179 TAYENILNAIKAAedaanraaSASESALQTVIKE--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ-------------EV 2243
Cdd:TIGR02168 786 ELEAQIEQLKEEL--------KALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedieSL 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2244 SPALNNLQQT-------LNIVTVQKEVIDTNLTTLRDglhgiQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVE 2316
Cdd:TIGR02168 858 AAEIEELEELieeleseLEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887604 2317 RIKDTYGRTQ---NEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2378
Cdd:TIGR02168 933 GLEVRIDNLQerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1407-1449 |
1.87e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167887604 1407 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1449
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1736-1779 |
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 167887604 1736 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1779
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1840-2187 |
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 167887604 1840 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1919
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1920 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEgnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEAD-K 1998
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----------LEELEEELEEAEEELEEAEAELAEAEEAlL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1999 RESQLLLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLQEAAAqakqangLNQENERALGAIQRQVKEINSL 2078
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLER-------LEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2079 QSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSdkvRELSRSAGKTSLVEEAEKHARSLQELAKQL 2158
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA---EAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340
....*....|....*....|....*....
gi 167887604 2159 EEIKRNASGDELVRCAVDAATAYENILNA 2187
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
4.62e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167887604 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFC 467
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1858-2156 |
1.49e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1858 LLEQMRHMETQAKDLRNQLlnyrSAISNHgskIEGLERELTDLNQEFETLQEK-AQVNSRKAQTLNNNVNRATQSAKELD 1936
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL----ASLEEE---LEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1937 VKIKNVIRNVHILLKQISGTDGEGNNVPSgDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQL--LLNRIRTWQKT 2014
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2015 HQgennglanSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL- 2093
Cdd:TIGR02169 380 FA--------ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIk 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 2094 -----LQTNIALqlMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 2156
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 ... |
1855-2384 |
1.55e-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: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1855 SAGLLEQMRHMETQAKDLRNQLLNYRSAIS-------NHGSKIEGLERELTDLNQEFETLQ-EKAQVNSRKAQtLNNNVN 1926
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQklqlekvTTEAKIKKLEEDILLLEDQNSKLSkERKLLEERISE-FTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1927 RATQSAKELDvKIKN----VIRNVHILLKQISGT-----------DGEgnnvpSGDFSREWAEAQRMMRELRnrnfgkhl 1991
Cdd:pfam01576 170 EEEEKAKSLS-KLKNkheaMISDLEERLKKEEKGrqelekakrklEGE-----STDLQEQIAELQAQIAELR-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1992 reAEADKRESQL--LLNRIrtwqKTHQGENNGLANSIRdslnEYEAKLSDLRARLqeaaaqakqanglnqENERALGAIQ 2069
Cdd:pfam01576 236 --AQLAKKEEELqaALARL----EEETAQKNNALKKIR----ELEAQISELQEDL---------------ESERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2070 RQVK-----EINSLQsdfTKYLTTADSsllqTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktslveea 2144
Cdd:pfam01576 291 EKQRrdlgeELEALK---TELEDTLDT----TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMR------------ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2145 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDAANRAASASESALQTV---------IKEDL 2214
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQDSEHKRKKLEGQLQELqarlseserQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2215 PRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LNIVTVQKEVIDTNLTTLRDGLHGIQrgdidamis 2288
Cdd:pfam01576 432 AEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETRQKLNLSTRLRQLEDERNSLQ--------- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2289 saksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2368
Cdd:pfam01576 503 --------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
570
....*....|....*.
gi 167887604 2369 SDNMDRIRELIQQARD 2384
Cdd:pfam01576 568 YDKLEKTKNRLQQELD 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1970-2391 |
1.70e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1970 REWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaa 2049
Cdd:COG4717 88 EEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERL----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2050 qakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2129
Cdd:COG4717 156 ---------EELRELEEELEELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2130 ELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAED 2193
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2194 AANRAASASESALQTVIKEDLPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnltt 2270
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE-------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2271 LRDGLHGIQRGDIDAMISSAK------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKL 2344
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 167887604 2345 TNKLpdlwRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAV 2391
Cdd:COG4717 452 REEL----AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2799-2903 |
2.16e-08 |
|
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: 55.12 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2799 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGSP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2873
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 167887604 2874 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2903
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
633-684 |
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 167887604 633 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 684
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1689-1731 |
2.43e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167887604 1689 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1731
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
633-673 |
4.67e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.67e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 167887604 633 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 673
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
633-683 |
4.70e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 4.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 633 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 683
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2628-2744 |
5.39e-08 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 54.25 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2628 IQTTVDRGLLFFAE--NGDRFISLNIEDGKLMVRYKLNSELPKERGvGDAINNGRDHSI---------QIKIGKLQKRMW 2696
Cdd:pfam00054 1 FRTTEPSGLLLYNGtqTERDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVelerngrsgTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 167887604 2697 INVDVQNTIIDGEvfdfSTYYLGGIPIAI--RERFNISTPaFRGCMKNLK 2744
Cdd:pfam00054 80 ESPLGATTDLDVD----GPLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1858-2354 |
8.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1858 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1936
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1937 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2016
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2017 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2096
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2097 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2152
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2153 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2232
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2233 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2312
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 167887604 2313 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2354
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1840-2356 |
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 167887604 1840 EQLRLVKSQLQGLSASAG-LLEQMRHMETQAKDLrnQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1918
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDrILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1919 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnNVPSGDFSREWAEAQR----MMRElRNRNFGKHLREA 1994
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG-------YFPNKKQLEDWLHSKSkeinQTRD-RLAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1995 EADKresqlllNRIRTWQKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAAQAKQANG-----------LNQEN 2061
Cdd:TIGR00606 604 EQNK-------NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDEN 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2062 ERALGAIQRQVK---EINSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT 2138
Cdd:TIGR00606 677 QSCCPVCQRVFQteaELQEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2139 -SLVEEAEKHARSLQELAKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRK 2217
Cdd:TIGR00606 754 qKVNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2218 AKTLSSNSDKLLNEAKMTQkKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTtlrdglhgiQRGDID----AMISSAKSM 2293
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ---------RRQQFEeqlvELSTEVQSL 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887604 2294 VRKANDITDEVLDGLNPIQTDVERiKDTYGRTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 2356
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1843-2182 |
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 167887604 1843 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN 1922
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1923 NNVNRATQSAKELDvkiknvirnvhillKQISGTDGEGNNVPSgdfSREWAEAQR-MMRELRNRNFGKhLREAEADKRES 2001
Cdd:PRK02224 377 EAVEDRREEIEELE--------------EEIEELRERFGDAPV---DLGNAEDFLeELREERDELRER-EAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2002 QlllNRIRtwqkthqgENNGL--------------ANSIRDSLNEYEAKLSDLRARLqeaAAQAKQANGLNQENERA--L 2065
Cdd:PRK02224 439 R---ERVE--------EAEALleagkcpecgqpveGSPHVETIEEDRERVEELEAEL---EDLEEEVEEVEERLERAedL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2066 GAIQRQVKEINSLQSDFTKYLTTADSSllqtnialqLMEKSQKeyeklAASLNEARQELSDKVRELSRSAgkTSLVEEAE 2145
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRET---------IEEKRER-----AEELRERAAELEAEAEEKREAA--AEAEEEAE 568
|
330 340 350
....*....|....*....|....*....|....*..
gi 167887604 2146 KHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYE 2182
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1840-2176 |
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 167887604 1840 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEkaqvnsrKAQ 1919
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1920 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVpsgdfsreWAEAQRMMRELRNRNFGKHLREAEADKR 1999
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL--------EQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2000 ESQL--LLNRIRTWQKTHQGENNGLANSIRDSLnEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINS 2077
Cdd:COG4372 156 EEQLesLQEELAALEQELQALSEAEAEQALDEL-LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2078 LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQ 2157
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330
....*....|....*....
gi 167887604 2158 LEEIKRNASGDELVRCAVD 2176
Cdd:COG4372 315 DALLAALLELAKKLELALA 333
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1840-2167 |
4.33e-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: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1840 EQLRLVKSQLQGLSAS-AGLLEQMRHMEtqakdlrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1918
Cdd:TIGR02169 674 AELQRLRERLEGLKRElSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1919 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQIsgtdgegnNVPSGDFSRE-WAEAQRMMREL---RNRNFG------ 1988
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--------NDLEARLSHSrIPEIQAELSKLeeeVSRIEArlreie 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1989 -----KHLREAEADKrESQLLLNRIRTWQ------KTHQGENNGLANSIRDSLNEYEAKLSDLRARLQeaaaqakqanGL 2057
Cdd:TIGR02169 819 qklnrLTLEKEYLEK-EIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLG----------DL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2058 NQENERA---LGAIQRQVKEINSlqsdftkYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-------- 2126
Cdd:TIGR02169 888 KKERDELeaqLRELERKIEELEA-------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqael 960
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 167887604 2127 -KVRELSRSAGKTSL--VEEAEKHARSLQELAKQLEEIKRNASG 2167
Cdd:TIGR02169 961 qRVEEEIRALEPVNMlaIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1840-2160 |
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 167887604 1840 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNhgskiegLERELTDLNQEFETLQEKAQvnsrKAQ 1919
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-------IEKRLSRLEEEINGIEERIK----ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1920 TLNNNVNRATQSAKELDVKIkNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNfgKHLRE------ 1993
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEeiskit 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1994 ---AEADKRESQLLLNRI-------------RTWQKTHQGEnnglansirdSLNEYEAKLSDLRARLQEAaaqakqangl 2057
Cdd:PRK03918 412 ariGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKE----------LLEEYTAELKRIEKELKEI---------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2058 nQENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLNEARQELSDKVREL 2131
Cdd:PRK03918 472 -EEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350
....*....|....*....|....*....|...
gi 167887604 2132 SRSAG----KTSLVEEAEKHARSLQELAKQLEE 2160
Cdd:PRK03918 549 EKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
587-630 |
4.94e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.89 E-value: 4.94e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 167887604 587 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 630
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1950-2163 |
5.66e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1950 LKQISGTDgegnnvpsgDFSREWAEAQRMMRELRNRnfgkhlREAEAD--KRESQLLlNRIRTwQKTHQGENNGLANSIR 2027
Cdd:PRK03918 151 VRQILGLD---------DYENAYKNLGEVIKEIKRR------IERLEKfiKRTENIE-ELIKE-KEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2028 DSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKylTTADSSLLQTNIA-LQLMEKS 2106
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKeLKELKEK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887604 2107 QKEYEKLAASLNEARQELSDKVRELSR----SAGKTSLVEEAEKHARSLQELAKQLEEIKR 2163
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 167887604 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 ... |
3002-3140 |
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 167887604 3002 KLPQELLkPRSQFAVDM-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 3075
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887604 3076 GHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 3140
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2059-2377 |
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 167887604 2059 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2138
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2139 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2218
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2219 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2295
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2296 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2371
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 167887604 2372 MDRIRE 2377
Cdd:COG5185 529 FMRARG 534
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1801-2255 |
2.51e-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: 53.82 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1801 HPLTGDCINQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSA----SAGLLEQMRHMET--QAKDLRN 1874
Cdd:TIGR00618 279 LEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkqQSSIEEQRRLLQTlhSQEIHIR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1875 QLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA-TQSAKELDVKIKNVIRNVHILLKQI 1953
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRDLQGQLAHAKKQQELQQR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1954 SGTDGE--GNNVPSGDFSREwAEAQRMMRELRNRNFGK------HLREAEADKRESQLLLNrirtwqktHQGENNGLANS 2025
Cdd:TIGR00618 439 YAELCAaaITCTAQCEKLEK-IHLQESAQSLKEREQQLqtkeqiHLQETRKKAVVLARLLE--------LQEEPCPLCGS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2026 IRdslnEYEAKLSDL-----RARLQEAAAQAKQANGLNQENERALG-AIQRQVK----EINSLQSDFTKYLTTADSSLLQ 2095
Cdd:TIGR00618 510 CI----HPNPARQDIdnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRAslkeQMQEIQQSFSILTQCDNRSKED 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2096 TNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE----LV 2171
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehAL 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2172 RCAVDAATAYENILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQ 2251
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
....
gi 167887604 2252 QTLN 2255
Cdd:TIGR00618 743 QSLK 746
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1973-2245 |
4.99e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.34 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1973 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2048
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2049 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2117
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2118 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2189
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 167887604 2190 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2245
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
6.65e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.42 E-value: 6.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1839-2244 |
6.68e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1839 GEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRnQLLNYRSAISnhgSKIEGLERELTDLNQEFETLQEKAQvnsrkA 1918
Cdd:COG4717 63 GRKPELNLKELKELE------EELKEAEEKEEEYA-ELQEELEELE---EELEELEAELEELREELEKLEKLLQ-----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1919 QTLNNNVNRATQSAKELDVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEADK 1998
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-------LEERL----------------EELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1999 RESQLLLNRIRTWQKTHQgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER--------ALGAIQR 2070
Cdd:COG4717 185 QLSLATEEELQDLAEELE-ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2071 QVKEINSLQSDFTKYLTTAdSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-KVRELSRSAG-----KTSLVEEA 2144
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLV-LGLLALLFLLLAREKASLGKEAEELQALPALEELEEeELEELLAALGlppdlSPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2145 EKHARSLQELAKQLEEIKR------------------NASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESAL 2206
Cdd:COG4717 343 LDRIEELQELLREAEELEEelqleeleqeiaallaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 167887604 2207 QTVIKEDLPRKAKTLSSNSDKL---LNEAKMTQKKLKQEVS 2244
Cdd:COG4717 423 EALDEEELEEELEELEEELEELeeeLEELREELAELEAELE 463
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
686-729 |
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 167887604 686 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 729
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
686-724 |
1.08e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.08e-05
10 20 30
....*....|....*....|....*....|....*....
gi 167887604 686 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 724
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1860-2170 |
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 167887604 1860 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTD-------LNQEFETLQEKAQVNSRKAQTLNNNVNRATQSA 1932
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrdeLNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1933 KELDVKIKNVIRNVHILLKQISGTDGEGNNVPS--------------GDFSREW-----AEAQRMMRELRNRnfgKHLRE 1993
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqqtEVLSPEEekelvEKIKELEKELEKA---KKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1994 AEADKREsqlLLNRIRTWQKthqgenngLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEneralgaIQRQVK 2073
Cdd:COG1340 158 KNEKLKE---LRAELKELRK--------EAEEIHKKIKELAEEAQELHEEMIE----------LYKE-------ADELRK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2074 EINSLQSDFTKYLTTADssllqtnialqlMEKsqKEYEKLAASLNEARQELsDKVRELSRSAGKTSLVEEAEKHARSLqe 2153
Cdd:COG1340 210 EADELHKEIVEAQEKAD------------ELH--EEIIELQKELRELRKEL-KKLRKKQRALKREKEKEELEEKAEEI-- 272
|
330
....*....|....*....
gi 167887604 2154 lakqLEEIKRNA--SGDEL 2170
Cdd:COG1340 273 ----FEKLKKGEklTTEEL 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1911-2278 |
1.45e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1911 AQVNSRKAQTLNNnVNRATQSAKELDVKIKNVIRNVHILLKQisgtdgegnnvpsgdfsREWAEA-QRMMRELRNRNFGK 1989
Cdd:TIGR02169 166 AEFDRKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRRE-----------------REKAERyQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1990 HLREAEADKRESQLLLNRIrtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQakqangLNQENER--ALGA 2067
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL---------------ASLEEELEKLTEEISELEKRLEEIEQL------LEELNKKikDLGE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2068 iqrqvKEINSLQSDFTKylTTADSSLLQTNIAL--QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-KTSLVEE- 2143
Cdd:TIGR02169 287 -----EEQLRVKEKIGE--LEAEIASLERSIAEkeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrRDKLTEEy 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2144 -----------------AEKHARSLQELAK----------QLEEIKRNAS--GDELVRcavdAATAYENILNAIKAAEDA 2194
Cdd:TIGR02169 360 aelkeeledlraeleevDKEFAETRDELKDyrekleklkrEINELKRELDrlQEELQR----LSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2195 ANRAASASESAlQTVIKEDlPRKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQQTLNIVTVQKEVIDT-------N 2267
Cdd:TIGR02169 436 INELEEEKEDK-ALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEErvrggraV 512
|
410
....*....|.
gi 167887604 2268 LTTLRDGLHGI 2278
Cdd:TIGR02169 513 EEVLKASIQGV 523
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1859-2390 |
1.48e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 50.79 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1859 LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK 1938
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1939 IKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNR---IRTWQKTH 2015
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLAlalLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2016 QGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINslQSDFTKYLTTadssllq 2095
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDV------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2096 tnialqlmeKSQKEYEKLAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcav 2175
Cdd:COG0840 232 ---------DSKDEIGQLADAFNRMIENLRELVGQVRESA--EQVASASEELAASAEELAAGAEEQAASLE--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2176 DAATAYENILNAIKaaedaanraaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQKKLK---QEVSPALNNL-- 2250
Cdd:COG0840 292 ETAAAMEELSATVQ----------EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGIEEIResvEETAETIEELge 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2251 --QQTLNIVTVQKEVID-TNLTTL-------RDGLHGiqRG--------------------DIDAMISSAKSMVRKANDI 2300
Cdd:COG0840 359 ssQEIGEIVDVIDDIAEqTNLLALnaaieaaRAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2301 TDEVLDGlnpIQTDVERIKDTygrtqnedfKKALTDADNSVNKLTNKLpdlwRKI-ESINQQLLPLGNISDNMDRIRELI 2379
Cdd:COG0840 437 MEEGSEE---VEEGVELVEEA---------GEALEEIVEAVEEVSDLI----QEIaAASEEQSAGTEEVNQAIEQIAAAA 500
|
570
....*....|.
gi 167887604 2380 QQARDAASKVA 2390
Cdd:COG0840 501 QENAASVEEVA 511
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1858-2389 |
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 167887604 1858 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1937
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1938 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2017
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2018 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2081
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2082 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2154
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2155 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2216
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2217 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2289
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2290 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2357
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 167887604 2358 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2389
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 ... |
2064-2350 |
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 167887604 2064 ALGAIQRQVKEINSLQSDFTKYLTtadSSLLQTNIALQLMEKSQKEYEklaaSLNEARQELSDKVRELSRSAGK------ 2137
Cdd:pfam06008 6 SLTGALPAPYKINYNLENLTKQLQ---EYLSPENAHKIQIEILEKELS----SLAQETEELQKKATQTLAKAQQvnaese 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2138 ------TSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcavdaATAYENILNAIKAAEDAANRAASASESALQTVIK 2211
Cdd:pfam06008 79 rtlghaKELAEAIKNLIDNIKEINEKVATLGENDF-----------ALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2212 EDLpRKAKtlssnsdKLLNEAKMTQKKLKQEVSPALNNLQQTLNivtvqkeviDTNlttlrDGLHgiqrgDIDAMISSAK 2291
Cdd:pfam06008 148 AEL-KAAQ-------DLLSRIQTWFQSPQEENKALANALRDSLA---------EYE-----AKLS-----DLRELLREAA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887604 2292 SMVRKANDITDEVLDGLNPIQTDVERIkdtygRTQNEDFKKALTDADNSV---NKLTNKLPD 2350
Cdd:pfam06008 201 AKTRDANRLNLANQANLREFQRKKEEV-----SEQKNQLEETLKTARDSLdaaNLLLQEIDD 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1840-2377 |
2.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1840 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1909
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1910 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1988
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1989 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2060
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2061 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2131
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2132 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2210
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2211 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2288
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2289 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2368
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 167887604 2369 SDNMDRIRE 2377
Cdd:PRK02224 697 RERREALEN 705
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1842-2172 |
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 167887604 1842 LRLVKSQLQG-----LSASAGL---LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 1913
Cdd:pfam15921 435 LKAMKSECQGqmerqMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1914 NSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDgegnnvpsgdfsrEWAEAQRMMRELRNRNFGKH 1990
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKD-------------KVIEILRQQIENMTQLVGQH 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1991 LREAEADKRESQLLLNRIRTwQKTHQGENNGLANSIRDSLNEYEAKLSDL---RARLQEAAAQA-KQANGLNQENERALG 2066
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEIND-RRLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSERlRAVKDIKQERDQLLN 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2067 AIQRQVKEINSLQSDF---------------------TKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLneaRQELS 2125
Cdd:pfam15921 661 EVKTSRNELNSLSEDYevlkrnfrnkseemetttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM---QKQIT 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 167887604 2126 DKVRELSRSAGKTSLVEEA------EKH------ARSLQELAKQLEEIKRNASGDELVR 2172
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAmtnankEKHflkeekNKLSQELSTVATEKNKMAGELEVLR 796
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1810-2078 |
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 167887604 1810 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGlsasaglLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1889
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-------AEDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1890 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDGEGNNVPSg 1966
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKlaeLKERIESLERIRTLLAAIADAEDEIER- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1967 dfSREWAEAQRMMRELRnrnfgkhlREAEADKREsqlllnRIRTWQKTHQGENNGLANSIRDSLNEY----EAKLSDLRA 2042
Cdd:PRK02224 611 --LREKREALAELNDER--------RERLAEKRE------RKRELEAEFDEARIEEAREDKERAEEYleqvEEKLDELRE 674
|
250 260 270
....*....|....*....|....*....|....*.
gi 167887604 2043 RlqeaaaqakqanglNQENERALGAIQRQVKEINSL 2078
Cdd:PRK02224 675 E--------------RDDLQAEIGAVENELEELEEL 696
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1973-2189 |
3.28e-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: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1973 AEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRtwqkthqgENNGL------ANSIRDSLNEYEAKLSDLRARLQE 2046
Cdd:COG3206 171 EEARKALEFLEEQ-----LPELRKELEEAEAALEEFR--------QKNGLvdlseeAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2047 AAAQAKQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLT--TADSSL---LQTNIAlQLMEKSQKEYEKLAA 2115
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSAryTPNHPDviaLRAQIA-ALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887604 2116 SLNEARQELSDKVRELSRSagktslVEEAEKHARSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 2189
Cdd:COG3206 317 SLEAELEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1975-2304 |
4.00e-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: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1975 AQRMmRELRNRnfgkhLREAEADkresqLLLNRIRtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQA 2054
Cdd:TIGR02168 212 AERY-KELKAE-----LRELELA-----LLVLRLE--------ELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2055 NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL--LQTNIA-----LQLMEKSQKEYEKLAASLNEARQELSDK 2127
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2128 VrelsrsagkTSLVEEAEKHARSLQELAKQLEEIKRNAsgdELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQ 2207
Cdd:TIGR02168 353 L---------ESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2208 TVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQrgdidAMI 2287
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQ-----ARL 491
|
330
....*....|....*..
gi 167887604 2288 SSAKSMVRKANDITDEV 2304
Cdd:TIGR02168 492 DSLERLQENLEGFSEGV 508
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2094-2258 |
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 167887604 2094 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2171
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2172 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2246
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 167887604 2247 LNNLQQTLNIVT 2258
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1991-2309 |
4.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1991 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQR 2070
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEEL----------EELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2071 QVKEINSLQSDFTKY------LTTADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEA 2144
Cdd:COG4372 99 AQEELESLQEEAEELqeeleeLQKERQDLEQQRKQL---EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2145 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSN 2224
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2225 SDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEV 2304
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
....*
gi 167887604 2305 LDGLN 2309
Cdd:COG4372 336 LAELA 340
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1810-1940 |
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 167887604 1810 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1889
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 1890 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIK 1940
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.10e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 5.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887604 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 ... |
2439-2565 |
5.68e-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: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2439 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2514
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 167887604 2515 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2565
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1827-2140 |
5.91e-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: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1827 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFE 1905
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1906 TLQEKaqvnsrkaqtlnnnVNRATQSAKELDVKIKNVIRNvhillkqisgtdgegnnvpsgdfsrewaeAQRMMRE---- 1981
Cdd:COG4942 87 ELEKE--------------IAELRAELEAQKEELAELLRA-----------------------------LYRLGRQppla 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1982 --LRNRNFGKHLREAEADKRESQLLLNRIRTWQKThqgennglansiRDSLNEYEAKLSDLRARLqeaaaqakqanglnq 2059
Cdd:COG4942 124 llLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------LAELAALRAELEAERAEL--------------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2060 enERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2139
Cdd:COG4942 177 --EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 167887604 2140 L 2140
Cdd:COG4942 255 L 255
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1871-2392 |
7.25e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1871 DLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN---NNVNRATQSAKELDVKIK------- 1940
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKtaesdls 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1941 ----------------------------NVIRNVHILLKQI-------SGTDGEGNNVPSG--------DFSREWAEAQR 1977
Cdd:PRK01156 267 meleknnyykeleerhmkiindpvyknrNYINDYFKYKNDIenkkqilSNIDAEINKYHAIikklsvlqKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1978 MMRELRN-------------------RNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLS 2038
Cdd:PRK01156 347 RYDDLNNqilelegyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2039 DLRARLQEAAAQAK----QANGLNQENERALGAIQRQVKEINSLQSDFTKylttaDSSLLQTNIalqlmeksqKEYEKLA 2114
Cdd:PRK01156 427 SLNQRIRALRENLDelsrNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE-----KKSRLEEKI---------REIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2115 ASLNEARQELsdkVRELSRSAGKTslVEEAEKHARSLQELAKQLEEIKrnasgDELVRCAvDAATAYENILNAIKAAEDA 2194
Cdd:PRK01156 493 KDIDEKIVDL---KKRKEYLESEE--INKSINEYNKIESARADLEDIK-----IKINELK-DKHDKYEEIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2195 ANRAASASESALQTVI-----------KEDLPRKAKTLSSNSDKLLNE----AKMTQKKLKqEVSPALNNLQQTLNIVTV 2259
Cdd:PRK01156 562 DLDSKRTSWLNALAVIslidietnrsrSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIR-EIENEANNLNNKYNEIQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2260 QKEVIDTNLTTLRDglHGIQRGDIDAMISSAKSMVRKANDITDEvldgLNPIQTDVERIKDTYGRtqnedfKKALTDADN 2339
Cdd:PRK01156 641 NKILIEKLRGKIDN--YKKQIAEIDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRAR------LESTIEILR 708
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 167887604 2340 S-VNKLTNKLPDLWRKIESINQQLLPLGNIsdnmDRIREliqqardAASKVAVP 2392
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 ... |
1835-2180 |
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 167887604 1835 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN----- 1901
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1902 --QEFETLQEKAQVNSRKAQTLNNNVN--RATQSAKE------------------------------LDVKiknvIRNVH 1947
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVDalRLRLEEKEsflnkktkqlqdlteekstlageirdlkdmLDVK----ERKIN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1948 ILLKQISgtdgegnnvpsgDFSREWAEAQRMMRELRNRNFGKH------------LREAEADK------------RESQL 2003
Cdd:pfam10174 398 VLQKKIE------------NLQEQLRDKDKQLAGLKERVKSLQtdssntdtalttLEEALSEKeriierlkeqreREDRE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2004 LLNRIRTWQKthqgENNGL---ANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENEralGAIQRQVKEINSLQS 2080
Cdd:pfam10174 466 RLEELESLKK----ENKDLkekVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE---IAVEQKKEECSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2081 DFTKYLTTADSSLLQTNIA--LQLME-----------KSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL-VEEAEK 2146
Cdd:pfam10174 539 QLKKAHNAEEAVRTNPEINdrIRLLEqevarykeesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRqMKEQNK 618
|
410 420 430
....*....|....*....|....*....|....
gi 167887604 2147 HARSLQelAKQLEEIKRNASGDELVRCAVDAATA 2180
Cdd:pfam10174 619 KVANIK--HGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1861-2092 |
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 167887604 1861 QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQsakeldvKIK 1940
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1941 NVIRNVhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFGKHLREAEADKRESQLLLNRIRTWQK 2013
Cdd:COG3883 90 ERARAL-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887604 2014 THQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSS 2092
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1834-2158 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1834 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE 1909
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1910 KAQVNSRkaQTLNNNVNRATQSAKELDVKiknvirnvHILLKQISGTDGEGNnvpsgdfsREWAEAQRMMRELRNR--NF 1987
Cdd:COG4913 742 LARLELR--ALLEERFAAALGDAVERELR--------ENLEERIDALRARLN--------RAEEELERAMRAFNREwpAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1988 GKHLREAEADKRESQLLLNRIrtwqkthqgENNGLAnsirdslnEYEAKLSDLRARLQEAAAQakqanGLNQENERALGA 2067
Cdd:COG4913 804 TADLDADLESLPEYLALLDRL---------EEDGLP--------EYEERFKELLNENSIEFVA-----DLLSKLRRAIRE 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2068 IQRQVKEIN-SL-QSDFtkyltTADSSllqtniaLQLmeksqkEYEKlaaSLNEARQELSDKVRELSRSAGKTSLvEEAE 2145
Cdd:COG4913 862 IKERIDPLNdSLkRIPF-----GPGRY-------LRL------EARP---RPDPEVREFRQELRAVTSGASLFDE-ELSE 919
|
330
....*....|...
gi 167887604 2146 KHARSLQELAKQL 2158
Cdd:COG4913 920 ARFAALKRLIERL 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1885-2395 |
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 167887604 1885 NHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNvirnvHILLKQISGTDGEGNNVP 1964
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA-----RDSLIQSLATRLELDGFE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1965 SGDFS-REWAEAQRMMRELRN---RNFGKHLREAEADKRESQLLLNRIRTwqkthqgENNGLANSIRDSLNEYEAKLSDL 2040
Cdd:TIGR00606 384 RGPFSeRQIKNFHTLVIERQEdeaKTAAQLCADLQSKERLKQEQADEIRD-------EKKGLGRTIELKKEILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2041 RARLqeaaaqakqanglnQENERALGAIQRQVKeinsLQSDFTKYLttADSSLLQTNIALQLMEKSQKEYEKLAASLNEA 2120
Cdd:TIGR00606 457 KFVI--------------KELQQLEGSSDRILE----LDQELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2121 RQELSDKVRELSRSagKTSLvEEAEKHARSLQELAKQLEEIKRNASgDELVRCA---------VDAATAYENILNAIKAA 2191
Cdd:TIGR00606 517 LRKLDQEMEQLNHH--TTTR-TQMEMLTKDKMDKDEQIRKIKSRHS-DELTSLLgyfpnkkqlEDWLHSKSKEINQTRDR 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2192 EDAANRAASASESaLQTVIKEDLPRKAKTLSSNSDKLLN-------EAKMtqKKLKQEVSPAlnnlQQTLNIVTVQKEVI 2264
Cdd:TIGR00606 593 LAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDvcgsqdeESDL--ERLKEEIEKS----SKQRAMLAGATAVY 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2265 DTNLTTLRDGLHG----IQR-----GDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEdfkkalt 2335
Cdd:TIGR00606 666 SQFITQLTDENQSccpvCQRvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI------- 738
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887604 2336 dadnsVNKLTNKLPDLWRKIESINQQLLPL-GNISDN---MDRIRELIQQARDAASKVAVPMRF 2395
Cdd:TIGR00606 739 -----IDLKEKEIPELRNKLQKVNRDIQRLkNDIEEQetlLGTIMPEEESAKVCLTDVTIMERF 797
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.05e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887604 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. |
686-724 |
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 167887604 686 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 724
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1840-2133 |
3.40e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1840 EQLRLVKSQLQGLSASAGLLEQMRH--------METQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA 1911
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1912 QVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQI----SGTDGEGNnvpsgdfSREWAEAQRMMRELRNRNF 1987
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleSELEALLN-------ERASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1988 GKHLREAEADKRESQLLLNRIRTwqkthqgennglansirdSLNEYEAKLSDLRARLQEAAAQakqangLNQENERALGA 2067
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELRE------------------KLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEE 955
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887604 2068 IQRQVKEINSLQS---DFTKYLTTADSSLLQTNI-ALQLMEKSQKEYEKLAA---SLNEARQELSDKVRELSR 2133
Cdd:TIGR02168 956 AEALENKIEDDEEearRRLKRLENKIKELGPVNLaAIEEYEELKERYDFLTAqkeDLTEAKETLEEAIEEIDR 1028
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1866-2139 |
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 167887604 1866 ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRN 1945
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1946 VhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFgkhLREAEADKREsqlllnrirtwqkthqge 2018
Cdd:COG3883 95 L-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADL---LEELKADKAE------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2019 nnglansirdsLNEYEAKLSDLRARLQEaaaqakqangLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2098
Cdd:COG3883 145 -----------LEAKKAELEAKLAELEA----------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 167887604 2099 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2139
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1696-1788 |
6.38e-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: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1696 NQCQDGSGICVNCQHNTAGEhCERCQEGYYGNAV-HGSCRacPCPHTNSFATGCVVNG----GDVRCSCKAGYT------ 1764
Cdd:cd13406 16 HECPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVnYEPCK--PCTQCNQRSGSEEKQKctktSDTVCRCRPGTQpldsyk 92
|
90 100
....*....|....*....|....*
gi 167887604 1765 -GTQCERCAPGYFGNPQkfGGSCQP 1788
Cdd:cd13406 93 pGVDCVPCPPGHFSRGD--NQACKP 115
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
588-630 |
6.51e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.03 E-value: 6.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167887604 588 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 630
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
588-630 |
6.89e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 6.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167887604 588 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 630
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1889-2166 |
7.19e-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: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1889 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAK----ELDVK-IKNVIRNVHILLKQISGTdgegnnv 1963
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdEIDVAsAEREIAELEAELERLDAS------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1964 pSGDFS---REWAEAQRMMRELRnrnfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYeakLSDL 2040
Cdd:COG4913 684 -SDDLAaleEQLEELEAELEELE-----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2041 RARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFtKYLTTADSSLLQTNIAlqLMEKSQKEYEKLAAS-LNE 2119
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDADLE--SLPEYLALLDRLEEDgLPE 831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 167887604 2120 ARQELSDKVRELSRsAGKTSLVEEAEKHARSLQElakQLEEIkrNAS 2166
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 ... |
2055-2255 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2055 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 2130
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2131 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 2187
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887604 2188 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 2255
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEELKEKLT 317
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.32e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167887604 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1831-2123 |
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 167887604 1831 LLNDLAT--MGEQLRLVKSQLQglSASAGLLEQMRHMETQAKDLRNQLLNYRSA--ISNHGSKIEGLERELTDLNQEFET 1906
Cdd:COG3206 153 VANALAEayLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1907 LQEKAQVNSRKAQTLNNNVNRATQSAKEL--DVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRN 1984
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQ-------LRAQL-------------------AELEAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1985 RNFGKHLREAEADKRESQLllnrirtwqkthqgeNNGLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEnera 2064
Cdd:COG3206 285 RYTPNHPDVIALRAQIAAL---------------RAQLQQEAQRILASLEAELEALQAREAS----------LQAQ---- 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 167887604 2065 LGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEKSQKEYEKLAASLNEARQE 2123
Cdd:COG3206 336 LAQLEARLAELPELEAELRR---------LEREV-----EVARELYESLLQRLEEARLA 380
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1883-2370 |
1.81e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1883 ISNHGSKIEGLERELTDLN---QEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE 1959
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIeliKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEEL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1960 GNNVPSG--DFSREWAEAQRMMRELRNRNFGKHLREAEAD-----------------KRESQLLLNRIR----------- 2009
Cdd:PTZ00440 604 INEALFNkeKFINEKNDLQEKVKYILNKFYKGDLQELLDElshflddhkylyheaksKEDLQTLLNTSKneyeklefmks 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2010 ------------------TWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQR 2070
Cdd:PTZ00440 684 dnidniiknlkkelqnllSLKENIIKKQlNNIEQDISNSLNQYTIKYNDLKSSI--------------EEYKEEEEKLEV 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2071 QVKEINSLQSDFTKYLTTADSSLLQ-TNIALQLMEK----SQKEyEKLAASLNEARQELSDKVRELSRSAGKTSLVE-EA 2144
Cdd:PTZ00440 750 YKHQIINRKNEFILHLYENDKDLPDgKNTYEEFLQYkdtiLNKE-NKISNDINILKENKKNNQDLLNSYNILIQKLEaHT 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2145 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAAS------ASESALQTV--------- 2209
Cdd:PTZ00440 829 EKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTlniainRSNSNKQLVehllnnkid 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2210 IKEDLPRKAKTLSSN-----SDK--LLNEAKMTQKKLKQEVSPA-LNNL----QQTLNIVTVQKEVIDTNLTTLRDGLHG 2277
Cdd:PTZ00440 909 LKNKLEQHMKIINTDniiqkNEKlnLLNNLNKEKEKIEKQLSDTkINNLkmqiEKTLEYYDKSKENINGNDGTHLEKLDK 988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2278 IQ------RGDIDAMISSAKSMVRKANDIT----DEVLDGLNPIQTD---------------VERIKDTYG-RTQNEDFK 2331
Cdd:PTZ00440 989 EKdewehfKSEIDKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEkgkeieekvdqyislLEKMKTKLSsFHFNIDIK 1068
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 167887604 2332 KALTDA-DNSVNKLTNKLPDLWRKIESINQQLLPLGNISD 2370
Cdd:PTZ00440 1069 KYKNPKiKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSH 1108
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2056-2335 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2056 GLNQENERALGAIQRQVKEIN-SLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYE-----------KLAASLNEARQE 2123
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtgiqnltaeieQGQESLTENLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2124 LSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA--SGDELVRCAVDAATAYENILNAIKAAEDAANRAASA 2201
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2202 SESALQTVIKEdLPRKAKTLSSNSDKLLNEAkmtQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRG 2281
Cdd:COG5185 439 VSKLLNELISE-LNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887604 2282 DIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDT-----------YGRTQNEDFKKALT 2335
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASnaktdgqaanlRTAVIDELTQYLST 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1818-1997 |
2.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1818 AEECDDCDSCVMTLlnDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHG--------S 1888
Cdd:COG4913 268 RERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1889 KIEGLERELTDLNQEFETLQEKAQV--------------NSRKAQ----TLNNNVNRATQSAKELDVKIKNVIRNVHILL 1950
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAAlglplpasaeefaaLRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 167887604 1951 KQISGTDGEGNNVPsgdfsrewAEAQRMMRELRnrnfgKHLREAEAD 1997
Cdd:COG4913 426 AEIASLERRKSNIP--------ARLLALRDALA-----EALGLDEAE 459
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1667-1790 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1667 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1742
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 167887604 1743 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1790
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1834-2427 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1834 DLATMGEQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA-- 1911
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD-IETAAADQ-EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIke 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1912 ------------QVNSRKA----------------QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE---- 1959
Cdd:pfam12128 387 qnnrdiagikdkLAKIREArdrqlavaeddlqaleSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllql 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1960 GNNVPSGDFSREWAE--------AQRMMRELRNR--NFGKHLREAEA---------DKRESQL------LLNRIRT---- 2010
Cdd:pfam12128 467 ENFDERIERAREEQEaanaeverLQSELRQARKRrdQASEALRQASRrleerqsalDELELQLfpqagtLLHFLRKeapd 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2011 -----------------------WQKTHQGENN--GLANSI-RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERA 2064
Cdd:pfam12128 547 weqsigkvispellhrtdldpevWDGSVGGELNlyGVKLDLkRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2065 LGAIQRQVKEINSLQSDFTKYLTTADSSLLQ-----TNIALQLME-------KSQKEYEKLAASLN-------------- 2118
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRlfdekQSEKDKKNKalaerkdSANERLNSLEAQLKqldkkhqawleeqk 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2119 ----EARQELSDKVREL--SRSAGKTSLVEEAEKHARSLQELAKQLEE------IKRNASGDELVRCAVDAATAYENILN 2186
Cdd:pfam12128 707 eqkrEARTEKQAYWQVVegALDAQLALLKAAIAARRSGAKAELKALETwykrdlASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2187 AIKAAEDAANRAASASESALQtvikeDLPRKAKTLSSNSDKLLnEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDT 2266
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQ-----RRPRLATQLSNIERAIS-ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2267 NLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERikdtygrtQNEDFKKALTDADNSvnkltn 2346
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK--------YVEHFKNVIADHSGS------ 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2347 klpDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVrLPNDLEDLkgYTSLSLFLQRPN 2426
Cdd:pfam12128 927 ---GLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSI-LGVDLTEF--YDVLADFDRRIA 1000
|
.
gi 167887604 2427 S 2427
Cdd:pfam12128 1001 S 1001
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1860-2388 |
3.57e-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: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1860 EQMRHMETQAKDLRNQLLNyrsaISNHGSKIEGLERELTDLNQEFETLQE--KAQVNSRKaqTLNNNVNRATQSAKELDV 1937
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLE----IDDEIIYINKLKLELKEKIKNISDKNEyiKKAIDLKK--IIENNNAYIDELAKISPY 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1938 KIKNVIRNVHILLKQISGtdgEGNNVPSGDFSREWAEAQRMMRE----------------------------LRNRNFGK 1989
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKS---ELSKIYEDDIDALYNELSSIVKEnaidntedkaklddlkskidkeydkiqnMETATVEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1990 HLREAEADKREsqlLLNRIRTWQKTHQGENNG---------------LANSI------RDSLNEYEAKLSDLRARLqeaA 2048
Cdd:TIGR01612 723 HLSNIENKKNE---LLDIIVEIKKHIHGEINKdlnkiledfknkekeLSNKIndyakeKDELNKYKSKISEIKNHY---N 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2049 AQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLT----TADSSLLQTNIALQL----MEKSQKEYEKLAASLNEA 2120
Cdd:TIGR01612 797 DQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINemkfMKDDFLNKVDKFINFenncKEKIDSEHEQFAELTNKI 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2121 RQELSDKvrELSRSAGK----TSLVEEA----EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNA-IKAA 2191
Cdd:TIGR01612 877 KAEISDD--KLNDYEKKfndsKSLINEInksiEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKnIDTI 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2192 EDAANRAASASESALQTVI--KEDLPRKAKTLS-----SNSDKLL---NEAKMTQKKLKQ--------EVSPALNNLQQt 2253
Cdd:TIGR01612 955 KESNLIEKSYKDKFDNTLIdkINELDKAFKDASlndyeAKNNELIkyfNDLKANLGKNKEnmlyhqfdEKEKATNDIEQ- 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2254 lNIVTVQKEV------IDTNLTTLRDglhgiqrgDIDAMISSAKSMVRKanditdEVLDGLNPIQTDVERIKDTYGRTQN 2327
Cdd:TIGR01612 1034 -KIEDANKNIpnieiaIHTSIYNIID--------EIEKEIGKNIELLNK------EILEEAEINITNFNEIKEKLKHYNF 1098
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887604 2328 EDF-KKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDN-MDRIRELIQQARDAASK 2388
Cdd:TIGR01612 1099 DDFgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENyIDEIKAQINDLEDVADK 1161
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1971-2158 |
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 167887604 1971 EWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS----LNEYEAKLSDLRARLqe 2046
Cdd:COG4913 282 RLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLEREL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2047 aaaqakqanglnQENERALGAIQRQVKEI----NSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQ 2122
Cdd:COG4913 355 ------------EERERRRARLEALLAALglplPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRR 419
|
170 180 190
....*....|....*....|....*....|....*.
gi 167887604 2123 ELSDKVRELSRSAGKTSLVEEAEKHARslQELAKQL 2158
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 ... |
2057-2152 |
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 167887604 2057 LNQENERA-LGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRsa 2135
Cdd:pfam06009 24 QNLENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ----LEVNSSSLSDNISRIKE-- 97
|
90
....*....|....*..
gi 167887604 2136 gktsLVEEAEKHARSLQ 2152
Cdd:pfam06009 98 ----LIAQARKAANSIK 110
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1967-2172 |
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 167887604 1967 DFSREWAEAQRMMRELRNRnFGKHLREAEADKRESQLLlnrirtwQKTHQgennglanSIRDSLN-------------EY 2033
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDL-------EQDYQ--------AASDHLNlvqtalrqqekieRY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2034 EAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQK----- 2108
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglp 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887604 2109 --EYEKLAASLNEAR---QELSDKVRELSRsagKTSLVEEA-EKHARSLQELAKQLEEIKRNASGD---ELVR 2172
Cdd:PRK04863 434 dlTADNAEDWLEEFQakeQEATEELLSLEQ---KLSVAQAAhSQFEQAYQLVRKIAGEVSRSEAWDvarELLR 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1836-2118 |
5.32e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1836 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVN 1914
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1915 SRKAQTLNNNvnratqsaKELDvkiknvirnvhILLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRnrnfgKHLREA 1994
Cdd:COG1579 79 EEQLGNVRNN--------KEYE-----------ALQKEI-------------------ESLKRRISDLE-----DEILEL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1995 EaDKREsqlllnrirtwqkthqgennglanSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQrqvKE 2074
Cdd:COG1579 116 M-ERIE------------------------ELEEELAELEAELAELEAEL----------EEKKAELDEELAELE---AE 157
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 167887604 2075 INSLQSDFTKYLTTADSSLLqtnialqlmeksqKEYEKLAASLN 2118
Cdd:COG1579 158 LEELEAEREELAAKIPPELL-------------ALYERIRKRKN 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1860-2178 |
6.16e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1860 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1936
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1937 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2003
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2004 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2075
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2076 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2149
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 167887604 2150 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2178
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2093-2189 |
6.35e-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: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2093 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2166
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 167887604 2167 GDELvrcavdaATAYENILNAIK 2189
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3174-3310 |
6.60e-03 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 40.42 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 3174 HSVLLGPEFKLVFSIRPR-SLTGILIHI-GSQPGKHLCVYLEAGKVTAS-MDSGAGGTSTSVT-PKQSLCDGQWHSVAVT 3249
Cdd:smart00210 46 FPSGLPEDFSLLTTFRQTpKSRGVLFAIyDAQNVRQFGLEVDGRANTLLlRYQGVDGKQHTVSfRNLPLADGQWHKLALS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887604 3250 IKQHILHLELDTDSsytAGQIPFPPAStQEPLHLGGapANLTTLRIPVWKSFFGCLRNIHV 3310
Cdd:smart00210 126 VSGSSATLYVDCNE---IDSRPLDRPG-QPPIDTDG--IEVRGAQAADRKPFQGDLQQLKI 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1991-2169 |
8.50e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 1991 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQE---NERALGA 2067
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRI----------RALEQElaaLEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887604 2068 IQRQV----KEINSLQSDFTKYLTTA--------------DSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2129
Cdd:COG4942 88 LEKEIaelrAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 167887604 2130 ELSR-SAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE 2169
Cdd:COG4942 168 ELEAeRAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| |
