|
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 ... |
1847-2104 |
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 46020022 1847 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1926
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1927 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2006
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2007 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2086
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 46020022 2087 ADSSLLQTNIALQLMEKS 2104
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.64e-102 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 327.78 E-value: 5.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 46020022 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.04e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 46020022 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 ... |
2288-2416 |
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 46020022 2288 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2358
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 2359 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2416
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1518-1652 |
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 46020022 1518 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1595
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 46020022 1596 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1652
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1514-1641 |
9.21e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1514 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1593
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46020022 1594 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1641
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3158-3309 |
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 46020022 3158 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3236
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46020022 3237 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3309
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3181-3310 |
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 46020022 3181 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3258
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 3259 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3310
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3186-3311 |
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 46020022 3186 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3265
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 46020022 3266 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3311
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2994-3134 |
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 46020022 2994 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3071
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46020022 3072 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3134
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3011-3136 |
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 46020022 3011 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3087
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 3088 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3136
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2602-2742 |
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 46020022 2602 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2678
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 2679 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2742
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2621-2742 |
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 46020022 2621 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2697
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46020022 2698 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2742
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3018-3136 |
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 46020022 3018 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3094
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 46020022 3095 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3136
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2769-2901 |
1.20e-20 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 90.94 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2769 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2845
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46020022 2846 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2901
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2794-2903 |
4.85e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2794 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2869
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 46020022 2870 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2903
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1266-1314 |
8.05e-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: 73.54 E-value: 8.05e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 1266 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1314
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2628-2742 |
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 46020022 2628 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2706
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 46020022 2707 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2742
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1265-1307 |
2.74e-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: 2.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 1265 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1307
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1838-2341 |
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 46020022 1838 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1899
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1900 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1969
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1970 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2045
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2046 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2125
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2126 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2204
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2205 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2278
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2279 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2339
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 46020022 2340 NK 2341
Cdd:TIGR04523 738 NK 739
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1266-1307 |
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 46020022 1266 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1307
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1356-1407 |
5.06e-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: 62.76 E-value: 5.06e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1407
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
5.61e-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: 5.61e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
7.82e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.82e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1356-1401 |
8.37e-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: 8.37e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1401
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1356-1402 |
1.78e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.78e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1402
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1404-1454 |
1.85e-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: 1.85e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1404 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1454
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2435-2570 |
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 46020022 2435 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2508
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46020022 2509 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2570
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1686-1732 |
2.27e-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: 2.27e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1686 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1732
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
491-538 |
3.50e-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: 3.50e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1829-2163 |
6.69e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1829 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1907
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1908 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1979
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1980 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2048
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2049 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2122
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 46020022 2123 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2163
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1734-1784 |
7.59e-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: 7.59e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1784
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2390-2568 |
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 46020022 2390 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2469
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2470 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2543
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 46020022 2544 PPDFKLPSRLSFPPYKGCIELDDLN 2568
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1405-1453 |
1.21e-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: 1.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 1405 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1453
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
536-583 |
1.49e-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: 58.52 E-value: 1.49e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 46020022 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 583
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.62e-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: 1.62e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-531 |
2.59e-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: 58.13 E-value: 2.59e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 46020022 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
5.77e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 491 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 533
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1733-1785 |
6.30e-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: 6.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 46020022 1733 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1785
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 46020022 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. |
1687-1734 |
1.41e-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: 55.82 E-value: 1.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1687 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1734
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1405-1447 |
1.88e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.88e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 1405 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1447
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1734-1777 |
2.14e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 46020022 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1777
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 |
4.94e-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: 54.28 E-value: 4.94e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 46020022 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 ... |
2797-2901 |
7.36e-09 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 56.27 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2797 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2871
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 46020022 2872 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2901
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.40e-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: 2.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1687-1729 |
2.45e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.45e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 1687 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1729
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
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 46020022 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
631-681 |
5.08e-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: 5.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1856-2352 |
8.02e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1856 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1934
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1935 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2014
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2015 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2094
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2095 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2150
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2151 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2230
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2231 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2310
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 46020022 2311 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2352
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
5.24e-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: 48.50 E-value: 5.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 46020022 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.07e-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: 1.07e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2057-2375 |
1.40e-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: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2057 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2136
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2137 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2216
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2217 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2293
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2294 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2369
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 46020022 2370 MDRIRE 2375
Cdd:COG5185 529 FMRARG 534
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1971-2243 |
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 46020022 1971 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2046
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2047 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2115
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2116 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2187
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 46020022 2188 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2243
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 |
7.11e-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: 7.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.15e-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: 7.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 46020022 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.07e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....*....
gi 46020022 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1856-2387 |
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 46020022 1856 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1935
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1936 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2015
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2016 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2079
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2080 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2152
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2153 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2214
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2215 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2287
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2288 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2355
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 46020022 2356 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2387
Cdd:TIGR01612 1336 khnsdINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEI 1374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1838-2375 |
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 46020022 1838 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1907
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1908 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1986
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1987 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2058
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2059 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2129
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2130 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2208
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2209 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2286
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2287 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2366
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 46020022 2367 SDNMDRIRE 2375
Cdd:PRK02224 697 RERREALEN 705
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2092-2256 |
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 46020022 2092 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2169
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2170 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2244
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 46020022 2245 LNNLQQTLNIVT 2256
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.25e-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: 5.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46020022 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 ... |
2437-2563 |
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 46020022 2437 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2512
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 2513 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2563
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.08e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46020022 356 CNCH--GHASN-CYYDpdverqqaslntqgiyagGGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPD------------------TGQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
684-722 |
3.52e-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: 3.52e-04
10 20 30
....*....|....*....|....*....|....*....
gi 46020022 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
6.57e-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: 6.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 46020022 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
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 46020022 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
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 46020022 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 ... |
1665-1788 |
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 46020022 1665 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1740
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46020022 1741 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1788
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1858-2176 |
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 46020022 1858 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1934
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1935 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2001
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2002 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2073
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2074 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2147
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 46020022 2148 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2176
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2091-2187 |
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 46020022 2091 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2164
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 46020022 2165 GDELvrcavdaATAYENILNAIK 2187
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 ... |
1847-2104 |
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 46020022 1847 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1926
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1927 TQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRI 2006
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2007 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2086
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 46020022 2087 ADSSLLQTNIALQLMEKS 2104
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
5.64e-102 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 327.78 E-value: 5.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 46020022 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.04e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 46020022 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 ... |
2288-2416 |
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 46020022 2288 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2358
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 2359 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2416
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1518-1652 |
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 46020022 1518 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1595
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 46020022 1596 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1652
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1514-1641 |
9.21e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1514 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1593
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46020022 1594 HASSRaPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASD 1641
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3158-3309 |
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 46020022 3158 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3236
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46020022 3237 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3309
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3181-3310 |
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 46020022 3181 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3258
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 3259 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3310
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3186-3311 |
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 46020022 3186 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3265
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 46020022 3266 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3311
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2994-3134 |
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 46020022 2994 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3071
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46020022 3072 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3134
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3011-3136 |
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 46020022 3011 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3087
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 3088 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3136
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2602-2742 |
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 46020022 2602 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2678
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 2679 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2742
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2621-2742 |
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 46020022 2621 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2697
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46020022 2698 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2742
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3018-3136 |
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 46020022 3018 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3094
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 46020022 3095 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3136
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2769-2901 |
1.20e-20 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 90.94 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2769 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2845
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46020022 2846 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2901
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3018-3138 |
3.48e-18 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 83.14 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 3018 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 3093
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46020022 3094 LPGNSTISIRAPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPL 3138
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
2794-2903 |
4.85e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2794 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2869
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 46020022 2870 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2903
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1266-1314 |
8.05e-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: 73.54 E-value: 8.05e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 1266 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSC 1314
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2628-2742 |
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 46020022 2628 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2706
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 46020022 2707 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2742
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1265-1307 |
2.74e-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: 2.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 1265 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1307
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1838-2341 |
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 46020022 1838 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN------------ 1899
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqrelee 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1900 --QEFETL--------QEKAQVNSRKaQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnnvpsgDFSRE 1969
Cdd:TIGR04523 368 kqNEIEKLkkenqsykQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------------RLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1970 WAEAQRMMRELRNRNFGKHLREAEadkresqllLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAKLSDLrarlqea 2045
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKN---------LDNTRESLETQLKVLSRSINKIKQNLEqkqkELKSKEKEL------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2046 aaqakqaNGLNQENeralgaiqRQVKEINslqsdftKYLTTADSSLLQTNIALQLmEKSQKEyeklaaslnearQELSDK 2125
Cdd:TIGR04523 499 -------KKLNEEK--------KELEEKV-------KDLTKKISSLKEKIEKLES-EKKEKE------------SKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2126 VREL-SRSAGKTSLVEEAEKharslQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaanraasaSESAL 2204
Cdd:TIGR04523 544 EDELnKDDFELKKENLEKEI-----DEKNKEIEELKQT----------------QKSLKK---------------KQEEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2205 QTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIqr 2278
Cdd:TIGR04523 588 QELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI-- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2279 gdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DFKKALTDADNSV 2339
Cdd:TIGR04523 665 ------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEFSKELENIIKNF 737
|
..
gi 46020022 2340 NK 2341
Cdd:TIGR04523 738 NK 739
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3186-3313 |
3.24e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 71.96 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 3186 IRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSVAVTIKQHILHLELD------ 3258
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDgearpt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 46020022 3259 -TDSSYTAGQIPFPpastqEPLHLGGAPANLTTLRI-PVWKSFFGCLRNIHVNHIPV 3313
Cdd:pfam00054 79 gESPLGATTDLDVD-----GPLYVGGLPSLGVKKRRlAISPSFDGCIRDVIVNGKPL 130
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1835-2286 |
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 46020022 1835 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEF-ETLQEKAQVns 1913
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQF-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1914 rkaqtlnnnvnraTQSAKELDVKIKNVIRNVHILLKQISgTDGEGNNvpsgdfsREWAE-------AQRMMRELRNRNFG 1986
Cdd:pfam15921 369 -------------SQESGNLDDQLQKLLADLHKREKELS-LEKEQNK-------RLWDRdtgnsitIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1987 KHLREA--EADKRESQLLLNRirtWQKTHQGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAAQAKQANGL 2055
Cdd:pfam15921 428 VQRLEAllKAMKSECQGQMER---QMAAIQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2056 NQENERALGAIQRQVKEINS---LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRS 2132
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2133 AG-----KTSLVEEAEKHARSLQEL--------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKA 2188
Cdd:pfam15921 585 AGamqveKAQLEKEINDRRLELQEFkilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2189 aedaanraasaSESALQTvIKEDLPRKAKTLSSNSDkllnEAKMTQKKLKQEVSPALNNLQQTLNIVTvQKEVIDTNLTT 2268
Cdd:pfam15921 665 -----------SRNELNS-LSEDYEVLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMK 727
|
490 500
....*....|....*....|.
gi 46020022 2269 LRDGLHG---IQRGDIDAMIS 2286
Cdd:pfam15921 728 VAMGMQKqitAKRGQIDALQS 748
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1266-1307 |
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 46020022 1266 CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1307
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1356-1407 |
5.06e-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: 62.76 E-value: 5.06e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNC 1407
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
535-577 |
5.61e-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: 5.61e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
7.82e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.82e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYD--FPHC 579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1356-1401 |
8.37e-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: 8.37e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1401
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1836-2378 |
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 46020022 1836 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqEKAQVNSRK 1915
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1916 AQTLNNNVNRatqSAKELDVKIKNVIRN-VHI--LLKQISGTDGEGNNVpSGDFSREWAEAQRMMRELRNRNFGKHLREA 1992
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLeVELnkLEKQKKENKKNIDKF-LTEIKKKEKELEKLNNKYNDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1993 EADKRESQLllnrirtwqktHQGENNglANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKE 2072
Cdd:TIGR04523 174 ELNLLEKEK-----------LNIQKN--IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2073 INSLQSDF----TKYLTTADSsllQTNIALQLMEKsQKEYEK-------LAASLNEARQELSD----KVRELSRsagktS 2137
Cdd:TIGR04523 241 INEKTTEIsntqTQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQLNQLKSEISDlnnqKEQDWNK-----E 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2138 LVEEAEKHARSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKaaedaANRAASASE-SALQTVIKEDLpRKA 2216
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLK-----KELTNSESEnSEKQRELEEKQ-NEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2217 KTLSSNSDKLLNEAkmtqKKLKQEVspalNNLQQTLNIVTVQKEVIDTNLTTLRdglhgIQRGDIDAMISSAKSMVRKAN 2296
Cdd:TIGR04523 373 EKLKKENQSYKQEI----KNLESQI----NDLESKIQNQEKLNQQKDEQIKKLQ-----QEKELLEKEIERLKETIIKNN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2297 DITDEVLDGLNPIQTDVERIKDTygrtqNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPL--------GNISD 2368
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneekkeleEKVKD 514
|
570
....*....|
gi 46020022 2369 NMDRIRELIQ 2378
Cdd:TIGR04523 515 LTKKISSLKE 524
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1356-1402 |
1.78e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.78e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYR--FPEC 1402
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1404-1454 |
1.85e-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: 1.85e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1404 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1454
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2435-2570 |
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 46020022 2435 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2508
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46020022 2509 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2570
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1686-1732 |
2.27e-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: 2.27e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1686 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1732
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1871-2159 |
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 46020022 1871 RNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK---AQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHIL 1947
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1948 LKQISGTDGEgnnvpsgdfsrewAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIrtwqkthqgenNGLANSIRDS 2027
Cdd:TIGR02168 749 IAQLSKELTE-------------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------KEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2028 LNEYEAKLSDLRARLQEAAAQAKQA-----------NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2096
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLerriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46020022 2097 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSagKTSLVEEAEKHARSLQELAKQLEEI 2159
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1831-2387 |
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 46020022 1831 NDLATMGEQLRLVKSQLQglsasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSKIE---GLERELTDLNQEFETLQE 1907
Cdd:TIGR04523 162 NDLKKQKEELENELNLLE---------KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1908 KAQVNSRKAQTLNNNVNRATQ----------------SAKELDV-KIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREW 1970
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTqlnqlkdeqnkikkqlSEKQKELeQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1971 AEaqrmmrELRNRNfgKHLREAEADKRESQLLLNR-------IRTWQKTHQGENNglanSIRDSLNEYEAKLSDLrarlq 2043
Cdd:TIGR04523 313 KS------ELKNQE--KKLEEIQNQISQNNKIISQlneqisqLKKELTNSESENS----EKQRELEEKQNEIEKL----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2044 eaaaqakqanglNQENERALGAIQRQVKEINSLQSDFTKYltTADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQE 2121
Cdd:TIGR04523 376 ------------KKENQSYKQEIKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2122 LSDKVRElsrsagKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASE 2201
Cdd:TIGR04523 442 IKDLTNQ------DSVKELIIKNLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2202 SALQTVIKE---------DLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV--IDTNLTTLR 2270
Cdd:TIGR04523 496 KELKKLNEEkkeleekvkDLTKKISSLKEKIEKLESEKKEKESKISDLED-ELNKDDFELKKENLEKEIdeKNKEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2271 DglhgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIkdtygrtqnEDFKKALTDADNSVNKLTNKLPDLW 2350
Cdd:TIGR04523 575 Q--------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI---------SSLEKELEKAKKENEKLSSIIKNIK 637
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 46020022 2351 RKIESINQQllpLGNISDNMDRIR----ELIQQARDAASKV 2387
Cdd:TIGR04523 638 SKKNKLKQE---VKQIKETIKEIRnkwpEIIKKIKESKTKI 675
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
491-538 |
3.50e-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: 3.50e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1829-2163 |
6.69e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1829 LLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK-IEGLERELTDLNQEFETLQE 1907
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1908 KAQVNSRKAQTLNNNVNRATQSAkeLDVKIKNVIRNVHILLKQISG-TDGEGNNVPSGDFSREWAEAQRM-------MRE 1979
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAAlLALLGLGGSLLSLILTIAGVLFLvlgllalLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1980 LRNRNfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQ 2048
Cdd:COG4717 292 LLARE--KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2049 AKQANGLNQ---ENERALGAIQRQVKEINSLQSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQEL 2122
Cdd:COG4717 370 QEIAALLAEagvEDEEELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 46020022 2123 SDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA 2163
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1734-1784 |
7.59e-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: 7.59e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1784
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2390-2568 |
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 46020022 2390 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2469
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2470 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2543
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 46020022 2544 PPDFKLPSRLSFPPYKGCIELDDLN 2568
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1405-1453 |
1.21e-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: 1.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46020022 1405 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGC 1453
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
536-583 |
1.49e-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: 58.52 E-value: 1.49e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 46020022 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 583
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.62e-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: 1.62e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-531 |
2.59e-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: 58.13 E-value: 2.59e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 46020022 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
5.77e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 491 CDCNLEGVLPEICDA-HGRCLCRPGVEGPRCDTCRSGFY--SFPIC 533
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1733-1785 |
6.30e-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: 6.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 46020022 1733 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1785
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 46020022 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. |
1687-1734 |
1.41e-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: 55.82 E-value: 1.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1687 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1734
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1829-2376 |
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 46020022 1829 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHmETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK 1908
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIE-ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1909 AQVNSRKAQTLNNNVNRATQ---SAKELDVKIKNVIRNVHILLK---QISGTDG---EGNNVPSGdFSR--EWAEAQRM- 1976
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKnqsGLSGILGvlsELISVDEG-YEAaiEAALGGRLq 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1977 MRELRNRNFGK----HLREAEADKReSQLLLNRIR--------TWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQE 2044
Cdd:TIGR02168 549 AVVVENLNAAKkaiaFLKQNELGRV-TFLPLDSIKgteiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2045 AAAQAKQANGLNQENERAL------------GAIQRQ-VKEINSLQS------DFTKYLTTADSSLLQTNIALQLMEKSQ 2105
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRivtldgdlvrpgGVITGGsAKTNSSILErrreieELEEKIEELEEKIAELEKALAELRKEL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2106 KEYEKLAASLNEARQELSDKVRELSRSAGKtsLVEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAA 2176
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLAR--LEAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIE 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2177 TAYENILNAIKAAedaanraaSASESALQTVIKE--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ-------------EV 2241
Cdd:TIGR02168 786 ELEAQIEQLKEEL--------KALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedieSL 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2242 SPALNNLQQT-------LNIVTVQKEVIDTNLTTLRDglhgiQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVE 2314
Cdd:TIGR02168 858 AAEIEELEELieeleseLEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46020022 2315 RIKDTYGRTQ---NEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2376
Cdd:TIGR02168 933 GLEVRIDNLQerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1405-1447 |
1.88e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.88e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 46020022 1405 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1447
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1734-1777 |
2.14e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 46020022 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1777
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1838-2185 |
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 46020022 1838 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1917
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1918 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEgnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEAD-K 1996
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----------LEELEEELEEAEEELEEAEAELAEAEEAlL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1997 RESQLLLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLQEAAAqakqangLNQENERALGAIQRQVKEINSL 2076
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLER-------LEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2077 QSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSdkvRELSRSAGKTSLVEEAEKHARSLQELAKQL 2156
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA---EAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340
....*....|....*....|....*....
gi 46020022 2157 EEIKRNASGDELVRCAVDAATAYENILNA 2185
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 |
4.94e-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: 54.28 E-value: 4.94e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 46020022 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 ... |
2797-2901 |
7.36e-09 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 56.27 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2797 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2871
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 46020022 2872 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2901
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1856-2154 |
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 46020022 1856 LLEQMRHMETQAKDLRNQLlnyrSAISNHgskIEGLERELTDLNQEFETLQEK-AQVNSRKAQTLNNNVNRATQSAKELD 1934
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL----ASLEEE---LEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1935 VKIKNVIRNVHILLKQISGTDGEGNNVPSgDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQL--LLNRIRTWQKT 2012
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2013 HQgennglanSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL- 2091
Cdd:TIGR02169 380 FA--------ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIk 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 2092 -----LQTNIALqlMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 2154
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 ... |
1853-2382 |
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 46020022 1853 SAGLLEQMRHMETQAKDLRNQLLNYRSAIS-------NHGSKIEGLERELTDLNQEFETLQ-EKAQVNSRKAQtLNNNVN 1924
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQklqlekvTTEAKIKKLEEDILLLEDQNSKLSkERKLLEERISE-FTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1925 RATQSAKELDvKIKN----VIRNVHILLKQISGT-----------DGEgnnvpSGDFSREWAEAQRMMRELRnrnfgkhl 1989
Cdd:pfam01576 170 EEEEKAKSLS-KLKNkheaMISDLEERLKKEEKGrqelekakrklEGE-----STDLQEQIAELQAQIAELR-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1990 reAEADKRESQL--LLNRIrtwqKTHQGENNGLANSIRdslnEYEAKLSDLRARLqeaaaqakqanglnqENERALGAIQ 2067
Cdd:pfam01576 236 --AQLAKKEEELqaALARL----EEETAQKNNALKKIR----ELEAQISELQEDL---------------ESERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2068 RQVK-----EINSLQsdfTKYLTTADSsllqTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktslveea 2142
Cdd:pfam01576 291 EKQRrdlgeELEALK---TELEDTLDT----TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMR------------ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2143 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDAANRAASASESALQTV---------IKEDL 2212
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQDSEHKRKKLEGQLQELqarlseserQRAEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2213 PRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LNIVTVQKEVIDTNLTTLRDGLHGIQrgdidamis 2286
Cdd:pfam01576 432 AEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETRQKLNLSTRLRQLEDERNSLQ--------- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2287 saksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2366
Cdd:pfam01576 503 --------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
570
....*....|....*.
gi 46020022 2367 SDNMDRIRELIQQARD 2382
Cdd:pfam01576 568 YDKLEKTKNRLQQELD 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1968-2389 |
1.69e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1968 REWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaa 2047
Cdd:COG4717 88 EEYAELQEELEELEEE-----LEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERL----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2048 qakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2127
Cdd:COG4717 156 ---------EELRELEEELEELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2128 ELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAED 2191
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2192 AANRAASASESALQTVIKEDLPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnltt 2268
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE-------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2269 LRDGLHGIQRGDIDAMISSAK------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKL 2342
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 46020022 2343 TNKLpdlwRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAV 2389
Cdd:COG4717 452 REEL----AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.40e-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: 2.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 46020022 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1687-1729 |
2.45e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.45e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 1687 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1729
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
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 46020022 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYF 671
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
631-681 |
5.08e-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: 5.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2626-2742 |
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 46020022 2626 IQTTVDRGLLFFAE--NGDRFISLNIEDGKLMVRYKLNSELPKERGvGDAINNGRDHSI---------QIKIGKLQKRMW 2694
Cdd:pfam00054 1 FRTTEPSGLLLYNGtqTERDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVelerngrsgTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 46020022 2695 INVDVQNTIIDGEvfdfSTYYLGGIPIAI--RERFNISTPaFRGCMKNLK 2742
Cdd:pfam00054 80 ESPLGATTDLDVD----GPLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1856-2352 |
8.02e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1856 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNvnratQSAKELD 1934
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLE-----GSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1935 VKIKNVIRNVHILLKQISGTDGEGNNVPSgdfSREWAEAQRMMRELRNrNFGKHLREAEadKRESQlLLNRIRTWQKTHQ 2014
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSEFYE-EYLDELREIE--KRLSR-LEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2015 GennglANSIRDSLNEYEAKLSDLRARLQEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYlttadsSLLQT 2094
Cdd:PRK03918 332 E-----LEEKEERLEELKKKLKELEKRLEEL-----------EERHELYEEAKAKKEELERLKKRLTGL------TPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2095 NIALQLMEKSQKEYEK-------LAASLNEARQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQ 2150
Cdd:PRK03918 390 EKELEELEKAKEEIEEeiskitaRIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2151 ELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEA 2230
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2231 KMTQKKLKQEVSpALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQ 2310
Cdd:PRK03918 538 KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAE 611
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 46020022 2311 TDVERIKDTYGRTQNE--DFKKALTDADNSVNKLTNKLPDLWRK 2352
Cdd:PRK03918 612 KELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKK 655
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1838-2354 |
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 46020022 1838 EQLRLVKSQLQGLSASAG-LLEQMRHMETQAKDLrnQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1916
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDrILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1917 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISgtdgegnNVPSGDFSREWAEAQR----MMRElRNRNFGKHLREA 1992
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG-------YFPNKKQLEDWLHSKSkeinQTRD-RLAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1993 EADKresqlllNRIRTWQKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAAQAKQANG-----------LNQEN 2059
Cdd:TIGR00606 604 EQNK-------NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDEN 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2060 ERALGAIQRQVK---EINSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT 2136
Cdd:TIGR00606 677 QSCCPVCQRVFQteaELQEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2137 -SLVEEAEKHARSLQELAKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRK 2215
Cdd:TIGR00606 754 qKVNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2216 AKTLSSNSDKLLNEAKMTQkKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTtlrdglhgiQRGDID----AMISSAKSM 2291
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ---------RRQQFEeqlvELSTEVQSL 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46020022 2292 VRKANDITDEVLDGLNPIQTDVERiKDTYGRTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 2354
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1841-2180 |
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 46020022 1841 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN 1920
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1921 NNVNRATQSAKELDvkiknvirnvhillKQISGTDGEGNNVPSgdfSREWAEAQR-MMRELRNRNFGKhLREAEADKRES 1999
Cdd:PRK02224 377 EAVEDRREEIEELE--------------EEIEELRERFGDAPV---DLGNAEDFLeELREERDELRER-EAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2000 QlllNRIRtwqkthqgENNGL--------------ANSIRDSLNEYEAKLSDLRARLqeaAAQAKQANGLNQENERA--L 2063
Cdd:PRK02224 439 R---ERVE--------EAEALleagkcpecgqpveGSPHVETIEEDRERVEELEAEL---EDLEEEVEEVEERLERAedL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2064 GAIQRQVKEINSLQSDFTKYLTTADSSllqtnialqLMEKSQKeyeklAASLNEARQELSDKVRELSRSAgkTSLVEEAE 2143
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRET---------IEEKRER-----AEELRERAAELEAEAEEKREAA--AEAEEEAE 568
|
330 340 350
....*....|....*....|....*....|....*..
gi 46020022 2144 KHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYE 2180
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1838-2174 |
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 46020022 1838 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEkaqvnsrKAQ 1917
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1918 TLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVpsgdfsreWAEAQRMMRELRNRNFGKHLREAEADKR 1997
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL--------EQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1998 ESQL--LLNRIRTWQKTHQGENNGLANSIRDSLnEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINS 2075
Cdd:COG4372 156 EEQLesLQEELAALEQELQALSEAEAEQALDEL-LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2076 LQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQ 2155
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330
....*....|....*....
gi 46020022 2156 LEEIKRNASGDELVRCAVD 2174
Cdd:COG4372 315 DALLAALLELAKKLELALA 333
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1838-2165 |
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 46020022 1838 EQLRLVKSQLQGLSAS-AGLLEQMRHMEtqakdlrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKA 1916
Cdd:TIGR02169 674 AELQRLRERLEGLKRElSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1917 QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQIsgtdgegnNVPSGDFSRE-WAEAQRMMREL---RNRNFG------ 1986
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--------NDLEARLSHSrIPEIQAELSKLeeeVSRIEArlreie 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1987 -----KHLREAEADKrESQLLLNRIRTWQ------KTHQGENNGLANSIRDSLNEYEAKLSDLRARLQeaaaqakqanGL 2055
Cdd:TIGR02169 819 qklnrLTLEKEYLEK-EIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLG----------DL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2056 NQENERA---LGAIQRQVKEINSlqsdftkYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-------- 2124
Cdd:TIGR02169 888 KKERDELeaqLRELERKIEELEA-------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqael 960
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 46020022 2125 -KVRELSRSAGKTSL--VEEAEKHARSLQELAKQLEEIKRNASG 2165
Cdd:TIGR02169 961 qRVEEEIRALEPVNMlaIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1838-2158 |
4.73e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1838 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNhgskiegLERELTDLNQEFETLQEKAQvnsrKAQ 1917
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-------IEKRLSRLEEEINGIEERIK----ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1918 TLNNNVNRATQSAKELDVKIkNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNfgKHLRE------ 1991
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEeiskit 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1992 ---AEADKRESQLLLNRI-------------RTWQKTHQGEnnglansirdSLNEYEAKLSDLRARLQEAaaqakqangl 2055
Cdd:PRK03918 412 ariGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKE----------LLEEYTAELKRIEKELKEI---------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2056 nQENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLNEARQELSDKVREL 2129
Cdd:PRK03918 472 -EEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350
....*....|....*....|....*....|...
gi 46020022 2130 SRSAG----KTSLVEEAEKHARSLQELAKQLEE 2158
Cdd:PRK03918 549 EKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
5.24e-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: 48.50 E-value: 5.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 46020022 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1948-2161 |
5.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1948 LKQISGTDgegnnvpsgDFSREWAEAQRMMRELRNRnfgkhlREAEAD--KRESQLLlNRIRTwQKTHQGENNGLANSIR 2025
Cdd:PRK03918 151 VRQILGLD---------DYENAYKNLGEVIKEIKRR------IERLEKfiKRTENIE-ELIKE-KEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2026 DSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKylTTADSSLLQTNIA-LQLMEKS 2104
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKeLKELKEK 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46020022 2105 QKEYEKLAASLNEARQELSDKVRELSR----SAGKTSLVEEAEKHARSLQELAKQLEEIKR 2161
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRleeeINGIEERIKELEEKEERLEELKKKLKELEK 352
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.07e-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: 1.07e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 46020022 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 ... |
3000-3138 |
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 46020022 3000 KLPQELLkPRSQFAVDM-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 3073
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46020022 3074 GHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 3138
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2057-2375 |
1.40e-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: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2057 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2136
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2137 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2216
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2217 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2293
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2294 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2369
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 46020022 2370 MDRIRE 2375
Cdd:COG5185 529 FMRARG 534
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1799-2253 |
2.53e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1799 HPLTGDCINQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSA----SAGLLEQMRHMET--QAKDLRN 1872
Cdd:TIGR00618 279 LEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkqQSSIEEQRRLLQTlhSQEIHIR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1873 QLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA-TQSAKELDVKIKNVIRNVHILLKQI 1951
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRDLQGQLAHAKKQQELQQR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1952 SGTDGE--GNNVPSGDFSREwAEAQRMMRELRNRNFGK------HLREAEADKRESQLLLNrirtwqktHQGENNGLANS 2023
Cdd:TIGR00618 439 YAELCAaaITCTAQCEKLEK-IHLQESAQSLKEREQQLqtkeqiHLQETRKKAVVLARLLE--------LQEEPCPLCGS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2024 IRdslnEYEAKLSDL-----RARLQEAAAQAKQANGLNQENERALG-AIQRQVK----EINSLQSDFTKYLTTADSSLLQ 2093
Cdd:TIGR00618 510 CI----HPNPARQDIdnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRAslkeQMQEIQQSFSILTQCDNRSKED 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2094 TNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE----LV 2169
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehAL 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2170 RCAVDAATAYENILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQ 2249
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
....
gi 46020022 2250 QTLN 2253
Cdd:TIGR00618 743 QSLK 746
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1971-2243 |
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 46020022 1971 AEAQR----MMRELRNRNFGKHLREAEadkRESQLLLNRIRTwqkthqgennglANSIRDSLNEYEAKLSDLRARLQEAA 2046
Cdd:pfam05701 206 AEEHRigaaLAREQDKLNWEKELKQAE---EELQRLNQQLLS------------AKDLKSKLETASALLLDLKAELAAYM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2047 AQAKQANGLNQENER--------ALGAIQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASL 2115
Cdd:pfam05701 271 ESKLKEEADGEGNEKktstsiqaALASAKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2116 NEARQE-------LSDKVRELSRSAGKTSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIK 2187
Cdd:pfam05701 338 ASLRQRegmasiaVSSLEAELNRTKSEIALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAK 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 46020022 2188 AAEDAANRAASASESALQTVIKEDLPRKA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2243
Cdd:pfam05701 412 EEAEQAKAAASTVESRLEAVLKEIEAAKAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1837-2242 |
6.62e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1837 GEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRnQLLNYRSAISnhgSKIEGLERELTDLNQEFETLQEKAQvnsrkA 1916
Cdd:COG4717 63 GRKPELNLKELKELE------EELKEAEEKEEEYA-ELQEELEELE---EELEELEAELEELREELEKLEKLLQ-----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1917 QTLNNNVNRATQSAKELDVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsREWAEAQRMMRELRNRNFGKHLREAEADK 1996
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-------LEERL----------------EELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1997 RESQLLLNRIRTWQKTHQgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER--------ALGAIQR 2068
Cdd:COG4717 185 QLSLATEEELQDLAEELE-ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2069 QVKEINSLQSDFTKYLTTAdSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSD-KVRELSRSAG-----KTSLVEEA 2142
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLV-LGLLALLFLLLAREKASLGKEAEELQALPALEELEEeELEELLAALGlppdlSPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2143 EKHARSLQELAKQLEEIKR------------------NASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESAL 2204
Cdd:COG4717 343 LDRIEELQELLREAEELEEelqleeleqeiaallaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 46020022 2205 QTVIKEDLPRKAKTLSSNSDKL---LNEAKMTQKKLKQEVS 2242
Cdd:COG4717 423 EALDEEELEEELEELEEELEELeeeLEELREELAELEAELE 463
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
7.11e-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: 7.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.15e-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: 7.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 46020022 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.07e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....*....
gi 46020022 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1858-2168 |
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 46020022 1858 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTD-------LNQEFETLQEKAQVNSRKAQTLNNNVNRATQSA 1930
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrdeLNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1931 KELDVKIKNVIRNVHILLKQISGTDGEGNNVPS--------------GDFSREW-----AEAQRMMRELRNRnfgKHLRE 1991
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqqtEVLSPEEekelvEKIKELEKELEKA---KKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1992 AEADKREsqlLLNRIRTWQKthqgenngLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEneralgaIQRQVK 2071
Cdd:COG1340 158 KNEKLKE---LRAELKELRK--------EAEEIHKKIKELAEEAQELHEEMIE----------LYKE-------ADELRK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2072 EINSLQSDFTKYLTTADssllqtnialqlMEKsqKEYEKLAASLNEARQELsDKVRELSRSAGKTSLVEEAEKHARSLqe 2151
Cdd:COG1340 210 EADELHKEIVEAQEKAD------------ELH--EEIIELQKELRELRKEL-KKLRKKQRALKREKEKEELEEKAEEI-- 272
|
330
....*....|....*....
gi 46020022 2152 lakqLEEIKRNA--SGDEL 2168
Cdd:COG1340 273 ----FEKLKKGEklTTEEL 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1909-2276 |
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 46020022 1909 AQVNSRKAQTLNNnVNRATQSAKELDVKIKNVIRNVHILLKQisgtdgegnnvpsgdfsREWAEA-QRMMRELRNRNFGK 1987
Cdd:TIGR02169 166 AEFDRKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRRE-----------------REKAERyQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1988 HLREAEADKRESQLLLNRIrtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQakqangLNQENER--ALGA 2065
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL---------------ASLEEELEKLTEEISELEKRLEEIEQL------LEELNKKikDLGE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2066 iqrqvKEINSLQSDFTKylTTADSSLLQTNIAL--QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-KTSLVEE- 2141
Cdd:TIGR02169 287 -----EEQLRVKEKIGE--LEAEIASLERSIAEkeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrRDKLTEEy 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2142 -----------------AEKHARSLQELAK----------QLEEIKRNAS--GDELVRcavdAATAYENILNAIKAAEDA 2192
Cdd:TIGR02169 360 aelkeeledlraeleevDKEFAETRDELKDyrekleklkrEINELKRELDrlQEELQR----LSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2193 ANRAASASESAlQTVIKEDlPRKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQQTLNIVTVQKEVIDT-------N 2265
Cdd:TIGR02169 436 INELEEEKEDK-ALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEErvrggraV 512
|
410
....*....|.
gi 46020022 2266 LTTLRDGLHGI 2276
Cdd:TIGR02169 513 EEVLKASIQGV 523
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1857-2388 |
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 46020022 1857 LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK 1936
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1937 IKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNR---IRTWQKTH 2013
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLAlalLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2014 QGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINslQSDFTKYLTTadssllq 2093
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIA--EGDLTVRIDV------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2094 tnialqlmeKSQKEYEKLAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcav 2173
Cdd:COG0840 232 ---------DSKDEIGQLADAFNRMIENLRELVGQVRESA--EQVASASEELAASAEELAAGAEEQAASLE--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2174 DAATAYENILNAIKaaedaanraaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQKKLK---QEVSPALNNL-- 2248
Cdd:COG0840 292 ETAAAMEELSATVQ----------EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGIEEIResvEETAETIEELge 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2249 --QQTLNIVTVQKEVID-TNLTTL-------RDGLHGiqRG--------------------DIDAMISSAKSMVRKANDI 2298
Cdd:COG0840 359 ssQEIGEIVDVIDDIAEqTNLLALnaaieaaRAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2299 TDEVLDGlnpIQTDVERIKDTygrtqnedfKKALTDADNSVNKLTNKLpdlwRKI-ESINQQLLPLGNISDNMDRIRELI 2377
Cdd:COG0840 437 MEEGSEE---VEEGVELVEEA---------GEALEEIVEAVEEVSDLI----QEIaAASEEQSAGTEEVNQAIEQIAAAA 500
|
570
....*....|.
gi 46020022 2378 QQARDAASKVA 2388
Cdd:COG0840 501 QENAASVEEVA 511
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1856-2387 |
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 46020022 1856 LLEQMRHMETQAKDLRNQLLNYRSaisNHGSKIEGLERELTDLNQEFetlqeKAQVNSRKAQTLNNNVNRATQSAKELDV 1935
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFEN---NCKEKIDSEHEQFAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINK 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1936 KIKNVIRNVHIlLKQISGTDGEGNNvpSGDFSREWAEAQRMMRELRNRNFgKHLREAEADKRESQlllnriRTWQKTHQG 2015
Cdd:TIGR01612 905 SIEEEYQNINT-LKKVDEYIKICEN--TKESIEKFHNKQNILKEILNKNI-DTIKESNLIEKSYK------DKFDNTLID 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2016 ENNGLANSIRD-SLNEYEAK-------LSDLRARLqeaaaQAKQANGLNQ---ENERALGAIQRQVKEINSLQSD----- 2079
Cdd:TIGR01612 975 KINELDKAFKDaSLNDYEAKnnelikyFNDLKANL-----GKNKENMLYHqfdEKEKATNDIEQKIEDANKNIPNieiai 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2080 FTKYLTTAD--SSLLQTNIALqLMEKSQKEYEKLAASLNEARQEL-----SDKVRElsrsaGKTSLVEEAEKHARSLQEL 2152
Cdd:TIGR01612 1050 HTSIYNIIDeiEKEIGKNIEL-LNKEILEEAEINITNFNEIKEKLkhynfDDFGKE-----ENIKYADEINKIKDDIKNL 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2153 AKQ-------LEEIKRNAsgdelvrcavdaatayENILNAIKaaedaanRAASASESALQTVIKEDLPR----------- 2214
Cdd:TIGR01612 1124 DQKidhhikaLEEIKKKS----------------ENYIDEIK-------AQINDLEDVADKAISNDDPEeiekkienivt 1180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2215 ---KAKTLSSNSDKLLNE-AKMTQKKLKQEVSPALN-NLQQTLNIVTVQKevIDTNLTTLRDGLHGIQR--GDIDAmISS 2287
Cdd:TIGR01612 1181 kidKKKNIYDEIKKLLNEiAEIEKDKTSLEEVKGINlSYGKNLGKLFLEK--IDEEKKKSEHMIKAMEAyiEDLDE-IKE 1257
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2288 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDfkKALTDADNSVNKLT------NKLPDLWRKIES------ 2355
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIREKSLKIIedfseeSDINDIKKELQKnlldaq 1335
|
570 580 590
....*....|....*....|....*....|....*....
gi 46020022 2356 -----INQQLLPLGNISD--NMDRIRELIQQARDAASKV 2387
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 ... |
2062-2348 |
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 46020022 2062 ALGAIQRQVKEINSLQSDFTKYLTtadSSLLQTNIALQLMEKSQKEYEklaaSLNEARQELSDKVRELSRSAGK------ 2135
Cdd:pfam06008 6 SLTGALPAPYKINYNLENLTKQLQ---EYLSPENAHKIQIEILEKELS----SLAQETEELQKKATQTLAKAQQvnaese 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2136 ------TSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcavdaATAYENILNAIKAAEDAANRAASASESALQTVIK 2209
Cdd:pfam06008 79 rtlghaKELAEAIKNLIDNIKEINEKVATLGENDF-----------ALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2210 EDLpRKAKtlssnsdKLLNEAKMTQKKLKQEVSPALNNLQQTLNivtvqkeviDTNlttlrDGLHgiqrgDIDAMISSAK 2289
Cdd:pfam06008 148 AEL-KAAQ-------DLLSRIQTWFQSPQEENKALANALRDSLA---------EYE-----AKLS-----DLRELLREAA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46020022 2290 SMVRKANDITDEVLDGLNPIQTDVERIkdtygRTQNEDFKKALTDADNSV---NKLTNKLPD 2348
Cdd:pfam06008 201 AKTRDANRLNLANQANLREFQRKKEEV-----SEQKNQLEETLKTARDSLdaaNLLLQEIDD 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1838-2375 |
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 46020022 1838 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 1907
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1908 KAQVNSRKAQTLNNNVNRATQSAKELDVkiknviRNVHILLK-QISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRnFG 1986
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEE------ERDDLLAEaGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1987 KHLREAE-----ADKRESQllLNRIRTWQKTHQGENNGLANSIRD---SLNEYEAKLSDLRARLQEAAAQAKQANGLNQE 2058
Cdd:PRK02224 339 AHNEEAEslredADDLEER--AEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2059 NERALGAIQRQVKEinslqsdftkylTTADSSLLQTNI--ALQLMEKSQ-------KEYEKLAASLNEARQELSDKVREL 2129
Cdd:PRK02224 417 LREERDELREREAE------------LEATLRTARERVeeAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2130 SRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVI 2208
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2209 KEDlprKAKTLSSNSDKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMIS 2286
Cdd:PRK02224 556 KRE---AAAEAEEEAEEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2287 SAKSMVRKANDITDEVLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNI 2366
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
....*....
gi 46020022 2367 SDNMDRIRE 2375
Cdd:PRK02224 697 RERREALEN 705
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1840-2170 |
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 46020022 1840 LRLVKSQLQG-----LSASAGL---LEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 1911
Cdd:pfam15921 435 LKAMKSECQGqmerqMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1912 NSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDgegnnvpsgdfsrEWAEAQRMMRELRNRNFGKH 1988
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKD-------------KVIEILRQQIENMTQLVGQH 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1989 LREAEADKRESQLLLNRIRTwQKTHQGENNGLANSIRDSLNEYEAKLSDL---RARLQEAAAQA-KQANGLNQENERALG 2064
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEIND-RRLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSERlRAVKDIKQERDQLLN 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2065 AIQRQVKEINSLQSDF---------------------TKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLneaRQELS 2123
Cdd:pfam15921 661 EVKTSRNELNSLSEDYevlkrnfrnkseemetttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM---QKQIT 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 46020022 2124 DKVRELSRSAGKTSLVEEA------EKH------ARSLQELAKQLEEIKRNASGDELVR 2170
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAmtnankEKHflkeekNKLSQELSTVATEKNKMAGELEVLR 796
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1808-2076 |
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 46020022 1808 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGlsasaglLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1887
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-------AEDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1888 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVK---IKNVIRNVHILLKQISGTDGEGNNVPSg 1964
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKlaeLKERIESLERIRTLLAAIADAEDEIER- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1965 dfSREWAEAQRMMRELRnrnfgkhlREAEADKREsqlllnRIRTWQKTHQGENNGLANSIRDSLNEY----EAKLSDLRA 2040
Cdd:PRK02224 611 --LREKREALAELNDER--------RERLAEKRE------RKRELEAEFDEARIEEAREDKERAEEYleqvEEKLDELRE 674
|
250 260 270
....*....|....*....|....*....|....*.
gi 46020022 2041 RlqeaaaqakqanglNQENERALGAIQRQVKEINSL 2076
Cdd:PRK02224 675 E--------------RDDLQAEIGAVENELEELEEL 696
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1971-2187 |
3.27e-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: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1971 AEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRtwqkthqgENNGL------ANSIRDSLNEYEAKLSDLRARLQE 2044
Cdd:COG3206 171 EEARKALEFLEEQ-----LPELRKELEEAEAALEEFR--------QKNGLvdlseeAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2045 AAAQAKQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLT--TADSSL---LQTNIAlQLMEKSQKEYEKLAA 2113
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSAryTPNHPDviaLRAQIA-ALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46020022 2114 SLNEARQELSDKVRELSRSagktslVEEAEKHARSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 2187
Cdd:COG3206 317 SLEAELEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1973-2302 |
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 46020022 1973 AQRMmRELRNRnfgkhLREAEADkresqLLLNRIRtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQA 2052
Cdd:TIGR02168 212 AERY-KELKAE-----LRELELA-----LLVLRLE--------ELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2053 NGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL--LQTNIA-----LQLMEKSQKEYEKLAASLNEARQELSDK 2125
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2126 VrelsrsagkTSLVEEAEKHARSLQELAKQLEEIKRNAsgdELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQ 2205
Cdd:TIGR02168 353 L---------ESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2206 TVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQrgdidAMI 2285
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQ-----ARL 491
|
330
....*....|....*..
gi 46020022 2286 SSAKSMVRKANDITDEV 2302
Cdd:TIGR02168 492 DSLERLQENLEGFSEGV 508
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2092-2256 |
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 46020022 2092 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2169
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2170 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2244
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 46020022 2245 LNNLQQTLNIVT 2256
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1989-2307 |
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 46020022 1989 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQR 2068
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEEL----------EELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2069 QVKEINSLQSDFTKY------LTTADSSLLQTNIALqlmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEA 2142
Cdd:COG4372 99 AQEELESLQEEAEELqeeleeLQKERQDLEQQRKQL---EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2143 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSN 2222
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2223 SDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEV 2302
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
....*
gi 46020022 2303 LDGLN 2307
Cdd:COG4372 336 LAELA 340
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1808-1938 |
5.00e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1808 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1887
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 1888 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIK 1938
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.25e-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: 5.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46020022 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 ... |
2437-2563 |
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 46020022 2437 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2512
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 46020022 2513 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2563
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1825-2138 |
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 46020022 1825 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFE 1903
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1904 TLQEKaqvnsrkaqtlnnnVNRATQSAKELDVKIKNVIRNvhillkqisgtdgegnnvpsgdfsrewaeAQRMMRE---- 1979
Cdd:COG4942 87 ELEKE--------------IAELRAELEAQKEELAELLRA-----------------------------LYRLGRQppla 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1980 --LRNRNFGKHLREAEADKRESQLLLNRIRTWQKThqgennglansiRDSLNEYEAKLSDLRARLqeaaaqakqanglnq 2057
Cdd:COG4942 124 llLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------LAELAALRAELEAERAEL--------------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2058 enERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2137
Cdd:COG4942 177 --EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 46020022 2138 L 2138
Cdd:COG4942 255 L 255
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1869-2390 |
7.31e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1869 DLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN---NNVNRATQSAKELDVKIK------- 1938
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKtaesdls 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1939 ----------------------------NVIRNVHILLKQI-------SGTDGEGNNVPSG--------DFSREWAEAQR 1975
Cdd:PRK01156 267 meleknnyykeleerhmkiindpvyknrNYINDYFKYKNDIenkkqilSNIDAEINKYHAIikklsvlqKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1976 MMRELRN-------------------RNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLS 2036
Cdd:PRK01156 347 RYDDLNNqilelegyemdynsylksiESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2037 DLRARLQEAAAQAK----QANGLNQENERALGAIQRQVKEINSLQSDFTKylttaDSSLLQTNIalqlmeksqKEYEKLA 2112
Cdd:PRK01156 427 SLNQRIRALRENLDelsrNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE-----KKSRLEEKI---------REIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2113 ASLNEARQELsdkVRELSRSAGKTslVEEAEKHARSLQELAKQLEEIKrnasgDELVRCAvDAATAYENILNAIKAAEDA 2192
Cdd:PRK01156 493 KDIDEKIVDL---KKRKEYLESEE--INKSINEYNKIESARADLEDIK-----IKINELK-DKHDKYEEIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2193 ANRAASASESALQTVI-----------KEDLPRKAKTLSSNSDKLLNE----AKMTQKKLKqEVSPALNNLQQTLNIVTV 2257
Cdd:PRK01156 562 DLDSKRTSWLNALAVIslidietnrsrSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIR-EIENEANNLNNKYNEIQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2258 QKEVIDTNLTTLRDglHGIQRGDIDAMISSAKSMVRKANDITDEvldgLNPIQTDVERIKDTYGRtqnedfKKALTDADN 2337
Cdd:PRK01156 641 NKILIEKLRGKIDN--YKKQIAEIDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRAR------LESTIEILR 708
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 46020022 2338 S-VNKLTNKLPDLWRKIESINQQLLPLGNIsdnmDRIREliqqardAASKVAVP 2390
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 ... |
1833-2178 |
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 46020022 1833 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN----- 1899
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1900 --QEFETLQEKAQVNSRKAQTLNNNVN--RATQSAKE------------------------------LDVKiknvIRNVH 1945
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVDalRLRLEEKEsflnkktkqlqdlteekstlageirdlkdmLDVK----ERKIN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1946 ILLKQISgtdgegnnvpsgDFSREWAEAQRMMRELRNRNFGKH------------LREAEADK------------RESQL 2001
Cdd:pfam10174 398 VLQKKIE------------NLQEQLRDKDKQLAGLKERVKSLQtdssntdtalttLEEALSEKeriierlkeqreREDRE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2002 LLNRIRTWQKthqgENNGL---ANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENEralGAIQRQVKEINSLQS 2078
Cdd:pfam10174 466 RLEELESLKK----ENKDLkekVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE---IAVEQKKEECSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2079 DFTKYLTTADSSLLQTNIA--LQLME-----------KSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL-VEEAEK 2144
Cdd:pfam10174 539 QLKKAHNAEEAVRTNPEINdrIRLLEqevarykeesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRqMKEQNK 618
|
410 420 430
....*....|....*....|....*....|....
gi 46020022 2145 HARSLQelAKQLEEIKRNASGDELVRCAVDAATA 2178
Cdd:pfam10174 619 KVANIK--HGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1859-2090 |
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 46020022 1859 QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQsakeldvKIK 1938
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1939 NVIRNVhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFGKHLREAEADKRESQLLLNRIRTWQK 2011
Cdd:COG3883 90 ERARAL-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46020022 2012 THQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSS 2090
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1832-2156 |
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 46020022 1832 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE 1907
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1908 KAQVNSRkaQTLNNNVNRATQSAKELDVKiknvirnvHILLKQISGTDGEGNnvpsgdfsREWAEAQRMMRELRNR--NF 1985
Cdd:COG4913 742 LARLELR--ALLEERFAAALGDAVERELR--------ENLEERIDALRARLN--------RAEEELERAMRAFNREwpAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1986 GKHLREAEADKRESQLLLNRIrtwqkthqgENNGLAnsirdslnEYEAKLSDLRARLQEAAAQakqanGLNQENERALGA 2065
Cdd:COG4913 804 TADLDADLESLPEYLALLDRL---------EEDGLP--------EYEERFKELLNENSIEFVA-----DLLSKLRRAIRE 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2066 IQRQVKEIN-SL-QSDFtkyltTADSSllqtniaLQLmeksqkEYEKlaaSLNEARQELSDKVRELSRSAGKTSLvEEAE 2143
Cdd:COG4913 862 IKERIDPLNdSLkRIPF-----GPGRY-------LRL------EARP---RPDPEVREFRQELRAVTSGASLFDE-ELSE 919
|
330
....*....|...
gi 46020022 2144 KHARSLQELAKQL 2156
Cdd:COG4913 920 ARFAALKRLIERL 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1883-2393 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1883 NHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNvirnvHILLKQISGTDGEGNNVP 1962
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA-----RDSLIQSLATRLELDGFE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1963 SGDFS-REWAEAQRMMRELRN---RNFGKHLREAEADKRESQLLLNRIRTwqkthqgENNGLANSIRDSLNEYEAKLSDL 2038
Cdd:TIGR00606 384 RGPFSeRQIKNFHTLVIERQEdeaKTAAQLCADLQSKERLKQEQADEIRD-------EKKGLGRTIELKKEILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2039 RARLqeaaaqakqanglnQENERALGAIQRQVKeinsLQSDFTKYLttADSSLLQTNIALQLMEKSQKEYEKLAASLNEA 2118
Cdd:TIGR00606 457 KFVI--------------KELQQLEGSSDRILE----LDQELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2119 RQELSDKVRELSRSagKTSLvEEAEKHARSLQELAKQLEEIKRNASgDELVRCA---------VDAATAYENILNAIKAA 2189
Cdd:TIGR00606 517 LRKLDQEMEQLNHH--TTTR-TQMEMLTKDKMDKDEQIRKIKSRHS-DELTSLLgyfpnkkqlEDWLHSKSKEINQTRDR 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2190 EDAANRAASASESaLQTVIKEDLPRKAKTLSSNSDKLLN-------EAKMtqKKLKQEVSPAlnnlQQTLNIVTVQKEVI 2262
Cdd:TIGR00606 593 LAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDvcgsqdeESDL--ERLKEEIEKS----SKQRAMLAGATAVY 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2263 DTNLTTLRDGLHG----IQR-----GDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEdfkkalt 2333
Cdd:TIGR00606 666 SQFITQLTDENQSccpvCQRvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI------- 738
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46020022 2334 dadnsVNKLTNKLPDLWRKIESINQQLLPL-GNISDN---MDRIRELIQQARDAASKVAVPMRF 2393
Cdd:TIGR00606 739 -----IDLKEKEIPELRNKLQKVNRDIQRLkNDIEEQetlLGTIMPEEESAKVCLTDVTIMERF 797
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.08e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46020022 356 CNCH--GHASN-CYYDpdverqqaslntqgiyagGGVCInCQHNTAGVNCEQCAKGYYRpygvpvDAPDGC 423
Cdd:smart00180 1 CDCDpgGSASGtCDPD------------------TGQCE-CKPNVTGRRCDRCAPGYYG------DGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1838-2131 |
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 46020022 1838 EQLRLVKSQLQGLSASAGLLEQMRH--------METQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA 1909
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1910 QVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQI----SGTDGEGNnvpsgdfSREWAEAQRMMRELRNRNF 1985
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleSELEALLN-------ERASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1986 GKHLREAEADKRESQLLLNRIRTwqkthqgennglansirdSLNEYEAKLSDLRARLQEAAAQakqangLNQENERALGA 2065
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELRE------------------KLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEE 955
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46020022 2066 IQRQVKEINSLQS---DFTKYLTTADSSLLQTNI-ALQLMEKSQKEYEKLAA---SLNEARQELSDKVRELSR 2131
Cdd:TIGR02168 956 AEALENKIEDDEEearRRLKRLENKIKELGPVNLaAIEEYEELKERYDFLTAqkeDLTEAKETLEEAIEEIDR 1028
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
684-722 |
3.52e-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: 3.52e-04
10 20 30
....*....|....*....|....*....|....*....
gi 46020022 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1864-2137 |
3.69e-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: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1864 ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRN 1943
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1944 VhillkQISGTDG-------EGNNVpsGDFSREWAEAQRMMRelRNRNFgkhLREAEADKREsqlllnrirtwqkthqge 2016
Cdd:COG3883 95 L-----YRSGGSVsyldvllGSESF--SDFLDRLSALSKIAD--ADADL---LEELKADKAE------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2017 nnglansirdsLNEYEAKLSDLRARLQEaaaqakqangLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNI 2096
Cdd:COG3883 145 -----------LEAKKAELEAKLAELEA----------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 46020022 2097 ALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTS 2137
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1694-1786 |
6.50e-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: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1694 NQCQDGSGICVNCQHNTAGEhCERCQEGYYGNAV-HGSCRacPCPHTNSFATGCVVNG----GDVRCSCKAGYT------ 1762
Cdd:cd13406 16 HECPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVnYEPCK--PCTQCNQRSGSEEKQKctktSDTVCRCRPGTQpldsyk 92
|
90 100
....*....|....*....|....*
gi 46020022 1763 -GTQCERCAPGYFGNPQkfGGSCQP 1786
Cdd:cd13406 93 pGVDCVPCPPGHFSRGD--NQACKP 115
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
6.57e-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: 6.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 46020022 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
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 46020022 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1887-2164 |
7.12e-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: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1887 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAK----ELDVK-IKNVIRNVHILLKQISGTdgegnnv 1961
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdEIDVAsAEREIAELEAELERLDAS------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1962 pSGDFS---REWAEAQRMMRELRnrnfgKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYeakLSDL 2038
Cdd:COG4913 684 -SDDLAaleEQLEELEAELEELE-----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2039 RARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFtKYLTTADSSLLQTNIAlqLMEKSQKEYEKLAAS-LNE 2117
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDADLE--SLPEYLALLDRLEEDgLPE 831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 46020022 2118 ARQELSDKVRELSRsAGKTSLVEEAEKHARSLQElakQLEEIkrNAS 2164
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 ... |
2053-2253 |
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 46020022 2053 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 2128
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2129 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 2185
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46020022 2186 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 2253
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 46020022 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1829-2121 |
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 46020022 1829 LLNDLAT--MGEQLRLVKSQLQglSASAGLLEQMRHMETQAKDLRNQLLNYRSA--ISNHGSKIEGLERELTDLNQEFET 1904
Cdd:COG3206 153 VANALAEayLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1905 LQEKAQVNSRKAQTLNNNVNRATQSAKEL--DVKIKNvirnvhiLLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRN 1982
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQ-------LRAQL-------------------AELEAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1983 RNFGKHLREAEADKRESQLllnrirtwqkthqgeNNGLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEnera 2062
Cdd:COG3206 285 RYTPNHPDVIALRAQIAAL---------------RAQLQQEAQRILASLEAELEALQAREAS----------LQAQ---- 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 46020022 2063 LGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEKSQKEYEKLAASLNEARQE 2121
Cdd:COG3206 336 LAQLEARLAELPELEAELRR---------LEREV-----EVARELYESLLQRLEEARLA 380
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1881-2368 |
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 46020022 1881 ISNHGSKIEGLERELTDLN---QEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE 1957
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIeliKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEEL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1958 GNNVPSG--DFSREWAEAQRMMRELRNRNFGKHLREAEAD-----------------KRESQLLLNRIR----------- 2007
Cdd:PTZ00440 604 INEALFNkeKFINEKNDLQEKVKYILNKFYKGDLQELLDElshflddhkylyheaksKEDLQTLLNTSKneyeklefmks 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2008 ------------------TWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQR 2068
Cdd:PTZ00440 684 dnidniiknlkkelqnllSLKENIIKKQlNNIEQDISNSLNQYTIKYNDLKSSI--------------EEYKEEEEKLEV 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2069 QVKEINSLQSDFTKYLTTADSSLLQ-TNIALQLMEK----SQKEyEKLAASLNEARQELSDKVRELSRSAGKTSLVE-EA 2142
Cdd:PTZ00440 750 YKHQIINRKNEFILHLYENDKDLPDgKNTYEEFLQYkdtiLNKE-NKISNDINILKENKKNNQDLLNSYNILIQKLEaHT 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2143 EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAAS------ASESALQTV--------- 2207
Cdd:PTZ00440 829 EKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTlniainRSNSNKQLVehllnnkid 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2208 IKEDLPRKAKTLSSN-----SDK--LLNEAKMTQKKLKQEVSPA-LNNL----QQTLNIVTVQKEVIDTNLTTLRDGLHG 2275
Cdd:PTZ00440 909 LKNKLEQHMKIINTDniiqkNEKlnLLNNLNKEKEKIEKQLSDTkINNLkmqiEKTLEYYDKSKENINGNDGTHLEKLDK 988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2276 IQ------RGDIDAMISSAKSMVRKANDIT----DEVLDGLNPIQTD---------------VERIKDTYG-RTQNEDFK 2329
Cdd:PTZ00440 989 EKdewehfKSEIDKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEkgkeieekvdqyislLEKMKTKLSsFHFNIDIK 1068
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 46020022 2330 KALTDA-DNSVNKLTNKLPDLWRKIESINQQLLPLGNISD 2368
Cdd:PTZ00440 1069 KYKNPKiKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSH 1108
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2054-2333 |
2.17e-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: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2054 GLNQENERALGAIQRQVKEIN-SLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYE-----------KLAASLNEARQE 2121
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtgiqnltaeieQGQESLTENLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2122 LSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA--SGDELVRCAVDAATAYENILNAIKAAEDAANRAASA 2199
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2200 SESALQTVIKEdLPRKAKTLSSNSDKLLNEAkmtQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRG 2279
Cdd:COG5185 439 VSKLLNELISE-LNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46020022 2280 DIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDT-----------YGRTQNEDFKKALT 2333
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASnaktdgqaanlRTAVIDELTQYLST 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1816-1995 |
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 46020022 1816 AEECDDCDSCVMTLlnDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHG--------S 1886
Cdd:COG4913 268 RERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1887 KIEGLERELTDLNQEFETLQEKAQV--------------NSRKAQ----TLNNNVNRATQSAKELDVKIKNVIRNVHILL 1948
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAAlglplpasaeefaaLRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46020022 1949 KQISGTDGEGNNVPsgdfsrewAEAQRMMRELRnrnfgKHLREAEAD 1995
Cdd:COG4913 426 AEIASLERRKSNIP--------ARLLALRDALA-----EALGLDEAE 459
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1665-1788 |
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 46020022 1665 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1740
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46020022 1741 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1788
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1832-2425 |
2.90e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1832 DLATMGEQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLrNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA-- 1909
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD-IETAAADQ-EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIke 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1910 ------------QVNSRKA----------------QTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGE---- 1957
Cdd:pfam12128 387 qnnrdiagikdkLAKIREArdrqlavaeddlqaleSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllql 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1958 GNNVPSGDFSREWAE--------AQRMMRELRNR--NFGKHLREAEA---------DKRESQL------LLNRIRT---- 2008
Cdd:pfam12128 467 ENFDERIERAREEQEaanaeverLQSELRQARKRrdQASEALRQASRrleerqsalDELELQLfpqagtLLHFLRKeapd 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2009 -----------------------WQKTHQGENN--GLANSI-RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERA 2062
Cdd:pfam12128 547 weqsigkvispellhrtdldpevWDGSVGGELNlyGVKLDLkRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2063 LGAIQRQVKEINSLQSDFTKYLTTADSSLLQ-----TNIALQLME-------KSQKEYEKLAASLN-------------- 2116
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRlfdekQSEKDKKNKalaerkdSANERLNSLEAQLKqldkkhqawleeqk 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2117 ----EARQELSDKVREL--SRSAGKTSLVEEAEKHARSLQELAKQLEE------IKRNASGDELVRCAVDAATAYENILN 2184
Cdd:pfam12128 707 eqkrEARTEKQAYWQVVegALDAQLALLKAAIAARRSGAKAELKALETwykrdlASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2185 AIKAAEDAANRAASASESALQtvikeDLPRKAKTLSSNSDKLLnEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDT 2264
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQ-----RRPRLATQLSNIERAIS-ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2265 NLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERikdtygrtQNEDFKKALTDADNSvnkltn 2344
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK--------YVEHFKNVIADHSGS------ 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2345 klpDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVrLPNDLEDLkgYTSLSLFLQRPN 2424
Cdd:pfam12128 927 ---GLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSI-LGVDLTEF--YDVLADFDRRIA 1000
|
.
gi 46020022 2425 S 2425
Cdd:pfam12128 1001 S 1001
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1858-2386 |
3.60e-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: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1858 EQMRHMETQAKDLRNQLLNyrsaISNHGSKIEGLERELTDLNQEFETLQE--KAQVNSRKaqTLNNNVNRATQSAKELDV 1935
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLE----IDDEIIYINKLKLELKEKIKNISDKNEyiKKAIDLKK--IIENNNAYIDELAKISPY 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1936 KIKNVIRNVHILLKQISGtdgEGNNVPSGDFSREWAEAQRMMRE----------------------------LRNRNFGK 1987
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKS---ELSKIYEDDIDALYNELSSIVKEnaidntedkaklddlkskidkeydkiqnMETATVEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1988 HLREAEADKREsqlLLNRIRTWQKTHQGENNG---------------LANSI------RDSLNEYEAKLSDLRARLqeaA 2046
Cdd:TIGR01612 723 HLSNIENKKNE---LLDIIVEIKKHIHGEINKdlnkiledfknkekeLSNKIndyakeKDELNKYKSKISEIKNHY---N 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2047 AQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLT----TADSSLLQTNIALQL----MEKSQKEYEKLAASLNEA 2118
Cdd:TIGR01612 797 DQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINemkfMKDDFLNKVDKFINFenncKEKIDSEHEQFAELTNKI 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2119 RQELSDKvrELSRSAGK----TSLVEEA----EKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNA-IKAA 2189
Cdd:TIGR01612 877 KAEISDD--KLNDYEKKfndsKSLINEInksiEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKnIDTI 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2190 EDAANRAASASESALQTVI--KEDLPRKAKTLS-----SNSDKLL---NEAKMTQKKLKQ--------EVSPALNNLQQt 2251
Cdd:TIGR01612 955 KESNLIEKSYKDKFDNTLIdkINELDKAFKDASlndyeAKNNELIkyfNDLKANLGKNKEnmlyhqfdEKEKATNDIEQ- 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2252 lNIVTVQKEV------IDTNLTTLRDglhgiqrgDIDAMISSAKSMVRKanditdEVLDGLNPIQTDVERIKDTYGRTQN 2325
Cdd:TIGR01612 1034 -KIEDANKNIpnieiaIHTSIYNIID--------EIEKEIGKNIELLNK------EILEEAEINITNFNEIKEKLKHYNF 1098
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46020022 2326 EDF-KKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDN-MDRIRELIQQARDAASK 2386
Cdd:TIGR01612 1099 DDFgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENyIDEIKAQINDLEDVADK 1161
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1969-2156 |
3.65e-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: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1969 EWAEAQRMMRELRNRnfgkhLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDS----LNEYEAKLSDLRARLqe 2044
Cdd:COG4913 282 RLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLEREL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2045 aaaqakqanglnQENERALGAIQRQVKEI----NSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQ 2120
Cdd:COG4913 355 ------------EERERRRARLEALLAALglplPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRR 419
|
170 180 190
....*....|....*....|....*....|....*.
gi 46020022 2121 ELSDKVRELSRSAGKTSLVEEAEKHARslQELAKQL 2156
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 ... |
2055-2150 |
3.66e-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: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2055 LNQENERA-LGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRsa 2133
Cdd:pfam06009 24 QNLENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ----LEVNSSSLSDNISRIKE-- 97
|
90
....*....|....*..
gi 46020022 2134 gktsLVEEAEKHARSLQ 2150
Cdd:pfam06009 98 ----LIAQARKAANSIK 110
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1965-2170 |
4.01e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1965 DFSREWAEAQRMMRELRNRnFGKHLREAEADKRESQLLlnrirtwQKTHQgennglanSIRDSLN-------------EY 2031
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDL-------EQDYQ--------AASDHLNlvqtalrqqekieRY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2032 EAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQK----- 2106
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglp 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46020022 2107 --EYEKLAASLNEAR---QELSDKVRELSRsagKTSLVEEA-EKHARSLQELAKQLEEIKRNASGD---ELVR 2170
Cdd:PRK04863 434 dlTADNAEDWLEEFQakeQEATEELLSLEQ---KLSVAQAAhSQFEQAYQLVRKIAGEVSRSEAWDvarELLR 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1834-2116 |
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 46020022 1834 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVN 1912
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1913 SRKAQTLNNNvnratqsaKELDvkiknvirnvhILLKQIsgtdgegnnvpsgdfsrewAEAQRMMRELRnrnfgKHLREA 1992
Cdd:COG1579 79 EEQLGNVRNN--------KEYE-----------ALQKEI-------------------ESLKRRISDLE-----DEILEL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1993 EaDKREsqlllnrirtwqkthqgennglanSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQrqvKE 2072
Cdd:COG1579 116 M-ERIE------------------------ELEEELAELEAELAELEAEL----------EEKKAELDEELAELE---AE 157
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 46020022 2073 INSLQSDFTKYLTTADSSLLqtnialqlmeksqKEYEKLAASLN 2116
Cdd:COG1579 158 LEELEAEREELAAKIPPELL-------------ALYERIRKRKN 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1858-2176 |
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 46020022 1858 EQM-RHMETQAKDLRNQLlnyrsaisnhgskieglERELTDLN-QEFETLQEKAQVNSR-KAQTLNNNVNRATQSAKELD 1934
Cdd:NF041483 75 EQLlRNAQIQADQLRADA-----------------ERELRDARaQTQRILQEHAEHQARlQAELHTEAVQRRQQLDQELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1935 VKIKNVIRNVH---ILLKQISG-TDGEGNNVPsgDFSREWA---------EAQRMMRELRNRNFGkhlrEAEADKRESQL 2001
Cdd:NF041483 138 ERRQTVESHVNenvAWAEQLRArTESQARRLL--DESRAEAeqalaaaraEAERLAEEARQRLGS----EAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2002 LLNRIR-------TWQKTHQGENNGLANSIRDSlneyEAKLSDlRARLQEAAAQAKQANGLnQENERALGAIQRQV-KEI 2073
Cdd:NF041483 212 ILRRARkdaerllNAASTQAQEATDHAEQLRSS----TAAESD-QARRQAAELSRAAEQRM-QEAEEALREARAEAeKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2074 NSLQSDFTKYLTTADSSLLQ------TNIAlQLMEKSQKEYEKLAAslnEARQELSDKVRELSRsagktsLVEEAEKHAR 2147
Cdd:NF041483 286 AEAKEAAAKQLASAESANEQrtrtakEEIA-RLVGEATKEAEALKA---EAEQALADARAEAEK------LVAEAAEKAR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 46020022 2148 SL--QELAKQL-------EEIKRNASGD--ELVRCAVDAA 2176
Cdd:NF041483 356 TVaaEDTAAQLakaartaEEVLTKASEDakATTRAAAEEA 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2091-2187 |
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 46020022 2091 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2164
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 46020022 2165 GDELvrcavdaATAYENILNAIK 2187
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3172-3308 |
6.59e-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: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 3172 HSVLLGPEFKLVFSIRPR-SLTGILIHI-GSQPGKHLCVYLEAGKVTAS-MDSGAGGTSTSVT-PKQSLCDGQWHSVAVT 3247
Cdd:smart00210 46 FPSGLPEDFSLLTTFRQTpKSRGVLFAIyDAQNVRQFGLEVDGRANTLLlRYQGVDGKQHTVSfRNLPLADGQWHKLALS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46020022 3248 IKQHILHLELDTDSsytAGQIPFPPAStQEPLHLGGapANLTTLRIPVWKSFFGCLRNIHV 3308
Cdd:smart00210 126 VSGSSATLYVDCNE---IDSRPLDRPG-QPPIDTDG--IEVRGAQAADRKPFQGDLQQLKI 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1989-2167 |
8.49e-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: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 1989 LREAEADKRESQLLLNRIRTWQKTHQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQE---NERALGA 2065
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRI----------RALEQElaaLEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46020022 2066 IQRQV----KEINSLQSDFTKYLTTA--------------DSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVR 2127
Cdd:COG4942 88 LEKEIaelrAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46020022 2128 ELSR-SAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE 2167
Cdd:COG4942 168 ELEAeRAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| |
