|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
6.79e-102 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 327.39 E-value: 6.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 732170491 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.50e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 732170491 282 VTRRYYYSIKDISIGG 297
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1847-2048 |
2.16e-70 |
|
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: 237.70 E-value: 2.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1847 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1926
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1927 TQSAKELDVKIKNVIRNVH--------------------------------------------------------MLNRI 1950
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKeinekvatlgendfalpssdlsrmlaeaqrmlgeirsrdfgtqlqnaeaelkaaqdLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1951 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2030
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 732170491 2031 ADSSLLQTNIALQLMEKS 2048
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2232-2360 |
2.40e-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: 2.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2232 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2302
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 2303 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2360
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1518-1652 |
1.45e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1518 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1595
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 732170491 1596 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1652
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1514-1641 |
9.05e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1514 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1593
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170491 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 ... |
3102-3253 |
5.02e-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: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3102 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3180
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732170491 3181 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3253
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3125-3254 |
3.33e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3125 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3202
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 3203 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3254
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3130-3255 |
9.80e-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: 9.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3130 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3209
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 732170491 3210 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3255
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2938-3078 |
4.11e-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: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2938 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3015
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 3016 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3078
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2955-3080 |
7.28e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2955 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3031
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 3032 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3080
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2546-2686 |
2.36e-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: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2546 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2622
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 2623 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2686
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2565-2686 |
2.33e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2565 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2641
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170491 2642 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2686
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2962-3080 |
1.17e-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: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2962 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3038
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 732170491 3039 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3080
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2713-2845 |
1.18e-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: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2713 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2789
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170491 2790 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2845
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2738-2847 |
4.76e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2738 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2813
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 732170491 2814 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2847
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 |
9.44e-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: 9.44e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 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 ... |
2572-2686 |
5.28e-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: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2572 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2650
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 732170491 2651 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2686
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1838-2285 |
8.83e-15 |
|
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: 81.22 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 1911
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1912 NSRKAQTLNNNVNRATQSAKELDVKIKNV---IRNVHMLNRIRTWQ-KTHQGENNGLANSIRDSLNEYE---AKLSDLRA 1984
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETIIknnSEIKDLTN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1985 RLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQ 2064
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2065 ELS-------DKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaa 2137
Cdd:TIGR04523 528 KLEsekkekeSKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----------------QKSLKK--------- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2138 nraasaSESALQTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLT 2211
Cdd:TIGR04523 583 ------KQEEKQELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2212 TLRDGLHGIqrgdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DF 2272
Cdd:TIGR04523 656 EIRNKWPEI--------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEF 726
|
490
....*....|...
gi 732170491 2273 KKALTDADNSVNK 2285
Cdd:TIGR04523 727 SKELENIIKNFNK 739
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1265-1307 |
3.24e-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: 68.92 E-value: 3.24e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 1265 PCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFP 1307
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1266-1307 |
1.34e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.25 E-value: 1.34e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 732170491 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 |
5.71e-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: 5.71e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 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 |
6.32e-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: 6.32e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
9.25e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 9.25e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 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 |
1.00e-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: 61.99 E-value: 1.00e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1401
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| LamG |
smart00282 |
Laminin G domain; |
2379-2514 |
2.06e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2379 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2452
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170491 2453 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2514
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1356-1402 |
2.12e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.12e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 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 |
2.21e-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: 2.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1404 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1454
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1686-1732 |
2.66e-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: 60.83 E-value: 2.66e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 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 |
4.03e-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: 4.03e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1838-2105 |
4.11e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1917
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1918 TLNNNVNRATQSAKELDVKIKNVIRnvhmlnRIRTWQKTHQGENNGLAnSIRDSLNEYEAKLSDLRARLqeaaaqakqan 1997
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE------ELAELEEELEELEEELE-ELEEELEEAEEELEEAEAEL----------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1998 glnQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVREL--SR 2075
Cdd:COG1196 361 ---AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeEE 437
|
250 260 270
....*....|....*....|....*....|
gi 732170491 2076 SAGKTSLVEEAEKHARSLQELAKQLEEIKR 2105
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2334-2512 |
8.24e-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: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2334 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2413
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2414 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2487
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 732170491 2488 PPDFKLPSRLSFPPYKGCIELDDLN 2512
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1734-1784 |
8.39e-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: 59.29 E-value: 8.39e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1784
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1829-2098 |
1.29e-10 |
|
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: 67.79 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLA------TMGEQLRlVKSQLQGLSASAGLLE-QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQE 1901
Cdd:TIGR02169 273 LLEELNkkikdlGEEEQLR-VKEKIGELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1902 FETLQEkaQVNSRKaQTLNNNVNRATQSAKELD---VKIKNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAK 1978
Cdd:TIGR02169 352 RDKLTE--EYAELK-EELEDLRAELEEVDKEFAetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1979 LSDLRARLqeaaaqakqaNGLNQENERALGAIQRQVKEINSLQSDftkylttadssllqtnialqlMEKSQKEYEKLAAS 2058
Cdd:TIGR02169 429 IAGIEAKI----------NELEEEKEDKALEIKKQEWKLEQLAAD---------------------LSKYEQELYDLKEE 477
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 732170491 2059 LNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 2098
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1405-1453 |
1.31e-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: 1.31e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 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 |
1.61e-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: 1.61e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 732170491 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 |
1.86e-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: 1.86e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 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 |
2.95e-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: 57.75 E-value: 2.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 732170491 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
6.70e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 6.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 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 |
7.25e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 7.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 732170491 1733 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1785
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
1.26e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 1.26e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 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 |
1.59e-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: 1.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1687 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1734
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1405-1447 |
2.23e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 1405 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1447
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1734-1777 |
2.48e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.48e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1777
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2003-2320 |
3.22e-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: 63.15 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2003 NERALGAIQRQvKEINSLQSDFTKylttADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKtsL 2082
Cdd:TIGR02168 666 AKTNSSILERR-REIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR--L 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2083 VEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAATAYENILNAIKAAedaanraaSASESALQTVIK 2153
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIEELEAQIEQLKEEL--------KALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2154 E--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ-------------EVSPALNNLQQT-------LNIVTVQKEVIDTNLT 2211
Cdd:TIGR02168 811 EltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedieSLAAEIEELEELieeleseLEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2212 TLRDglhgiQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQ---NEDFKKALTDADNSVNKLTN 2288
Cdd:TIGR02168 891 LLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlSEEYSLTLEEAEALENKIED 965
|
330 340 350
....*....|....*....|....*....|..
gi 732170491 2289 KLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2320
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
5.52e-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: 5.52e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFC 467
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1856-2333 |
5.72e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1856 LLEQMRHMetqakdLRNQLLNYRSAISN-HGSKIEGLERELTDLNQEFETLQEKAQVNSRKA---QTLNNNVNRATQSAK 1931
Cdd:COG4717 39 LLAFIRAM------LLERLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1932 ELDVKIKNVirnVHMLNRIRTWQKTHQgennglansIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQ 2011
Cdd:COG4717 113 ELREELEKL---EKLLQLLPLYQELEA---------LEAELAELPERLEELEERL--------------EELRELEEELE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2012 RQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAR 2091
Cdd:COG4717 167 ELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2092 SLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAEDAANRAASASESALQTVIKED 2155
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASLGKEAEELQALPALEELEEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2156 LPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnlttLRDGLHGIQRGDIDAMISSA 2232
Cdd:COG4717 321 LEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE--------IAALLAEAGVEDEEELRAAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2233 K------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLpdlwRKIESINQQLLP 2306
Cdd:COG4717 392 EqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL----AELEAELEQLEE 467
|
490 500
....*....|....*....|....*..
gi 732170491 2307 LGNISDNMDRIRELIQQARDAASKVAV 2333
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAA 494
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2741-2845 |
7.23e-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: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2741 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2815
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 732170491 2816 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2845
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.79e-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: 2.79e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1687-1729 |
2.81e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.81e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 1687 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1729
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
5.37e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.37e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 732170491 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 |
5.51e-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: 5.51e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1828-2296 |
2.76e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1828 TLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRH-------METQAKDLRNQLL-------NYRSAISNHGS---KIEG 1890
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKdyndyikKKSRYDDLNNQILelegyemDYNSYLKSIESlkkKIEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1891 LERELTDLNQEFETLQEKAQVN-----------SRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLN--RIRTWQKTH 1957
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDpdaikkelneiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqSVCPVCGTT 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1958 QGEnnglaNSIRDSLNEYEAKLSdlrarlqeaaaqakqanGLNQEneraLGAIQRQVKEINSLQSDFTKylttadsslLQ 2037
Cdd:PRK01156 462 LGE-----EKSNHIINHYNEKKS-----------------RLEEK----IREIEIEVKDIDEKIVDLKK---------RK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2038 TNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRSAGKTSLVEEAEKHARS--LQEL-AKQLEEIKRNAsgdelVR 2114
Cdd:PRK01156 507 EYLESEEINKSINEYNK----IESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkLEDLdSKRTSWLNALA-----VI 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2115 CAVDaatayeniLNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSS------------NSDKLLNEAKMTQKKLK 2182
Cdd:PRK01156 578 SLID--------IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSireieneannlnNKYNEIQENKILIEKLR 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2183 QEV------SPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTD 2256
Cdd:PRK01156 650 GKIdnykkqIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-----DAKANRARLESTIEILRTRINELSDRINDINET 724
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 732170491 2257 VERIKdtygrtqneDFKKALTDADNSVNKLT-NKLPDLWRK 2296
Cdd:PRK01156 725 LESMK---------KIKKAIGDLKRLREAFDkSGVPAMIRK 756
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
5.79e-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: 5.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 732170491 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1829-2102 |
1.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQmRHMETQ-AKDLRNQLLNYRSAISnhGSKIEGLERELTDLNQEFETLQE 1907
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEeAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1908 K-AQVNSRKAQtLNNNVNRATQSAKELdvkiKNVIRNVHMLNRIRTwqKTHQGEnnglansirdSLNEYEAKLSDLRARL 1986
Cdd:PRK03918 406 EiSKITARIGE-LKKEIKELKKAIEEL----KKAKGKCPVCGRELT--EEHRKE----------LLEEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1987 QEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLN 2060
Cdd:PRK03918 469 KEI-----------EEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLI 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 732170491 2061 EARQELSDKVRELSRSAG----KTSLVEEAEKHARSLQELAKQLEE 2102
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.20e-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: 1.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.99e-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: 7.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
8.10e-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: 8.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.17e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.17e-05
10 20 30
....*....|....*....|....*....|....*....
gi 732170491 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2036-2200 |
4.25e-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: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2036 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2113
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2114 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2188
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 732170491 2189 LNNLQQTLNIVT 2200
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2381-2507 |
5.58e-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: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2381 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2456
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 2457 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2507
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.98e-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: 42.73 E-value: 5.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170491 355 ACNCHGHAS---NCYYdpdverqqaslntqgiyaGGGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDP------------------GTGQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.61e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170491 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 |
3.74e-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: 40.41 E-value: 3.74e-04
10 20 30
....*....|....*....|....*....|....*....
gi 732170491 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 |
7.49e-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: 39.64 E-value: 7.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 732170491 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
7.62e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 7.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 732170491 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1997-2197 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1997 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 2072
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2073 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 2129
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 2130 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 2197
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEELKEKLT 317
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.46e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 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 |
2.90e-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: 41.13 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1665 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1740
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170491 1741 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1788
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2035-2131 |
6.24e-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: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2035 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2108
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 732170491 2109 GDELvrcavdaATAYENILNAIK 2131
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1856-2099 |
8.66e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1856 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLnqefetLQEKAQVNSRKaqtlnnnvnratqSAKELDV 1935
Cdd:cd22656 126 LLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDL------LTDEGGAIARK-------------EIKDLQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1936 KIKNvirnvhmlnrirtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQRQVK 2015
Cdd:cd22656 187 ELEK--------------------LNEEYAAKLKAKIDELKALIADDEAKL--------------AAALRLIADLTAADT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2016 EINSLQSDFTKylttadssllqtniALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQE 2095
Cdd:cd22656 233 DLDNLLALIGP--------------AIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAE 298
|
....
gi 732170491 2096 LAKQ 2099
Cdd:cd22656 299 KADK 302
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
46-297 |
6.79e-102 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 327.39 E-value: 6.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 46 SLHPTYFNLAEAARIWATATCGErgpgegrPQPELYCKLVGgptapgsgHTIQGQFCDYCNSEDPRKAHPVTNAIDGSE- 124
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDGNNp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 125 ---RWWQSPPLSSGTQYnrVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSvDFGSTYSPWQYFAHskvDCLKEFGRE 201
Cdd:smart00136 71 nnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTFGRP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 202 ANMAVTR--DDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAqrd 279
Cdd:smart00136 144 PRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--- 220
|
250
....*....|....*...
gi 732170491 280 PTVTRRYYYSIKDISIGG 297
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
47-297 |
2.50e-95 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 308.36 E-value: 2.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 47 LHPTYFNLAEAARIWATATCGERGPgegrpqpELYCKLVGGPtapgsghtiQGQFCDYCNSEDPRKAHPVTNAIDGSER- 125
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP-------ERYCILSGLE---------GGKKCFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 126 ---WWQSPPLSSgtQYNRVNLTLDLGQLFHVAYILIKFAnSPRPDLWVLERSVDFGSTYSPWQYFAHskvDCLKEFGREA 202
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGRPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 203 -NMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLiskaQRDPT 281
Cdd:pfam00055 139 gPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 732170491 282 VTRRYYYSIKDISIGG 297
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1847-2048 |
2.16e-70 |
|
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: 237.70 E-value: 2.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1847 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 1926
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1927 TQSAKELDVKIKNVIRNVH--------------------------------------------------------MLNRI 1950
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKeinekvatlgendfalpssdlsrmlaeaqrmlgeirsrdfgtqlqnaeaelkaaqdLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1951 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 2030
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 732170491 2031 ADSSLLQTNIALQLMEKS 2048
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2232-2360 |
2.40e-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: 2.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2232 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 2302
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 2303 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 2360
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1518-1652 |
1.45e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1518 WVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmVLLEKKPDVQLTGQHMSIIYEETNTPRPDR--LHHGRVHVVEGNFRHa 1595
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 732170491 1596 SSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVE 1652
Cdd:pfam00052 80 SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1514-1641 |
9.05e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.71 E-value: 9.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1514 HSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDmvLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFR 1593
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170491 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 ... |
3102-3253 |
5.02e-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: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3102 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 3180
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732170491 3181 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 3253
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3125-3254 |
3.33e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3125 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 3202
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 3203 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 3254
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3130-3255 |
9.80e-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: 9.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3130 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 3209
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 732170491 3210 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 3255
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2938-3078 |
4.11e-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: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2938 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 3015
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 3016 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 3078
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2955-3080 |
7.28e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2955 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 3031
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 3032 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 3080
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2546-2686 |
2.36e-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: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2546 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 2622
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 2623 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 2686
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
2565-2686 |
2.33e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2565 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 2641
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170491 2642 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 2686
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2962-3080 |
1.17e-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: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2962 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 3038
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 732170491 3039 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 3080
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2713-2845 |
1.18e-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: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2713 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 2789
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170491 2790 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 2845
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2962-3082 |
3.42e-18 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 83.14 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2962 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 3037
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170491 3038 LPGNSTISIRAPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPL 3082
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
2738-2847 |
4.76e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 76.99 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2738 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 2813
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 732170491 2814 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 2847
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 |
9.44e-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: 9.44e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 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 ... |
2572-2686 |
5.28e-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: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2572 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 2650
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 732170491 2651 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 2686
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1838-2285 |
8.83e-15 |
|
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: 81.22 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 1911
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1912 NSRKAQTLNNNVNRATQSAKELDVKIKNV---IRNVHMLNRIRTWQ-KTHQGENNGLANSIRDSLNEYE---AKLSDLRA 1984
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETIIknnSEIKDLTN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1985 RLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQ 2064
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2065 ELS-------DKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaa 2137
Cdd:TIGR04523 528 KLEsekkekeSKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----------------QKSLKK--------- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2138 nraasaSESALQTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLT 2211
Cdd:TIGR04523 583 ------KQEEKQELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2212 TLRDGLHGIqrgdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DF 2272
Cdd:TIGR04523 656 EIRNKWPEI--------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEF 726
|
490
....*....|...
gi 732170491 2273 KKALTDADNSVNK 2285
Cdd:TIGR04523 727 SKELENIIKNFNK 739
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3130-3257 |
3.19e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 71.96 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3130 IRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSVAVTIKQHILHLELD------ 3202
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDgearpt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 732170491 3203 -TDSSYTAGQIPFPpastqEPLHLGGAPANLTTLRI-PVWKSFFGCLRNIHVNHIPV 3257
Cdd:pfam00054 79 gESPLGATTDLDVD-----GPLYVGGLPSLGVKKRRlAISPSFDGCIRDVIVNGKPL 130
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1265-1307 |
3.24e-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: 68.92 E-value: 3.24e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 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 ... |
1858-2331 |
3.15e-13 |
|
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: 75.83 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1858 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLqekaqvNSRKAQTLNNNVNRATQSAK----EL 1933
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL------NNQKEQDWNKELKSELKNQEkkleEI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1934 DVKIKNVIRNVHMLNR----IRTWQKTHQGENnglaNSIRDSLNEYEAKLSDlrarlqeaaaqakqangLNQENERALGA 2009
Cdd:TIGR04523 327 QNQISQNNKIISQLNEqisqLKKELTNSESEN----SEKQRELEEKQNEIEK-----------------LKKENQSYKQE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2010 IQRQVKEINSLQSDFTKYltTADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQELSDKVRElsrsagKTSLVEEAE 2087
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSEIKDLTNQ------DSVKELIIK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2088 KHARSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASESALQTVIKE--DLPRKAKTLSS 2165
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKEKELKKLNEEkkELEEKVKDLTK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2166 NSDKLLNeakmTQKKLKQEVSpalnnlQQTLNIVTVQKEVI--DTNLTtlRDGLHGIQRGdIDAMISSAK---SMVRKAN 2240
Cdd:TIGR04523 518 KISSLKE----KIEKLESEKK------EKESKISDLEDELNkdDFELK--KENLEKEIDE-KNKEIEELKqtqKSLKKKQ 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2241 DITDEVLDGLNPIQTDVERIKDTYGRTQNEdFKKALTDADNSVNKLTNKLPDLWRKIESINQQllpLGNISDNMDRIR-- 2318
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISS-LEKELEKAKKENEKLSSIIKNIKSKKNKLKQE---VKQIKETIKEIRnk 660
|
490
....*....|....*
gi 732170491 2319 --ELIQQARDAASKV 2331
Cdd:TIGR04523 661 wpEIIKKIKESKTKI 675
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1266-1307 |
1.34e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.25 E-value: 1.34e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 732170491 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 |
5.71e-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: 5.71e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 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 |
6.32e-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: 6.32e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 535 ACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFP 577
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
536-579 |
9.25e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 9.25e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 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 |
1.00e-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: 61.99 E-value: 1.00e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 1356 CNCSRRGTIEaamPECDRDSGQCRCKPRITGRQCDRCASGFYRFPE 1401
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| LamG |
smart00282 |
Laminin G domain; |
2379-2514 |
2.06e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2379 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 2452
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170491 2453 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 2514
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1356-1402 |
2.12e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.12e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 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 |
2.21e-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: 2.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1404 PCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGsFHLDPANLKGCT 1454
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1686-1732 |
2.66e-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: 60.83 E-value: 2.66e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1686 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 1732
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1836-2304 |
2.80e-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: 69.66 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1836 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqEKAQVNSRK 1915
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1916 AQTLNNNVNRatqSAKELDVKIKNVIRNVHMLNRIRTwQKTHQGEN-NGLANSIR---DSLNEYEAKLSDLRARLqeaaa 1991
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLEVELNKLEK-QKKENKKNiDKFLTEIKkkeKELEKLNNKYNDLKKQK----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1992 qakqangLNQENERALgaiqrQVKEINSLQSDftkyLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEAR-------- 2063
Cdd:TIGR04523 169 -------EELENELNL-----LEKEKLNIQKN----IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKkqnnqlkd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2064 ------QELSDKVRELSRSAGK-TSLVEEAEKHARSLQElaKQLEEIKRNASGDELvrcavdaatayENILNAIKaaeDA 2136
Cdd:TIGR04523 233 niekkqQEINEKTTEISNTQTQlNQLKDEQNKIKKQLSE--KQKELEQNNKKIKEL-----------EKQLNQLK---SE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2137 ANRAASASESALQTVIKEDLPRKAKTLS------SNSDKLLNEAKMTQKKLKQEVSPALNN---LQQTLN-----IVTVQ 2202
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEeiqnqiSQNNKIISQLNEQISQLKKELTNSESEnseKQRELEekqneIEKLK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2203 KEvIDTNLTTLRDgLHgIQRGDIDAMISSAKsmvrKANDITDEVLDGL----NPIQTDVERIKDTygRTQNEDFKKALTD 2278
Cdd:TIGR04523 377 KE-NQSYKQEIKN-LE-SQINDLESKIQNQE----KLNQQKDEQIKKLqqekELLEKEIERLKET--IIKNNSEIKDLTN 447
|
490 500
....*....|....*....|....*.
gi 732170491 2279 ADNSVNKLTNKLPdlwRKIESINQQL 2304
Cdd:TIGR04523 448 QDSVKELIIKNLD---NTRESLETQL 470
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
491-538 |
4.03e-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: 4.03e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFPICQACWC 538
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1838-2105 |
4.11e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 1917
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1918 TLNNNVNRATQSAKELDVKIKNVIRnvhmlnRIRTWQKTHQGENNGLAnSIRDSLNEYEAKLSDLRARLqeaaaqakqan 1997
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE------ELAELEEELEELEEELE-ELEEELEEAEEELEEAEAEL----------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1998 glnQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVREL--SR 2075
Cdd:COG1196 361 ---AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeEE 437
|
250 260 270
....*....|....*....|....*....|
gi 732170491 2076 SAGKTSLVEEAEKHARSLQELAKQLEEIKR 2105
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2334-2512 |
8.24e-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: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2334 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 2413
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2414 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 2487
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 732170491 2488 PPDFKLPSRLSFPPYKGCIELDDLN 2512
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1734-1784 |
8.39e-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: 59.29 E-value: 8.39e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 1784
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1829-2098 |
1.29e-10 |
|
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: 67.79 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLA------TMGEQLRlVKSQLQGLSASAGLLE-QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQE 1901
Cdd:TIGR02169 273 LLEELNkkikdlGEEEQLR-VKEKIGELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1902 FETLQEkaQVNSRKaQTLNNNVNRATQSAKELD---VKIKNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAK 1978
Cdd:TIGR02169 352 RDKLTE--EYAELK-EELEDLRAELEEVDKEFAetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1979 LSDLRARLqeaaaqakqaNGLNQENERALGAIQRQVKEINSLQSDftkylttadssllqtnialqlMEKSQKEYEKLAAS 2058
Cdd:TIGR02169 429 IAGIEAKI----------NELEEEKEDKALEIKKQEWKLEQLAAD---------------------LSKYEQELYDLKEE 477
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 732170491 2059 LNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 2098
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1405-1453 |
1.31e-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: 1.31e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 732170491 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 |
1.61e-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: 1.61e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 732170491 536 CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSS 583
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1838-2211 |
1.67e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 66.08 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEkaqvnsrKAQ 1917
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1918 TLNNNVNRATQSAKELDVKIKNVirnvhmlnrirtwqkthQGEnnglANSIRDSLNEYEAKLSDLRARLqeaaaqakqaN 1997
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESL-----------------QEE----AEELQEELEELQKERQDLEQQR----------K 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1998 GLNQENERALGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEKSQKEYEKLaaSLNEARQELSDKVRELSRSA 2077
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLES---------LQEEL-----AALEQELQAL--SEAEAEQALDELLKEANRNA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2078 GKTSLVEEAEKHARSLQELAKQLEEIKRNAsgDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLP 2157
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDS--LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 732170491 2158 RKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLT 2211
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-465 |
1.86e-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: 1.86e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 425 PCSCDPEHA--DGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFP 465
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1831-2103 |
1.91e-10 |
|
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: 67.00 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1831 NDLATMGEQLRLVKSQLQGLSASAGLLEQMRH--------METQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEF 1902
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1903 ETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTwqkthqgENNGLANSIRDSLNEYEAKLSDL 1982
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT-------LLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1983 RARLQEaaaqakqangLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEA 2062
Cdd:TIGR02168 837 ERRLED----------LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 732170491 2063 RQELSDKVRELSRSagKTSLVEEAEKHARSLQELAKQLEEI 2103
Cdd:TIGR02168 907 ESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-531 |
2.95e-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: 57.75 E-value: 2.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 732170491 491 CDCNLEGVLPEICDAH-GRCLCRPGVEGPRCDTCRSGFYSFP 531
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
491-533 |
6.70e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 6.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 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 |
7.25e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 7.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 732170491 1733 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 1785
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
426-466 |
1.26e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 1.26e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 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 |
1.59e-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: 1.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1687 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 1734
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1405-1447 |
2.23e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 732170491 1405 CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDP 1447
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1734-1777 |
2.48e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.48e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 1734 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNP 1777
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1853-2326 |
2.93e-09 |
|
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: 63.27 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1853 SAGLLEQMRHMETQAKDLRNQLLNYRSAisnhGSKIEgLERELTD-----LNQEFETLQEKAQVNSRKAQTLNNNVNRAT 1927
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAA----RQKLQ-LEKVTTEakikkLEEDILLLEDQNSKLSKERKLLEERISEFT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1928 QSAKELDVKIKNV--IRNVH------MLNRIRTWQKTHQG-ENN-----GLANSIRDSLNEYEAKLSDLRARLQEAAAQA 1993
Cdd:pfam01576 166 SNLAEEEEKAKSLskLKNKHeamisdLEERLKKEEKGRQElEKAkrkleGESTDLQEQIAELQAQIAELRAQLAKKEEEL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1994 KQANGLNQENERALGAIQRQVKE----INSLQSDFtkylttaDSSLLQTNIALQLMEKSQKEYEKLAASLNE------AR 2063
Cdd:pfam01576 246 QAALARLEEETAQKNNALKKIREleaqISELQEDL-------ESERAARNKAEKQRRDLGEELEALKTELEDtldttaAQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2064 QELSDK----VRELSRSAGKTSLVEEAE------KHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKA 2132
Cdd:pfam01576 319 QELRSKreqeVTELKKALEEETRSHEAQlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2133 AEDAANRAASASESALQTV---------IKEDLPRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LN 2197
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELqarlseserQRAELAEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2198 IVTVQKEVIDTNLTTLRDGLHGIQrgdidamissaksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALT 2277
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQ-----------------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLE 534
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 732170491 2278 DADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRELIQQARD 2326
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2003-2320 |
3.22e-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: 63.15 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2003 NERALGAIQRQvKEINSLQSDFTKylttADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKtsL 2082
Cdd:TIGR02168 666 AKTNSSILERR-REIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR--L 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2083 VEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAATAYENILNAIKAAedaanraaSASESALQTVIK 2153
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIEELEAQIEQLKEEL--------KALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2154 E--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ-------------EVSPALNNLQQT-------LNIVTVQKEVIDTNLT 2211
Cdd:TIGR02168 811 EltLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedieSLAAEIEELEELieeleseLEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2212 TLRDglhgiQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQ---NEDFKKALTDADNSVNKLTN 2288
Cdd:TIGR02168 891 LLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlSEEYSLTLEEAEALENKIED 965
|
330 340 350
....*....|....*....|....*....|..
gi 732170491 2289 KLPDLWRKIESINQQLLPLGNIsdNMDRIREL 2320
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-467 |
5.52e-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: 5.52e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 426 CSCDP--EHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFC 467
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1856-2333 |
5.72e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1856 LLEQMRHMetqakdLRNQLLNYRSAISN-HGSKIEGLERELTDLNQEFETLQEKAQVNSRKA---QTLNNNVNRATQSAK 1931
Cdd:COG4717 39 LLAFIRAM------LLERLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1932 ELDVKIKNVirnVHMLNRIRTWQKTHQgennglansIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQ 2011
Cdd:COG4717 113 ELREELEKL---EKLLQLLPLYQELEA---------LEAELAELPERLEELEERL--------------EELRELEEELE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2012 RQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAR 2091
Cdd:COG4717 167 ELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2092 SLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAEDAANRAASASESALQTVIKED 2155
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASLGKEAEELQALPALEELEEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2156 LPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnlttLRDGLHGIQRGDIDAMISSA 2232
Cdd:COG4717 321 LEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE--------IAALLAEAGVEDEEELRAAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2233 K------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLpdlwRKIESINQQLLP 2306
Cdd:COG4717 392 EqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL----AELEAELEQLEE 467
|
490 500
....*....|....*....|....*..
gi 732170491 2307 LGNISDNMDRIRELIQQARDAASKVAV 2333
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAA 494
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2741-2845 |
7.23e-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: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2741 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 2815
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 732170491 2816 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 2845
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1887-2105 |
9.04e-09 |
|
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: 61.62 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1887 KIEGLERELTDLNQEFET-------LQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQG 1959
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRienrldeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1960 ENNGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnqeNERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTN 2039
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARL----------------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 2040 IALQLMEKSQKEYEKLAASLNEARQELSDKVRELsrSAGKTSLVEEAEKHARSLQELAKQLEEIKR 2105
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL--NGKKEELEEELEELEAALRDLESRLGDLKK 889
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1835-2230 |
1.18e-08 |
|
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: 61.29 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1835 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEF-ETLQEKAQVnS 1913
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQF-S 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1914 RKAQTLNNNVNRAT----QSAKEL-----------DVKIKNVIRNVHM----------LNRIRTWQKTH----------- 1957
Cdd:pfam15921 370 QESGNLDDQLQKLLadlhKREKELslekeqnkrlwDRDTGNSITIDHLrrelddrnmeVQRLEALLKAMksecqgqmerq 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1958 ----QGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINS---LQ 2021
Cdd:pfam15921 450 maaiQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvdLK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2022 SDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-----KTSLVEEAEKHARSLQEL 2096
Cdd:pfam15921 530 LQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGamqveKAQLEKEINDRRLELQEF 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2097 --------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKAaedaanraasaSESALQTvIKEDLP 2157
Cdd:pfam15921 610 kilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT-----------SRNELNS-LSEDYE 677
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 2158 RKAKTLSSNSDkllnEAKMTQKKLKQEVSPALNNLQQTLNIVTvQKEVIDTNLTTLRDGLHG---IQRGDIDAMIS 2230
Cdd:pfam15921 678 VLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMKVAMGMQKqitAKRGQIDALQS 748
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-682 |
2.79e-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: 2.79e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEkSNYFGCQ 682
Cdd:cd00055 2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1687-1729 |
2.81e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.81e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 1687 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 1729
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1858-2112 |
3.36e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.00 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1858 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNnnvnratqsaKELDVKI 1937
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELR----------EKRDELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1938 KNVirnvhmlnrirtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQAKQANglnqENERALGAIQrqvKEI 2017
Cdd:COG1340 71 EKV-------------------------KELKEERDELNEKLNELREELDELRKELAELN----KAGGSIDKLR---KEI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2018 NSLQSDF-TKYLTTAD-------SSLLQTNI-ALQLMEKSQKEYEKLAASLNEARQELSDKVRELsrsagkTSLVEEAEK 2088
Cdd:COG1340 119 ERLEWRQqTEVLSPEEekelvekIKELEKELeKAKKALEKNEKLKELRAELKELRKEAEEIHKKI------KELAEEAQE 192
|
250 260
....*....|....*....|....
gi 732170491 2089 HARSLQELAKQLEEIKRNAsgDEL 2112
Cdd:COG1340 193 LHEEMIELYKEADELRKEA--DEL 214
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1858-2322 |
3.74e-08 |
|
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: 59.26 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1858 EQMRHMETQAKDLRNQLLnyrsaISNhgSKIEGLERELTDLN--------------QEFETLQEKAQVNSRKAQTLNNNV 1923
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLK-----KNK--DKINKLNSDLSKINseikndkeqknkleVELNKLEKQKKENKKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1924 NRATQSAKELDVKIKNVIRNVHML--------NRIRTWQKTHQGENNGLAN-----SIRDSLNE----YEAKLSDLRARl 1986
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELenelnlleKEKLNIQKNIDKIKNKLLKlelllSNLKKKIQknksLESQISELKKQ- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1987 qeaaaQAKQANGLNQENERalgaIQRQVKEINSLQsdfTKYLTTADSsllQTNIALQLMEKsQKEYEK-------LAASL 2059
Cdd:TIGR04523 227 -----NNQLKDNIEKKQQE----INEKTTEISNTQ---TQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2060 NEARQELSD----KVRELSRsagktSLVEEAEKHARSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKaaed 2135
Cdd:TIGR04523 291 NQLKSEISDlnnqKEQDWNK-----ELKSELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLK---- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2136 aANRAASASE-SALQTVIKEDLpRKAKTLSSNSDKLLNEAkmtqKKLKQEVspalNNLQQTLNIVTVQKEVIDTNLTTLR 2214
Cdd:TIGR04523 349 -KELTNSESEnSEKQRELEEKQ-NEIEKLKKENQSYKQEI----KNLESQI----NDLESKIQNQEKLNQQKDEQIKKLQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2215 dglhgIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTygrtqNEDFKKALTDADNSVNKLTNKLPDLW 2294
Cdd:TIGR04523 419 -----QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKQNLEQKQ 488
|
490 500 510
....*....|....*....|....*....|....*.
gi 732170491 2295 RKIESINQQLLPL--------GNISDNMDRIRELIQ 2322
Cdd:TIGR04523 489 KELKSKEKELKKLneekkeleEKVKDLTKKISSLKE 524
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2570-2686 |
5.29e-08 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 54.25 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2570 IQTTVDRGLLFFAE--NGDRFISLNIEDGKLMVRYKLNSELPKERGvGDAINNGRDHSI---------QIKIGKLQKRMW 2638
Cdd:pfam00054 1 FRTTEPSGLLLYNGtqTERDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVelerngrsgTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 732170491 2639 INVDVQNTIIDGEvfdfSTYYLGGIPIAI--RERFNISTPaFRGCMKNLK 2686
Cdd:pfam00054 80 ESPLGATTDLDVD----GPLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
631-671 |
5.37e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.37e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 732170491 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 |
5.51e-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: 5.51e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 631 CKCHKAGTVSGTgeCRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGC 681
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1825-2082 |
6.33e-08 |
|
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: 57.85 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1825 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFE 1903
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1904 TLQEK-----AQVNSRK---AQTLNNNVNRATQSAKELDVKIKNV---IRNVHMLNRIRTWQKThqgenngLANSIRDSL 1972
Cdd:COG4942 87 ELEKEiaelrAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFldaVRRLQYLKYLAPARRE-------QAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1973 NEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEY 2052
Cdd:COG4942 160 AELAALRAELEAER--------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260 270
....*....|....*....|....*....|
gi 732170491 2053 EKLAASLNEARQELSDKVRELSRSAGKTSL 2082
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1828-2330 |
1.19e-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: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1828 TLLNDLATMGEQLRLVKSQLQGLsasagllEQMR-HMETQAKDLRNQLLNYRSAI------SNHGSKIEGLERELTDLNQ 1900
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASL-------EQNKnHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSK 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1901 EFETLQEKAQVNSRKAQTLNNN-------VNRATQSAKELDVKIKNVirnVHMLNRIRTWQKTHQGENN----------G 1963
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDL---QSKLRLAPDKLKSTESELKkkekrrdemlG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1964 LANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTkylttadsslLQTNIALQ 2043
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT----------IMERFQME 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2044 LmEKSQKEYEKLAASLN---------EARQELSDKVRELSrsagktSLVEEAEKHARSLQELAKQLEEIKR--NASGDEL 2112
Cdd:TIGR00606 801 L-KDVERKIAQQAAKLQgsdldrtvqQVNQEKQEKQHELD------TVVSKIELNRKLIQDQQEQIQHLKSktNELKSEK 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2113 VRCAVDAATA---YENILNAIKAAEDAANRAASASE--SALQTVIKEDLPRKAKTLSSNSD---KLLNEAKMTQKKLKQE 2184
Cdd:TIGR00606 874 LQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEqdSPLETFLEKDQQEKEELISSKETsnkKAQDKVNDIKEKVKNI 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2185 V---SPALNNLQQTLNIVTVQKEvidTNLTTLRDGLHGIQR------GDIDAMISSAKSMVRKANDITDEV-LDGLNPIQ 2254
Cdd:TIGR00606 954 HgymKDIENKIQDGKDDYLKQKE---TELNTVNAQLEECEKhqekinEDMRLMRQDIDTQKIQERWLQDNLtLRKRENEL 1030
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2255 TDVERIKDTYGRTQNEDfkkALTDADNSVNKLTNKLpdlwRKIEsiNQQLLPLGNISDNMDRI----REL-IQQARDAAS 2329
Cdd:TIGR00606 1031 KEVEEELKQHLKEMGQM---QVLQMKQEHQKLEENI----DLIK--RNHVLALGRQKGYEKEIkhfkKELrEPQFRDAEE 1101
|
.
gi 732170491 2330 K 2330
Cdd:TIGR00606 1102 K 1102
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1828-2296 |
2.76e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1828 TLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRH-------METQAKDLRNQLL-------NYRSAISNHGS---KIEG 1890
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKdyndyikKKSRYDDLNNQILelegyemDYNSYLKSIESlkkKIEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1891 LERELTDLNQEFETLQEKAQVN-----------SRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLN--RIRTWQKTH 1957
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDpdaikkelneiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqSVCPVCGTT 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1958 QGEnnglaNSIRDSLNEYEAKLSdlrarlqeaaaqakqanGLNQEneraLGAIQRQVKEINSLQSDFTKylttadsslLQ 2037
Cdd:PRK01156 462 LGE-----EKSNHIINHYNEKKS-----------------RLEEK----IREIEIEVKDIDEKIVDLKK---------RK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2038 TNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRSAGKTSLVEEAEKHARS--LQEL-AKQLEEIKRNAsgdelVR 2114
Cdd:PRK01156 507 EYLESEEINKSINEYNK----IESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkLEDLdSKRTSWLNALA-----VI 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2115 CAVDaatayeniLNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSS------------NSDKLLNEAKMTQKKLK 2182
Cdd:PRK01156 578 SLID--------IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSireieneannlnNKYNEIQENKILIEKLR 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2183 QEV------SPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTD 2256
Cdd:PRK01156 650 GKIdnykkqIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-----DAKANRARLESTIEILRTRINELSDRINDINET 724
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 732170491 2257 VERIKdtygrtqneDFKKALTDADNSVNKLT-NKLPDLWRK 2296
Cdd:PRK01156 725 LESMK---------KIKKAIGDLKRLREAFDkSGVPAMIRK 756
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1856-2296 |
5.41e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1856 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNVNRATQSAK--- 1931
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKLEEKire 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1932 ------ELDVKIKNVIRNVHMLNRIRtWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER 2005
Cdd:PRK03918 264 leerieELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2006 ALGAIQRQVKEINSLQSDFTKY------LTTADSslLQTNIALQLMEKSQKEYEKLA-----------------ASLNEA 2062
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakakKEELER--LKKRLTGLTPEKLEKELEELEkakeeieeeiskitariGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2063 RQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQELAKQLEEIKRNASGDELVRCAVDAATAYEN 2125
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2126 ILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV 2205
Cdd:PRK03918 501 LAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2206 IDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQTDVERIKDTYGRTQNE--DFKKALTDADNSV 2283
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEEldKAFEELAETEKRL 642
|
490
....*....|...
gi 732170491 2284 NKLTNKLPDLWRK 2296
Cdd:PRK03918 643 EELRKELEELEKK 655
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
585-628 |
5.79e-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: 5.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 732170491 585 ACDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGC 628
Cdd:pfam00053 2 DCNPHGSLsdtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1829-2102 |
1.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQmRHMETQ-AKDLRNQLLNYRSAISnhGSKIEGLERELTDLNQEFETLQE 1907
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEeAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1908 K-AQVNSRKAQtLNNNVNRATQSAKELdvkiKNVIRNVHMLNRIRTwqKTHQGEnnglansirdSLNEYEAKLSDLRARL 1986
Cdd:PRK03918 406 EiSKITARIGE-LKKEIKELKKAIEEL----KKAKGKCPVCGRELT--EEHRKE----------LLEEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1987 QEAaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLN 2060
Cdd:PRK03918 469 KEI-----------EEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLI 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 732170491 2061 EARQELSDKVRELSRSAG----KTSLVEEAEKHARSLQELAKQLEE 2102
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
2944-3082 |
1.16e-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: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2944 KLPQELLkPRSQFAVDM-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 3017
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732170491 3018 GHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 3082
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-344 |
1.20e-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: 1.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170491 299 CVCNGHAEVCNINNPEKLfRCECQHHTCGETCDRCCTGYNQRRWRP 344
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2001-2319 |
1.42e-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: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2001 QENERALGAIQRQVKEINSLQSDFTKYLTTAdssLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagkt 2080
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEK---LGENA---ESSKRLNENANNLIKQFENTKEKIAEYTKSID------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2081 slveeAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKEDLPRKA 2160
Cdd:COG5185 307 -----IKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2161 KTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISSAKSMVR 2237
Cdd:COG5185 380 DSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2238 KANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPLGNISDN 2313
Cdd:COG5185 456 EADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQVAESLKD 528
|
....*.
gi 732170491 2314 MDRIRE 2319
Cdd:COG5185 529 FMRARG 534
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1846-2110 |
1.56e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 52.30 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1846 QLQGLSASAGLLEQmrhmETQAKDLRNQLLNYRSAISNHGSKIEGLE-------RELTDLNQEFETLQEKAQVNSRKAqt 1918
Cdd:pfam12795 1 KLDELEKAKLDEAA----KKKLLQDLQQALSLLDKIDASKQRAAAYQkalddapAELRELRQELAALQAKAEAAPKEI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1919 lnnnvnRATQSAKELDVKIKNVirnvhmLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLqeaaaqakqang 1998
Cdd:pfam12795 75 ------LASLSLEELEQRLLQT------SAQLQELQNQLAQLNS-QLIELQTRPERAQQQLSEARQRL------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1999 lnQENERALgaiqrqvkeiNSLQSDFTKyLTTADSSLLQTNIALQlmeKSQ-KEYEKLAASLNeARQELSDKVRELsrsa 2077
Cdd:pfam12795 130 --QQIRNRL----------NGPAPPGEP-LSEAQRWALQAELAAL---KAQiDMLEQELLSNN-NRQDLLKARRDL---- 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 732170491 2078 gKTSLVEEAEKHARSLQEL------------AKQLEEIKRNASGD 2110
Cdd:pfam12795 189 -LTLRIQRLEQQLQALQELlnekrlqeaeqaVAQTEQLAEEAAGD 232
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1838-2298 |
2.56e-06 |
|
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: 53.51 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLSASA-----------------GLLEQMRHMET---QAKDLRNQLLNYRSAISNHGSKIEGLERELTD 1897
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSdrileldqelrkaerelSKAEKNSLTETlkkEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1898 LNQEFETLQEKA-------QVNSRKAQTL--------NNNVNRATQSAKELDVKI---------KNVIRNVHMLNRIRTW 1953
Cdd:TIGR00606 534 RTQMEMLTKDKMdkdeqirKIKSRHSDELtsllgyfpNKKQLEDWLHSKSKEINQtrdrlaklnKELASLEQNKNHINNE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1954 QKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAAQAKQANG-----------LNQENERALGAIQRQVK---EI 2017
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDENQSCCPVCQRVFQteaEL 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2018 NSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT-SLVEEAEKHARSLQEL 2096
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqKVNRDIQRLKNDIEEQ 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2097 AKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKM 2176
Cdd:TIGR00606 771 ETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2177 TQkKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTtlrdglhgiQRGDID----AMISSAKSMVRKANDITDEVLDGLNP 2252
Cdd:TIGR00606 848 NR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ---------RRQQFEeqlvELSTEVQSLIREIKDAKEQDSPLETF 917
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 732170491 2253 IQTDVERiKDTYGRTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 2298
Cdd:TIGR00606 918 LEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1826-2332 |
3.32e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 52.72 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1826 VMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETL 1905
Cdd:COG0840 4 LLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1906 QEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRAR 1985
Cdd:COG0840 84 LLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1986 LQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQT-------NIALQLMEKSQKEYEKLAAS 2058
Cdd:COG0840 164 AALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVleriaegDLTVRIDVDSKDEIGQLADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2059 LNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcavDAATAYENILNAIKaaedaan 2138
Cdd:COG0840 244 FNRMIENLRELVGQVRESA--EQVASASEELAASAEELAAGAEEQAASLE---------ETAAAMEELSATVQ------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2139 raaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQKKLK---QEVSPALNNL----QQTLNIVTVQKEVID-TNL 2210
Cdd:COG0840 306 ---EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGIEEIResvEETAETIEELgessQEIGEIVDVIDDIAEqTNL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2211 TTL-------RDGLHGiqRG--------------------DIDAMISSAKSMVRKANDITDEVLDGlnpIQTDVERIKDT 2263
Cdd:COG0840 380 LALnaaieaaRAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEAMEEGSEE---VEEGVELVEEA 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2264 ygrtqnedfKKALTDADNSVNKLTNKLpdlwRKI-ESINQQLLPLGNISDNMDRIRELIQQARDAASKVA 2332
Cdd:COG0840 455 ---------GEALEEIVEAVEEVSDLI----QEIaAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVA 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1859-2081 |
3.62e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1859 QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKE------ 1932
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1933 --------LDV-----KIKNVIRNVHMLNRIRTwqktHQGENNGLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangL 1999
Cdd:COG3883 97 rsggsvsyLDVllgseSFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEA----------L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2000 NQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGK 2079
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
..
gi 732170491 2080 TS 2081
Cdd:COG3883 243 AA 244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1830-2101 |
3.77e-06 |
|
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: 53.20 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1830 LNDLATMGEQLRLVKSQLQGLSAsaglleQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEfetlqeka 1909
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKL------QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE-------- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1910 qVNSRKAQTLNNNVNRATQSAK--ELDVKIKNV-IRNVHMLN----RIRTWQKTHQgENNGLANSIRDSLNE-------Y 1975
Cdd:pfam15921 599 -INDRRLELQEFKILKDKKDAKirELEARVSDLeLEKVKLVNagseRLRAVKDIKQ-ERDQLLNEVKTSRNElnslsedY 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1976 EAKLSDLRARlqeAAAQAKQANGLNQENERALGAIQRQVKEINSLQ-SD---------FTKYLTTADSSL--LQTNIAL- 2042
Cdd:pfam15921 677 EVLKRNFRNK---SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgSDghamkvamgMQKQITAKRGQIdaLQSKIQFl 753
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2043 -QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEkhaRSLQELAKQLE 2101
Cdd:pfam15921 754 eEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQE---RRLKEKVANME 810
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1808-2087 |
4.33e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1808 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLsasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1887
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-------EDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1888 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTwqkthqgennglans 1967
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT--------------- 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1968 IRDSLNEYEAKLSDLRARLqeaaaqaKQANGLNQENERALGAIQRQVKE---------INSLQSD---FTKYLTTADSSL 2035
Cdd:PRK02224 597 LLAAIADAEDEIERLREKR-------EALAELNDERRERLAEKRERKREleaefdearIEEAREDkerAEEYLEQVEEKL 669
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170491 2036 ---------LQTNIAlqLMEKSQKEYEklaaSLNEARQELSDKVRELSrsagktSLVEEAE 2087
Cdd:PRK02224 670 delreerddLQAEIG--AVENELEELE----ELRERREALENRVEALE------ALYDEAE 718
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1871-2330 |
5.33e-06 |
|
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: 52.75 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1871 RNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqekaqvnsrkAQTLNNNVNRATQSAKELDVKIKNVIRNvhMLNRI 1950
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELH----------------LSNIENKKNELLDIIVEIKKHIHGEINK--DLNKI 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1951 RTWQKTHQGEnngLANSI------RDSLNEYEAKLSDLRARLQEAAAQAkqaNGLNQENERALGAIQRQVKEINSLQSDF 2024
Cdd:TIGR01612 757 LEDFKNKEKE---LSNKIndyakeKDELNKYKSKISEIKNHYNDQINID---NIKDEDAKQNYDKSKEYIKTISIKEDEI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2025 TKYLTTA----DSSLLQTNIALQL----MEKSQKEYEKLAASLNEARQELSDKvrELSRSAGK----TSLVEEA----EK 2088
Cdd:TIGR01612 831 FKIINEMkfmkDDFLNKVDKFINFenncKEKIDSEHEQFAELTNKIKAEISDD--KLNDYEKKfndsKSLINEInksiEE 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2089 HARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNA-IKAAEDAANRAASASESALQTVI--KEDLPRKAKTLS- 2164
Cdd:TIGR01612 909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKnIDTIKESNLIEKSYKDKFDNTLIdkINELDKAFKDASl 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2165 ----SNSDKLL---NEAKMTQKKLKQ--------EVSPALNNLQQtlNIVTVQKEVIDTNLTtLRDGLHGIQRgDIDAMI 2229
Cdd:TIGR01612 989 ndyeAKNNELIkyfNDLKANLGKNKEnmlyhqfdEKEKATNDIEQ--KIEDANKNIPNIEIA-IHTSIYNIID-EIEKEI 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2230 SSAKSMVRKanditdEVLDGLNPIQTDVERIKDTYGRTQNEDF-KKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLG 2308
Cdd:TIGR01612 1065 GKNIELLNK------EILEEAEINITNFNEIKEKLKHYNFDDFgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIK 1138
|
490 500
....*....|....*....|...
gi 732170491 2309 NISDN-MDRIRELIQQARDAASK 2330
Cdd:TIGR01612 1139 KKSENyIDEIKAQINDLEDVADK 1161
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1869-2353 |
6.19e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1869 DLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN---NNVNRATQSAKELDVKIKNVIRNVH 1945
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1946 MLNRIRTWQKTHQGENNGLANSI----RDSLNEY---EAKLSDLRARLqeaaaqakqaNGLNQEneraLGAIQRQVKEIN 2018
Cdd:PRK01156 267 MELEKNNYYKELEERHMKIINDPvyknRNYINDYfkyKNDIENKKQIL----------SNIDAE----INKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2019 SLQSDFTKYlttadssllqtnialqlmEKSQKEYEKLAASLNEARQELSDKVrelsrsagktSLVEEAEKHARSLQElak 2098
Cdd:PRK01156 333 VLQKDYNDY------------------IKKKSRYDDLNNQILELEGYEMDYN----------SYLKSIESLKKKIEE--- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2099 qlEEIKRNASGDELVRcAVDAATAYENILNAIKAAEDAANRAASASESALQTVI------KEDLPRKAKTLSSNS----- 2167
Cdd:PRK01156 382 --YSKNIERMSAFISE-ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIralrenLDELSRNMEMLNGQSvcpvc 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2168 DKLLNEAKMtqKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDeVL 2247
Cdd:PRK01156 459 GTTLGEEKS--NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2248 DGLNPI---QTDVERIKDTYG-----------------------------RTQNEDFKKALTDADNSVNKLTNKLPDLWR 2295
Cdd:PRK01156 536 IKINELkdkHDKYEEIKNRYKslkledldskrtswlnalavislidietnRSRSNEIKKQLNDLESRLQEIEIGFPDDKS 615
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732170491 2296 KIES----INQQLLPLGN----ISDN---MDRIRELIQQARDAASKvaVPMRFNGKSGVEVRLpNDLED 2353
Cdd:PRK01156 616 YIDKsireIENEANNLNNkyneIQENkilIEKLRGKIDNYKKQIAE--IDSIIPDLKEITSRI-NDIED 681
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
684-727 |
7.99e-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: 7.99e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLH 727
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
356-423 |
8.10e-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: 8.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 356 CNCHGHASNcyydpdverqqaslnTQGIYAGGGVCInCQHNTAGVNCEQCAKGYyrpYGVPVDAPDGC 423
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGY---YGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
684-722 |
1.17e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.17e-05
10 20 30
....*....|....*....|....*....|....*....
gi 732170491 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1876-2251 |
1.55e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1876 NYRSAISnhgsKIEGLERELTDLNQEFETLQ-EKAQVNSRkaqtlnnnvnrATQSAKELDVKIKNVirnvhmlnrirtwq 1954
Cdd:COG4372 32 QLRKALF----ELDKLQEELEQLREELEQAReELEQLEEE-----------LEQARSELEQLEEEL-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1955 kthqgennglaNSIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQRQVKEINSLQSdftkylttadss 2034
Cdd:COG4372 83 -----------EELNEQLQAAQAELAQAQEEL----------ESLQEEAEELQEELEELQKERQDLEQ------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2035 llqtniALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVR 2114
Cdd:COG4372 130 ------QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2115 CAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQ 2194
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 732170491 2195 TLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLN 2251
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1886-2187 |
1.97e-05 |
|
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: 50.41 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1886 SKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKI---KNVIRNVHMLN------RIR----- 1951
Cdd:pfam05701 138 AELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELiatKESLESAHAAHleaeehRIGaalar 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1952 -----TWQKT-HQGE------NNGL--ANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER--------ALGA 2009
Cdd:pfam05701 218 eqdklNWEKElKQAEeelqrlNQQLlsAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKktstsiqaALAS 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2010 IQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASLNEARQE-------LSDKVRELSRSAGK 2079
Cdd:pfam05701 298 AKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AELASLRQRegmasiaVSSLEAELNRTKSE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2080 TSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPR 2158
Cdd:pfam05701 365 IALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAA 438
|
330 340 350
....*....|....*....|....*....|
gi 732170491 2159 KA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 2187
Cdd:pfam05701 439 KAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1841-2124 |
2.57e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1841 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA----------- 1909
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAaeleseleear 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1910 -QVNSRKAQ------------------------------TLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQ 1958
Cdd:PRK02224 377 eAVEDRREEieeleeeieelrerfgdapvdlgnaedfleELREERDELREREAELEATLRTARERVEEAEALLEAGKCPE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1959 GENNGLANSIRDSLNEYEAKLSDLRARLqeaAAQAKQANGLNQENERA--LGAIQRQVKEINSLQSDFTKYLTTADSSll 2036
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDRERVEELEAEL---EDLEEEVEEVEERLERAedLVEAEDRIERLEERREDLEELIAERRET-- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2037 qtnialqLMEKSQKeyeklAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCA 2116
Cdd:PRK02224 532 -------IEEKRER-----AEELRERAAELEAEAEEKREAA--AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL 597
|
....*...
gi 732170491 2117 VDAATAYE 2124
Cdd:PRK02224 598 LAAIADAE 605
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1829-2107 |
2.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLATMGEQLRLVKSQLQGL--SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQ 1906
Cdd:COG4717 161 LEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1907 EKAQVNSRK---------------AQTLNNNVNR-----------------ATQSAKELDVKIKNVIRNVHMLNRIRTWQ 1954
Cdd:COG4717 241 LEERLKEARlllliaaallallglGGSLLSLILTiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1955 KTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQAKQANGLNQ---ENERALGAIQRQVKEINSL 2020
Cdd:COG4717 321 LEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQEL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2021 QSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELA 2097
Cdd:COG4717 401 KEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE 479
|
330
....*....|
gi 732170491 2098 KQLEEIKRNA 2107
Cdd:COG4717 480 ELKAELRELA 489
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1834-2060 |
2.75e-05 |
|
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: 48.38 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1834 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVN 1912
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1913 SRKAQTLNNNvnratqsaKELDvkikNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLqeaaaq 1992
Cdd:COG1579 79 EEQLGNVRNN--------KEYE----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL------ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 1993 akqaNGLNQENERALGAIQrqvKEINSLQSDFTKYLTTADSSLLqtnialqlmeksqKEYEKLAASLN 2060
Cdd:COG1579 141 ----EEKKAELDEELAELE---AELEELEAEREELAAKIPPELL-------------ALYERIRKRKN 188
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1835-2217 |
2.93e-05 |
|
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: 50.17 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1835 TMGEQLRLVKSQLQglsasaglleQMRHMETQA-KDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVN 1912
Cdd:pfam01576 335 ALEEETRSHEAQLQ----------EMRQKHTQAlEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQaKQDSE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1913 SRKA------QTLNNNVN---RATQSAKELDVKIKNVIRNV-HMLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAK 1978
Cdd:pfam01576 405 HKRKklegqlQELQARLSeseRQRAELAEKLSKLQSELESVsSLLNEAEGKNIKLSKDVSSLESQLQDTQEllqeETRQK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1979 LSdLRARLQEAAAQAkqaNGLNQ---ENERALGAIQRQVKEINSLQSDFTKYLTTADSSL---------LQTNI---ALQ 2043
Cdd:pfam01576 485 LN-LSTRLRQLEDER---NSLQEqleEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLealeegkkrLQRELealTQQ 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2044 LMEKSQkEYEKLAASLNEARQELSDKVRELSRsagKTSLVEEAEKHARSL-QELAKQLEEIKRNAsgDELVRCavdAATA 2122
Cdd:pfam01576 561 LEEKAA-AYDKLEKTKNRLQQELDDLLVDLDH---QRQLVSNLEKKQKKFdQMLAEEKAISARYA--EERDRA---EAEA 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2123 YENILNAIkaaedaanRAASASESALQTviKEDLPRKAKTLSSNSDKLLNEakmtqkklKQEVSPALNNLQQTLNIVTVQ 2202
Cdd:pfam01576 632 REKETRAL--------SLARALEEALEA--KEELERTNKQLRAEMEDLVSS--------KDDVGKNVHELERSKRALEQQ 693
|
410
....*....|....*
gi 732170491 2203 KEVIDTNLTTLRDGL 2217
Cdd:pfam01576 694 VEEMKTQLEELEDEL 708
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1829-2109 |
3.55e-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: 49.68 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLATMGEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTD-----LNQEFE 1903
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLE------QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1904 TLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHML-NRIRTWQKThQGENNGLANSIRDSLNEYEAKLSDL 1982
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkEQIKSIEKE-IENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1983 RARLQeaaaqakqanGLNQENERA---LGAIQRQVKEINSlqsdftkYLTTADSSLLQTNIALQLMEKSQKEYEKLAASL 2059
Cdd:TIGR02169 881 ESRLG----------DLKKERDELeaqLRELERKIEELEA-------QIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170491 2060 NEARQELSD---------KVRELSRSAGKTSL--VEEAEKHARSLQELAKQLEEIKRNASG 2109
Cdd:TIGR02169 944 EEIPEEELSledvqaelqRVEEEIRALEPVNMlaIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
2036-2200 |
4.25e-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: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2036 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 2113
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2114 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 2188
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 732170491 2189 LNNLQQTLNIVT 2200
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1829-2327 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQmrhmetQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK 1908
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEE------KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1909 -AQVNSRKAQtLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKthqgennglANSIRDSLNEYEAKLSDLRARLQ 1987
Cdd:TIGR02168 388 vAQLELQIAS-LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1988 EAAAQAKQANGLNQENERALGAIQRQVKE----INSLQSDFTKYLTtadsslLQTNIALQLMEKSQ-------------- 2049
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQlqarLDSLERLQENLEG------FSEGVKALLKNQSGlsgilgvlselisv 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2050 -KEYEK-LAASLNEARQEL-----------------SDKVR----ELSRSAGKTSLVEEAE--KHARSLQELAKQLEEIK 2104
Cdd:TIGR02168 532 dEGYEAaIEAALGGRLQAVvvenlnaakkaiaflkqNELGRvtflPLDSIKGTEIQGNDREilKNIEGFLGVAKDLVKFD 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2105 ---RNASGDELVRCAV----DAATAYENILNA-----------IKAAEDAANRAASASESALQTVIK-EDLPRKAKTLSS 2165
Cdd:TIGR02168 612 pklRKALSYLLGGVLVvddlDNALELAKKLRPgyrivtldgdlVRPGGVITGGSAKTNSSILERRREiEELEEKIEELEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2166 NSDKL---LNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDT------NLTTLRDGLHgIQRGDIDAMISSAKSMV 2236
Cdd:TIGR02168 692 KIAELekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaeveQLEERIAQLS-KELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2237 RKANDITDEVLDGLNPIQTDVERIKD--TYGRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQllpLGNISDNM 2314
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR---LEDLEEQI 847
|
570
....*....|...
gi 732170491 2315 DRIRELIQQARDA 2327
Cdd:TIGR02168 848 EELSEDIESLAAE 860
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1808-1938 |
4.92e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1808 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 1887
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 1888 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIK 1938
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2381-2507 |
5.58e-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: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2381 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 2456
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 732170491 2457 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 2507
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
355-423 |
5.98e-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: 42.73 E-value: 5.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170491 355 ACNCHGHAS---NCYYdpdverqqaslntqgiyaGGGVCInCQHNTAGVNCEQCAKGYYRPYgvpvDAPDGC 423
Cdd:cd00055 1 PCDCNGHGSlsgQCDP------------------GTGQCE-CKPNTTGRRCDRCAPGYYGLP----SQGGGC 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1877-2304 |
6.54e-05 |
|
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: 48.86 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1877 YRSAISNHGSKIEGLERELtdlnqefETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVhmlnrirtwqkt 1956
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKL-------KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQI------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1957 hqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLL 2036
Cdd:TIGR04523 85 ---------KDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2037 QTNIALQLMEKSQKEYEKlaaSLNEARQELSDKVRELSRSAGK--------TSLVEEAEKHaRSLQ----ELAKQLEEIK 2104
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKllklelllSNLKKKIQKN-KSLEsqisELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2105 RNAS--GDELVRCAVDAATAYENILNAIKaaedaanraasasesaLQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQkKLK 2182
Cdd:TIGR04523 232 DNIEkkQQEINEKTTEISNTQTQLNQLKD----------------EQNKIKKQLSEKQKELEQNNKKIKELEKQLN-QLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2183 QEVSpALNNlQQTLNIVTVQKEVIDTNLTTLRDglhgIQRgDIDAMISSAKSMVRKANDITDEVLDG----------LNP 2252
Cdd:TIGR04523 295 SEIS-DLNN-QKEQDWNKELKSELKNQEKKLEE----IQN-QISQNNKIISQLNEQISQLKKELTNSesensekqreLEE 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 732170491 2253 IQTDVERIKDtygrtQNEDFKKALTDADNSVNKLTNKLpdlwRKIESINQQL 2304
Cdd:TIGR04523 368 KQNEIEKLKK-----ENQSYKQEIKNLESQINDLESKI----QNQEKLNQQK 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1889-2246 |
1.43e-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: 47.74 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1889 EGLEReLTDLNQEFETlqekaQVNSRKAQTlnnnvnRATQSAKELdvkiKNVIRNVHmlnrIRTWQKTHQGENNGLANsI 1968
Cdd:TIGR02168 186 ENLDR-LEDILNELER-----QLKSLERQA------EKAERYKEL----KAELRELE----LALLVLRLEELREELEE-L 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1969 RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL--LQTNIA----- 2041
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEeleaq 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2042 LQLMEKSQKEYEKLAASLNEARQELSDKVrelsrsagkTSLVEEAEKHARSLQELAKQLEEIKRNAsgdELVRCAVDAAT 2121
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEEL---------ESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2122 AYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLNIVTV 2201
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELRE 468
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 732170491 2202 QKEVIDTNLTTLRDGLHGIQrgdidAMISSAKSMVRKANDITDEV 2246
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQ-----ARLDSLERLQENLEGFSEGV 508
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1856-2122 |
1.49e-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: 47.51 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1856 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKaqvNSRKAQTLNNNVNRATQSAKELDV 1935
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQ---REREDRERLEELESLKKENKDLKE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1936 KIknvirnvhmlnrirtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENEralGAIQRQVK 2015
Cdd:pfam10174 483 KV----------------------------SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE---IAVEQKKE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2016 EINSLQSDFTKYLTTADSSLLQTNIA--LQLME-----------KSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL 2082
Cdd:pfam10174 532 ECSKLENQLKKAHNAEEAVRTNPEINdrIRLLEqevarykeesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 732170491 2083 -VEEAEKHARSLQelAKQLEEIKRNASGDELVRCAVDAATA 2122
Cdd:pfam10174 612 qMKEQNKKVANIK--HGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1886-2147 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1886 SKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKnvirnvhmlnrirtwqkthqgenngla 1965
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1966 nSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnqenERALGAIQRQVKEINSLQ-----SDFTKYLTTAD--SSLL-Q 2037
Cdd:COG3883 69 -KLQAEIAEAEAEIEERREEL-----------------GERARALYRSGGSVSYLDvllgsESFSDFLDRLSalSKIAdA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2038 TNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktSLVEEAEKHARSLQELAKQLEEIKRNASgDELVRCAV 2117
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELE------AAKAELEAQQAEQEALLAQLSAEEAAAE-AQLAELEA 203
|
250 260 270
....*....|....*....|....*....|
gi 732170491 2118 DAATAYENILNAIKAAEDAANRAASASESA 2147
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1829-2065 |
1.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1829 LLNDLAT--MGEQLRLVKSQLQglSASAGLLEQMRHMETQAKDLRNQLLNYRSA--ISNHGSKIEGLERELTDLNQEFET 1904
Cdd:COG3206 153 VANALAEayLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1905 LQEKAQVNSRKAQTLNNNVNRATQSAKEL--DVKIKNVIRNVHMLNR-----IRTWQKTH----------QGENNGLANS 1967
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAelaelSARYTPNHpdvialraqiAALRAQLQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1968 IRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEneraLGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEK 2047
Cdd:COG3206 311 AQRILASLEAELEALQAREAS----------LQAQ----LAQLEARLAELPELEAELRR---------LEREV-----EV 362
|
250
....*....|....*...
gi 732170491 2048 SQKEYEKLAASLNEARQE 2065
Cdd:COG3206 363 ARELYESLLQRLEEARLA 380
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1916-2131 |
2.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1916 AQTLNNNVNRATQSAKELDVKIKNVIRNVHML-NRIRTWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLQEAAAQA 1993
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAeAALEEFRQKNGLVDlSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1994 KQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLT--TADSSL---LQTNIAlQLMEKSQKEYEKLAASLNEA 2062
Cdd:COG3206 243 AALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSAryTPNHPDviaLRAQIA-ALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2063 RQELSDKVRELSRSagktslVEEAEKHARSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 2131
Cdd:COG3206 322 LEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
356-423 |
3.61e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170491 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 |
3.74e-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: 40.41 E-value: 3.74e-04
10 20 30
....*....|....*....|....*....|....*....
gi 732170491 684 CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYY 722
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1883-2217 |
3.93e-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: 46.58 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1883 NHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNvirnvhmlnrirtwqkthqgenn 1962
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA----------------------- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1963 glansiRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERalgaIQRQVKEINSLQSDFTKYLTTADSSL------- 2035
Cdd:TIGR00606 366 ------RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIER----QEDEAKTAAQLCADLQSKERLKQEQAdeirdek 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2036 --LQTNIALQ--LMEKSQ-------KEYEKLAASLN---EARQELSDKVRELSRsAGKTSLVEEAEKHARSLQ------- 2094
Cdd:TIGR00606 436 kgLGRTIELKkeILEKKQeelkfviKELQQLEGSSDrilELDQELRKAERELSK-AEKNSLTETLKKEVKSLQnekadld 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2095 ----ELAKQLEEIKRNA-SGDELVRCAVDAATAYENILNaikaaedaanraASASESALQTVIKEDLPRKaKTLSSNSDK 2169
Cdd:TIGR00606 515 rklrKLDQEMEQLNHHTtTRTQMEMLTKDKMDKDEQIRK------------IKSRHSDELTSLLGYFPNK-KQLEDWLHS 581
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 732170491 2170 LLNEAKMTQKKLKqEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGL 2217
Cdd:TIGR00606 582 KSKEINQTRDRLA-KLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1832-2100 |
4.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1832 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE 1907
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1908 KAQVNSR-------KAQTLNNNVNRATQS-AKELDVKIKNVIRNVHMLNRI-RTWQKTHQGENNGLANSIrDSLNEYEAK 1978
Cdd:COG4913 742 LARLELRalleerfAAALGDAVERELRENlEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADL-ESLPEYLAL 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1979 LSDL--------RARLQEAAAQAKQAN--GLNQENERALGAIQRQVKEIN-SL-QSDFtkyltTADSSllqtniaLQLme 2046
Cdd:COG4913 821 LDRLeedglpeyEERFKELLNENSIEFvaDLLSKLRRAIREIKERIDPLNdSLkRIPF-----GPGRY-------LRL-- 886
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 732170491 2047 ksqkEYEKlaaSLNEARQELSDKVRELSRSAGKTSLvEEAEKHARSLQELAKQL 2100
Cdd:COG4913 887 ----EARP---RPDPEVREFRQELRAVTSGASLFDE-ELSEARFAALKRLIERL 932
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1828-2197 |
4.74e-04 |
|
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: 46.12 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1828 TLLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQA-------KDLRNQLLNYRSAIsnhgskieglereltDLNQ 1900
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCK---ELDILQREQATIdtrtsafRDLQGQLAHAKKQQ---------------ELQQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1901 EFETLQEKAQVNSRKAQTLNN-NVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKL 1979
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1980 SDL-----RARLQEAAAQAKQANGLNQENERALG-AIQRQVK----EINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQ 2049
Cdd:TIGR00618 518 QDIdnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRAslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2050 KEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE----LVRCAVDAATAYEN 2125
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehALSIRVLPKELLAS 677
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170491 2126 ILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLN 2197
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1858-2442 |
5.55e-04 |
|
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: 46.20 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1858 EQMRHMETQAKDLRNQLLNyrsaISNHGSKIEGLEREltdlnqefetLQEKAQVNSRKaqtlNNNVNRAtqsakeldVKI 1937
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLE----IDDEIIYINKLKLE----------LKEKIKNISDK----NEYIKKA--------IDL 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1938 KNVIRN----VHMLNRIRTWQKT-HQGENNGLANSIRDSLNE-YEAKLSDLRARLQEAAAQAKQAnglNQENERALGAIQ 2011
Cdd:TIGR01612 626 KKIIENnnayIDELAKISPYQVPeHLKNKDKIYSTIKSELSKiYEDDIDALYNELSSIVKENAID---NTEDKAKLDDLK 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2012 RQV-KEINSLQSDFTK----YLTTADSSllQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktSLVEEA 2086
Cdd:TIGR01612 703 SKIdKEYDKIQNMETAtvelHLSNIENK--KNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELS------NKINDY 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2087 EKHARSLQELAKQLEEIkRNASGDELvrcavdaatayeNILNaikaaedaanraaSASESALQTVikEDLPRKAKTLSSN 2166
Cdd:TIGR01612 775 AKEKDELNKYKSKISEI-KNHYNDQI------------NIDN-------------IKDEDAKQNY--DKSKEYIKTISIK 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2167 SD---KLLNEAKMtqkkLKQEVspaLNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGI-------QRGDIDAMISSAKSMV 2236
Cdd:TIGR01612 827 EDeifKIINEMKF----MKDDF---LNKVDKFINFENNCKEKIDSEHEQFAELTNKIkaeisddKLNDYEKKFNDSKSLI 899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2237 RKANDITDEVLDGLNPIQTDVERIKDTygrtqnEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDN--M 2314
Cdd:TIGR01612 900 NEINKSIEEEYQNINTLKKVDEYIKIC------ENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNtlI 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2315 DRIRELiqqarDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSLSLFLQRPNSRENGGTENMFVMYLGNKDASRdyIG 2394
Cdd:TIGR01612 974 DKINEL-----DKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPN--IE 1046
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 2395 MAVvdgqLTCVYNLGD-------REAELQVDQILTKSETKEAVMDRVKFQ-RIYQF 2442
Cdd:TIGR01612 1047 IAI----HTSIYNIIDeiekeigKNIELLNKEILEEAEINITNFNEIKEKlKHYNF 1098
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1868-2312 |
6.51e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.98 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1868 KDLRNQLLNY---RSAISNHGSKIEGLERELTDLNQEFETLQEKaqvNSRKAQTLNNNVNRATQSAKELDvkiKNVIRNv 1944
Cdd:PTZ00440 638 QELLDELSHFlddHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFM---KSDNIDNIIKNLKKELQNLLSLK---ENIIKK- 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1945 hMLNRIRTwqkthqgennglanSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQRQVKEINSLQSDF 2024
Cdd:PTZ00440 711 -QLNNIEQ--------------DISNSLNQYTIKYNDLKSSI--------------EEYKEEEEKLEVYKHQIINRKNEF 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2025 TKYLTTADSSLLQ-TNIALQLMEK----SQKEyEKLAASLNEARQELSDKVRELSRSAGKTSLVE-EAEKHARSLQELAK 2098
Cdd:PTZ00440 762 ILHLYENDKDLPDgKNTYEEFLQYkdtiLNKE-NKISNDINILKENKKNNQDLLNSYNILIQKLEaHTEKNDEELKQLLQ 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2099 QLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAAS------ASESALQTV---------IKEDLPRKAKTL 2163
Cdd:PTZ00440 841 KFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTlniainRSNSNKQLVehllnnkidLKNKLEQHMKII 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2164 SSN-----SDK--LLNEAKMTQKKLKQEVSPA-LNNL----QQTLNIVTVQKEVIDTNLTTLRDGLHGIQ------RGDI 2225
Cdd:PTZ00440 921 NTDniiqkNEKlnLLNNLNKEKEKIEKQLSDTkINNLkmqiEKTLEYYDKSKENINGNDGTHLEKLDKEKdewehfKSEI 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2226 DAMISSAKSMVRKANDIT----DEVLDGLNPIQTD---------------VERIKDTYG-RTQNEDFKKALTDA-DNSVN 2284
Cdd:PTZ00440 1001 DKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEkgkeieekvdqyislLEKMKTKLSsFHFNIDIKKYKNPKiKEEIK 1080
|
490 500
....*....|....*....|....*...
gi 732170491 2285 KLTNKLPDLWRKIESINQQLLPLGNISD 2312
Cdd:PTZ00440 1081 LLEEKVEALLKKIDENKNKLIEIKNKSH 1108
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
586-628 |
7.49e-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: 39.64 E-value: 7.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 732170491 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNLDkENPSGC 628
Cdd:cd00055 4 CNGHGSLsgqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
586-628 |
7.62e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 7.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 732170491 586 CDPAGTI----NSNLGYCQCKLHVEGPTCSRCKLLYWNldkENPSGC 628
Cdd:smart00180 3 CDPGGSAsgtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1694-1786 |
7.66e-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: 42.39 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1694 NQCQDGSGICVNCQHNTAGEhCERCQEGYYGNAV-HGSCRacPCPHTNSFATGCVVNG----GDVRCSCKAGYT------ 1762
Cdd:cd13406 16 HECPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVnYEPCK--PCTQCNQRSGSEEKQKctktSDTVCRCRPGTQpldsyk 92
|
90 100
....*....|....*....|....*
gi 732170491 1763 -GTQCERCAPGYFGNPQkfGGSCQP 1786
Cdd:cd13406 93 pGVDCVPCPPGHFSRGD--NQACKP 115
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1826-2317 |
9.10e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1826 VMTLLNDLATMGEQLRLVKSQLQGlsasaglleqmrHMETQAKDLRNQLLNY---RSAISNHGSKIEGLERELTDLNQEF 1902
Cdd:PTZ00440 1086 VEALLKKIDENKNKLIEIKNKSHE------------HVVNADKEKNKQTEHYnkkKKSLEKIYKQMEKTLKELENMNLED 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1903 ETLQEKAQVNSRKAQTL----NNNVNRATQSAKELDVKIKNVIRNV-HMLNRIRTWQKTHQGENNglANSIRDSLNEYEA 1977
Cdd:PTZ00440 1154 ITLNEVNEIEIEYERILidhiVEQINNEAKKSKTIMEEIESYKKDIdQVKKNMSKERNDHLTTFE--YNAYYDKATASYE 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1978 KLSDLrarlqeaaaqAKQANGLNQENERAlgaiqRQVKEINSLQSDFTKYLTTadsSLLQTNIalqlMEKSQKE----YE 2053
Cdd:PTZ00440 1232 NIEEL----------TTEAKGLKGEANRS-----TNVDELKEIKLQVFSYLQQ---VIKENNK----MENALHEiknmYE 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2054 KLAA-SLNEARQELSD---KVRELSRSAGKtslveEAEKHARSLQELAKQLEEIK--RNA--------SGDELVRCAVDA 2119
Cdd:PTZ00440 1290 FLISiDSEKILKEILNstkKAEEFSNDAKK-----ELEKTDNLIKQVEAKIEQAKehKNKiygsledkQIDDEIKKIEQI 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2120 ATAYENILNAIKAAEDAANRAASASESALQTV----IKEDLPRKAKTLSSNSDKLLNEAKMTQ--KKLKQEvspaLNNLQ 2193
Cdd:PTZ00440 1365 KEEISNKRKEINKYLSNIKSNKEKCDLHVRNAsrgkDKIDFLNKHEAIEPSNSKEVNIIKITDniNKCKQY----SNEAM 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2194 QTLNIVTVQKEVI---DTNLTTLrdglhgIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGR-TQN 2269
Cdd:PTZ00440 1441 ETENKADENNDSIikyEKEITNI------LNNSSILGKKTKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQlNEQ 1514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 732170491 2270 EDFKKALTDADNSVNKLTNKLPDLwrKIESINQQLLPLGNISDNMDRI 2317
Cdd:PTZ00440 1515 PNIKREGDVLNNDKSTIAYETIQY--NLGRVKHNLLNILNIKDEIETI 1560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1838-2185 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE---KAQVNSR 1914
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1915 ------KAQTLN------NNVNRATQSAKELDVKIKNVIRNVHM-LNRIRTWQKTHQgenngLANSIR---DSLNEY--- 1975
Cdd:PRK03918 444 elteehRKELLEeytaelKRIEKELKEIEEKERKLRKELRELEKvLKKESELIKLKE-----LAEQLKeleEKLKKYnle 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1976 ------------EAKLSDLRARLQEAAAQAKQANGLNQEN---ERALGAIQRQVKEINslqsdfTKYLTTADSSLLQTNI 2040
Cdd:PRK03918 519 elekkaeeyeklKEKLIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELL------KELEELGFESVEELEE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2041 ALQLMEKSQKEYeklaASLNEARQELSDKVRELSRSagKTSLVEEAEKHAR---SLQELAKQLEEIKRNASGDElvrcav 2117
Cdd:PRK03918 593 RLKELEPFYNEY----LELKDAEKELEREEKELKKL--EEELDKAFEELAEtekRLEELRKELEELEKKYSEEE------ 660
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 2118 daataYENILNaikaaedaANRAASASESALQTVIKEdLPRKAKTLSSNSDKLLNEaKMTQKKLKQEV 2185
Cdd:PRK03918 661 -----YEELRE--------EYLELSRELAGLRAELEE-LEKRREEIKKTLEKLKEE-LEEREKAKKEL 713
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1997-2197 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1997 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 2072
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2073 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 2129
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170491 2130 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 2197
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEELKEKLT 317
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
299-339 |
1.46e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 732170491 299 CVCN--GHA-EVCNINNpeklFRCECQHHTCGETCDRCCTGYNQ 339
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYG 40
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1833-2111 |
1.62e-03 |
|
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: 44.43 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1833 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN----- 1899
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1900 --QEFETLQEKAQVNSRKAQTLNNNVN--RATQSAKE--LDVKIKNvirnvhmLNRIRTWQKTHQGENNGLansiRDSLN 1973
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVDalRLRLEEKEsfLNKKTKQ-------LQDLTEEKSTLAGEIRDL----KDMLD 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1974 EYEAKLSDLRARLqeaaaqakqANGLNQ--ENERALGAIQRQVKeinSLQSdftkylttaDSSllQTNIALQLMEKSQKE 2051
Cdd:pfam10174 391 VKERKINVLQKKI---------ENLQEQlrDKDKQLAGLKERVK---SLQT---------DSS--NTDTALTTLEEALSE 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2052 YEKLAASLNEARqELSDKVRelsrsagktslVEEAEKHARSLQELAKQLEEIKRNASGDE 2111
Cdd:pfam10174 448 KERIIERLKEQR-EREDRER-----------LEELESLKKENKDLKEKVSALQPELTEKE 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1891-2111 |
1.72e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1891 LEReLTDLNQEFE----TLQEKAQVnSRKAQTLNnnvnratQSAKELDVKIknvirnvhMLNRIRTWQKTHQGENNGLA- 1965
Cdd:COG1196 188 LER-LEDILGELErqlePLERQAEK-AERYRELK-------EELKELEAEL--------LLLKLRELEAELEELEAELEe 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1966 -----NSIRDSLNEYEAKLSDLRARLQEAAAQAKQANG----LNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLL 2036
Cdd:COG1196 251 leaelEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 2037 QTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR-SAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE 2111
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1998-2277 |
2.15e-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: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1998 GLNQENERALGAIQRQVKEIN-SLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYE-----------KLAASLNEARQE 2065
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtgiqnltaeieQGQESLTENLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2066 LSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA--SGDELVRCAVDAATAYENILNAIKAAEDAANRAASA 2143
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2144 SESALQTVIKEdLPRKAKTLSSNSDKLLNEAkmtQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRG 2223
Cdd:COG5185 439 VSKLLNELISE-LNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732170491 2224 DIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDT-----------YGRTQNEDFKKALT 2277
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASnaktdgqaanlRTAVIDELTQYLST 579
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1830-2051 |
2.80e-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: 43.41 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1830 LNDLATMGEQLRLVKSQLQGLSASagLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEFEtlqeka 1909
Cdd:COG5185 369 EVELSKSSEELDSFKDTIESTKES--LDEIPQNQRGYAQEILATL---EDTLKAADRQIEELQRQIEQATSSNE------ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1910 qVNSRKAQTLNNNVNRATQSAKElDVKIKNVIRNVHMLNRIRTW-----QKTHQGENN--GLANSIRDSLNEYEAKLSDL 1982
Cdd:COG5185 438 -EVSKLLNELISELNKVMREADE-ESQSRLEEAYDEINRSVRSKkedlnEELTQIESRvsTLKATLEKLRAKLERQLEGV 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170491 1983 RARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSS---LLQTNIALQLMEKSQKE 2051
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTaviDELTQYLSTIESQQARE 587
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1665-1788 |
2.90e-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: 41.13 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1665 CQGCSPGY-YRDHKGLyTGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtn 1740
Cdd:cd13416 35 CEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP--- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170491 1741 sfatgcvvNGGDVRCSCKAGyTGTQCERCAPGYFGNPQKFGGSCQPCS 1788
Cdd:cd13416 101 --------PGQGVVQSCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCT 139
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1838-2118 |
3.20e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLSA---SAGLLEQMRHMEtQAKDLRNQLLNYRSA---ISNHGSKIEGLERELTDLN---QEFETLQEK 1908
Cdd:COG3096 864 QQLDQLKEQLQLLNKllpQANLLADETLAD-RLEELREELDAAQEAqafIQQHGKALAQLEPLVAVLQsdpEQFEQLQAD 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1909 aqvnsrkaqtlnnnVNRATQSAKELDVKI---KNVIRNVHMLNrirtWQKTHQ--GENNGLANSIRDSLNEYEAKLSDLR 1983
Cdd:COG3096 943 --------------YLQAKEQQRRLKQQIfalSEVVQRRPHFS----YEDAVGllGENSDLNEKLRARLEQAEEARREAR 1004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1984 ARLQEAAAQAKQANGLNQENERALGAIQRQVKEinsLQSDFTKYLTTADSSLLqtnialqlmEKSQKEYEKLAASLNEAR 2063
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQE---LEQELEELGVQADAEAE---------ERARIRRDELHEELSQNR 1072
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 2064 QELSDKVRELSRSAGK-TSLVEEAEKHARSLQELAKQLEEIKrnASGDELVRCAVD 2118
Cdd:COG3096 1073 SRRSQLEKQLTRCEAEmDSLQKRLRKAERDYKQEREQVVQAK--AGWCAVLRLARD 1126
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1967-2220 |
3.29e-03 |
|
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: 43.52 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1967 SIRDSLNEYEAKLSDLRARLQEAAAQakqangLNQENER--ALGAiqrqvKEINSLQSDFTKylTTADSSLLQTNIAL-- 2042
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQL------LEELNKKikDLGE-----EEQLRVKEKIGE--LEAEIASLERSIAEke 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2043 QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-KTSLVEE------------------AEKHARSLQELAK----- 2098
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrRDKLTEEyaelkeeledlraeleevDKEFAETRDELKDyrekl 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2099 -----QLEEIKRNAS--GDELVRcavdAATAYENILNAIKAAEDAANRAASASESAlQTVIKEDlPRKAKTLSSNSDKLL 2171
Cdd:TIGR02169 395 eklkrEINELKRELDrlQEELQR----LSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQ-EWKLEQLAADLSKYE 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 732170491 2172 NEAKMTQKKLkQEVSPALNNLQQTLNIVTVQKEVIDT-------NLTTLRDGLHGI 2220
Cdd:TIGR02169 469 QELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEErvrggraVEEVLKASIQGV 523
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
1999-2094 |
3.60e-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: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1999 LNQENERA-LGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRsa 2077
Cdd:pfam06009 24 QNLENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ----LEVNSSSLSDNISRIKE-- 97
|
90
....*....|....*..
gi 732170491 2078 gktsLVEEAEKHARSLQ 2094
Cdd:pfam06009 98 ----LIAQARKAANSIK 110
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1838-2107 |
3.84e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKSQLQGLSASAGLLEQMRHMEtQAKDLRNQLLNYRSA---ISNHGSKIEGLERELTDLN---QEFETLQEKAQV 1911
Cdd:PRK04863 868 EQAKEGLSALNRLLPRLNLLADETLAD-RVEEIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQ 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1912 NSRKAQTLNNNVnRAtqsakeldvkIKNVIRNVHMLNrirtWQKTHQ--GENNGLANSIRDSLNEYEAKLSDLRARLQEA 1989
Cdd:PRK04863 947 AQQTQRDAKQQA-FA----------LTEVVQRRAHFS----YEDAAEmlAKNSDLNEKLRQRLEQAEQERTRAREQLRQA 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1990 AAQAKQANGLNQENERALGAIQRQVKEinsLQSDFTKYLTTADSSLLqtnialqlmEKSQKEYEKLAASLNEARQelsdK 2069
Cdd:PRK04863 1012 QAQLAQYNQVLASLKSSYDAKRQMLQE---LKQELQDLGVPADSGAE---------ERARARRDELHARLSANRS----R 1075
|
250 260 270
....*....|....*....|....*....|....*....
gi 732170491 2070 VRELSRSAGKTSL-VEEAEKHARSLQELAKQLEEIKRNA 2107
Cdd:PRK04863 1076 RNQLEKQLTFCEAeMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1863-2196 |
4.91e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1863 METQAKDLrnqlLNYRSAISNHGSKIEGLERELTDLNQEFeTLQEKAQVNSRKAQTLNN--NVNRATQSAKELDVKIKNV 1940
Cdd:PTZ00440 2246 VETQKKKL----LDNKNKINNIKDKINDKEKELINVDSSF-TLESIKTFNEIYDDIKSNigDLYKLEDTNNDELKKVKLY 2320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1941 IRNV-HMLNRIRTWQK---THQGENNG--LANSIRDSLNEYEAKLSDlrarlqeaaaqakQANGLNQENERALGAIQR-- 2012
Cdd:PTZ00440 2321 IENItHLLNRINTLINdldNYQDENYGkdKNIELNNENNSYIIKTKE-------------KINNLKEEFSKLLKNIKRnn 2387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2013 QVKEINSLQ---SDFTKYLTTadsslLQTNIALQLMEKsqkeyEKLaASLNEARQELSDKVRELSRSAGKTSLVEEAEKH 2089
Cdd:PTZ00440 2388 TLCNNNNIKdfiSNIGKSVET-----IKQRFSSNLPEK-----EKL-HQIEENLNEIKNIMNETKRISNVDAFTNKILQD 2456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2090 ARslQELAKqLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKE--DLPRKAKTLSSNS 2167
Cdd:PTZ00440 2457 ID--NEKNK-ENNNMNAEKIDDLIENVTSHNEKIKSELLIINDALRRVKEKKDEMNKLFNSLTENnnNNNNSAKNIVDNS 2533
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 732170491 2168 DKLLNE-----AKMTQ---------KKLKQEVSPALNNLQQTL 2196
Cdd:PTZ00440 2534 TYIINEleshvSKLNEllsyidneiKELENEKLKLLEKAKIEE 2576
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1831-2100 |
4.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1831 NDLATMGEQLRlvksQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAIsnhgsKIEGLERELTDLNQEFETLQEKAQ 1910
Cdd:COG4913 242 EALEDAREQIE----LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1911 VNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNvhmlnRIRTWQKTHQgennglanSIRDSLNEYEAKLSDLRARLQeaa 1990
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLER-----EIERLERELE--------ERERRRARLEALLAALGLPLP--- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1991 aqakqanglnqENERALGAIQRQVKEInslqsdftkyLTTADssllqtnialQLMEKSQKEYEKLAASLNEARQELSDKV 2070
Cdd:COG4913 377 -----------ASAEEFAALRAEAAAL----------LEALE----------EELEALEEALAEAEAALRDLRRELRELE 425
|
250 260 270
....*....|....*....|....*....|
gi 732170491 2071 RELSRSAGKTSLVEEAEKHARslQELAKQL 2100
Cdd:COG4913 426 AEIASLERRKSNIPARLLALR--DALAEAL 453
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2035-2131 |
6.24e-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: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2035 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 2108
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 732170491 2109 GDELvrcavdaATAYENILNAIK 2131
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3116-3252 |
6.48e-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: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 3116 HSVLLGPEFKLVFSIRPR-SLTGILIHI-GSQPGKHLCVYLEAGKVTAS-MDSGAGGTSTSVT-PKQSLCDGQWHSVAVT 3191
Cdd:smart00210 46 FPSGLPEDFSLLTTFRQTpKSRGVLFAIyDAQNVRQFGLEVDGRANTLLlRYQGVDGKQHTVSfRNLPLADGQWHKLALS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170491 3192 IKQHILHLELDTDSsytAGQIPFPPAStQEPLHLGGapANLTTLRIPVWKSFFGCLRNIHV 3252
Cdd:smart00210 126 VSGSSATLYVDCNE---IDSRPLDRPG-QPPIDTDG--IEVRGAQAADRKPFQGDLQQLKI 180
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1856-2099 |
8.66e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1856 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLnqefetLQEKAQVNSRKaqtlnnnvnratqSAKELDV 1935
Cdd:cd22656 126 LLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDL------LTDEGGAIARK-------------EIKDLQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1936 KIKNvirnvhmlnrirtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQRQVK 2015
Cdd:cd22656 187 ELEK--------------------LNEEYAAKLKAKIDELKALIADDEAKL--------------AAALRLIADLTAADT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2016 EINSLQSDFTKylttadssllqtniALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQE 2095
Cdd:cd22656 233 DLDNLLALIGP--------------AIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAE 298
|
....
gi 732170491 2096 LAKQ 2099
Cdd:cd22656 299 KADK 302
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1838-2097 |
9.14e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1838 EQLRLVKS--QLQGLSASAG---LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLE---RELTDLN---QEFETLQ 1906
Cdd:COG0497 133 EHQSLLDPdaQRELLDAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRfqlEELEAAAlqpGEEEELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1907 EKAQVNSRkAQTLNNNVNRATQSAKELDVKIknvirnVHMLNRIRTWQKTHQGENNGLANsIRDSLNEYEAKLSDLRARL 1986
Cdd:COG0497 213 EERRRLSN-AEKLREALQEALEALSGGEGGA------LDLLGQALRALERLAEYDPSLAE-LAERLESALIELEEAASEL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1987 QEAAaqakqaNGLNQENERaLGAIQRQVKEINSLQSdftKYLTTADSSL-LQTNIA--LQLMEKSQKEYEKLAASLNEAR 2063
Cdd:COG0497 285 RRYL------DSLEFDPER-LEEVEERLALLRRLAR---KYGVTVEELLaYAEELRaeLAELENSDERLEELEAELAEAE 354
|
250 260 270
....*....|....*....|....*....|....*.
gi 732170491 2064 QELSDKVRELS--RSAGKTSLVEEAEKHarsLQELA 2097
Cdd:COG0497 355 AELLEAAEKLSaaRKKAAKKLEKAVTAE---LADLG 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1887-2131 |
9.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1887 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNN--NVNRATQSAKELDVKIKNVIRnvhmlnRIRTWQKTHQG---EN 1961
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSWDEIDVASAER------EIAELEAELERldaSS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 1962 NGLAnSIRDSLNEYEAKLSDLRARLqeaaaqaKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTnia 2041
Cdd:COG4913 685 DDLA-ALEEQLEELEAELEELEEEL-------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE--- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170491 2042 lqlmeksQKEYEKLAASLNEARQELSDKVRELsrsagktslveeAEKHARSLQELAKQLEEIKR---NASGDelVRCAVD 2118
Cdd:COG4913 754 -------RFAAALGDAVERELRENLEERIDAL------------RARLNRAEEELERAMRAFNRewpAETAD--LDADLE 812
|
250
....*....|...
gi 732170491 2119 AATAYENILNAIK 2131
Cdd:COG4913 813 SLPEYLALLDRLE 825
|
|
| |
