|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
45-298 |
8.82e-98 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 315.29 E-value: 8.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 45 LHPPYFNLAEGARIAASATCGEEAPargsprpteDLYCKLVGGPvaggdpnqtiRGQYCDICTAANSNKAHPASNAIDGT 124
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP---------ERYCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 125 ER----WWQSPPLSrgLEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSMDFGRTYQPWQFFASskrDCLERFG 200
Cdd:pfam00055 62 NGtnetWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 201 -PQTLERITRDDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLmgkaLR 279
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 317373598 280 DPTVTRRYYYSIKDISIGG 298
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2192-2450 |
4.87e-94 |
|
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: 305.88 E-value: 4.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2192 LRGINASSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEAT 2271
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2272 LGHAKTLLAAIRAVDRTLSELMSQTGHLGLaNASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLAR 2351
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE-NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2352 VQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLH 2431
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 317373598 2432 AARDTLASVFRLLHSLDQA 2450
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-298 |
6.97e-94 |
|
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: 304.67 E-value: 6.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 44 SLHPPYFNLAEGARIAASATCGEEAPARgsprptedlYCKLVGGpvaggdpnqTIRGQYCDICTAANSNKAHPASNAIDG 123
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 124 TE----RWWQSPPLSRGLEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSmDFGRTYQPWQFFASskrDCLERF 199
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 200 GPQTLERITR--DDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLMGKA 277
Cdd:smart00136 141 GRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 317373598 278 lrdPTVTRRYYYSIKDISIGG 298
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1693-1829 |
5.12e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 168.99 E-value: 5.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 1693 YWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVfvPMESRPDVVLQGNQMSITFLEPA--YPTPGHVHRGQLQLVEGNFR 1770
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSSPDqpPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 1771 HTeTRNTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASPAGQGALASNVE 1829
Cdd:pfam00052 79 DS-DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1689-1818 |
2.08e-44 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 158.19 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 1689 FPELYWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVFVpmeSRPDVVLQGNQMSITFLEPAYPTPGHVHRGQLQLVEGN 1768
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHV---SAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 317373598 1769 FRHTETRnTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASP 1818
Cdd:smart00281 79 WQYYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2641-2762 |
2.44e-40 |
|
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: 146.86 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2641 DTATRVQSQLQAMQENVERWQGQYEGLRGQ---------DLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLa 2711
Cdd:pfam06009 10 ETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 2712 lSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTPRDLADLAAYTAL 2762
Cdd:pfam06009 89 -SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3340-3497 |
4.43e-28 |
|
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: 112.51 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3340 SYQFGGSlsSHLEFVGiLARHRNWPSLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQR 3419
Cdd:cd00110 1 GVSFSGS--SYVRLPT-LPAPRTRLSISFSFRTTSPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317373598 3420 SRPGRWHKVSVRWEKNRILLVTDGARAWSQEGPHRQHQGaehPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLH 3497
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALL---NLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3521-3671 |
1.05e-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: 105.58 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3521 GLFFPGSGGViTLDLPGATLPDVGLELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGefSTSVTRPSVL 3600
Cdd:cd00110 1 GVSFSGSSYV-RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 3601 CDGQWHRLAVMKSGNVLRLEVD-AQSNHTVGPLLAAAAGAPAPLYLGGLPEPMAV--QPWPPAYCGCMRRLAVN 3671
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSpgLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3365-3499 |
1.78e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 104.34 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3365 SLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQRS-RPGRWHKVSVRWEKNRILLVTDG 3443
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 3444 ARAWSQEGPhRQHQGAEHPQPhtLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3499
Cdd:smart00282 80 GNRVSGESP-GGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3372-3499 |
1.65e-22 |
|
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: 95.56 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3372 PRSSRGLLLFTARLRpgSPSLALFLSNGHFVAQME-GLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQE 3450
Cdd:pfam02210 3 TRQPNGLLLYAGGGG--SDFLALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 317373598 3451 GPHRQHQgaeHPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3499
Cdd:pfam02210 81 PPGESLL---LNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3545-3672 |
1.76e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 92.79 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3545 LELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEFSTSVTRPSVlCDGQWHRLAVMKSGNVLRLEVDAQ 3624
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPL-NDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 3625 SN-HTVGPLLAAAAGAPAPLYLGGLPEPM--AVQPWPPAYCGCMRRLAVNR 3672
Cdd:smart00282 81 NRvSGESPGGLTILNLDGPLYLGGLPEDLklPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3549-3671 |
9.60e-20 |
|
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: 87.86 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3549 VRPLAVTGLIFHLGQARTPpYLQLQVTEKQVLLRADDGAGEFSTSVTrPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHT 3628
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSS-GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 317373598 3629 VGPLLAAAAGAPAPL-YLGGLPEP--MAVQPWPPAYCGCMRRLAVN 3671
Cdd:pfam02210 79 SLPPGESLLLNLNGPlYLGGLPPLllLPALPVRAGFVGCIRDVRVN 124
|
|
| LamG |
smart00282 |
Laminin G domain; |
2781-2908 |
1.71e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.84 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2781 FVMYMGSRQaTGDYMGVSLRDKKVHWVYQLGeAGPAVLSIDEDI---GeQFAAVSLDRTLQFGHMSVTVERQMIQETkgd 2857
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPTPlndG-QWHRVAVERNGRSVTLSVDGGNRVSGES--- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 2858 tvaPGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIEMDTLNEE 2908
Cdd:smart00282 88 ---PGGLTILNL---DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2347-2619 |
9.59e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATL 2426
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2427 QATLHAARDTLAsvfRLLHSLDQAKEELERLAASLDGARTPLLQRmqtfspAGSKLRLVEAAEAHAQQLGQLALNLSSII 2506
Cdd:COG1196 329 EEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2507 LDVNQDRLTQRAIEASNAysRILQAVQAAEDAAGQALQQADHTwatvvrQGLVDRAQQLLANSTALEEAMLQEQQRLGlv 2586
Cdd:COG1196 400 AQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEE------EEALEEAAEEEAELEEEEEALLELLAELL-- 469
|
250 260 270
....*....|....*....|....*....|...
gi 317373598 2587 wAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2619
Cdd:COG1196 470 -EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2943-3095 |
3.06e-14 |
|
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: 72.84 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2943 GSYLDGTGFARISFDSQISTTKRFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGlkkAVPLQPPPPL 3020
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSG---SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 3021 -TSASKAIQVFLLGgsrKRVLVRVER---ATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3095
Cdd:cd00110 78 nDGQWHSVSVERNG---RSVTLSVDGervVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2206-2695 |
8.21e-14 |
|
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: 78.29 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2206 HRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAV 2285
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2286 DRTLSELMSQTGHL--GLANasapsgEQLLRTLAEVERllwemraRDLGAPQAAAEAELAAAQRLLArVQEQLSSLWEE- 2362
Cdd:pfam01576 263 LKKIRELEAQISELqeDLES------ERAARNKAEKQR-------RDLGEELEALKTELEDTLDTTA-AQQELRSKREQe 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2363 ----NQALATQTRdrlaQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAlqrKQELSRDNATLQATlhaardtla 2438
Cdd:pfam01576 329 vtelKKALEEETR----SHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKA---KQALESENAELQAE--------- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2439 svfrlLHSLDQAKEELERLAASLDGArtplLQRMQTFSPAGSKLRlVEAAEahaqQLGQLALNLSSI--ILDVNQDRLTQ 2516
Cdd:pfam01576 393 -----LRTLQQAKQDSEHKRKKLEGQ----LQELQARLSESERQR-AELAE----KLSKLQSELESVssLLNEAEGKNIK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2517 RAIEASNAYSRiLQAVQaaedaagQALQQadhtwatvvrqglvdRAQQLLANSTALEEAmlqEQQRLGLvwaalqgaRTQ 2596
Cdd:pfam01576 459 LSKDVSSLESQ-LQDTQ-------ELLQE---------------ETRQKLNLSTRLRQL---EDERNSL--------QEQ 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2597 LRDVRAKKDQLEAHIQAAQAMLAmdtdETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRG------Q 2670
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLS----DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtknrlqQ 580
|
490 500 510
....*....|....*....|....*....|.
gi 317373598 2671 DLGQAVLDAGHS---VSTLEK---TLPQLLA 2695
Cdd:pfam01576 581 ELDDLLVDLDHQrqlVSNLEKkqkKFDQMLA 611
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2173-2736 |
1.83e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.73 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2173 LLLDDLERAGALLPAIHEQLRGINAssmawARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARR 2249
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNL-----KELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2250 LggqavgtrDQASQLLAgteatlghaktLLAAIRAVDRTLSELMSQTghlglanasapsgEQLLRTLAEVERLLWEMRAR 2329
Cdd:COG4717 121 L--------EKLLQLLP-----------LYQELEALEAELAELPERL-------------EELEERLEELRELEEELEEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2330 DlgapqaaaeaelaaaqRLLARVQEQLSSLWEEnqaLATQTRDRLAqheaglmDLREALNRAVDATREAQELNSRNQERL 2409
Cdd:COG4717 169 E----------------AELAELQEELEELLEQ---LSLATEEELQ-------DLAEELEELQQRLAELEEELEEAQEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2410 EEALQRKQELSRD--NATLQATLHAARdTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEA 2487
Cdd:COG4717 223 EELEEELEQLENEleAAALEERLKEAR-LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2488 AEAHAQQLGQLALNLSSIILdvnQDRLTQRAIEASNAYSRILQAVQAAEDAAgQALQQADHTWATVVRQGLVDRAQQLLA 2567
Cdd:COG4717 302 KEAEELQALPALEELEEEEL---EELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIAALLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2568 NSTALEEAMLQEqqrlglvWAALQGARTQLR-DVRAKKDQLEAHIQAAQAMLAMDTDETskkiahakavaaeAQDTATRV 2646
Cdd:COG4717 378 EAGVEDEEELRA-------ALEQAEEYQELKeELEELEEQLEELLGELEELLEALDEEE-------------LEEELEEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2647 QSQLQAMQENVERWQGQYEGLRGQdlgQAVLDAGHSVSTLEKTLPQLLAKLSILENRgvhNASLALsasigrVRELIAQA 2726
Cdd:COG4717 438 EEELEELEEELEELREELAELEAE---LEQLEEDGELAELLQELEELKAELRELAEE---WAALKL------ALELLEEA 505
|
570
....*....|
gi 317373598 2727 RGAASKVKVP 2736
Cdd:COG4717 506 REEYREERLP 515
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1438-1486 |
2.91e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 2.91e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 1438 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFPNCRPCDC 1486
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2965-3099 |
4.57e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 68.91 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2965 RFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGLKKAVPlQPPPPLTSASKAIQVFLLGgsrKRVLVR 3042
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNDGQWHRVAVERNG---RSVTLS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3043 V---ERATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIKALGK 3099
Cdd:smart00282 77 VdggNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1577-1625 |
4.84e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.84 E-value: 4.84e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 1577 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSLDAANPKGC 1625
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
540-583 |
4.09e-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: 63.14 E-value: 4.09e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 317373598 540 PCQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPL 583
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
587-634 |
1.18e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 1.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFPNCQACTC 634
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1576-1626 |
1.19e-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: 1.19e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 1576 PCDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSlDAANPKGCT 1626
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2069-2115 |
1.20e-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: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 317373598 2069 PCAC-GPAAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQ--GCR 2115
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
676-718 |
1.21e-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: 61.99 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 317373598 676 PCHCSAEGSLHAACDPRSGQCSCRPRVTGLRCDTCVPGAYNFP 718
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2175-2623 |
1.51e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2175 LDDLERAGALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARRLG 2251
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2252 GQ-AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRT----LAEVERLLWEM 2326
Cdd:COG4717 184 EQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2327 RARDLGAPQAAAEAELAAAQRLLA-----RVQEQLSSLWEENQALATQTRDRLAQHEagLMDLREALNRAVDATREAQEL 2401
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLAllfllLAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2402 NSRNQERLEEALQRKQELSRdnatlQATLHAARDTLASVFRLLHSLDqaKEELERLAAsldgartpLLQRMQtfspagsk 2481
Cdd:COG4717 342 LLDRIEELQELLREAEELEE-----ELQLEELEQEIAALLAEAGVED--EEELRAALE--------QAEEYQ-------- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2482 lRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAysriLQAVQAAEDAAGQALQQADHTWATVVRQGLVDR 2561
Cdd:COG4717 399 -ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE----LEELEEELEELREELAELEAELEQLEEDGELAE 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373598 2562 AQQllanstalEEAMLQEQ-QRLGLVWAALQGARTQLRDVR--AKKDQLEAHIQAAQAMLAMDTD 2623
Cdd:COG4717 474 LLQ--------ELEELKAElRELAEEWAALKLALELLEEAReeYREERLPPVLERASEYFSRLTD 530
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1437-1479 |
2.28e-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: 2.28e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 317373598 1437 PCGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFP 1479
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2070-2114 |
2.49e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.49e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 2070 CACGPA-AEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGC 2114
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3124-3267 |
2.96e-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: 64.36 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3124 AMTFHGHGFLRLALSNVAPLTGNVysGFGFHSAQDSALLYYrASPDGLC---QVSLQQGRVSLQL----LRTEVKTQAGF 3196
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSI--SFSFRTTSPNGLLLY-AGSQNGGdflALELEDGRLVLRYdlgsGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 3197 ADGAPHYVAFYSNATGVWLYVDD--QLQQMKPHRGPPPELqpqpegPPRLLLGGLPESG------TIYNFSGCISNVFV 3267
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGerVVESGSPGGSALLNL------DGPLYLGGLPEDLkspglpVSPGFVGCIRDLKV 150
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
541-582 |
3.18e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 3.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 317373598 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFP 582
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
541-589 |
4.12e-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: 4.12e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPLCQLCGC 589
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1528-1579 |
4.68e-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: 4.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 317373598 1528 CNCSGPGIqelTDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYPRCRPCDC 1579
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2023-2067 |
5.18e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 5.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 317373598 2023 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGcGGC 2067
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP-PGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1577-1625 |
5.88e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 5.88e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 1577 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFsldAANPKGC 1625
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1968-2021 |
6.00e-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: 60.06 E-value: 6.00e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 317373598 1968 PCDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGNCT 2021
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2022-2068 |
6.62e-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: 59.68 E-value: 6.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 317373598 2022 RCDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCG-GCR 2068
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2023-2067 |
8.58e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 8.58e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 317373598 2023 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCGGC 2067
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
494-541 |
1.02e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 1.02e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 317373598 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPC 541
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1528-1572 |
1.08e-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: 59.29 E-value: 1.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 1528 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1572
Cdd:cd00055 2 CDCNGHGSL---SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2070-2117 |
1.14e-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: 59.29 E-value: 1.14e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 2070 CACGP-AAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGCRRC 2117
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1528-1572 |
1.98e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.98e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 1528 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1572
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2203-2734 |
2.51e-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: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGgqavgtrDQASQLLAGTEATLGHAKTLLAAI 2282
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE-------EKLEELKEELESLEAELEELEAEL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2283 RAVDRTLSELmsQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLWEE 2362
Cdd:TIGR02168 368 EELESRLEEL--EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2363 NQALAtQTRDRLAQHEAGLMDLREALNRA----VDATREAQELNSRnQERLEEALQRKQELSRDNATL---QATLHAARD 2435
Cdd:TIGR02168 446 EEELE-ELQEELERLEEALEELREELEEAeqalDAAERELAQLQAR-LDSLERLQENLEGFSEGVKALlknQSGLSGILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2436 TLASVFR--------------------LLHSLDQAKEELERLAASLDGARTPLL---------------QRMQTFSPAGS 2480
Cdd:TIGR02168 524 VLSELISvdegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndreILKNIEGFLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2481 KLRLVEAAEAhAQQLGQLALNLSSIILDVNQ----------------------------------------------DRL 2514
Cdd:TIGR02168 604 AKDLVKFDPK-LRKALSYLLGGVLVVDDLDNalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrreiEEL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2515 TQRAIEASNAYSRILQAVQAAE---DAAGQALQQADHTWATVVRQglVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQ 2591
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQ--ISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2592 GARTQLRDVRAK----KDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDT---ATRVQSQLQAMQENVERWQGQY 2664
Cdd:TIGR02168 761 AEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRL 840
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 317373598 2665 EGLRGQ--DLGQAVLDAGHSVSTLEKTLPQLLAKLSILEN-RGVHNASLALSASigRVRELIAQARGAASKVK 2734
Cdd:TIGR02168 841 EDLEEQieELSEDIESLAAEIEELEELIEELESELEALLNeRASLEEALALLRS--ELEELSEELRELESKRS 911
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1438-1481 |
2.95e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 1438 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWG--FPNC 1481
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
677-725 |
3.61e-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: 57.75 E-value: 3.61e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 677 CHCSAEGSLHAACDPRSGQCSCRPRVTGLRCDTCVPGAYNFPYCEAGSC 725
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
677-719 |
4.32e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 4.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 317373598 677 CHCSAEGSLHAACDPRSGQCSCRPRVTGLRCDTCVPGAYNFPY 719
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
494-543 |
5.72e-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: 57.36 E-value: 5.72e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYG-PGCQPCQC 543
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPETGQCLCKPGVTGRHCDRCKPGYYGlPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
494-543 |
7.93e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 7.93e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 317373598 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPCQC 543
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
587-627 |
9.65e-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: 9.65e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 317373598 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFP 627
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2174-2614 |
1.02e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2174 LLDDLERAGALlpaihEQLRGiNASSmawARL--HRLNASIADLQSQLRSPLGPRHETA--QQLEVLEQQSTSLGQDARR 2249
Cdd:PRK02224 154 MIDDLLQLGKL-----EEYRE-RASD---ARLgvERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2250 LGGQ---AVGTRDQASQLLAGTEATLGHAKTLLAAIRAV---------------------DRTLSELMSQTGHL----GL 2301
Cdd:PRK02224 225 YEEQreqARETRDEADEVLEEHEERREELETLEAEIEDLretiaeterereelaeevrdlRERLEELEEERDDLlaeaGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2302 ANASAPSGEQLLRTL----AEVERLLWEMRArDLGAPQAAAEAELAAAQRLLAR---VQEQLSSLWEENQALATQTRDR- 2373
Cdd:PRK02224 305 DDADAEAVEARREELedrdEELRDRLEECRV-AAQAHNEEAESLREDADDLEERaeeLREEAAELESELEEAREAVEDRr 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2374 --LAQHEAGLMDLREALNRAVDATREAQElnsrnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLL------- 2444
Cdd:PRK02224 384 eeIEELEEEIEELRERFGDAPVDLGNAED-------FLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2445 ---------H--SLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSklrLVEaAEAHAQQLGQLALNLSSIILD----V 2509
Cdd:PRK02224 457 cgqpvegspHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED---LVE-AEDRIERLEERREDLEELIAErretI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2510 NQDRLtqrAIEASNAYSRILQA-VQAAEDAAGQALQQADHTWATVV-----RQGLVDRAQQL--LANSTALEEAMLQEQQ 2581
Cdd:PRK02224 533 EEKRE---RAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnskLAELKERIESLerIRTLLAAIADAEDEIE 609
|
490 500 510
....*....|....*....|....*....|....*..
gi 317373598 2582 RLGLVWAALQG----ARTQLRDVRAKKDQLEAHIQAA 2614
Cdd:PRK02224 610 RLREKREALAElndeRRERLAEKRERKRELEAEFDEA 646
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
632-679 |
1.46e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.46e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHGFPSCVPCHC 679
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2736-2901 |
3.07e-09 |
|
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: 58.58 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2736 PMKFNGRSGVQLRTPRDLADlaaYTALKFYLQGPEPEpgqGtedrFVMYMGSrQATGDYMGVSLRDKKVHWVYQLGEaGP 2815
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPN---G----LLLYAGS-QNGGDFLALELEDGRLVLRYDLGS-GS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2816 AVLSIDEDIGE-QFAAVSLDRTLQFGHMSVTVERQMiqetkgDTVAPGAEGLLNLRPDdfvFYVGGYPSTFTPPPLLRFP 2894
Cdd:cd00110 69 LVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPVSP 139
|
....*..
gi 317373598 2895 GYRGCIE 2901
Cdd:cd00110 140 GFVGCIR 146
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
775-827 |
3.44e-09 |
|
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: 55.05 E-value: 3.44e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 775 RCSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGlDQADYFGCR 827
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
3151-3269 |
4.84e-09 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 57.35 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3151 FGFHSAQDSALLYYRASPDG---LcQVSLQQGRVSLQLLR--TEVKTQAG---FADGAPHYVAFYSNATGVWLYVDDQLQ 3222
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGgdyL-ALELRDGRLVLRYDLgsGPARLTSDptpLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 3223 QMKPHRGPPPELQPqpegPPRLLLGGLPESG------TIYNFSGCISNVFVQR 3269
Cdd:smart00282 83 VSGESPGGLTILNL----DGPLYLGGLPEDLklpplpVTPGFRGCIRNLKVNG 131
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
587-629 |
5.45e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHG--FPNC 629
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1969-2019 |
5.81e-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: 5.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 1969 CDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGN 2019
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2203-2696 |
6.34e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.54 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRSPLGPRHEtaQQLEVLEQQSTSLGQDARRLGGQAvgtRDQASQLL-------AGTEATLgHA 2275
Cdd:NF041483 50 AKLHEARRSLASRPAYDGADIGYQAE--QLLRNAQIQADQLRADAERELRDA---RAQTQRILqehaehqARLQAEL-HT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2276 KTLLAAIRaVDRTLSElMSQT--GHLglaNASAPSGEQL-LRTLAEVERLLWEMRARdlgaPQAAAEAELAAAQRLLARV 2352
Cdd:NF041483 124 EAVQRRQQ-LDQELAE-RRQTveSHV---NENVAWAEQLrARTESQARRLLDESRAE----AEQALAAARAEAERLAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEENQALATQTRDRlAQHEAGLMdLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRD-NATLQATLH 2431
Cdd:NF041483 195 RQRLGSEAESARAEAEAILRR-ARKDAERL-LNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAaEQRMQEAEE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2432 AARDTLASVFRLlhsLDQAKEELERLAASLDGARTpllQRMQTfspAGSKL-RLV-------EAAEAHAQQLGQLAlnls 2503
Cdd:NF041483 273 ALREARAEAEKV---VAEAKEAAAKQLASAESANE---QRTRT---AKEEIaRLVgeatkeaEALKAEAEQALADA---- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2504 siilDVNQDRLTQRAIEASNAysrilqavQAAEDAAGQaLQQADHTwatvvrqglvdrAQQLLanSTALEEAmlQEQQRl 2583
Cdd:NF041483 340 ----RAEAEKLVAEAAEKART--------VAAEDTAAQ-LAKAART------------AEEVL--TKASEDA--KATTR- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2584 glvwAALQGARTQLRDVRAKKDQL--EAHIQAAQAMLAM--DTDETSKKIahakavaaeaqdtatrVQsqlqaMQENVER 2659
Cdd:NF041483 390 ----AAAEEAERIRREAEAEADRLrgEAADQAEQLKGAAkdDTKEYRAKT----------------VE-----LQEEARR 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 317373598 2660 WQGQYEGLRGQDL-------GQAVLDAGHSVSTLEKTLPQLLAK 2696
Cdd:NF041483 445 LRGEAEQLRAEAVaegerirGEARREAVQQIEEAARTAEELLTK 488
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2970-3095 |
1.06e-08 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 56.27 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2970 LRLVSYSGVLFFLK-QQSQFLCLAVQEGSLVLLYDFGAGlkkavplqpPPPLTSASKAiqvfLLGGSRKRVLVRVERATV 3048
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3049 ySVEQDND-------------LELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3095
Cdd:pfam02210 68 -TLSVDGQtvvsslppgesllLNLNGPLYLGGLPPLLLLPAL----PVRAGFVGCIRDVR 122
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2227-2655 |
1.33e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.38 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2227 HETAQQLEVLEQQST--------SLGQDARRLGGQAVGTRDQAsqlLAGTEATLGHA-KTLLAAIRAVDRTLSELmsqtg 2297
Cdd:NF041483 414 ADQAEQLKGAAKDDTkeyraktvELQEEARRLRGEAEQLRAEA---VAEGERIRGEArREAVQQIEEAARTAEEL----- 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2298 hlgLANASAPSGEqlLRTLA--EVERLLWEM--RARDLgapqaaaeaeLAAAQRLLARVQEQLSSLWEENQALATQTRdr 2373
Cdd:NF041483 486 ---LTKAKADADE--LRSTAtaESERVRTEAieRATTL----------RRQAEETLERTRAEAERLRAEAEEQAEEVR-- 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2374 lAQHEAGLMDLREALNRAV-----DATREAQELNSRNQERL---EEAL----QRKQELSRDNATLQATLhaaRDTLASVF 2441
Cdd:NF041483 549 -AAAERAARELREETERAIaarqaEAAEELTRLHTEAEERLtaaEEALadarAEAERIRREAAEETERL---RTEAAERI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2442 RLLHSldQAKEELERL--AASLDGARTpllqRMQTFSPAgskLRLVEAAEAHAQQLGQLALNlssiildvNQDRLtqRAi 2519
Cdd:NF041483 625 RTLQA--QAEQEAERLrtEAAADASAA----RAEGENVA---VRLRSEAAAEAERLKSEAQE--------SADRV--RA- 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2520 EASNAYSRI-------LQAVQ--------AAEDAAGQALQQADHTwatvvRQGLVDRAQQLLANS-TALEEAMlQEQQRL 2583
Cdd:NF041483 685 EAAAAAERVgteaaeaLAAAQeeaarrrrEAEETLGSARAEADQE-----RERAREQSEELLASArKRVEEAQ-AEAQRL 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2584 ---------GLVWAALQGARtQLRD-VRAKKDQLEAHIQAAQAMLAMDTDETSKKiahakavaaeAQDTATRVQSQLQAM 2653
Cdd:NF041483 759 veeadrratELVSAAEQTAQ-QVRDsVAGLQEQAEEEIAGLRSAAEHAAERTRTE----------AQEEADRVRSDAYAE 827
|
..
gi 317373598 2654 QE 2655
Cdd:NF041483 828 RE 829
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
776-826 |
2.16e-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: 52.74 E-value: 2.16e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 776 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGLDQADYFGC 826
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2347-2659 |
2.69e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQEQLSSLWEENQALatqtRDRLA-------------QHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL 2413
Cdd:PRK04863 314 RELAELNEAESDLEQDYQAA----SDHLNlvqtalrqqekieRYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2414 QRKQELSRDNATLQATL----------HAARDTLASVFRLLH----SLDQAKEELERLAASLDGARTPLLQrmqtfspAG 2479
Cdd:PRK04863 390 EEVDELKSQLADYQQALdvqqtraiqyQQAVQALERAKQLCGlpdlTADNAEDWLEEFQAKEQEATEELLS-------LE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2480 SKLRLveaAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYS--RILQAVQAAEDAAGQALQQADHTWATVVRqg 2557
Cdd:PRK04863 463 QKLSV---AQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLReqRHLAEQLQQLRMRLSELEQRLRQQQRAER-- 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2558 LVDRAQQLLANSTALEEAMLQEQQRLGlvwAALQGARTQLRDV-------RAKKDQLEAHIQ----------AAQAMLAM 2620
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELE---ARLESLSESVSEArerrmalRQQLEQLQARIQrlaarapawlAAQDALAR 614
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 317373598 2621 ------DTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVER 2659
Cdd:PRK04863 615 lreqsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
776-817 |
3.57e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.57e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 317373598 776 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFG 817
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1913-1966 |
3.73e-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: 51.97 E-value: 3.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 317373598 1913 CPCPLSVPSNnfaEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVLGSSC 1966
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1863-1899 |
7.90e-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: 51.20 E-value: 7.90e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 317373598 1863 PCQCHGH---SDRCLPGSGVCVdCQHNTEGAHCERCQAGF 1899
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2783-2901 |
9.83e-08 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 53.19 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2783 MYMGSRQatGDYMGVSLRDKKVHWVYQLGEAGPAVLSIDEDI--GeQFAAVSLDRTLQFGHMSVTverqmiQETKGDTVA 2860
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGNTLTLSVD------GQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 317373598 2861 PGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIE 2901
Cdd:pfam02210 82 PGESLLLNL---NGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1864-1913 |
1.05e-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: 50.81 E-value: 1.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 1864 CQCHGH---SDRCLPGSGVCvDCQHNTEGAHCERCQAGFVssrDDPSAPCVSC 1913
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYY---GLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1913-1959 |
1.30e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.30e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 317373598 1913 CPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNP 1959
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
828-867 |
1.84e-07 |
|
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: 50.05 E-value: 1.84e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 317373598 828 SCRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 867
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
429-473 |
2.78e-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: 49.66 E-value: 2.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 429 CNC-ESDFTDGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPSCYP 473
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
428-470 |
3.12e-07 |
|
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: 49.27 E-value: 3.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 317373598 428 RCNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPS 470
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-347 |
3.21e-07 |
|
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: 49.27 E-value: 3.21e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 299 RCVCHGHADACDAKDPTDpfrLQCTCQHNTCGGTCDRCCPGFNQQPWKP 347
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-673 |
4.89e-07 |
|
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: 48.89 E-value: 4.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 317373598 631 ACTCDPRGALDQLCGAG-GLCRCRPGYTGTACQECSPGFHGFPS 673
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| TorS_sensor_domain |
cd16172 |
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide ... |
2287-2578 |
7.47e-07 |
|
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide (TMAO) reductase (Tor) pathway, which consists TorT, a periplasmic binding protein that binds TMAO; TorS, a sensor histidine kinase that forms a complex with TorT, and TorR, the response regulator. The Tor pathway is involved in regulating a cellular response to trimethylamine-N-oxide (TMAO), a terminal electron receptor in anaerobic respiration. TorS consists of a periplasmic sensor domain, as well as a HAMP domain, a histidine kinase domain, and a receiver domain.
Pssm-ID: 293930 [Multi-domain] Cd Length: 261 Bit Score: 53.74 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2287 RTLSELMSQTGHLG--LANAsapsgeqllRTLAEverllWEMRARDLGapqaaaeaelaaaqRLLARVQEQLSSLweENQ 2364
Cdd:cd16172 2 RQLSELSSRIIASAqlLANA---------DSEAE-----RQQQGRQLT--------------AQLEALLRLLKAL--GQD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2365 ALATQTRDRLAQHEAGLMDLREALNRAVdatREAQELNSRNQERLEEALQRKQE---LSR---DNATLQATlhaARdtLA 2438
Cdd:cd16172 52 SFDSFLLSRLEQTVQEIIDNLAQLGELV---GQRLQLRQQFQQLFERLRAAAGElaqLARtqvANASTIAV---AN--VS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2439 SVFRLL--HSLDQAKEELERLAA-SLDgartpLLQRMqtfspagSKLRLveaaeaHAQQLGQLALNLSSIildVNQDRLt 2515
Cdd:cd16172 124 GLYDLIeqNDKEAAYQALDRLIEvDLD-----LLERM-------HELRL------LALQLGNLINELRTA---SDIARL- 181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2516 QRAIEASNAYSRILQA-VQAAED-----AAGQALQQADHtwatvvRQGLVDRAQQLLANSTALEEAMLQ 2578
Cdd:cd16172 182 AELRQQFNANLAILQRrVQAVEDpgrraQMAQLLSDLEQ------GQGLFALRRQLLALEQRLQALMQN 244
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
429-471 |
9.24e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 9.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 429 CNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTG--FPSC 471
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
829-867 |
9.33e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 9.33e-07
10 20 30
....*....|....*....|....*....|....*....
gi 317373598 829 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 867
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1912-1967 |
1.24e-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: 1.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 1912 SCPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVlGSSCQ 1967
Cdd:cd00055 1 PCDCN---GHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1969-2013 |
2.56e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 2.56e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 1969 CDCSGNGDpnlLFSDCDPLTGACRgCLRHTTGPRCEICAPGFYGN 2013
Cdd:smart00180 1 CDCDPGGS---ASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2203-2462 |
4.44e-06 |
|
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: 53.14 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRsplgpRHETAQQLevLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTL---- 2278
Cdd:TIGR02168 719 KELEELSRQISALRKDLA-----RLEAEVEQ--LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqi 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2279 ---LAAIRAVDRTLSELMSQTGHLGLANASAPSG-EQLLRTLAEVERLLWEM--RARDLGAPQAAAEAELAAAQRLLARV 2352
Cdd:TIGR02168 792 eqlKEELKALREALDELRAELTLLNEEAANLRERlESLERRIAATERRLEDLeeQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEE----NQALATQtRDRLAQHEAglmDLREALNRAVDATREAQELNSRN---QERLEEALQRKQEL-SRDNA 2424
Cdd:TIGR02168 872 ESELEALLNEraslEEALALL-RSELEELSE---ELRELESKRSELRRELEELREKLaqlELRLEGLEVRIDNLqERLSE 947
|
250 260 270
....*....|....*....|....*....|....*...
gi 317373598 2425 TLQATLHAArdtLASVFRLLHSLDQAKEELERLAASLD 2462
Cdd:TIGR02168 948 EYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIK 982
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
632-674 |
4.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 4.66e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHG--FPSC 674
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3153-3267 |
1.43e-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: 47.03 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3153 FHSAQDSALLYYRAS--PDGLCqVSLQQGRVSLQL-----LRTEVKTQAGFADGAPHYVAF-YSNATGVwLYVDDQlqqm 3224
Cdd:pfam02210 1 FRTRQPNGLLLYAGGggSDFLA-LELVNGRLVLRYdlgsgPESLLSSGKNLNDGQWHSVRVeRNGNTLT-LSVDGQ---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 317373598 3225 KPHRGPPPELQPQPEGPPRLLLGGLPESGTIY------NFSGCISNVFV 3267
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPalpvraGFVGCIRDVRV 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1864-1899 |
2.84e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.84e-05
10 20 30
....*....|....*....|....*....|....*....
gi 317373598 1864 CQCHG---HSDRCLPGSGVCvDCQHNTEGAHCERCQAGF 1899
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQC-ECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
829-867 |
3.18e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.88 E-value: 3.18e-05
10 20 30
....*....|....*....|....*....|....*....
gi 317373598 829 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 867
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
358-421 |
5.12e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 5.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373598 358 SCNCYGHAtdcyydpevdrrrasqSLDGT-YQGGGVCIdCQHHTTGVNCERCLPGFYRSPNHPLD 421
Cdd:cd00055 1 PCDCNGHG----------------SLSGQcDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
359-426 |
9.28e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.34 E-value: 9.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317373598 359 CNCYGHATdcyydpevdrrrasqSLDGTYQGGGVCiDCQHHTTGVNCERCLPGFYRSPNhplDSPHVC 426
Cdd:pfam00053 1 CDCNPHGS---------------LSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2117-2145 |
2.71e-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: 41.18 E-value: 2.71e-04
10 20 30
....*....|....*....|....*....|....
gi 317373598 2117 CQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2145
Cdd:pfam00053 1 CDCNPhgslsDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2116-2145 |
3.92e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 3.92e-04
10 20 30
....*....|....*....|....*....|....*
gi 317373598 2116 RCQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2145
Cdd:cd00055 1 PCDCNGhgslsGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2117-2145 |
4.67e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 4.67e-04
10 20 30
....*....|....*....|....*....|....
gi 317373598 2117 CQCP-----GGRCDPHTGRCNCPPGLSGERCDTC 2145
Cdd:smart00180 1 CDCDpggsaSGTCDPDTGQCECKPNVTGRRCDRC 34
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
300-345 |
5.00e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 5.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 317373598 300 CVCH--GHADacdakDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQPW 345
Cdd:smart00180 1 CDCDpgGSAS-----GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
387-416 |
5.36e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 5.36e-04
10 20 30
....*....|....*....|....*....|
gi 317373598 387 YQGGGVCiDCQHHTTGVNCERCLPGFYRSP 416
Cdd:smart00180 14 DPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
300-344 |
1.53e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.87 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 300 CVCHGHADAcdaKDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQP 344
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
45-298 |
8.82e-98 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 315.29 E-value: 8.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 45 LHPPYFNLAEGARIAASATCGEEAPargsprpteDLYCKLVGGPvaggdpnqtiRGQYCDICTAANSNKAHPASNAIDGT 124
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP---------ERYCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 125 ER----WWQSPPLSrgLEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSMDFGRTYQPWQFFASskrDCLERFG 200
Cdd:pfam00055 62 NGtnetWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 201 -PQTLERITRDDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLmgkaLR 279
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 317373598 280 DPTVTRRYYYSIKDISIGG 298
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2192-2450 |
4.87e-94 |
|
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: 305.88 E-value: 4.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2192 LRGINASSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEAT 2271
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2272 LGHAKTLLAAIRAVDRTLSELMSQTGHLGLaNASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLAR 2351
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE-NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2352 VQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLH 2431
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 317373598 2432 AARDTLASVFRLLHSLDQA 2450
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-298 |
6.97e-94 |
|
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: 304.67 E-value: 6.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 44 SLHPPYFNLAEGARIAASATCGEEAPARgsprptedlYCKLVGGpvaggdpnqTIRGQYCDICTAANSNKAHPASNAIDG 123
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 124 TE----RWWQSPPLSRGLEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSmDFGRTYQPWQFFASskrDCLERF 199
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 200 GPQTLERITR--DDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLMGKA 277
Cdd:smart00136 141 GRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 317373598 278 lrdPTVTRRYYYSIKDISIGG 298
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1693-1829 |
5.12e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 168.99 E-value: 5.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 1693 YWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVfvPMESRPDVVLQGNQMSITFLEPA--YPTPGHVHRGQLQLVEGNFR 1770
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSSPDqpPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 1771 HTeTRNTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASPAGQGALASNVE 1829
Cdd:pfam00052 79 DS-DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1689-1818 |
2.08e-44 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 158.19 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 1689 FPELYWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVFVpmeSRPDVVLQGNQMSITFLEPAYPTPGHVHRGQLQLVEGN 1768
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHV---SAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 317373598 1769 FRHTETRnTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASP 1818
Cdd:smart00281 79 WQYYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2641-2762 |
2.44e-40 |
|
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: 146.86 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2641 DTATRVQSQLQAMQENVERWQGQYEGLRGQ---------DLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLa 2711
Cdd:pfam06009 10 ETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 2712 lSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTPRDLADLAAYTAL 2762
Cdd:pfam06009 89 -SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3340-3497 |
4.43e-28 |
|
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: 112.51 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3340 SYQFGGSlsSHLEFVGiLARHRNWPSLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQR 3419
Cdd:cd00110 1 GVSFSGS--SYVRLPT-LPAPRTRLSISFSFRTTSPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317373598 3420 SRPGRWHKVSVRWEKNRILLVTDGARAWSQEGPHRQHQGaehPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLH 3497
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALL---NLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3521-3671 |
1.05e-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: 105.58 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3521 GLFFPGSGGViTLDLPGATLPDVGLELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGefSTSVTRPSVL 3600
Cdd:cd00110 1 GVSFSGSSYV-RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 3601 CDGQWHRLAVMKSGNVLRLEVD-AQSNHTVGPLLAAAAGAPAPLYLGGLPEPMAV--QPWPPAYCGCMRRLAVN 3671
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSpgLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3365-3499 |
1.78e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 104.34 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3365 SLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQRS-RPGRWHKVSVRWEKNRILLVTDG 3443
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 3444 ARAWSQEGPhRQHQGAEHPQPhtLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3499
Cdd:smart00282 80 GNRVSGESP-GGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3372-3499 |
1.65e-22 |
|
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: 95.56 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3372 PRSSRGLLLFTARLRpgSPSLALFLSNGHFVAQME-GLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQE 3450
Cdd:pfam02210 3 TRQPNGLLLYAGGGG--SDFLALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 317373598 3451 GPHRQHQgaeHPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3499
Cdd:pfam02210 81 PPGESLL---LNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3545-3672 |
1.76e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 92.79 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3545 LELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEFSTSVTRPSVlCDGQWHRLAVMKSGNVLRLEVDAQ 3624
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPL-NDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 3625 SN-HTVGPLLAAAAGAPAPLYLGGLPEPM--AVQPWPPAYCGCMRRLAVNR 3672
Cdd:smart00282 81 NRvSGESPGGLTILNLDGPLYLGGLPEDLklPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3549-3671 |
9.60e-20 |
|
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: 87.86 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3549 VRPLAVTGLIFHLGQARTPpYLQLQVTEKQVLLRADDGAGEFSTSVTrPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHT 3628
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSS-GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 317373598 3629 VGPLLAAAAGAPAPL-YLGGLPEP--MAVQPWPPAYCGCMRRLAVN 3671
Cdd:pfam02210 79 SLPPGESLLLNLNGPlYLGGLPPLllLPALPVRAGFVGCIRDVRVN 124
|
|
| LamG |
smart00282 |
Laminin G domain; |
2781-2908 |
1.71e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.84 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2781 FVMYMGSRQaTGDYMGVSLRDKKVHWVYQLGeAGPAVLSIDEDI---GeQFAAVSLDRTLQFGHMSVTVERQMIQETkgd 2857
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPTPlndG-QWHRVAVERNGRSVTLSVDGGNRVSGES--- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 2858 tvaPGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIEMDTLNEE 2908
Cdd:smart00282 88 ---PGGLTILNL---DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2347-2619 |
9.59e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATL 2426
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2427 QATLHAARDTLAsvfRLLHSLDQAKEELERLAASLDGARTPLLQRmqtfspAGSKLRLVEAAEAHAQQLGQLALNLSSII 2506
Cdd:COG1196 329 EEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2507 LDVNQDRLTQRAIEASNAysRILQAVQAAEDAAGQALQQADHTwatvvrQGLVDRAQQLLANSTALEEAMLQEQQRLGlv 2586
Cdd:COG1196 400 AQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEE------EEALEEAAEEEAELEEEEEALLELLAELL-- 469
|
250 260 270
....*....|....*....|....*....|...
gi 317373598 2587 wAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2619
Cdd:COG1196 470 -EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2943-3095 |
3.06e-14 |
|
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: 72.84 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2943 GSYLDGTGFARISFDSQISTTKRFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGlkkAVPLQPPPPL 3020
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSG---SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 3021 -TSASKAIQVFLLGgsrKRVLVRVER---ATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3095
Cdd:cd00110 78 nDGQWHSVSVERNG---RSVTLSVDGervVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2206-2695 |
8.21e-14 |
|
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: 78.29 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2206 HRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAV 2285
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2286 DRTLSELMSQTGHL--GLANasapsgEQLLRTLAEVERllwemraRDLGAPQAAAEAELAAAQRLLArVQEQLSSLWEE- 2362
Cdd:pfam01576 263 LKKIRELEAQISELqeDLES------ERAARNKAEKQR-------RDLGEELEALKTELEDTLDTTA-AQQELRSKREQe 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2363 ----NQALATQTRdrlaQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAlqrKQELSRDNATLQATlhaardtla 2438
Cdd:pfam01576 329 vtelKKALEEETR----SHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKA---KQALESENAELQAE--------- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2439 svfrlLHSLDQAKEELERLAASLDGArtplLQRMQTFSPAGSKLRlVEAAEahaqQLGQLALNLSSI--ILDVNQDRLTQ 2516
Cdd:pfam01576 393 -----LRTLQQAKQDSEHKRKKLEGQ----LQELQARLSESERQR-AELAE----KLSKLQSELESVssLLNEAEGKNIK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2517 RAIEASNAYSRiLQAVQaaedaagQALQQadhtwatvvrqglvdRAQQLLANSTALEEAmlqEQQRLGLvwaalqgaRTQ 2596
Cdd:pfam01576 459 LSKDVSSLESQ-LQDTQ-------ELLQE---------------ETRQKLNLSTRLRQL---EDERNSL--------QEQ 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2597 LRDVRAKKDQLEAHIQAAQAMLAmdtdETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRG------Q 2670
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLS----DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtknrlqQ 580
|
490 500 510
....*....|....*....|....*....|.
gi 317373598 2671 DLGQAVLDAGHS---VSTLEK---TLPQLLA 2695
Cdd:pfam01576 581 ELDDLLVDLDHQrqlVSNLEKkqkKFDQMLA 611
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2173-2736 |
1.83e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.73 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2173 LLLDDLERAGALLPAIHEQLRGINAssmawARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARR 2249
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNL-----KELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2250 LggqavgtrDQASQLLAgteatlghaktLLAAIRAVDRTLSELMSQTghlglanasapsgEQLLRTLAEVERLLWEMRAR 2329
Cdd:COG4717 121 L--------EKLLQLLP-----------LYQELEALEAELAELPERL-------------EELEERLEELRELEEELEEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2330 DlgapqaaaeaelaaaqRLLARVQEQLSSLWEEnqaLATQTRDRLAqheaglmDLREALNRAVDATREAQELNSRNQERL 2409
Cdd:COG4717 169 E----------------AELAELQEELEELLEQ---LSLATEEELQ-------DLAEELEELQQRLAELEEELEEAQEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2410 EEALQRKQELSRD--NATLQATLHAARdTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEA 2487
Cdd:COG4717 223 EELEEELEQLENEleAAALEERLKEAR-LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2488 AEAHAQQLGQLALNLSSIILdvnQDRLTQRAIEASNAYSRILQAVQAAEDAAgQALQQADHTWATVVRQGLVDRAQQLLA 2567
Cdd:COG4717 302 KEAEELQALPALEELEEEEL---EELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIAALLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2568 NSTALEEAMLQEqqrlglvWAALQGARTQLR-DVRAKKDQLEAHIQAAQAMLAMDTDETskkiahakavaaeAQDTATRV 2646
Cdd:COG4717 378 EAGVEDEEELRA-------ALEQAEEYQELKeELEELEEQLEELLGELEELLEALDEEE-------------LEEELEEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2647 QSQLQAMQENVERWQGQYEGLRGQdlgQAVLDAGHSVSTLEKTLPQLLAKLSILENRgvhNASLALsasigrVRELIAQA 2726
Cdd:COG4717 438 EEELEELEEELEELREELAELEAE---LEQLEEDGELAELLQELEELKAELRELAEE---WAALKL------ALELLEEA 505
|
570
....*....|
gi 317373598 2727 RGAASKVKVP 2736
Cdd:COG4717 506 REEYREERLP 515
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1438-1486 |
2.91e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 2.91e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 1438 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFPNCRPCDC 1486
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2965-3099 |
4.57e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 68.91 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2965 RFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGLKKAVPlQPPPPLTSASKAIQVFLLGgsrKRVLVR 3042
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNDGQWHRVAVERNG---RSVTLS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3043 V---ERATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIKALGK 3099
Cdd:smart00282 77 VdggNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1577-1625 |
4.84e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.84 E-value: 4.84e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 1577 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSLDAANPKGC 1625
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3549-3675 |
1.01e-12 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 67.73 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3549 VRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEfsTSVTRPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHT 3628
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGA--AVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 3629 VGPLLAAAAG--APAPLYLGGLPEpMAVQPWP----PAYCGCMRRLAVNRSPV 3675
Cdd:pfam00054 79 GESPLGATTDldVDGPLYVGGLPS-LGVKKRRlaisPSFDGCIRDVIVNGKPL 130
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2203-2727 |
2.52e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRsPLGPRHETAQ-------QLEVLEQQSTSL-----GQDARRLGGQAVGTRDQASQL---LAG 2267
Cdd:COG1196 186 ENLERLEDILGELERQLE-PLERQAEKAEryrelkeELKELEAELLLLklrelEAELEELEAELEELEAELEELeaeLAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2268 TEATLGHAKTLLAAIR-AVDRTLSELMSQTGHLG-LANASAPSGEQLLRTLAEVERLLWEMRArdlgapqaaaeaelaaa 2345
Cdd:COG1196 265 LEAELEELRLELEELElELEEAQAEEYELLAELArLEQDIARLEERRRELEERLEELEEELAE----------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2346 qrLLARVQEQLSSLwEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNAT 2425
Cdd:COG1196 328 --LEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2426 LQATLHAARDTLAsvfRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFspAGSKLRLVEAAEAHAQQLGQLALNLSSI 2505
Cdd:COG1196 405 LEEAEEALLERLE---RLEEELEELEEALAELEEEEEEEEEALEEAAEEE--AELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2506 I-LDVNQDRLTQRA---IEASNAYSRILQAVQAAEDAAGQALQQADH----TWATVVRQGLVDRAQQLLAN------STA 2571
Cdd:COG1196 480 AeLLEELAEAAARLlllLEAEADYEGFLEGVKAALLLAGLRGLAGAVavliGVEAAYEAALEAALAAALQNivveddEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2572 LEEAMLQEQQRLGLVwAALQGARTQLRDVRAKKDQLEAhIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQ 2651
Cdd:COG1196 560 AAAIEYLKAAKAGRA-TFLPLDKIRARAALAAALARGA-IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 2652 AMQENVERWQGqyEGLRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQAR 2727
Cdd:COG1196 638 RAVTLAGRLRE--VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
540-583 |
4.09e-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: 63.14 E-value: 4.09e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 317373598 540 PCQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPL 583
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
587-634 |
1.18e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 1.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFPNCQACTC 634
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1576-1626 |
1.19e-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: 1.19e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 1576 PCDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSlDAANPKGCT 1626
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2069-2115 |
1.20e-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: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 317373598 2069 PCAC-GPAAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQ--GCR 2115
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
676-718 |
1.21e-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: 61.99 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 317373598 676 PCHCSAEGSLHAACDPRSGQCSCRPRVTGLRCDTCVPGAYNFP 718
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2175-2623 |
1.51e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2175 LDDLERAGALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARRLG 2251
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2252 GQ-AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRT----LAEVERLLWEM 2326
Cdd:COG4717 184 EQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2327 RARDLGAPQAAAEAELAAAQRLLA-----RVQEQLSSLWEENQALATQTRDRLAQHEagLMDLREALNRAVDATREAQEL 2401
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLAllfllLAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2402 NSRNQERLEEALQRKQELSRdnatlQATLHAARDTLASVFRLLHSLDqaKEELERLAAsldgartpLLQRMQtfspagsk 2481
Cdd:COG4717 342 LLDRIEELQELLREAEELEE-----ELQLEELEQEIAALLAEAGVED--EEELRAALE--------QAEEYQ-------- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2482 lRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAysriLQAVQAAEDAAGQALQQADHTWATVVRQGLVDR 2561
Cdd:COG4717 399 -ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE----LEELEEELEELREELAELEAELEQLEEDGELAE 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373598 2562 AQQllanstalEEAMLQEQ-QRLGLVWAALQGARTQLRDVR--AKKDQLEAHIQAAQAMLAMDTD 2623
Cdd:COG4717 474 LLQ--------ELEELKAElRELAEEWAALKLALELLEEAReeYREERLPPVLERASEYFSRLTD 530
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1437-1479 |
2.28e-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: 2.28e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 317373598 1437 PCGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFP 1479
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2070-2114 |
2.49e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.49e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 2070 CACGPA-AEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGC 2114
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2385-2726 |
2.68e-11 |
|
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: 70.37 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2385 REALNRAVDATRE---AQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASV---FRLLHSLDQAKEELERLA 2458
Cdd:COG3096 281 RELSERALELRRElfgARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVqtaLRQQEKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2459 ASLdgartpllqRMQTFSPAGSKLRLVEA-AEAHAQQL------GQLAlnlssiilDVNQ--DRLTQRAIeasnAYSril 2529
Cdd:COG3096 361 ERL---------EEQEEVVEEAAEQLAEAeARLEAAEEevdslkSQLA--------DYQQalDVQQTRAI----QYQ--- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2530 QAVQAAEDAAGQaLQQADHTWAtvvrqGLVDRAQQLLANSTALEEAMLQEQQRLGLVWA--------------------- 2588
Cdd:COG3096 417 QAVQALEKARAL-CGLPDLTPE-----NAEDYLAAFRAKEQQATEEVLELEQKLSVADAarrqfekayelvckiagever 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2589 --ALQGARTQLRDVRakkdQLEAHIQAAQAmLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAmQENVERWQGQYEG 2666
Cdd:COG3096 491 sqAWQTARELLRRYR----SQQALAQRLQQ-LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEA 564
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2667 LRgQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGvhNASLALSASIGRVRELIAQA 2726
Cdd:COG3096 565 QL-EELEEQAAEAVEQRSELRQQLEQLRARIKELAARA--PAWLAAQDALERLREQSGEA 621
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3124-3267 |
2.96e-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: 64.36 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3124 AMTFHGHGFLRLALSNVAPLTGNVysGFGFHSAQDSALLYYrASPDGLC---QVSLQQGRVSLQL----LRTEVKTQAGF 3196
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSI--SFSFRTTSPNGLLLY-AGSQNGGdflALELEDGRLVLRYdlgsGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 3197 ADGAPHYVAFYSNATGVWLYVDD--QLQQMKPHRGPPPELqpqpegPPRLLLGGLPESG------TIYNFSGCISNVFV 3267
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGerVVESGSPGGSALLNL------DGPLYLGGLPEDLkspglpVSPGFVGCIRDLKV 150
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
541-582 |
3.18e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 3.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 317373598 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFP 582
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
541-589 |
4.12e-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: 4.12e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPLCQLCGC 589
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1528-1579 |
4.68e-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: 4.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 317373598 1528 CNCSGPGIqelTDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYPRCRPCDC 1579
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2023-2067 |
5.18e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 5.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 317373598 2023 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGcGGC 2067
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP-PGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1577-1625 |
5.88e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 5.88e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 1577 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFsldAANPKGC 1625
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1968-2021 |
6.00e-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: 60.06 E-value: 6.00e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 317373598 1968 PCDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGNCT 2021
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2022-2068 |
6.62e-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: 59.68 E-value: 6.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 317373598 2022 RCDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCG-GCR 2068
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2023-2067 |
8.58e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 8.58e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 317373598 2023 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCGGC 2067
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2174-2547 |
9.94e-11 |
|
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: 68.44 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2174 LLDDLERAGALLPAIHEQLrginasSMAWARLHRLNASIADLQSQLrsplgprhetAQQLEVLEQQSTSLGQDArrlggQ 2253
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQL------AEAEARLEAAEEEVDSLKSQL----------ADYQQALDVQQTRAIQYQ-----Q 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2254 AVGTRDQASQLLAGTEATLGHAKTLLAAIRA-VDRTLSELMSQTGHLGLANASAPSGE---QLLRTLA-EVERL-LWEmR 2327
Cdd:COG3096 418 AVQALEKARALCGLPDLTPENAEDYLAAFRAkEQQATEEVLELEQKLSVADAARRQFEkayELVCKIAgEVERSqAWQ-T 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2328 ARDLgapqaaaeaelaaaqrlLARvqeqlsslWEENQALAtqtrDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQE 2407
Cdd:COG3096 497 AREL-----------------LRR--------YRSQQALA----QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2408 RLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASldgartpllqrmqtfSPAGSKLRlvEA 2487
Cdd:COG3096 548 QLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR---------------APAWLAAQ--DA 610
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2488 AEAHAQQLGQlALNLSSIILDVNQdRLTQRAIEASNAYSRILQAVQAAEDAAGQaLQQAD 2547
Cdd:COG3096 611 LERLREQSGE-ALADSQEVTAAMQ-QLLEREREATVERDELAARKQALESQIER-LSQPG 667
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
494-541 |
1.02e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 1.02e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 317373598 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPC 541
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1528-1572 |
1.08e-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: 59.29 E-value: 1.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 1528 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1572
Cdd:cd00055 2 CDCNGHGSL---SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2070-2117 |
1.14e-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: 59.29 E-value: 1.14e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 2070 CACGP-AAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGCRRC 2117
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1528-1572 |
1.98e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.98e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 1528 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1572
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3373-3502 |
2.44e-10 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 60.79 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3373 RSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQEGP 3452
Cdd:pfam00054 4 TEPSGLLLYNGT-QTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGESP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 317373598 3453 HRQHQgaeHPQ-PHTLFVGGLP-ASSHSSKLPVTVGFSGCVKRLRLHGRPLG 3502
Cdd:pfam00054 83 LGATT---DLDvDGPLYVGGLPsLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2203-2734 |
2.51e-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: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGgqavgtrDQASQLLAGTEATLGHAKTLLAAI 2282
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE-------EKLEELKEELESLEAELEELEAEL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2283 RAVDRTLSELmsQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLWEE 2362
Cdd:TIGR02168 368 EELESRLEEL--EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2363 NQALAtQTRDRLAQHEAGLMDLREALNRA----VDATREAQELNSRnQERLEEALQRKQELSRDNATL---QATLHAARD 2435
Cdd:TIGR02168 446 EEELE-ELQEELERLEEALEELREELEEAeqalDAAERELAQLQAR-LDSLERLQENLEGFSEGVKALlknQSGLSGILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2436 TLASVFR--------------------LLHSLDQAKEELERLAASLDGARTPLL---------------QRMQTFSPAGS 2480
Cdd:TIGR02168 524 VLSELISvdegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndreILKNIEGFLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2481 KLRLVEAAEAhAQQLGQLALNLSSIILDVNQ----------------------------------------------DRL 2514
Cdd:TIGR02168 604 AKDLVKFDPK-LRKALSYLLGGVLVVDDLDNalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrreiEEL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2515 TQRAIEASNAYSRILQAVQAAE---DAAGQALQQADHTWATVVRQglVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQ 2591
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQ--ISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2592 GARTQLRDVRAK----KDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDT---ATRVQSQLQAMQENVERWQGQY 2664
Cdd:TIGR02168 761 AEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRL 840
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 317373598 2665 EGLRGQ--DLGQAVLDAGHSVSTLEKTLPQLLAKLSILEN-RGVHNASLALSASigRVRELIAQARGAASKVK 2734
Cdd:TIGR02168 841 EDLEEQieELSEDIESLAAEIEELEELIEELESELEALLNeRASLEEALALLRS--ELEELSEELRELESKRS 911
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1438-1481 |
2.95e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 1438 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWG--FPNC 1481
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
677-725 |
3.61e-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: 57.75 E-value: 3.61e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 677 CHCSAEGSLHAACDPRSGQCSCRPRVTGLRCDTCVPGAYNFPYCEAGSC 725
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
677-719 |
4.32e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 4.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 317373598 677 CHCSAEGSLHAACDPRSGQCSCRPRVTGLRCDTCVPGAYNFPY 719
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
494-543 |
5.72e-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: 57.36 E-value: 5.72e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYG-PGCQPCQC 543
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPETGQCLCKPGVTGRHCDRCKPGYYGlPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2174-2653 |
6.05e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2174 LLDDLERAGALLPAIHEQLRGINAssmawaRLHRLNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGQDARRLGGQ 2253
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEE------ELEELEEELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2254 AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASApSGEQLLRTLAEVERLLWEMRARDLga 2333
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEALEEAAEEEAELEEE-- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2334 pqaaaeaelaaAQRLLARVQEQLSS--LWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELnsRNQERLEE 2411
Cdd:COG1196 458 -----------EEALLELLAELLEEaaLLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--AGLRGLAG 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2412 ALQrkqELSRDNATLQATLhAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPL-LQRMQTFSPAGSKLRLVEAAEA 2490
Cdd:COG1196 525 AVA---VLIGVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpLDKIRARAALAAALARGAIGAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2491 HAqqLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQG------------- 2557
Cdd:COG1196 601 VD--LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGsrrellaalleae 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2558 -----LVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHA 2632
Cdd:COG1196 679 aeleeLAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
490 500
....*....|....*....|.
gi 317373598 2633 KAVAAEAQDTATRVQSQLQAM 2653
Cdd:COG1196 759 PPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2361-2668 |
6.73e-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: 65.46 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2361 EENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLAsv 2440
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2441 fRLLHSLDQAKEELERLAASLDGARTPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSIildvnQDRLTQRAIE 2520
Cdd:TIGR02168 299 -RLEQQKQILRERLANLERQLEELEAQLEELES------KLDELAEELAELEEKLEELKEELESL-----EAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2521 ASNAYSRILQAVQAAEDAAG---QALQQADHTWATVVR-----QGLVDRAQQLLAN----STALEEAMLQE-QQRLGLVW 2587
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSkvaQLELQIASLNNEIERlearlERLEDRRERLQQEieelLKKLEEAELKElQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2588 AALQGARTQLRDVRAKKDQLEAHIQAAQAMLamdtdetskkiahakavaAEAQDTATRVQSQLQAMQENVERWQGQYEGL 2667
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQAL------------------DAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
.
gi 317373598 2668 R 2668
Cdd:TIGR02168 509 K 509
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
494-543 |
7.93e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 7.93e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 317373598 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPCQC 543
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2176-2730 |
9.56e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2176 DDLERAGALLPAIHEQ---LRGINAssmAWARLHRLNASIADLQsQLRSPLgpRHETAQQ-LEVLEQQSTSLGQDARRLG 2251
Cdd:COG4913 235 DDLERAHEALEDAREQielLEPIRE---LAERYAAARERLAELE-YLRAAL--RLWFAQRrLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2252 GQAVGTRDQASQLLAgteatlgHAKTLLAAIRAVDrtlselmsqtghlglanasapsGEQLLRTLAEVERLLWEMRARdl 2331
Cdd:COG4913 309 AELERLEARLDALRE-------ELDELEAQIRGNG----------------------GDRLEQLEREIERLERELEER-- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2332 gapqaaaeaelaaaQRLLARVQEQLSSL----------WEENQALATQTRDRLAQHEAglmDLREALNRAVDATREAQEl 2401
Cdd:COG4913 358 --------------ERRRARLEALLAALglplpasaeeFAALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRR- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2402 nsrnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHS--------LDQAKEELE-RLAAS--LDGARTPLLQ 2470
Cdd:COG4913 420 ------ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgelIEVRPEEERwRGAIErvLGGFALTLLV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2471 RMQTFSPAGS-------KLRLV-EAAEAHAQQLGQLALNLSSIIldvnqDRLTQRAIEASNAYSRILQ---AVQAAEDAa 2539
Cdd:COG4913 494 PPEHYAAALRwvnrlhlRGRLVyERVRTGLPDPERPRLDPDSLA-----GKLDFKPHPFRAWLEAELGrrfDYVCVDSP- 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2540 gQALQQadHTWAtVVRQGLV---------------DRAQQLLANSTALEEAMLQEQQRLGlvwAALQGARTQLRDVRAKK 2604
Cdd:COG4913 568 -EELRR--HPRA-ITRAGQVkgngtrhekddrrriRSRYVLGFDNRAKLAALEAELAELE---EELAEAEERLEALEAEL 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2605 DQLEAHIQAAQAMLAM-----DTDETSKKIahakavaAEAQDTATRV---QSQLQAMQENVERWQGQYEGLRGQ--DLGQ 2674
Cdd:COG4913 641 DALQERREALQRLAEYswdeiDVASAEREI-------AELEAELERLdasSDDLAALEEQLEELEAELEELEEEldELKG 713
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 2675 AVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSAsigRVRELIAQARGAA 2730
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE---RFAAALGDAVERE 766
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
587-627 |
9.65e-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: 9.65e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 317373598 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFP 627
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2174-2614 |
1.02e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2174 LLDDLERAGALlpaihEQLRGiNASSmawARL--HRLNASIADLQSQLRSPLGPRHETA--QQLEVLEQQSTSLGQDARR 2249
Cdd:PRK02224 154 MIDDLLQLGKL-----EEYRE-RASD---ARLgvERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2250 LGGQ---AVGTRDQASQLLAGTEATLGHAKTLLAAIRAV---------------------DRTLSELMSQTGHL----GL 2301
Cdd:PRK02224 225 YEEQreqARETRDEADEVLEEHEERREELETLEAEIEDLretiaeterereelaeevrdlRERLEELEEERDDLlaeaGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2302 ANASAPSGEQLLRTL----AEVERLLWEMRArDLGAPQAAAEAELAAAQRLLAR---VQEQLSSLWEENQALATQTRDR- 2373
Cdd:PRK02224 305 DDADAEAVEARREELedrdEELRDRLEECRV-AAQAHNEEAESLREDADDLEERaeeLREEAAELESELEEAREAVEDRr 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2374 --LAQHEAGLMDLREALNRAVDATREAQElnsrnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLL------- 2444
Cdd:PRK02224 384 eeIEELEEEIEELRERFGDAPVDLGNAED-------FLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2445 ---------H--SLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSklrLVEaAEAHAQQLGQLALNLSSIILD----V 2509
Cdd:PRK02224 457 cgqpvegspHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED---LVE-AEDRIERLEERREDLEELIAErretI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2510 NQDRLtqrAIEASNAYSRILQA-VQAAEDAAGQALQQADHTWATVV-----RQGLVDRAQQL--LANSTALEEAMLQEQQ 2581
Cdd:PRK02224 533 EEKRE---RAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnskLAELKERIESLerIRTLLAAIADAEDEIE 609
|
490 500 510
....*....|....*....|....*....|....*..
gi 317373598 2582 RLGLVWAALQG----ARTQLRDVRAKKDQLEAHIQAA 2614
Cdd:PRK02224 610 RLREKREALAElndeRRERLAEKRERKRELEAEFDEA 646
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
632-679 |
1.46e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.46e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHGFPSCVPCHC 679
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
2173-2601 |
1.50e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 64.27 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2173 LLLDDLERAGALLPAIHEQLRginaSSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGG 2252
Cdd:COG3903 509 LRGPDQLAWLARLDAEHDNLR----AALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAA 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2253 QAVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLG 2332
Cdd:COG3903 585 AAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2333 APQAAAEAELAAAQRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEA 2412
Cdd:COG3903 665 ALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAA 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2413 LQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHA 2492
Cdd:COG3903 745 LALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAA 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2493 QQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTAL 2572
Cdd:COG3903 825 AAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAA 904
|
410 420
....*....|....*....|....*....
gi 317373598 2573 EEAMLQEQQRLGLVWAALQGARTQLRDVR 2601
Cdd:COG3903 905 LAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2215-2624 |
2.11e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 63.38 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2215 LQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRlggqavgTRDQASQLLAGTEATLGHAKTLLAAIRavdRTLSELMS 2294
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKR-------DREQWERQRRELESRVAELKEELRQSR---EKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2295 QtgHLGLANASApsgeqllrTLAEVERLLWEMRARDlgapqaaaeaelaaaqrlLARVQEqlssLWEENQALATQTRDRl 2374
Cdd:pfam07888 102 K--YKELSASSE--------ELSEEKDALLAQRAAH------------------EARIRE----LEEDIKTLTQRVLER- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2375 aqhEAGLMDLREALNRAVDATREAQELNSRNQERLEealQRKQELSRDNATLQA--TLHAARDTLA-----SVFRLLHSL 2447
Cdd:pfam07888 149 ---ETELERMKERAKKAGAQRKEEEAERKQLQAKLQ---QTEEELRSLSKEFQElrNSLAQRDTQVlqlqdTITTLTQKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2448 DQAKE---ELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQ--------QLGQLALNLSSIILDVNQDRLT- 2515
Cdd:pfam07888 223 TTAHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQaelhqarlQAAQLTLQLADASLALREGRARw 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2516 -------QRAIEASNaySRIL---QAVQAAEdaagQALQQadhtwATVVRQGL-VDRAQQLLANSTALEEAM--LQEQQr 2582
Cdd:pfam07888 303 aqeretlQQSAEADK--DRIEklsAELQRLE----ERLQE-----ERMEREKLeVELGREKDCNRVQLSESRreLQELK- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 317373598 2583 lglvwAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDE 2624
Cdd:pfam07888 371 -----ASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2736-2901 |
3.07e-09 |
|
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: 58.58 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2736 PMKFNGRSGVQLRTPRDLADlaaYTALKFYLQGPEPEpgqGtedrFVMYMGSrQATGDYMGVSLRDKKVHWVYQLGEaGP 2815
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPN---G----LLLYAGS-QNGGDFLALELEDGRLVLRYDLGS-GS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2816 AVLSIDEDIGE-QFAAVSLDRTLQFGHMSVTVERQMiqetkgDTVAPGAEGLLNLRPDdfvFYVGGYPSTFTPPPLLRFP 2894
Cdd:cd00110 69 LVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPVSP 139
|
....*..
gi 317373598 2895 GYRGCIE 2901
Cdd:cd00110 140 GFVGCIR 146
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
775-827 |
3.44e-09 |
|
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: 55.05 E-value: 3.44e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 775 RCSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGlDQADYFGCR 827
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
3151-3269 |
4.84e-09 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 57.35 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3151 FGFHSAQDSALLYYRASPDG---LcQVSLQQGRVSLQLLR--TEVKTQAG---FADGAPHYVAFYSNATGVWLYVDDQLQ 3222
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGgdyL-ALELRDGRLVLRYDLgsGPARLTSDptpLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 3223 QMKPHRGPPPELQPqpegPPRLLLGGLPESG------TIYNFSGCISNVFVQR 3269
Cdd:smart00282 83 VSGESPGGLTILNL----DGPLYLGGLPEDLklpplpVTPGFRGCIRNLKVNG 131
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
587-629 |
5.45e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHG--FPNC 629
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1969-2019 |
5.81e-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: 5.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 1969 CDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGN 2019
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2354-2689 |
5.87e-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: 62.38 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2354 EQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAA 2433
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2434 RDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMqtfspAGSKLRLVEAAEAHAQQLGQLALNLSSII-LDVNQD 2512
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRI-----AATERRLEDLEEQIEELSEDIESLAAEIEeLEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2513 RLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADhtwatvvrqglvdraqqllanstALEEAMLQEQQrlglvwaALQG 2592
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELR-----------------------ELESKRSELRR-------ELEE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2593 ARTQLRDVRAKKDQLEAHIQAAQAMLA----MDTDETSKKIAHAKAVAAEAQDTATRVQSQLQ--------AMQEnVERW 2660
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaAIEE-YEEL 998
|
330 340 350
....*....|....*....|....*....|.
gi 317373598 2661 QGQYEGLRGQ--DLGQAvldaghsVSTLEKT 2689
Cdd:TIGR02168 999 KERYDFLTAQkeDLTEA-------KETLEEA 1022
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2203-2696 |
6.34e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.54 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRSPLGPRHEtaQQLEVLEQQSTSLGQDARRLGGQAvgtRDQASQLL-------AGTEATLgHA 2275
Cdd:NF041483 50 AKLHEARRSLASRPAYDGADIGYQAE--QLLRNAQIQADQLRADAERELRDA---RAQTQRILqehaehqARLQAEL-HT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2276 KTLLAAIRaVDRTLSElMSQT--GHLglaNASAPSGEQL-LRTLAEVERLLWEMRARdlgaPQAAAEAELAAAQRLLARV 2352
Cdd:NF041483 124 EAVQRRQQ-LDQELAE-RRQTveSHV---NENVAWAEQLrARTESQARRLLDESRAE----AEQALAAARAEAERLAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEENQALATQTRDRlAQHEAGLMdLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRD-NATLQATLH 2431
Cdd:NF041483 195 RQRLGSEAESARAEAEAILRR-ARKDAERL-LNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAaEQRMQEAEE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2432 AARDTLASVFRLlhsLDQAKEELERLAASLDGARTpllQRMQTfspAGSKL-RLV-------EAAEAHAQQLGQLAlnls 2503
Cdd:NF041483 273 ALREARAEAEKV---VAEAKEAAAKQLASAESANE---QRTRT---AKEEIaRLVgeatkeaEALKAEAEQALADA---- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2504 siilDVNQDRLTQRAIEASNAysrilqavQAAEDAAGQaLQQADHTwatvvrqglvdrAQQLLanSTALEEAmlQEQQRl 2583
Cdd:NF041483 340 ----RAEAEKLVAEAAEKART--------VAAEDTAAQ-LAKAART------------AEEVL--TKASEDA--KATTR- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2584 glvwAALQGARTQLRDVRAKKDQL--EAHIQAAQAMLAM--DTDETSKKIahakavaaeaqdtatrVQsqlqaMQENVER 2659
Cdd:NF041483 390 ----AAAEEAERIRREAEAEADRLrgEAADQAEQLKGAAkdDTKEYRAKT----------------VE-----LQEEARR 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 317373598 2660 WQGQYEGLRGQDL-------GQAVLDAGHSVSTLEKTLPQLLAK 2696
Cdd:NF041483 445 LRGEAEQLRAEAVaegerirGEARREAVQQIEEAARTAEELLTK 488
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2349-2616 |
8.08e-09 |
|
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: 62.28 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEqlsslweenqalATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQA 2428
Cdd:COG3096 336 LNLVQT------------ALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2429 TL----------HAARDTLASVFRLLH----SLDQAKEELERLAASLDGARTPLLQRMQtfspagsKLRLveaAEAHAQQ 2494
Cdd:COG3096 404 ALdvqqtraiqyQQAVQALEKARALCGlpdlTPENAEDYLAAFRAKEQQATEEVLELEQ-------KLSV---ADAARRQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2495 LGQ-LALnLSSIILDVNQDRLTQRAIEASNAYsRILQAVQAAEDAAGQAL---QQADHTWATVVRQ--GLVDRAQQLLAN 2568
Cdd:COG3096 474 FEKaYEL-VCKIAGEVERSQAWQTARELLRRY-RSQQALAQRLQQLRAQLaelEQRLRQQQNAERLleEFCQRIGQQLDA 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 317373598 2569 STALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQ--AAQA 2616
Cdd:COG3096 552 AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelAARA 601
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2353-2730 |
8.54e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.78 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL---------QRKQELSRD- 2422
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHgafldadieTAAADQEQLp 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2423 ---------NATLQATLHAARDTLASVFRL--------------LHS-LDQAKEELERLAAS----LDGARTPLLQRMQt 2474
Cdd:pfam12128 351 swqselenlEERLKALTGKHQDVTAKYNRRrskikeqnnrdiagIKDkLAKIREARDRQLAVaeddLQALESELREQLE- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2475 fspaGSKLRLVEAAEAHAQQLGQLALNLSSII--------LDVNQDRL--TQRAIEASNAYSRILQ----AVQAAEDAAG 2540
Cdd:pfam12128 430 ----AGKLEFNEEEYRLKSRLGELKLRLNQATatpelllqLENFDERIerAREEQEAANAEVERLQselrQARKRRDQAS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2541 QALQQAdHTWATVVRQGLVDRAQQLLANSTALEEAMLQE----QQRLGLVWAALQGARTQL------------------- 2597
Cdd:pfam12128 506 EALRQA-SRRLEERQSALDELELQLFPQAGTLLHFLRKEapdwEQSIGKVISPELLHRTDLdpevwdgsvggelnlygvk 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2598 ---------------RDVRAKKDQLEAHIQAAQAMLAmdtdETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQG 2662
Cdd:pfam12128 585 ldlkridvpewaaseEELRERLDKAEEALQSAREKQA----AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2663 QYEGLR---GQDLGQAVLDAGHSVSTLEKTLPQLLAKL---------SILENRGVHNASL-----ALSASIGRVRELIAQ 2725
Cdd:pfam12128 661 EKQSEKdkkNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkeQKREARTEKQAYWqvvegALDAQLALLKAAIAA 740
|
....*
gi 317373598 2726 ARGAA 2730
Cdd:pfam12128 741 RRSGA 745
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2970-3095 |
1.06e-08 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 56.27 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2970 LRLVSYSGVLFFLK-QQSQFLCLAVQEGSLVLLYDFGAGlkkavplqpPPPLTSASKAiqvfLLGGSRKRVLVRVERATV 3048
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3049 ySVEQDND-------------LELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3095
Cdd:pfam02210 68 -TLSVDGQtvvsslppgesllLNLNGPLYLGGLPPLLLLPAL----PVRAGFVGCIRDVR 122
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2227-2655 |
1.33e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.38 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2227 HETAQQLEVLEQQST--------SLGQDARRLGGQAVGTRDQAsqlLAGTEATLGHA-KTLLAAIRAVDRTLSELmsqtg 2297
Cdd:NF041483 414 ADQAEQLKGAAKDDTkeyraktvELQEEARRLRGEAEQLRAEA---VAEGERIRGEArREAVQQIEEAARTAEEL----- 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2298 hlgLANASAPSGEqlLRTLA--EVERLLWEM--RARDLgapqaaaeaeLAAAQRLLARVQEQLSSLWEENQALATQTRdr 2373
Cdd:NF041483 486 ---LTKAKADADE--LRSTAtaESERVRTEAieRATTL----------RRQAEETLERTRAEAERLRAEAEEQAEEVR-- 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2374 lAQHEAGLMDLREALNRAV-----DATREAQELNSRNQERL---EEAL----QRKQELSRDNATLQATLhaaRDTLASVF 2441
Cdd:NF041483 549 -AAAERAARELREETERAIaarqaEAAEELTRLHTEAEERLtaaEEALadarAEAERIRREAAEETERL---RTEAAERI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2442 RLLHSldQAKEELERL--AASLDGARTpllqRMQTFSPAgskLRLVEAAEAHAQQLGQLALNlssiildvNQDRLtqRAi 2519
Cdd:NF041483 625 RTLQA--QAEQEAERLrtEAAADASAA----RAEGENVA---VRLRSEAAAEAERLKSEAQE--------SADRV--RA- 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2520 EASNAYSRI-------LQAVQ--------AAEDAAGQALQQADHTwatvvRQGLVDRAQQLLANS-TALEEAMlQEQQRL 2583
Cdd:NF041483 685 EAAAAAERVgteaaeaLAAAQeeaarrrrEAEETLGSARAEADQE-----RERAREQSEELLASArKRVEEAQ-AEAQRL 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2584 ---------GLVWAALQGARtQLRD-VRAKKDQLEAHIQAAQAMLAMDTDETSKKiahakavaaeAQDTATRVQSQLQAM 2653
Cdd:NF041483 759 veeadrratELVSAAEQTAQ-QVRDsVAGLQEQAEEEIAGLRSAAEHAAERTRTE----------AQEEADRVRSDAYAE 827
|
..
gi 317373598 2654 QE 2655
Cdd:NF041483 828 RE 829
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
776-826 |
2.16e-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: 52.74 E-value: 2.16e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 317373598 776 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGLDQADYFGC 826
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2175-2619 |
2.40e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2175 LDDLERAGALLPAIHEQLRGINASsmawARLHRLNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGQDARRLGGQA 2254
Cdd:COG4913 271 LAELEYLRAALRLWFAQRRLELLE----AELEELRAELARLEAELE-------RLEARLDALREELDELEAQIRGNGGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2255 VgtrDQASQLLAGTEATLghaktllaaiRAVDRTLSELMSQTGHLGLANASapSGEQLLRTLAEVERLLwemraRDLGAP 2334
Cdd:COG4913 340 L---EQLEREIERLEREL----------EERERRRARLEALLAALGLPLPA--SAEEFAALRAEAAALL-----EALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2335 QAAAEAELAAAQRLLARVQEQLSSLWEENQALAT----------QTRDRLAQHeAG-----------LMDLRE------- 2386
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERrksniparllALRDALAEA-LGldeaelpfvgeLIEVRPeeerwrg 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2387 ---------------------ALNRAVDATREAQELNSrnqERLEEALQRKQELSRDNATLQATL----HAARDTLASvf 2441
Cdd:COG4913 479 aiervlggfaltllvppehyaAALRWVNRLHLRGRLVY---ERVRTGLPDPERPRLDPDSLAGKLdfkpHPFRAWLEA-- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2442 RLLHSLDQAK----EELERL--AASLDG------------ARTPLLQRMQT-FSPAgsklRLVEAAEAHAQQLGQLALNL 2502
Cdd:COG4913 554 ELGRRFDYVCvdspEELRRHprAITRAGqvkgngtrhekdDRRRIRSRYVLgFDNR----AKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2503 SSIILDVNQ--DRLTQRAieasNAYSRILQAVQAAEDAAGQALQQADHTwatvvrqglvDRAQQLLANSTALEEAmlqeQ 2580
Cdd:COG4913 630 EERLEALEAelDALQERR----EALQRLAEYSWDEIDVASAEREIAELE----------AELERLDASSDDLAAL----E 691
|
490 500 510
....*....|....*....|....*....|....*....
gi 317373598 2581 QRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2619
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2377-2703 |
2.48e-08 |
|
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: 60.46 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2377 HEAG--LMDLREALNRAVDATREaqeLNsRNQERLE---EALQRKQELSRDNATLQATLHAARdtlasvfrllhsLDQAK 2451
Cdd:TIGR02168 175 KETErkLERTRENLDRLEDILNE---LE-RQLKSLErqaEKAERYKELKAELRELELALLVLR------------LEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2452 EELERLAASLDGAR------TPLLQRMQTfSPAGSKLRLVEAAEAHAQQLGQLaLNLSSIIldvnqDRLTQRAIEASNAY 2525
Cdd:TIGR02168 239 EELEELQEELKEAEeeleelTAELQELEE-KLEELRLEVSELEEEIEELQKEL-YALANEI-----SRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2526 SRILQAVQAAEDAAGQALQQADHTWATVVRqgLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKD 2605
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAE--LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2606 QLEAHIQAAQAMLamdtdetskkiahakavaaeaqdtaTRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVST 2685
Cdd:TIGR02168 390 QLELQIASLNNEI-------------------------ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330
....*....|....*...
gi 317373598 2686 LEKTLPQLLAKLSILENR 2703
Cdd:TIGR02168 445 LEEELEELQEELERLEEA 462
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2347-2659 |
2.69e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQEQLSSLWEENQALatqtRDRLA-------------QHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL 2413
Cdd:PRK04863 314 RELAELNEAESDLEQDYQAA----SDHLNlvqtalrqqekieRYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2414 QRKQELSRDNATLQATL----------HAARDTLASVFRLLH----SLDQAKEELERLAASLDGARTPLLQrmqtfspAG 2479
Cdd:PRK04863 390 EEVDELKSQLADYQQALdvqqtraiqyQQAVQALERAKQLCGlpdlTADNAEDWLEEFQAKEQEATEELLS-------LE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2480 SKLRLveaAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYS--RILQAVQAAEDAAGQALQQADHTWATVVRqg 2557
Cdd:PRK04863 463 QKLSV---AQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLReqRHLAEQLQQLRMRLSELEQRLRQQQRAER-- 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2558 LVDRAQQLLANSTALEEAMLQEQQRLGlvwAALQGARTQLRDV-------RAKKDQLEAHIQ----------AAQAMLAM 2620
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELE---ARLESLSESVSEArerrmalRQQLEQLQARIQrlaarapawlAAQDALAR 614
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 317373598 2621 ------DTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVER 2659
Cdd:PRK04863 615 lreqsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
776-817 |
3.57e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.57e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 317373598 776 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFG 817
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1913-1966 |
3.73e-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: 51.97 E-value: 3.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 317373598 1913 CPCPLSVPSNnfaEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVLGSSC 1966
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2349-2619 |
3.90e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEQLSSLWEENQALATQ---TRDRLAQHEAGLMDLREALNRAVDATREAQ-ELNSRNQErLEEALQRKQELSRDNA 2424
Cdd:COG4372 47 LEQLREELEQAREELEQLEEEleqARSELEQLEEELEELNEQLQAAQAELAQAQeELESLQEE-AEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2425 TLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSS 2504
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2505 IILDVNQDRLTQRAIEA----SNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQ 2580
Cdd:COG4372 206 EKLIESLPRELAEELLEakdsLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
250 260 270
....*....|....*....|....*....|....*....
gi 317373598 2581 QRLGlvwaaLQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2619
Cdd:COG4372 286 EALE-----EAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2153-2602 |
7.31e-08 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 58.67 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2153 VPGGPVGHSIHCEVCDHCVVLLLDDLERAGALLPAIHEQLRGINASSMAWARLH---RLNASIAdLQSQLRSPLGPRHET 2229
Cdd:COG2203 253 LGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLvdgRLIGVLA-LYSKEPRAFTEEDLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2230 -----AQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANA 2304
Cdd:COG2203 332 llealADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAAD 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2305 SAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDL 2384
Cdd:COG2203 412 LSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2385 REALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGA 2464
Cdd:COG2203 492 LLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2465 RTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQ 2544
Cdd:COG2203 572 LSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALA 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 317373598 2545 QADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRA 2602
Cdd:COG2203 652 SLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSV 709
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1863-1899 |
7.90e-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: 51.20 E-value: 7.90e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 317373598 1863 PCQCHGH---SDRCLPGSGVCVdCQHNTEGAHCERCQAGF 1899
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| DAHL |
pfam19443 |
DAHL domain; The DAHL (Double All-Helical Ligand-binding) domain is a novel periplasmic ... |
2347-2548 |
9.40e-08 |
|
DAHL domain; The DAHL (Double All-Helical Ligand-binding) domain is a novel periplasmic sensory domain, which is found in major types of bacterial signal transduction proteins: histidine kinases and diguanylate cyclases/phosphodiesterases, and, occasionally in chemoreceptors. The majority of the DAHL domain-containing proteins were found in alpha-, beta-, gamma- and epsilonproteobacteria. It is also present in some cyanobacterial species. Secondary structure prediction suggested that DAHL consists predominantly of alpha-helical regions. The DAHL domain was identified in the Tlp10 chemoreceptor from the human pathogen Campylobacter jejuni and in the VirA sensor histidine kinase from a plant pathogen Agrobacterium tumefaciens. This domain recognizes Asp, Ile, purine, fumarate, malate, alpha-ketoglutarate, mannose, rhamnose, fucose, sialic acid, Arg, thiamine and galactose (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 466085 [Multi-domain] Cd Length: 222 Bit Score: 55.52 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQeQLSSLWEENqALATQTR-----DRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELS- 2420
Cdd:pfam19443 11 SALRQLK-QLDAELNRD-VLKARAGllrnyDPLVAALAELRRLLERLELPSFLLAGDSAELDAALAALRAALQEKEELVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2421 ---RDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAAS-LDGARTP---------LLQRMQTFSPAGSKLR-LVE 2486
Cdd:pfam19443 89 rfkSQNALLRNSLAYFPTLVDELLAASPAEPALAAALNELLRAvLLYNLSSdpalaeieaLLERLEALAESAPALRaALQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 317373598 2487 AAEAHAQQLgqlaLNLSSIIldvnqDRLTQRAIEASNAYSriLQAVQAA-EDAAGQALQQADH 2548
Cdd:pfam19443 169 LLLAHARLI----LRLLPQV-----DALLQEILALPTAAA--LEALEAAyLAAYQQALARAER 220
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2783-2901 |
9.83e-08 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 53.19 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2783 MYMGSRQatGDYMGVSLRDKKVHWVYQLGEAGPAVLSIDEDI--GeQFAAVSLDRTLQFGHMSVTverqmiQETKGDTVA 2860
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGNTLTLSVD------GQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 317373598 2861 PGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIE 2901
Cdd:pfam02210 82 PGESLLLNL---NGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1864-1913 |
1.05e-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: 50.81 E-value: 1.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 1864 CQCHGH---SDRCLPGSGVCvDCQHNTEGAHCERCQAGFVssrDDPSAPCVSC 1913
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYY---GLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1913-1959 |
1.30e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.30e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 317373598 1913 CPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNP 1959
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2203-2735 |
1.36e-07 |
|
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: 58.06 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLG---------------QDARR--LGGQAVGTRDQ----- 2260
Cdd:TIGR00618 358 RDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkeldilqreqatidtRTSAFrdLQGQLAHAKKQqelqq 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2261 --ASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTG-----HLGLANASAPSGEQLLRtLAEVERLLwEMRARDLGA 2333
Cdd:TIGR00618 438 ryAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeqiHLQETRKKAVVLARLLE-LQEEPCPL-CGSCIHPNP 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2334 PQAAAEAELAAAQRLLARVQE-------------QLSSLWEENQALATQTRdRLAQHEAGLMDLREALNRAVDATR-EAQ 2399
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTyaqletseedvyhQLTSERKQRASLKEQMQ-EIQQSFSILTQCDNRSKEDIPNLQnITV 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2400 ELNSRNQERLEEALQRKQELSRDNATLQATLHAardtlasvFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAG 2479
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL--------QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2480 SK---LRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEAS-NAYSRILQAVQAAEDAAGQALQQADHTWATVVR 2555
Cdd:TIGR00618 667 IRvlpKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHiEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2556 QGlvdRAQQllanSTALEEAMLQEQQRLGLVWAALQgARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAV 2635
Cdd:TIGR00618 747 EL---MHQA----RTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2636 AAEAQDT-ATRVQSQLQAMQEN------VERWQGQYEGLRGQ---------DLGQAVLDAGH----SVSTLEKTLPQLLA 2695
Cdd:TIGR00618 819 LNLQCETlVQEEEQFLSRLEEKsatlgeITHQLLKYEECSKQlaqltqeqaKIIQLSDKLNGinqiKIQFDGDALIKFLH 898
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 317373598 2696 KLSILENrgVHNASLALSASIGRVRELIAQARGAASKVKV 2735
Cdd:TIGR00618 899 EITLYAN--VRLANQSEGRFHGRYADSHVNARKYQGLALL 936
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2234-2730 |
1.38e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 57.95 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2234 EVLEQQ-STSLGQDARRLGGQ--AVGTRDQASQLL--AGTEATLGHAktLLAAIRAVDRTLSELMSQTG-------HLGL 2301
Cdd:COG3899 674 RALEARgPEPLEERLFELAHHlnRAGERDRAARLLlrAARRALARGA--YAEALRYLERALELLPPDPEeeyrlalLLEL 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2302 ANASAPSG-----EQLLRTLAEvERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSsLWEENQALATQTRDRLAQ 2376
Cdd:COG3899 752 AEALYLAGrfeeaEALLERALA-ARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYE-FGELALALAERLGDRRLE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2377 HEAGLM---------DLREALNRAVDATREAQELNSRnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSL 2447
Cdd:COG3899 830 ARALFNlgfilhwlgPLREALELLREALEAGLETGDA---ALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAA 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2448 DQAKEELERLAASLDGARTPLLQRMQtfspagskLRLVEAAEAHAQQLGQLALN-----------LSSIILDVNQDRLTQ 2516
Cdd:COG3899 907 AAAAAALAAAELARLAAAAAAAAALA--------LAAAAAAAAAAALAAAAAAAalaaalalaaaAAAAAAAALAAAAAA 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2517 RAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQ 2596
Cdd:COG3899 979 AAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAA 1058
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2597 LRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAV 2676
Cdd:COG3899 1059 AAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLL 1138
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2677 LDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAA 2730
Cdd:COG3899 1139 AAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAA 1192
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
828-867 |
1.84e-07 |
|
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: 50.05 E-value: 1.84e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 317373598 828 SCRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 867
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2203-2438 |
1.87e-07 |
|
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: 56.31 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQL---LAGTEATLGHAKTLL 2279
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2280 AA-IRAVDRtlselMSQTGHLGLAnASAPSGEQLLRTLAEVERLLWEMRARdlgapqaaaeaelaaaQRLLARVQEQLss 2358
Cdd:COG4942 107 AElLRALYR-----LGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARREQ----------------AEELRADLAEL-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2359 lwEENQALATQTRDRLAQHEAGLMDLREALNRAVDatrEAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLA 2438
Cdd:COG4942 163 --AALRAELEAERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
429-473 |
2.78e-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: 49.66 E-value: 2.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 429 CNC-ESDFTDGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPSCYP 473
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
428-470 |
3.12e-07 |
|
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: 49.27 E-value: 3.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 317373598 428 RCNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPS 470
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-347 |
3.21e-07 |
|
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: 49.27 E-value: 3.21e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 317373598 299 RCVCHGHADACDAKDPTDpfrLQCTCQHNTCGGTCDRCCPGFNQQPWKP 347
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2175-2543 |
4.03e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2175 LDDLERAGALLPAIHEQLRGINASSMAWAR----LHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRL 2250
Cdd:PRK04863 316 LAELNEAESDLEQDYQAASDHLNLVQTALRqqekIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2251 GGQ--------------------AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGH-LGLANASAPSG 2309
Cdd:PRK04863 396 KSQladyqqaldvqqtraiqyqqAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQkLSVAQAAHSQF 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2310 E---QLLRTLA-EVERL-LWEMrARDlgapqaaaeaelaaaqrLLARvqeqlsslWEENQALAtqtrDRLAQHEAGLMDL 2384
Cdd:PRK04863 476 EqayQLVRKIAgEVSRSeAWDV-ARE-----------------LLRR--------LREQRHLA----EQLQQLRMRLSEL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2385 REALNRAVDATREAQELNSRNQERLE-----EALQRKQELSRDNATLQ-ATLHAARDTLAsvfrllHSLDQAKEELERLA 2458
Cdd:PRK04863 526 EQRLRQQQRAERLLAEFCKRLGKNLDdedelEQLQEELEARLESLSESvSEARERRMALR------QQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2459 asldgARTPllqRMQTFSPAGSKLR-----LVEAAEAHAQQLGQLALNLSSiiLDVNQDRLTQRaIEASNAYSRILQAVQ 2533
Cdd:PRK04863 600 -----ARAP---AWLAAQDALARLReqsgeEFEDSQDVTEYMQQLLERERE--LTVERDELAAR-KQALDEEIERLSQPG 668
|
410
....*....|
gi 317373598 2534 AAEDAAGQAL 2543
Cdd:PRK04863 669 GSEDPRLNAL 678
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-673 |
4.89e-07 |
|
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: 48.89 E-value: 4.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 317373598 631 ACTCDPRGALDQLCGAG-GLCRCRPGYTGTACQECSPGFHGFPS 673
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2347-2711 |
7.18e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 54.69 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQEQLSSLWEENQALATQ----------TRDRLAQHEAGLMDLREALN--RAVDATREAQelnSRNQER-LEEAL 2413
Cdd:pfam19220 55 ALLAQERAAYGKLRRELAGLTRRlsaaegeleeLVARLAKLEAALREAEAAKEelRIELRDKTAQ---AEALERqLAAET 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2414 QRKQELSRDNATLQATLHAARDTLAsvfRLLHSLDQAKEELERLAAslDGARtplLQ-RMQTFSPAGSKL--RLVE---A 2487
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQ---RAEGELATARERLALLEQ--ENRR---LQaLSEEQAAELAELtrRLAEletQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2488 AEAHAQQLGQLALNLssiildVNQDRLTQRAieasnaysrilqavQAAEDAAGQALQqadhtwatvvrqglVDRAQQLLA 2567
Cdd:pfam19220 204 LDATRARLRALEGQL------AAEQAERERA--------------EAQLEEAVEAHR--------------AERASLRMK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2568 NSTALEEAMLQEQqrlglvwaALQGARTQLRDvrakkdqLEAHIQAAQAMLAmdtdETSKkiahakavaaeAQDTATRVQ 2647
Cdd:pfam19220 250 LEALTARAAATEQ--------LLAEARNQLRD-------RDEAIRAAERRLK----EASI-----------ERDTLERRL 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2648 SQLQAMQENVERwqgqyeglRGQDLGQAVLDAGHSVSTLEKTLPqllAKLSILENRGVHNASLA 2711
Cdd:pfam19220 300 AGLEADLERRTQ--------QFQEMQRARAELEERAEMLTKALA---AKDAALERAEERIASLS 352
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2289-2612 |
7.27e-07 |
|
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: 55.73 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2289 LSELMSQtgHLGLANASAPsgEQLLRTLA----EVERllwemrardlgapqaaaeaELAAAQRLLARVQEQLSSLWEENQ 2364
Cdd:COG3096 818 FSQFVGG--HLAVAFAPDP--EAELAALRqrrsELER-------------------ELAQHRAQEQQLRQQLDQLKEQLQ 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2365 ALatqtrDRLAQH-----EAGLMDLREALNRAVDATREAQELNSRNQERLEealqrkqELSRDNATLQATlHAARDTLAs 2439
Cdd:COG3096 875 LL-----NKLLPQanllaDETLADRLEELREELDAAQEAQAFIQQHGKALA-------QLEPLVAVLQSD-PEQFEQLQ- 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2440 vfrllHSLDQAKEELERLAASLDgARTPLLQRMQTFSPAGSKLRLVEAAEahaqqlgqlaLNlssiildvnqDRLTQRai 2519
Cdd:COG3096 941 -----ADYLQAKEQQRRLKQQIF-ALSEVVQRRPHFSYEDAVGLLGENSD----------LN----------EKLRAR-- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2520 easnaysriLQAVQAAEDAAGQALQQAD--HTWATVVRQGLV---DRAQQLLAnstaleeAMLQEQQRLGLVWA--ALQG 2592
Cdd:COG3096 993 ---------LEQAEEARREAREQLRQAQaqYSQYNQVLASLKssrDAKQQTLQ-------ELEQELEELGVQADaeAEER 1056
|
330 340
....*....|....*....|....*..
gi 317373598 2593 ART-------QLRDVRAKKDQLEAHIQ 2612
Cdd:COG3096 1057 ARIrrdelheELSQNRSRRSQLEKQLT 1083
|
|
| TorS_sensor_domain |
cd16172 |
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide ... |
2287-2578 |
7.47e-07 |
|
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide (TMAO) reductase (Tor) pathway, which consists TorT, a periplasmic binding protein that binds TMAO; TorS, a sensor histidine kinase that forms a complex with TorT, and TorR, the response regulator. The Tor pathway is involved in regulating a cellular response to trimethylamine-N-oxide (TMAO), a terminal electron receptor in anaerobic respiration. TorS consists of a periplasmic sensor domain, as well as a HAMP domain, a histidine kinase domain, and a receiver domain.
Pssm-ID: 293930 [Multi-domain] Cd Length: 261 Bit Score: 53.74 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2287 RTLSELMSQTGHLG--LANAsapsgeqllRTLAEverllWEMRARDLGapqaaaeaelaaaqRLLARVQEQLSSLweENQ 2364
Cdd:cd16172 2 RQLSELSSRIIASAqlLANA---------DSEAE-----RQQQGRQLT--------------AQLEALLRLLKAL--GQD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2365 ALATQTRDRLAQHEAGLMDLREALNRAVdatREAQELNSRNQERLEEALQRKQE---LSR---DNATLQATlhaARdtLA 2438
Cdd:cd16172 52 SFDSFLLSRLEQTVQEIIDNLAQLGELV---GQRLQLRQQFQQLFERLRAAAGElaqLARtqvANASTIAV---AN--VS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2439 SVFRLL--HSLDQAKEELERLAA-SLDgartpLLQRMqtfspagSKLRLveaaeaHAQQLGQLALNLSSIildVNQDRLt 2515
Cdd:cd16172 124 GLYDLIeqNDKEAAYQALDRLIEvDLD-----LLERM-------HELRL------LALQLGNLINELRTA---SDIARL- 181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2516 QRAIEASNAYSRILQA-VQAAED-----AAGQALQQADHtwatvvRQGLVDRAQQLLANSTALEEAMLQ 2578
Cdd:cd16172 182 AELRQQFNANLAILQRrVQAVEDpgrraQMAQLLSDLEQ------GQGLFALRRQLLALEQRLQALMQN 244
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
429-471 |
9.24e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 9.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 429 CNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTG--FPSC 471
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
829-867 |
9.33e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 9.33e-07
10 20 30
....*....|....*....|....*....|....*....
gi 317373598 829 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 867
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2782-2906 |
9.47e-07 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 50.78 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2782 VMYMGSrQATGDYMGVSLRDKKVHWVYQLGeAGPAVLSIDEDIGE-QFAAVSLDRTLQFGHMSVT-VERQMIQETKGDTV 2859
Cdd:pfam00054 10 LLYNGT-QTERDFLALELRDGRLEVSYDLG-SGAAVVRSGDKLNDgKWHSVELERNGRSGTLSVDgEARPTGESPLGATT 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 317373598 2860 APGAEGLLnlrpddfvfYVGGYPSTFTPPPLLRF-PGYRGCIEMDTLN 2906
Cdd:pfam00054 88 DLDVDGPL---------YVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2232-2471 |
9.75e-07 |
|
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: 53.07 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2232 QLEVLEQQSTSLGQDArrlggQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLG----------L 2301
Cdd:pfam12795 1 KLDELEKAKLDEAAKK-----KLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQakaeaapkeiL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2302 ANASAPSGEQLL-----------RTLAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARVQEQLSslweENQALATQT 2370
Cdd:pfam12795 76 ASLSLEELEQRLlqtsaqlqelqNQLAQLNSQLIELQTR-------------------PERAQQQLS----EARQRLQQI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2371 RDRLAQHEAGLMDLREALNRAVDAtrEAQELNSRNQErLEEALQ---RKQELS---RDNATLQ-ATLHAARDTLASV--F 2441
Cdd:pfam12795 133 RNRLNGPAPPGEPLSEAQRWALQA--ELAALKAQIDM-LEQELLsnnNRQDLLkarRDLLTLRiQRLEQQLQALQELlnE 209
|
250 260 270
....*....|....*....|....*....|
gi 317373598 2442 RLLHSLDQAKEELERLAASLDGArTPLLQR 2471
Cdd:pfam12795 210 KRLQEAEQAVAQTEQLAEEAAGD-HPLVQQ 238
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1912-1967 |
1.24e-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: 1.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 1912 SCPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVlGSSCQ 1967
Cdd:cd00055 1 PCDCN---GHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2362-2621 |
2.17e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 53.54 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2362 ENQAL---ATQTR--DRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEA-LQRKQ--ELsrDNATLQA----T 2429
Cdd:COG0497 133 EHQSLldpDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELdLLRFQleEL--EAAALQPgeeeE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2430 LHAARDTLASVFRLLHSLDQAkeeLERLAASLDGArTPLLQRMqtfspagskLRLVEAAEAHAQQLGQLALNLSSIILDV 2509
Cdd:COG0497 211 LEEERRRLSNAEKLREALQEA---LEALSGGEGGA-LDLLGQA---------LRALERLAEYDPSLAELAERLESALIEL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2510 NqdrltqraiEASNAYSRILQAVQAaeDAagQALQQAD---HTWATVVR------QGLVDRAQQL---LANSTALEEAML 2577
Cdd:COG0497 278 E---------EAASELRRYLDSLEF--DP--ERLEEVEerlALLRRLARkygvtvEELLAYAEELraeLAELENSDERLE 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 317373598 2578 QEQQRLGLVWAALQGARTQLRDVRAKK-DQLEAHIQAAQAMLAMD 2621
Cdd:COG0497 345 ELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTAELADLGMP 389
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1969-2013 |
2.56e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 2.56e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 1969 CDCSGNGDpnlLFSDCDPLTGACRgCLRHTTGPRCEICAPGFYGN 2013
Cdd:smart00180 1 CDCDPGGS---ASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2348-2656 |
2.94e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2348 LLARVQEQLSSLWEENQALATQTRDRLAQHEaglmDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQ 2427
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELE----QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2428 ATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSIIL 2507
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA------EREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2508 DVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVW 2587
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2588 AALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQEN 2656
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2383-2758 |
3.32e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2383 DLREALNRAVDATRE---AQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASV---FRLLHSLDQAKEELER 2456
Cdd:PRK04863 280 ERRVHLEEALELRRElytSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVqtaLRQQEKIERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2457 LAASLDGartpllqrmQTFSPAGSKLRlVEAAEAHAQQLGQLALNLSSIILDVNQ--DRLTQRAIeasnAYSrilQAVQA 2534
Cdd:PRK04863 360 LEERLEE---------QNEVVEEADEQ-QEENEARAEAAEEEVDELKSQLADYQQalDVQQTRAI----QYQ---QAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2535 AEDAAGQaLQQADHTWAtvvrqGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALqgartqlrdvrakkdqlEAHIQAA 2614
Cdd:PRK04863 423 LERAKQL-CGLPDLTAD-----NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH-----------------SQFEQAY 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2615 QAMLAMdTDETSkkiahakavaaeaqdtatRVQSQLQAMQenVERwqgQYEGLRGQDlgqavldaghsvstleKTLPQLL 2694
Cdd:PRK04863 480 QLVRKI-AGEVS------------------RSEAWDVARE--LLR---RLREQRHLA----------------EQLQQLR 519
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2695 AKLSILENRgvhnasLALSAsigRVRELIAQargaaskvkvpmkFNGRSGVQLRTPRDLADLAA 2758
Cdd:PRK04863 520 MRLSELEQR------LRQQQ---RAERLLAE-------------FCKRLGKNLDDEDELEQLQE 561
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2412-2703 |
3.60e-06 |
|
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: 53.14 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2412 ALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPL-LQRMQtfspagsKLRLVEAAEA 2490
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsALRKD-------LARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2491 HAQQLGQLALNLSSiiLDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADhtwatVVRQGLVDRAQQLlansT 2570
Cdd:TIGR02168 745 LEERIAQLSKELTE--LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-----ALREALDELRAEL----T 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2571 ALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAmDTDETSKKIahakavaaeaQDTATRVQSQL 2650
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEEL----------ESELEALLNER 882
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 317373598 2651 QAMQENVERWQGQYEGLRGQ--DLGQAVLDAGHSVSTLEKTLPQLLAKLSILENR 2703
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEElrELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2203-2462 |
4.44e-06 |
|
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: 53.14 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRsplgpRHETAQQLevLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTL---- 2278
Cdd:TIGR02168 719 KELEELSRQISALRKDLA-----RLEAEVEQ--LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqi 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2279 ---LAAIRAVDRTLSELMSQTGHLGLANASAPSG-EQLLRTLAEVERLLWEM--RARDLGAPQAAAEAELAAAQRLLARV 2352
Cdd:TIGR02168 792 eqlKEELKALREALDELRAELTLLNEEAANLRERlESLERRIAATERRLEDLeeQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEE----NQALATQtRDRLAQHEAglmDLREALNRAVDATREAQELNSRN---QERLEEALQRKQEL-SRDNA 2424
Cdd:TIGR02168 872 ESELEALLNEraslEEALALL-RSELEELSE---ELRELESKRSELRRELEELREKLaqlELRLEGLEVRIDNLqERLSE 947
|
250 260 270
....*....|....*....|....*....|....*...
gi 317373598 2425 TLQATLHAArdtLASVFRLLHSLDQAKEELERLAASLD 2462
Cdd:TIGR02168 948 EYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2174-2619 |
4.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2174 LLDDLERAGALLPAIHEQLRGINASSMA--WARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLG 2251
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2252 GQAVGTRDQASQLLAGTEATLGHAKT----LLAAIRAVDRTLSELMSQTG---------------HLGLANASAP----- 2307
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAalrdLRRELRELEAEIASLERRKSniparllalrdalaeALGLDEAELPfvgel 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2308 ------------SGEQLLRTLA---------------EVERLLWEMRAR--DLGAPQAAAEAELAAAQRLLARVQeqlss 2358
Cdd:COG4913 467 ievrpeeerwrgAIERVLGGFAltllvppehyaaalrWVNRLHLRGRLVyeRVRTGLPDPERPRLDPDSLAGKLD----- 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2359 lWEENQAlatqtRDRLAQHEAGLMDLR-----EALNRAVDA-TREAQ--------ELNSR------------NQERLEEA 2412
Cdd:COG4913 542 -FKPHPF-----RAWLEAELGRRFDYVcvdspEELRRHPRAiTRAGQvkgngtrhEKDDRrrirsryvlgfdNRAKLAAL 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2413 LQRKQElsrdnatLQATLHAARDTLAsvfrllhsldQAKEELERLAASLDgartpLLQRMQTFSPAGSKLRLVEAAEAHA 2492
Cdd:COG4913 616 EAELAE-------LEEELAEAEERLE----------ALEAELDALQERRE-----ALQRLAEYSWDEIDVASAEREIAEL 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2493 QQlgQLA-LNLSSIILDVNQDRLTQRAIEasnaysriLQAVQAAEDAAGQALQQADHTWATVVRQglVDRAQQLLANstA 2571
Cdd:COG4913 674 EA--ELErLDASSDDLAALEEQLEELEAE--------LEELEEELDELKGEIGRLEKELEQAEEE--LDELQDRLEA--A 739
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 317373598 2572 LEEAMLQEQQRLGLVWAALQGARtQLRDVRAkkdQLEAHIQAAQAMLA 2619
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDA-VERELRE---NLEERIDALRARLN 783
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
632-674 |
4.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 4.66e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 317373598 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHG--FPSC 674
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2371-2610 |
6.25e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2371 RDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLeEALQRKQELS---RDNATLQATLHAARDTLAsvfrllhSL 2447
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSwdeIDVASAEREIAELEAELE-------RL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2448 DQAKEELERLAASLDGARtpllQRMQtfspagsklRLVEAAEAHAQQLGQLALNLSSI--ILDVNQDRLTQRAIEASNAY 2525
Cdd:COG4913 681 DASSDDLAALEEQLEELE----AELE---------ELEEELDELKGEIGRLEKELEQAeeELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2526 SRILQAV--QAAEDAAGQALQQadhtWATVVRQGLVDRAQQLlanSTALEEAMLQEQQRlglvW-AALQGARTQL---RD 2599
Cdd:COG4913 748 RALLEERfaAALGDAVERELRE----NLEERIDALRARLNRA---EEELERAMRAFNRE----WpAETADLDADLeslPE 816
|
250
....*....|.
gi 317373598 2600 VRAKKDQLEAH 2610
Cdd:COG4913 817 YLALLDRLEED 827
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2211-2505 |
6.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2211 SIADLQSQLRSPLGPRHETAQQLevleqqstsLgqdARRLGGQAVGT-----RDQ---ASQLLAGTEATLGHAKTLLAAI 2282
Cdd:COG4913 174 SFSAYLARLRRRLGIGSEKALRL---------L---HKTQSFKPIGDlddfvREYmleEPDTFEAADALVEHFDDLERAH 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2283 RAVDRTLSelmsQTGHLGLANASAPSGEQLLRTLAEVERL-----LWEMRARDlgapqaaaeaelaaaqRLLARVQEQLS 2357
Cdd:COG4913 242 EALEDARE----QIELLEPIRELAERYAAARERLAELEYLraalrLWFAQRRL----------------ELLEAELEELR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2358 SLWEENQALATQTRDRLAQHEAGLMDLREALNRAvdATREAQELNSRnQERLEEALQRKQELSRDNATLQATLHAARDTL 2437
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLERE-IERLERELEERERRRARLEALLAALGLPLPAS 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2438 ASVF-RLLHSLDQAKEELERLAASLDGARTPLLQRmqtfspagsKLRLVEAAEAHAQQLGQLALNLSSI 2505
Cdd:COG4913 379 AEEFaALRAEAAALLEALEEELEALEEALAEAEAA---------LRDLRRELRELEAEIASLERRKSNI 438
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1844-1913 |
7.63e-06 |
|
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: 48.84 E-value: 7.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 1844 ECAPGFYRDVKGlflGRCVPCQchghsdRCLPGSGVCVDCQHNTEgAHCERCQAGFVSSRDDPSAPCVSC 1913
Cdd:cd13416 79 ECAYGYYLDEDS---GTCEPCT------VCPPGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDPCLPC 138
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2406-2619 |
8.62e-06 |
|
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: 51.30 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2406 QERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTfspagSKLRLV 2485
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-----LEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2486 EAAEAHAQQLGQLALNLSSIILDVNQDRLT--------QRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVV--R 2555
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2556 QGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2619
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2401-2730 |
1.31e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2401 LNSRNQER---LEEA------LQRKQE-LSRdnatlqatlhaardtlasvfrllhsLDQAKEELERL---AASLDGARTP 2467
Cdd:COG1196 150 IEAKPEERraiIEEAagiskyKERKEEaERK-------------------------LEATEENLERLediLGELERQLEP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2468 L------LQRMQTFSpagSKLRLVEAA------EAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRI-LQAVQA 2534
Cdd:COG1196 205 LerqaekAERYRELK---EELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeLEELEL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2535 AEDAAGQALQQADHTWATVVRQG--LVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQ 2612
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2613 AAQAMLAMDT---DETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVSTLEKT 2689
Cdd:COG1196 362 EAEEALLEAEaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 317373598 2690 LPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAA 2730
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3153-3267 |
1.43e-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: 47.03 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3153 FHSAQDSALLYYRAS--PDGLCqVSLQQGRVSLQL-----LRTEVKTQAGFADGAPHYVAF-YSNATGVwLYVDDQlqqm 3224
Cdd:pfam02210 1 FRTRQPNGLLLYAGGggSDFLA-LELVNGRLVLRYdlgsgPESLLSSGKNLNDGQWHSVRVeRNGNTLT-LSVDGQ---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 317373598 3225 KPHRGPPPELQPQPEGPPRLLLGGLPESGTIY------NFSGCISNVFV 3267
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPalpvraGFVGCIRDVRV 123
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2349-2546 |
1.62e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEQLSSLWEE--------NQALA--TQTRDRLAQHEAGLMDLREALNRAVDA----TREAQE-------------- 2400
Cdd:COG3883 32 LEAAQAELDALQAEleelneeyNELQAelEALQAEIDKLQAEIAEAEAEIEERREElgerARALYRsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2401 ---------------LNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGAR 2465
Cdd:COG3883 112 esfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2466 TPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQ 2545
Cdd:COG3883 192 AAAEAQLA------ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
.
gi 317373598 2546 A 2546
Cdd:COG3883 266 G 266
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2208-2434 |
1.63e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2208 LNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGqdarrLGGQAvgtrDQASQLLAGTEATLGHAKTLLAAIRAVDR 2287
Cdd:COG3206 180 LEEQLPELRKELE-------EAEAALEEFRQKNGLVD-----LSEEA----KLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2288 TLSELMSQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRAR------DLgapqaaaeaelaaaQRLLARVQEQLSSLWE 2361
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpDV--------------IALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2362 ENQALATQTRDRLAQHEAGLMDLREALNRavdATREAQELNSRNQERLEeaLQRKQELSRDN-ATLQATLHAAR 2434
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQ---LEARLAELPELEAELRR--LEREVEVARELyESLLQRLEEAR 378
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2435-2695 |
2.05e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 48.52 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2435 DTLASVFR-LLHSLDQAKEELERLaasLDGArtplLQRMQtfspagskLRLVEAAEAHAQQLGQLALNlssiildvnQDR 2513
Cdd:pfam04012 3 KRLGRLVRaNIHEGLDKAEDPEKM---LEQA----IRDMQ--------SELVKARQALAQTIARQKQL---------ERR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2514 LTQRAIEASNAYSRILQAV-QAAEDAAGQALQQAdhtwatvvrqglvdraqQLLANSTALEEAMLQEQQRLGL-VWAALQ 2591
Cdd:pfam04012 59 LEQQTEQAKKLEEKAQAALtKGNEELAREALAEK-----------------KSLEKQAEALETQLAQQRSAVEqLRKQLA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2592 GARTQLRDVRAKKDQLEAHIQAAQAMLAMDTdeTSKKIahakavaaeaqDTATRVqSQLQAMQENVERWQGQ---YEGLR 2668
Cdd:pfam04012 122 ALETKIQQLKAKKNLLKARLKAAKAQEAVQT--SLGSL-----------STSSAT-DSFERIEEKIEEREARadaAAELA 187
|
250 260
....*....|....*....|....*...
gi 317373598 2669 G-QDLGQAVLDAGHSVSTLEKTLPQLLA 2695
Cdd:pfam04012 188 SaVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2375-2685 |
2.14e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2375 AQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLAsvfRLLHSLDQAKEEL 2454
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2455 ERLAASL--DGARTPLLQRM---QTFSPAGSKLRLVEAAEAHAQQlgqlalnlssIILDVNQDRltQRAIEASNAYSRIL 2529
Cdd:COG3883 89 GERARALyrSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADAD----------LLEELKADK--AELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2530 QAVQAAEDAAGQALQQAdhtwatvvrQGLVDRAQQLLANSTAlEEAMLQEQ-QRLGLVWAALQGARTQLRDvrAKKDQLE 2608
Cdd:COG3883 157 AELEALKAELEAAKAEL---------EAQQAEQEALLAQLSA-EEAAAEAQlAELEAELAAAEAAAAAAAA--AAAAAAA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317373598 2609 AHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVST 2685
Cdd:COG3883 225 AAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASG 301
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2230-2442 |
2.78e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2230 AQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAI--RAVDRTLSELMSQtghlgLANASAP 2307
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAE-----LERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2308 SGEqllrtLAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARVQEQLSSLWEEnqalATQTRDRLAQHEAGLMDLREA 2387
Cdd:COG4913 684 SDD-----LAALEEQLEELEAE-------------------LEELEEELDELKGE----IGRLEKELEQAEEELDELQDR 735
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2388 LNRAVDATREAQ--ELNSRNQERLEEALQRK--QELSRDNATLQATLHAARDTLASVFR 2442
Cdd:COG4913 736 LEAAEDLARLELraLLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELERAMR 794
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1864-1899 |
2.84e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.84e-05
10 20 30
....*....|....*....|....*....|....*....
gi 317373598 1864 CQCHG---HSDRCLPGSGVCvDCQHNTEGAHCERCQAGF 1899
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQC-ECKPNVTGRRCDRCAPGY 38
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
2349-2456 |
2.86e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 47.59 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEQLSSLWEENQALATQTR-----------------DRLAQHEAGLMDLREALNRAVDATREA-QELNSRNQE--R 2408
Cdd:pfam15619 20 LAELQSKLEELRKENRLLKRLQKrqekalgkyegteselpQLIARHNEEVRVLRERLRRLQEKERDLeRKLKEKEAEllR 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 317373598 2409 LEEALQRKQELSRDnATLqatlhAARDTLAsvfrllHSLDQAKEELER 2456
Cdd:pfam15619 100 LRDQLKRLEKLSED-KNL-----AEREELQ------KKLEQLEAKLED 135
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2364-2618 |
3.03e-05 |
|
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: 48.45 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2364 QALATQTRDRLAQHEAgLMDLREALNRaVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAA---RDTLASV 2440
Cdd:pfam12795 3 DELEKAKLDEAAKKKL-LQDLQQALSL-LDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAApkeILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2441 FRLLHSLDQAKEELERLAASLDGARTpLLQRMQTfSPAGSKLRLVEAAeahaQQLGQLALNLSSiiLDVNQDRLTQraie 2520
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNS-QLIELQT-RPERAQQQLSEAR----QRLQQIRNRLNG--PAPPGEPLSE---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2521 asnaysrilqavqaAEDAAGQALQQAdhtwatvvRQGLVDRAQQLLANSTALEEAmlqeqqrlglvwaalqgARTQLRDV 2600
Cdd:pfam12795 149 --------------AQRWALQAELAA--------LKAQIDMLEQELLSNNNRQDL-----------------LKARRDLL 189
|
250
....*....|....*...
gi 317373598 2601 RAKKDQLEAHIQAAQAML 2618
Cdd:pfam12795 190 TLRIQRLEQQLQALQELL 207
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
829-867 |
3.18e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.88 E-value: 3.18e-05
10 20 30
....*....|....*....|....*....|....*....
gi 317373598 829 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 867
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2976-3102 |
3.29e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 46.16 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2976 SGVLFFLKQQSQ--FLCLAVQEGSLVLLYDFGAGLKkavpLQPPPPLTSASKAIQVFLLGgSRKRVLVRVERATVYSVEQ 3053
Cdd:pfam00054 7 SGLLLYNGTQTErdFLALELRDGRLEVSYDLGSGAA----VVRSGDKLNDGKWHSVELER-NGRSGTLSVDGEARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 317373598 3054 ----DNDLELADAYYLGGVPPDQLppsLRRLFPTGGSVRGCVKGIKALGKYVD 3102
Cdd:pfam00054 82 plgaTTDLDVDGPLYVGGLPSLGV---KKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2364-2730 |
3.45e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 49.81 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2364 QALATQTRDRL--AQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVF 2441
Cdd:COG2203 334 EALADQAAIAIerARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2442 RLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEA 2521
Cdd:COG2203 414 GLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2522 SNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVR 2601
Cdd:COG2203 494 LLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLS 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2602 AKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGH 2681
Cdd:COG2203 574 VLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASL 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 317373598 2682 SVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAA 2730
Cdd:COG2203 654 VLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVA 702
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2174-2609 |
4.43e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2174 LLDDLERAGALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQ 2253
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2254 AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLGA 2333
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2334 PQAAAeaelaaaQRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL 2413
Cdd:COG1196 541 EAALA-------AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2414 QRKQelsRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTpllqrmqtfspAGSKLRLVEAAEAHAQ 2493
Cdd:COG1196 614 RYYV---LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-----------GGSRRELLAALLEAEA 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2494 QLGQLALNLSSIILDVNQDRLTQRAIEasnaysriLQAVQAAEDAAGQALQQADhtwatvVRQGLVDRAQQLLANSTALE 2573
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEE--------RELAEAEEERLEEELEEEA------LEEQLEAEREELLEELLEEE 745
|
410 420 430
....*....|....*....|....*....|....*.
gi 317373598 2574 EAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEA 2609
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
358-421 |
5.12e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 5.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373598 358 SCNCYGHAtdcyydpevdrrrasqSLDGT-YQGGGVCIdCQHHTTGVNCERCLPGFYRSPNHPLD 421
Cdd:cd00055 1 PCDCNGHG----------------SLSGQcDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2166-2462 |
5.80e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2166 VCDHCVVLLLDDLERAGALLPAIHEQLRGINASSMAWARlhrlnASIADLQSQLRSPLgprheTAQQLEVLEQQSTSLGQ 2245
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA-----AAIEYLKAAKAGRA-----TFLPLDKIRARAALAAA 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2246 DARRLGGQAVGTRDQASQLLAGTEATLGhaKTLLAAIRAVDRTLSelmsqtghlGLANASAPSGEQLLRTLAEVERLLWE 2325
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLG--DTLLGRTLVAARLEA---------ALRRAVTLAGRLREVTLEGEGGSAGG 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2326 MRARdlgapqaaaeaelaaaqrllARVQEQLSSLwEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRN 2405
Cdd:COG1196 661 SLTG--------------------GSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 317373598 2406 QERLEEALQRKQELSRDNATLQATLHAA-RDTLASVFRLLHSLDQAKEELERLAASLD 2462
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELlEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2347-2735 |
5.93e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 49.04 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQEQLsslweenqALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATL 2426
Cdd:COG2203 331 ELLEALADQA--------AIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAEL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2427 QATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSII 2506
Cdd:COG2203 403 LLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2507 LDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLV 2586
Cdd:COG2203 483 LLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLT 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2587 WAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEG 2666
Cdd:COG2203 563 LVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSAL 642
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2667 LRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAASKVKV 2735
Cdd:COG2203 643 LLRLALALASLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLE 711
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2203-2472 |
8.48e-05 |
|
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: 48.80 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2203 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLgqdaRRLGGQAVGTRDQ-ASQLLAGTEATLGHAKTLLAA 2281
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLL----NKLLPQANLLADEtLADRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2282 IRAVDRTLSELMSQTGHLglanASAP-SGEQLLRTLAEVERLLWEMRARdlgapqaaaeaeLAAAQRLLARVQ----EQL 2356
Cdd:COG3096 912 IQQHGKALAQLEPLVAVL----QSDPeQFEQLQADYLQAKEQQRRLKQQ------------IFALSEVVQRRPhfsyEDA 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2357 SSLWEENQALATQTRDRLAQHEAGLMDLREAL----NRAVDATREAQELNSR---NQERLEEALQRKQELS-RDNATLQA 2428
Cdd:COG3096 976 VGLLGENSDLNEKLRARLEQAEEARREAREQLrqaqAQYSQYNQVLASLKSSrdaKQQTLQELEQELEELGvQADAEAEE 1055
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 317373598 2429 TLHAARDTLASvfrLLHSLDQAKEELERLAASLDGARTPLLQRM 2472
Cdd:COG3096 1056 RARIRRDELHE---ELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2212-2610 |
9.08e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2212 IADLQSQLRSPLGPRHETAQQLEVLEQQstslgqdarrlggqavgtRDQASQLLAGTEATLGHAKTLLAAIRavdrtlSE 2291
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREE------------------LEQAREELEQLEEELEQARSELEQLE------EE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2292 LmsqtghlglanasapsgEQLLRTLAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARVQEQLSSLWEENQALATQtR 2371
Cdd:COG4372 82 L-----------------EELNEQLQAAQAELAQAQEE-------------------LESLQEEAEELQEELEELQKE-R 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2372 DRLAQHEAGLMDLREALNRAVDA-TREAQELNSR---NQERLEEALQRKQELSRDNAT--LQATLHAARDTLASVFRLLH 2445
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAErEEELKELEEQlesLQEELAALEQELQALSEAEAEqaLDELLKEANRNAEKEEELAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2446 SLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEAsNAY 2525
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI-AAL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2526 SRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRlGLVWAALQGARTQLRDVRAKKD 2605
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA-DLLQLLLVGLLDNDVLELLSKG 362
|
....*
gi 317373598 2606 QLEAH 2610
Cdd:COG4372 363 AEAGV 367
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
359-426 |
9.28e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.34 E-value: 9.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317373598 359 CNCYGHATdcyydpevdrrrasqSLDGTYQGGGVCiDCQHHTTGVNCERCLPGFYRSPNhplDSPHVC 426
Cdd:pfam00053 1 CDCNPHGS---------------LSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1983-2069 |
1.33e-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: 44.70 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 1983 DCDPLTGACRGClRHTTGPRCEICAPGFYGNAL---LPGNCTRCDCTPCGTE--ACDPHSG-HCLCKAGVT-------GR 2049
Cdd:cd13406 17 ECPPGEGMESRC-TGTQDTVCSPCEPGFYNEAVnyePCKPCTQCNQRSGSEEkqKCTKTSDtVCRCRPGTQpldsykpGV 95
|
90 100
....*....|....*....|
gi 317373598 2050 RCDRCQEGHFGFDGCGGCRP 2069
Cdd:cd13406 96 DCVPCPPGHFSRGDNQACKP 115
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2484-2697 |
1.71e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2484 LVEAAEAHAQQLGqlalnlssiildvNQDRLTQRAIEASNA----YSRILQAVQAA-EDAAGQALQQ-ADHtwatvvrQG 2557
Cdd:COG1842 39 LVEARQALAQVIA-------------NQKRLERQLEELEAEaekwEEKARLALEKGrEDLAREALERkAEL-------EA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2558 LVDRAQQLLANSTALEEAMLQEQQRLglvwaalqgaRTQLRDVRAKKDQLEAHIQAAQAMLAMdtDETSKKIahakavaa 2637
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQL----------ESKLEELKAKKDTLKARAKAAKAQEKV--NEALSGI-------- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 2638 eaqdTATRVQSQLQAMQENVERWQGQYEGL----RGQDLGQ--AVLDAGHSVstlEKTLPQLLAKL 2697
Cdd:COG1842 159 ----DSDDATSALERMEEKIEEMEARAEAAaelaAGDSLDDelAELEADSEV---EDELAALKAKM 217
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2207-2619 |
1.80e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2207 RLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSL---------GQDA-RRLG---GQAVGTRDQASQLLAGT---EA 2270
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawlaAQDAlARLReqsGEEFEDSQDVTEYMQQLlerER 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2271 TLGHAKTLLAA-IRAVDRTLSELmsqtghlglanaSAPSGEQL--LRTLAE---------------------VERLLWEM 2326
Cdd:PRK04863 642 ELTVERDELAArKQALDEEIERL------------SQPGGSEDprLNALAErfggvllseiyddvsledapyFSALYGPA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2327 R----ARDLGapqaaaeaelaaaqrllaRVQEQLSSLWE--ENQALATQTRDRLAQ--HEAglmdlrEALNRAV------ 2392
Cdd:PRK04863 710 RhaivVPDLS------------------DAAEQLAGLEDcpEDLYLIEGDPDSFDDsvFSV------EELEKAVvvkiad 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2393 ---------------DATREAQeLNSRNQERlEEALQRKQELSRDNATLQATLHAARDTLAS----VFR-----LLHSLD 2448
Cdd:PRK04863 766 rqwrysrfpevplfgRAAREKR-IEQLRAER-EELAERYATLSFDVQKLQRLHQAFSRFIGShlavAFEadpeaELRQLN 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2449 QAKEELERLAASLDGARtpLLQRMQtfspagsklrlVEAAEAHAQQLGQLALNLSsiILDVN--QDRLTQ------RAIE 2520
Cdd:PRK04863 844 RRRVELERALADHESQE--QQQRSQ-----------LEQAKEGLSALNRLLPRLN--LLADEtlADRVEEireqldEAEE 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2521 A-------SNAYSRI------LQAVQAAEDAAGQALQQADHTWATVVRQG-----LVDR--------AQQLLANSTALEE 2574
Cdd:PRK04863 909 AkrfvqqhGNALAQLepivsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfalteVVQRrahfsyedAAEMLAKNSDLNE 988
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 317373598 2575 AMlqeQQRLGLVWAALQGARTQLRDVRAKKDQ-------LEAHIQAAQAMLA 2619
Cdd:PRK04863 989 KL---RQRLEQAEQERTRAREQLRQAQAQLAQynqvlasLKSSYDAKRQMLQ 1037
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2481-2703 |
1.91e-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: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2481 KLRLVEAAEAHAQQLGQLALNLSSIiLDVNQDRLT------------QRAIEASNAYSR--ILQAVQAAEDAAGQALQQa 2546
Cdd:COG3206 102 KLNLDEDPLGEEASREAAIERLRKN-LTVEPVKGSnvieisytspdpELAAAVANALAEayLEQNLELRREEARKALEF- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2547 dhtwatvvrqgLVDRAQQLLANSTALEEAMLQEQQRLGLVWAA---------LQGARTQLRDVRAKKDQLEAHIQAAQAM 2617
Cdd:COG3206 180 -----------LEEQLPELRKELEEAEAALEEFRQKNGLVDLSeeaklllqqLSELESQLAEARAELAEAEARLAALRAQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2618 LAMDTDETSKKIAHAKAVAAEAQdtATRVQSQLQAMQEN-------VERWQGQYEGLRGQ---DLGQAVLDAGHSVSTLE 2687
Cdd:COG3206 249 LGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARytpnhpdVIALRAQIAALRAQlqqEAQRILASLEAELEALQ 326
|
250
....*....|....*.
gi 317373598 2688 KTLPQLLAKLSILENR 2703
Cdd:COG3206 327 AREASLQAQLAQLEAR 342
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2117-2145 |
2.71e-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: 41.18 E-value: 2.71e-04
10 20 30
....*....|....*....|....*....|....
gi 317373598 2117 CQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2145
Cdd:pfam00053 1 CDCNPhgslsDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
2353-2457 |
3.85e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 45.79 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEENQAL-------ATQTrDRLAQHEAGLM---------------DLREALNRAVDATREAQELNSRNQERLE 2410
Cdd:pfam04849 170 QEKLRGLEEENLKLrseashlKTET-DTYEEKEQQLMsdcveqlseanqqmaELSEELARKMEENLRQQEEITSLLAQIV 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 317373598 2411 EALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERL 2457
Cdd:pfam04849 249 DLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGM 295
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2116-2145 |
3.92e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 3.92e-04
10 20 30
....*....|....*....|....*....|....*
gi 317373598 2116 RCQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2145
Cdd:cd00055 1 PCDCNGhgslsGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
2349-2621 |
3.96e-04 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 45.83 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEQLSslweenqalatQTRDRLAQHEAGLMDLREAlnRAVDATREAQELNSRNQerLEEALQRKQELSRDNATLQA 2428
Cdd:TIGR01844 136 LAALKEQLD-----------LARARFDVGLGTRTDVLQA--EARYASARAQLIQAQNN--LDDAKAQLRRLVGQPELAPL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2429 TLHAARDtlasvfRLLHSLDQAKEELER-----LAA--SLDGARTPLLQR----MQTFSPAGSKLRLVEAAEAHAQQLGQ 2497
Cdd:TIGR01844 201 AVPSFPA------ELPEPLDQLLEIAEAsnpllLAAqaAVDAARYQVEQAraghLPTLSLTASTGNSDTSSGGSGNSDSD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2498 LAlnlsSIILDVN----QDRLTQRAIEAsnAYSRILQAVQAAEDAAGQALQQADHTWATVV--RQGLVDRAQQLLANSTA 2571
Cdd:TIGR01844 275 TY----SVGLNVSiplyQGGATSAQVRQ--AAHQLNQSRSTLESQKRTVRQQVRNAWSNLNaaAASVQAYEQQVASAQKA 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 317373598 2572 LeEAMLQEQQ---R--LGLVWA--ALQGARTQLrdVRAKKDQLEAHIQAAQAMLAMD 2621
Cdd:TIGR01844 349 L-DAYRQEYQvgtRtlLDVLNAeqELYQARQEL--ANARYDYLQAQLNLLSATGTLN 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2164-2456 |
4.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2164 CEVCDHcvvlLLDDLERAGaLLPAIHEQLRGINAssmawaRLHRLNASIADLQSQLR---------SPLGPRHETAQQLE 2234
Cdd:PRK03918 438 CPVCGR----ELTEEHRKE-LLEEYTAELKRIEK------ELKEIEEKERKLRKELRelekvlkkeSELIKLKELAEQLK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2235 VLEQQSTSLG--------QDARRLGGQAVGTRDQASQL---LAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLAn 2303
Cdd:PRK03918 507 ELEEKLKKYNleelekkaEEYEKLKEKLIKLKGEIKSLkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE- 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2304 asapSGEQLLRTLAEVERLLWE-MRARDlgapqaaaeaelaaAQRLLARVQEQLSSLWEEnqalATQTRDRLAQHEAGLM 2382
Cdd:PRK03918 586 ----SVEELEERLKELEPFYNEyLELKD--------------AEKELEREEKELKKLEEE----LDKAFEELAETEKRLE 643
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373598 2383 DLREALNravdatreaqELNSR-NQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELER 2456
Cdd:PRK03918 644 ELRKELE----------ELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2117-2145 |
4.67e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 4.67e-04
10 20 30
....*....|....*....|....*....|....
gi 317373598 2117 CQCP-----GGRCDPHTGRCNCPPGLSGERCDTC 2145
Cdd:smart00180 1 CDCDpggsaSGTCDPDTGQCECKPNVTGRRCDRC 34
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2175-2655 |
4.99e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2175 LDDLERAgalLPAihEQLRGinassmAWARLHRLNASIAD-----------LQSQLRSPLGPRHETAQQLEVLEQQSTSL 2243
Cdd:PRK10246 280 LAALSLA---QPA--RQLRP------HWERIQEQSAALAHtrqqieevntrLQSTMALRARIRHHAAKQSAELQAQQQSL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2244 GQ-----DARRLGGQAV-GTRDQASQL------LAGTEATLGHAKTLLAAIRAVDRTLSelmsqtghlglANASAPSGEQ 2311
Cdd:PRK10246 349 NTwlaehDRFRQWNNELaGWRAQFSQQtsdreqLRQWQQQLTHAEQKLNALPAITLTLT-----------ADEVAAALAQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2312 LLRTLAEVERLLwemrardlgapqaaaeaelaaaqRLLARVQEQLSSLwEENQALATQTRDRLAQHEAGLMDLRealnra 2391
Cdd:PRK10246 418 HAEQRPLRQRLV-----------------------ALHGQIVPQQKRL-AQLQVAIQNVTQEQTQRNAALNEMR------ 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2392 vdatreaQELNSRNQERLE-----EALQRKQELSRDNATLQA---------TLHAARDTLASVF-----RLLHSLDQAKE 2452
Cdd:PRK10246 468 -------QRYKEKTQQLADvkticEQEARIKDLEAQRAQLQAgqpcplcgsTSHPAVEAYQALEpgvnqSRLDALEKEVK 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2453 ELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTqraieASNAYSRIL--- 2529
Cdd:PRK10246 541 KLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLD-----AQEEHERQLrll 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2530 ---QAVQAAEDAAGQALQQADHTWATvVRQGLVDraqQLLANSTAL-----EEAMLQEQQRLGLVWAALQgarTQLRDVR 2601
Cdd:PRK10246 616 sqrHELQGQIAAHNQQIIQYQQQIEQ-RQQQLLT---ALAGYALTLpqedeEASWLATRQQEAQSWQQRQ---NELTALQ 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2602 AKKDQLEAHIQAAQAMLAMDTDETSkkiaHAKAVAAEAQDTATRVQSQLQAMQE 2655
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEET----VALDNWRQVHEQCLSLHSQLQTLQQ 738
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
300-345 |
5.00e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 5.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 317373598 300 CVCH--GHADacdakDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQPW 345
Cdd:smart00180 1 CDCDpgGSAS-----GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
387-416 |
5.36e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 5.36e-04
10 20 30
....*....|....*....|....*....|
gi 317373598 387 YQGGGVCiDCQHHTTGVNCERCLPGFYRSP 416
Cdd:smart00180 14 DPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2348-2495 |
5.64e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 43.79 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2348 LLARVQEQLSSLweenqalatqtRDRLAQHEAglmDLREALNRAVD--------ATREAQELNSRNQERLEEALQRKQEL 2419
Cdd:pfam01442 38 LRERLQKDLEEV-----------RAKLEPYLE---ELQAKLGQNVEelrqrlepYTEELRKRLNADAEELQEKLAPYGEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2420 SRDNA-----TLQATLHAARDtlasvfRLLHSLDQAKEEL-ERLAASLDGARTPLLQRMQtfspagsklRLVEAAEAHAQ 2493
Cdd:pfam01442 104 LRERLeqnvdALRARLAPYAE------ELRQKLAERLEELkESLAPYAEEVQAQLSQRLQ---------ELREKLEPQAE 168
|
..
gi 317373598 2494 QL 2495
Cdd:pfam01442 169 DL 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2349-2628 |
5.76e-04 |
|
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: 46.21 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEQLSSLWEENQALAtQTRDRLAQHEAGLMD-LREALNRAVDATREAQELN---SRNQERLEEALQRKQELSRDNA 2424
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQ-SELRRIENRLDELSQeLSDASRKIGEIEKEIEQLEqeeEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2425 TLQATLHAARDTLASVFRLLHSLdqaKEELERLAASLDGARTPLLQRM-----QTFSPAGSKLRLVEAAEAHAQQLGQLA 2499
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSRIPEIQAElskleEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2500 ----LNLSSIILDV-NQDRLTQRAIEASNAYSRILQAV----QAAE-----------------DAAGQALQQADHTWATV 2553
Cdd:TIGR02169 832 ekeiQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEleelEAALrdlesrlgdlkkerdelEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2554 vrqglVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQ---GARTQLRDVRAKKDQLEAHIQAAQA--MLAMDTDETSKK 2628
Cdd:TIGR02169 912 -----IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALEPvnMLAIQEYEEVLK 986
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2349-2583 |
7.24e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEQLSSLWEENQALATQTRDRL--AQHEAGLMDLREALNRAVDATREAQELNSR---NQERLEEALQRKQELSRDN 2423
Cdd:COG4913 636 LEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLAALEEQleeLEAELEELEEELDELKGEI 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2424 ATLQATLHAARDtlasvfrllhSLDQAKEELERLAASLDGARTPLLQRMqtfspagsklRLVEAAEAHAQQLGQlalNLS 2503
Cdd:COG4913 716 GRLEKELEQAEE----------ELDELQDRLEAAEDLARLELRALLEER----------FAAALGDAVERELRE---NLE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2504 SII--LDVNQDRLTQRAIEASNAYSR----ILQAVQAAEDAAGQALQQADhtwaTVVRQGLVDRAQQLLAnstALEEAML 2577
Cdd:COG4913 773 ERIdaLRARLNRAEEELERAMRAFNRewpaETADLDADLESLPEYLALLD----RLEEDGLPEYEERFKE---LLNENSI 845
|
....*.
gi 317373598 2578 QEQQRL 2583
Cdd:COG4913 846 EFVADL 851
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
2384-2624 |
7.62e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 44.33 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2384 LREALNRAVDATREAQELNS-------------RNQERLEEALQ-RKQELSRDNATLQATLHaardtLASVFRLLHSLDQ 2449
Cdd:COG2956 20 LNGQPDKAIDLLEEALELDPetveahlalgnlyRRRGEYDRAIRiHQKLLERDPDRAEALLE-----LAQDYLKAGLLDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2450 AKEELERLAASLDGARTPLLQRMQTFspagSKLRLVEAAEAHAQQLgqLALNLSSIILDVNQDRLTQRAIEASNAYSRIL 2529
Cdd:COG2956 95 AEELLEKLLELDPDDAEALRLLAEIY----EQEGDWEKAIEVLERL--LKLGPENAHAYCELAELYLEQGDYDEAIEALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2530 QAVQAAEDAAGQALQQADhtwaTVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAAL---QGARTQLRDVRAKKDQ 2606
Cdd:COG2956 169 KALKLDPDCARALLLLAE----LYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLgdpEEALELLRKALELDPS 244
|
250
....*....|....*...
gi 317373598 2607 LEAHIQAAQAMLAMDTDE 2624
Cdd:COG2956 245 DDLLLALADLLERKEGLE 262
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2353-2672 |
7.80e-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: 45.73 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRavdaTREAQELNSRNQERLEEALQRKQELSRdnatLQATLHA 2432
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQEEQLKKQQLLKQ----LRARIEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2433 ARDTLASVFRLLHSLDQAK------EELERLaASLDGARTPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSii 2506
Cdd:TIGR00618 272 LRAQEAVLEETQERINRARkaaplaAHIKAV-TQIEQQAQRIHTELQ------SKMRSRAKLLMKRAAHVKQQSSIEE-- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2507 ldvnQDRLTQraieasnaysRILQAVQAAEDAAGQALQQADH-TWATVVRQGLVDRAQQL-----LANSTALEEAMLQEQ 2580
Cdd:TIGR00618 343 ----QRRLLQ----------TLHSQEIHIRDAHEVATSIREIsCQQHTLTQHIHTLQQQKttltqKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2581 QrlglvwaALQGARTQ-LRDVRAKKDQLEAHIQAAQAMLAMD----TDETSKKIAHAKAVAAEAQDTATRVQ--SQLQAM 2653
Cdd:TIGR00618 409 Q-------ATIDTRTSaFRDLQGQLAHAKKQQELQQRYAELCaaaiTCTAQCEKLEKIHLQESAQSLKEREQqlQTKEQI 481
|
330
....*....|....*....
gi 317373598 2654 QENVERwQGQYEGLRGQDL 2672
Cdd:TIGR00618 482 HLQETR-KKAVVLARLLEL 499
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2467-2620 |
9.73e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.34 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2467 PLLQrmqtFSPAGSKLRLVEAAEAHAQQLGQLALNLSSI----ILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQA 2542
Cdd:pfam00529 47 VLFQ----LDPTDYQAALDSAEAQLAKAQAQVARLQAELdrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2543 LQQADHTWAT-----VVRQGLVDRAQQLLANSTALeeamLQEQQRLGLVWA-ALQGARTQLRDVRAKKDQLEAHIQAAQA 2616
Cdd:pfam00529 123 QIDLARRRVLapiggISRESLVTAGALVAQAQANL----LATVAQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
....
gi 317373598 2617 MLAM 2620
Cdd:pfam00529 199 ELKL 202
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2276-2490 |
9.96e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2276 KTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQL--LRT-LAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARV 2352
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLseLESqLAEARAELAEAEAR-------------------LAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLWEENQALAT-----QTRDRLAQHEAGLMDLREALN----RAVDATREAQELNSRNQERLEEALQrkqELSRDN 2423
Cdd:COG3206 246 RAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILA---SLEAEL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2424 ATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGAR---TPLLQRMQ----TFSPAGSKLRLVEAAEA 2490
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARelyESLLQRLEearlAEALTVGNVRVIDPAVV 396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2521-2676 |
1.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2521 ASNAYSRILQAVQAAEDAAGQALQQADHTWATV--VRQGLVDRAQQLLANSTALEEAMLQEQQRLglvwAALQGARTQLR 2598
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELeqLEEELEQARSELEQLEEELEELNEQLQAAQ----AELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2599 DVRAKKDQLEAHIQAAQA---MLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQA 2675
Cdd:COG4372 105 SLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
.
gi 317373598 2676 V 2676
Cdd:COG4372 185 L 185
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2353-2583 |
1.30e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2353 QEQLSSLweenQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQElnsrNQERLEEALQ--RKQELS-RDNA-TLQA 2428
Cdd:PRK04778 354 EKQLESL----EKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK----EQEKLSEMLQglRKDELEaREKLeRYRN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2429 TLHAARDTLASVfRL-------LHSLDQAKEELERLAASLDgaRTPLlqRMQTFSpagsklRLVEAAEAHAQQLGQLALN 2501
Cdd:PRK04778 426 KLHEIKRYLEKS-NLpglpedyLEMFFEVSDEIEALAEELE--EKPI--NMEAVN------RLLEEATEDVETLEEETEE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2502 LssiildVNQDRLTQRAIEASNAY----SRILQAVQAAE------------DAAGQALQQADhtwatvvrQGLVDRaqql 2565
Cdd:PRK04778 495 L------VENATLTEQLIQYANRYrsdnEEVAEALNEAErlfreydykaalEIIATALEKVE--------PGVTKR---- 556
|
250
....*....|....*...
gi 317373598 2566 lanstaLEEAMLQEQQRL 2583
Cdd:PRK04778 557 ------IEDSYEKEKETI 568
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2396-2565 |
1.45e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2396 REAQELNSRNQErLEEAL----QRKQELSRDNATLQATLHAARdtlasvfrllhsldQAKEELERLAASLDGARTPLLQR 2471
Cdd:PRK09039 53 SALDRLNSQIAE-LADLLslerQGNQDLQDSVANLRASLSAAE--------------AERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2472 MQTFSPAgsklrLVEAAEAHAQQLGQLALnlssiildVNQDrltqraIEASNaysRILQAVQAAEDAAGQALQQADHTWA 2551
Cdd:PRK09039 118 AGELAQE-----LDSEKQVSARALAQVEL--------LNQQ------IAALR---RQLAALEAALDASEKRDRESQAKIA 175
|
170
....*....|....*..
gi 317373598 2552 TVVRQ---GLVDRAQQL 2565
Cdd:PRK09039 176 DLGRRlnvALAQRVQEL 192
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
300-344 |
1.53e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.87 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 317373598 300 CVCHGHADAcdaKDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQP 344
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2391-2619 |
1.55e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2391 AVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASvfrllhsLDQAKEELERLAASLDGARTPLLQ 2470
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-------LEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2471 RMQTFspagsklrlveAAEAHAQQLGQLALNLSSIILDVNqdrltqraiEASNAYSRiLQAVQAAEDAAGQALQQADHTw 2550
Cdd:COG3883 84 RREEL-----------GERARALYRSGGSVSYLDVLLGSE---------SFSDFLDR-LSALSKIADADADLLEELKAD- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2551 atvvrQGLVDRAQQLLANSTALEEAMLQEQQrlglvwAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2619
Cdd:COG3883 142 -----KAELEAKKAELEAKLAELEALKAELE------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2201-2497 |
1.94e-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: 44.29 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2201 AWARLHRLNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATlghaktlla 2280
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIER-------QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE--------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2281 aIRAVDRTLSELMSQTghlglanasapsgEQLLRTLAEVERLLWEMRARdlgapqaaAEAELAAAQRLLARVqEQLSSLW 2360
Cdd:TIGR02169 289 -QLRVKEKIGELEAEI-------------ASLERSIAEKERELEDAEER--------LAKLEAEIDKLLAEI-EELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2361 EENQALATQTRDRLAQHEAGLMDLR---EALNRAVDATREaqELNSRnQERLEEA--------------LQRKQELSRDN 2423
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRaelEEVDKEFAETRD--ELKDY-REKLEKLkreinelkreldrlQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2424 ATLQATLHAARDTLASVFRLLHSLD----QAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVE----AAEAHAQQL 2495
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKAleikKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelaEAEAQARAS 502
|
..
gi 317373598 2496 GQ 2497
Cdd:TIGR02169 503 EE 504
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2385-2520 |
2.11e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2385 REALNRAVDATREAQELNSRNQERLEEALQRKQELsRDNATLQATLHAARdtlasvfrllhSLDQAKEELERLAASldgA 2464
Cdd:COG0711 37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEI-IAEARKEAEAIAEE-----------AKAEAEAEAERIIAQ---A 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317373598 2465 RtpllqrmqtfspagsklRLVEAAEAHA-----QQLGQLALNLSSIILDVN-----QDRLTQRAIE 2520
Cdd:COG0711 102 E-----------------AEIEQERAKAlaelrAEVADLAVAIAEKILGKEldaaaQAALVDRFIA 150
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2360-2835 |
2.24e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2360 WEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEE-ALQRKQELSRDNATLQAtlHAARDTLA 2438
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEeAREAKAEAEQRAAELAA--EAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2439 SVFRLLHSLDQAKEELERLA----ASLDGARTPLLQRMQTFSPAgsKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRL 2514
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAkeaeAAAAAEKAAAAAEKEKAEEA--KRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2515 TQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRA--QQLLANSTALEEAMLQEQQRLGLVWAALQG 2592
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAaaAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2593 ARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDL 2672
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2673 GQAVLDAGHSVSTLEKTL--PQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTP 2750
Cdd:COG3064 320 AAAAAGALVVRGGGAASLeaALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2751 RDLADLAAYTALKFYLQGPEPEPGQGTED-RFVMYMGSRQATGDYMGVSLRDKKVHWVYQLGEAGPAVLSIDEDIGEQFA 2829
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGaAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 317373598 2830 AVSLDR 2835
Cdd:COG3064 480 LLLLGG 485
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2352-2499 |
2.67e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2352 VQEQLSSLWEENQALATQtrdrLAQHEAGLMDLREALNRAVDATREAQELNSRNQERL-EEALQRKQELSRDNATLQATL 2430
Cdd:pfam04012 31 IRDMQSELVKARQALAQT----IARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELaREALAEKKSLEKQAEALETQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2431 HAARDTLASVFRLLHSLD----QAKEELERLAASLDGAR-----------------TPLLQRMQTfspagsklrLVEAAE 2489
Cdd:pfam04012 107 AQQRSAVEQLRKQLAALEtkiqQLKAKKNLLKARLKAAKaqeavqtslgslstssaTDSFERIEE---------KIEERE 177
|
170
....*....|
gi 317373598 2490 AHAQQLGQLA 2499
Cdd:pfam04012 178 ARADAAAELA 187
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2226-2548 |
2.74e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2226 RHETAQ-QLEVLEQQSTslgqdarrlgGQAVGTRDQASQLLAGTEATLGHAKTLLAAiravdrtlselmsqtghlglana 2304
Cdd:PRK10246 192 QHKSARtELEKLQAQAS----------GVALLTPEQVQSLTASLQVLTDEEKQLLTA----------------------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2305 sapsgEQLLRtlaevERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLweENQALATQTR---DRLAQHEAGL 2381
Cdd:PRK10246 239 -----QQQQQ-----QSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAAL--SLAQPARQLRphwERIQEQSAAL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2382 MDLRealnravdatREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLAS--VFRLLHS-----------LD 2448
Cdd:PRK10246 307 AHTR----------QQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEhdRFRQWNNelagwraqfsqQT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2449 QAKEELERLAASLDGARtpllQRMQTFSPAGSKLRLVEAAEAHAQQ-----LGQLALNLSSIILDVnQDRLTQRAIEASN 2523
Cdd:PRK10246 377 SDREQLRQWQQQLTHAE----QKLNALPAITLTLTADEVAAALAQHaeqrpLRQRLVALHGQIVPQ-QKRLAQLQVAIQN 451
|
330 340
....*....|....*....|....*
gi 317373598 2524 AYSRILQAVQAAEDAAGQALQQADH 2548
Cdd:PRK10246 452 VTQEQTQRNAALNEMRQRYKEKTQQ 476
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2398-2618 |
2.78e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2398 AQELNSRN--QERLEEALQRKQeLSRDNATLQATLhaaRDTLAsvfrLLHSLDQAKEELERLAASLDGArtPllQRMQTF 2475
Cdd:PRK11281 32 NGDLPTEAdvQAQLDALNKQKL-LEAEDKLVQQDL---EQTLA----LLDKIDRQKEETEQLKQQLAQA--P--AKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2476 SPAGSKLRLVEAAEAhAQQLGQLAL-NLSSIILDVNQD-RLTQRAIEASNAYSRILQA----VQAAEDAAGQALQQADHT 2549
Cdd:PRK11281 100 QAELEALKDDNDEET-RETLSTLSLrQLESRLAQTLDQlQNAQNDLAEYNSQLVSLQTqperAQAALYANSQRLQQIRNL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373598 2550 WATVVRQGLVDRA--QQLLANSTALEEAMLQEQQRLglvwaaLQGArTQLRD--------VRAKKDQLEAHIQAAQAML 2618
Cdd:PRK11281 179 LKGGKVGGKALRPsqRVLLQAEQALLNAQNDLQRKS------LEGN-TQLQDllqkqrdyLTARIQRLEHQLQLLQEAI 250
|
|
| NIT |
pfam08376 |
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ... |
2367-2612 |
2.81e-03 |
|
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in receptor components of signal transducing pathways in bacteria which control gene expression, cellular motility and enzyme activity in response to nitrate and nitrite concentrations. The NIT domain is predicted to be all alpha-helical in structure.
Pssm-ID: 462453 [Multi-domain] Cd Length: 227 Bit Score: 42.48 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2367 ATQTRDRLAQHeaglmdlREALNRAVDATREAQ---ELNSRNQERLEEALQRKQELS--RDNATLQATlhAARDTLASVF 2441
Cdd:pfam08376 20 GGRFAAELAAQ-------RAATDAALAALRAALaelALPARLADRLAALLRALDQLPalRRQVDAGAL--SALEALAAYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2442 RLLHSLdqakeeLERLAASLDGARTP-LLQRMQTFSPagsklrLVEAAEAHAQQLGQLALNLSSiildvnqDRLTQraie 2520
Cdd:pfam08376 91 ELIAAL------LDLVDELAAGSPDPeLARQLRALAA------LLRAKEAAGQERALLAAALAA-------GRFTA---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2521 asNAYSRILQAVQAAEDAAGQALQQADHTWATvvrqglvdRAQQLLANSTALEEAMLQEQQRLGLVWAALQGAR-TQLRD 2599
Cdd:pfam08376 148 --AEYRRFLSLVAAQRAALAEFRAAATPEQRA--------LYDATVTGPAVAAAERLRDRLVDAAAWFAASTARiDLLRE 217
|
250
....*....|...
gi 317373598 2600 VRakkDQLEAHIQ 2612
Cdd:pfam08376 218 VE---DRLADDLA 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2174-2485 |
2.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2174 LLDDLERAGALLPAIHEQLRGINASSMAWARLHRLN----------ASIADLQSQLRSPLgprhETAQQLEVLEQQSTSL 2243
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaeREIAELEAELERLD----ASSDDLAALEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2244 GQDARRLGGQavgtRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANA-SAPSGEQLLRTLAEverl 2322
Cdd:COG4913 698 EAELEELEEE----LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfAAALGDAVERELRE---- 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2323 lwemrardlgapqaaaeaelaaaqRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELN 2402
Cdd:COG4913 770 ------------------------NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2403 S----RNQERLEEALQRKQElsRDNATLQATLHAARDTlasvfrllhsldqAKEELERLAASLdgARTPllqrmqtFSPa 2478
Cdd:COG4913 826 EdglpEYEERFKELLNENSI--EFVADLLSKLRRAIRE-------------IKERIDPLNDSL--KRIP-------FGP- 880
|
....*..
gi 317373598 2479 GSKLRLV 2485
Cdd:COG4913 881 GRYLRLE 887
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2529-2619 |
2.83e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.18 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2529 LQAVQAAEDAAGQALQQADHTWATVvrQGLVDRAQQLLANSTAleEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLE 2608
Cdd:TIGR04320 270 LAAAQTALNTAQAALTSAQTAYAAA--QAALATAQKELANAQA--QALQTAQNNLATAQAALANAEARLAKAKEALANLN 345
|
90
....*....|.
gi 317373598 2609 AHIQAAQAMLA 2619
Cdd:TIGR04320 346 ADLAKKQAALD 356
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
2361-2494 |
2.96e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 41.96 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2361 EENQALaTQTRDRLAQHEAGLMDLREALNRAVDATRE----------------------AQELN---SRNQERLEEALQR 2415
Cdd:cd07596 1 EEDQEF-EEAKDYILKLEEQLKKLSKQAQRLVKRRRElgsalgefgkaliklakceeevGGELGealSKLGKAAEELSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2416 KQELSR-DNATLQATLH-------AARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEA 2487
Cdd:cd07596 80 SEAQANqELVKLLEPLKeylrycqAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAES 159
|
....*..
gi 317373598 2488 AEAHAQQ 2494
Cdd:cd07596 160 ALEEARK 166
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2168-2730 |
3.38e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.69 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2168 DHCVVLLLDDLERA-GALLPAIHEQLRGINASSMAW---------ARLHRLNASIADLQSQLRS----PLGP--RHETAQ 2231
Cdd:COG3899 432 ERPLVLVLDDLHWAdPASLELLEFLLRRLRDLPLLLvgtyrpeevPPAHPLRLLLAELRRAGAGvtrlELGPlsREEVAA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2232 QL-EVLEQQSTS-----------------LGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAvdRtLSELM 2293
Cdd:COG3899 512 LVaDLLGAAELPaelaellvertggnpffLEELLRALLEEGLLRFDGGGWRWDAALAALALPDTVVDLLAA--R-LDRLP 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2294 SQTGHLgLANASA---PSGEQLLRTL-----AEVERLLWEMRARDLgapQAAAEAELAAAQRLL-ARVQEQL-SSLWEEN 2363
Cdd:COG3899 589 PAARRV-LRLAAVlgrRFDLELLAAVlglseAELAAALEELVAAGL---LVPRGDAGGGRYRFRhDLVREAAyASLPPEE 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2364 ---------QALATQTRD-------RLAQH--EAGlmDLREALNRAVDATREAQELNSrnqerLEEA---LQRKQELSRD 2422
Cdd:COG3899 665 rralhrriaRALEARGPEpleerlfELAHHlnRAG--ERDRAARLLLRAARRALARGA-----YAEAlryLERALELLPP 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2423 NATLQATLhAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAE---AHAQQLGQLA 2499
Cdd:COG3899 738 DPEEEYRL-ALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLgdyEEAYEFGELA 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2500 LNLSSIILDVNQ---------------------DRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGL 2558
Cdd:COG3899 817 LALAERLGDRRLearalfnlgfilhwlgplreaLELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2559 VDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAE 2638
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2639 AQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGR 2718
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
650
....*....|..
gi 317373598 2719 VRELIAQARGAA 2730
Cdd:COG3899 1057 AAAAALAAAAAL 1068
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2354-2727 |
3.77e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2354 EQLSSLWEENQALATQTRdrlaqheagLMDLREALNRAVDATREAQELNSRNQERLE--EALQRKQELSRDNAT--LQAT 2429
Cdd:COG3206 71 SGLSSLSASDSPLETQIE---------ILKSRPVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSnvIEIS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2430 L------HAAR--DTLASVFrLLHSLDQAKEELERLAASLDGaRTPLLQRmqtfspagsKLRLVEAA-EAHAQQLGQLAL 2500
Cdd:COG3206 142 YtspdpeLAAAvaNALAEAY-LEQNLELRREEARKALEFLEE-QLPELRK---------ELEEAEAAlEEFRQKNGLVDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2501 NLSSIILDVNQDRLTQRAIEASNAysriLQAVQAAEDAAGQALQQADHTWATVVRQGLVdraQQLLANSTALEEAMLQEQ 2580
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEARAE----LAEAEARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2581 QRLGlvwaalqgarTQLRDVRAKKDQleahIQAAQAMLAMDTDETSKKIahakavaaeaQDTATRVQSQLQAMQENVERW 2660
Cdd:COG3206 284 ARYT----------PNHPDVIALRAQ----IAALRAQLQQEAQRILASL----------EAELEALQAREASLQAQLAQL 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317373598 2661 QGQYEGLRGQDLGQAVLDagHSVSTLEKTLPQLLAKLSilenrgvhNASLALSASIGRVReLIAQAR 2727
Cdd:COG3206 340 EARLAELPELEAELRRLE--REVEVARELYESLLQRLE--------EARLAEALTVGNVR-VIDPAV 395
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
2355-2718 |
4.44e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2355 QLSSLWEenQALATQTRdrLAQHEAGLMDLREALNRAVDATREAQEL----NSRNQERLEEALQRKQELSRDNATLQATL 2430
Cdd:COG1538 1 TLDELIE--RALANNPD--LRAARARVEAARAQLRQARAGLLPSQELdlggKRRARIEAAKAQAEAAEADLRAARLDLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2431 HAARdTLASVFRLLHSLDQAKEELERLAASLD--------GARTPL-LQRMQTFSpAGSKLRLVEAAEAHAQQLGQLALN 2501
Cdd:COG1538 77 EVAQ-AYFDLLAAQEQLALAEENLALAEELLElararyeaGLASRLdVLQAEAQL-AQARAQLAQAEAQLAQARNALALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2502 L-----SSIILDVNQDRLTQRAIEASNAYSRILQ---AVQAAEDAAGQALQQADHTWA------TVVRQGLVDRAQQLLA 2567
Cdd:COG1538 155 LglpppAPLDLPDPLPPLPPLPPSLPGLPSEALErrpDLRAAEAQLEAAEAEIGVARAaflpslSLSASYGYSSSDDLFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2568 NSTALEEAMLQEQQRL---GLVWAALQGARTQLRDVRAKKDQ--LEAHIQAAQAMLAMDTDetskkiahakavaaeaQDT 2642
Cdd:COG1538 235 GGSDTWSVGLSLSLPLfdgGRNRARVRAAKAQLEQAEAQYEQtvLQALQEVEDALAALRAA----------------REQ 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317373598 2643 ATRVQSQLQAMQENVERWQGQYE-GLRGQdlgQAVLDAghsvstlEKTLpqLLAKLSILENRG-VHNASLALSASIGR 2718
Cdd:COG1538 299 LEALEEALEAAEEALELARARYRaGLASL---LDVLDA-------QREL--LQAQLNLIQARYdYLLALVQLYRALGG 364
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2376-2675 |
4.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2376 QHEAG---LMD-LREALNRAVDatREAQELNSRNQERLEEALQRKQELSRDnatlqatLHAARDTLASVFRLLHSLDQAK 2451
Cdd:COG4717 31 PNEAGkstLLAfIRAMLLERLE--KEADELFKPQGRKPELNLKELKELEEE-------LKEAEEKEEEYAELQEELEELE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2452 EELERLAASLDGARtpllQRMQtfspagsKLRLVEAAEAHAQQLGQLALNLSSIildvnQDRLtqraieasnaysrilqa 2531
Cdd:COG4717 102 EELEELEAELEELR----EELE-------KLEKLLQLLPLYQELEALEAELAEL-----PERL----------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2532 vqaaedaagQALQQADHTWATVVRQgLVDRAQQLLANSTALEEAMLQEQQRlglVWAALQGARTQLRDVRAKKDQLEAHI 2611
Cdd:COG4717 149 ---------EELEERLEELRELEEE-LEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEEL 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 317373598 2612 QAAQamlamdtdetskkiahakavaaeaqdtatrvqsqlqamqENVERWQGQYEGLRGQDLGQA 2675
Cdd:COG4717 216 EEAQ---------------------------------------EELEELEEELEQLENELEAAA 240
|
|
| FlgL |
COG1344 |
Flagellin and related hook-associated protein FlgL [Cell motility]; |
2349-2546 |
4.88e-03 |
|
Flagellin and related hook-associated protein FlgL [Cell motility];
Pssm-ID: 440955 [Multi-domain] Cd Length: 245 Bit Score: 41.77 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2349 LARVQEQLSSLWEENQA--LATQTrdrlaqheAGLMDLREALNRAVDATREAQELNSRNQ------ERLEEALQRKQELs 2420
Cdd:COG1344 23 LAKLQEQLSSGKRINSAsdDPAGA--------AIALRLRSQIRGLEQYQRNANDAISRLQtaegalGEITDILQRAREL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2421 rdnaTLQA---TLHAA-RDTLASvfrllhSLDQAKEELERLAASLDGARTPLLQRMQTFSP---------AGSKLRLVEA 2487
Cdd:COG1344 94 ----AVQAangTLSDEdRAAIAA------ELEQLLDQLLSIANTTDFNGRYLFAGTATDTPpfqvdyqgdAGQRTAALGA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317373598 2488 AEAHAQQLGQLALNLSSII--LDVNQDRLTQRAIEASNAYSRI-----------LQAVQAAEDAAGQALQQA 2546
Cdd:COG1344 164 LDAALDNVSSARAELGARQnrLESAINNLSDLSENLTAALSRLedadmaeaitrLTKLQTLLQAALAALAQA 235
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2347-2465 |
5.26e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2347 RLLARVQEQLSSLweENQALA--TQTRDRLA--------QHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRK 2416
Cdd:COG1842 58 RQLEELEAEAEKW--EEKARLalEKGREDLArealerkaELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKK 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 317373598 2417 QEL-SRDNA-----TLQATLHAARDTLAsvfrlLHSLDQAKEELERLAASLDGAR 2465
Cdd:COG1842 136 DTLkARAKAakaqeKVNEALSGIDSDDA-----TSALERMEEKIEEMEARAEAAA 185
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
2260-2629 |
6.13e-03 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 42.76 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2260 QASQLLAGTEATLGH---AKTLLAAIRAVDRTLSELMSQtghLGLANASAPSGEQLLRTLAEVErllweMRARDLgapqa 2336
Cdd:TIGR02917 313 QAYQYLNQILKYAPNshqARRLLASIQLRLGRVDEAIAT---LSPALGLDPDDPAALSLLGEAY-----LALGDF----- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2337 aaeaelAAAQRLLARVQEQLSslweENQALATQT-RDRLAQ--HEAGLMDLREALNRAVDATR----------EAQELNS 2403
Cdd:TIGR02917 380 ------EKAAEYLAKATELDP----ENAAARTQLgISKLSQgdPSEAIADLETAAQLDPELGRadlllilsylRSGQFDK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2404 RN--QERLEE--------------ALQRKQELSRDNATLQATLHAARDTLASVFRLLH------SLDQAKEELERLAASL 2461
Cdd:TIGR02917 450 ALaaAKKLEKkqpdnaslhnllgaIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARidiqegNPDDAIQRFEKVLTID 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2462 DGARTPLLQ----RMQTFSPAGSKLRLVEAAEAHAQQLgQLALNLSSIILDVNQdrlTQRAIEASNAYSRILQAVQAAED 2537
Cdd:TIGR02917 530 PKNLRAILAlaglYLRTGNEEEAVAWLEKAAELNPQEI-EPALALAQYYLGKGQ---LKKALAILNEAADAAPDSPEAWL 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2538 AAGQA-LQQADHTWATVVRQGLVDRAQQllaNSTALEE-AMLQEQQRlglvwaALQGARTQLRdvRA---KKDQLEAHIQ 2612
Cdd:TIGR02917 606 MLGRAqLAAGDLNKAVSSFKKLLALQPD---SALALLLlADAYAVMK------NYAKAITSLK--RAlelKPDNTEAQIG 674
|
410
....*....|....*..
gi 317373598 2613 AAQAMLAMDTDETSKKI 2629
Cdd:TIGR02917 675 LAQLLLAAKRTESAKKI 691
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2350-2730 |
6.86e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2350 ARVQEQLSSLweENQALATQTRDRLAQHEA------GLMDLREALNRAVDATREAQ----ELNSRNQERLEEA------L 2413
Cdd:COG3064 12 AAAQERLEQA--EAEKRAAAEAEQKAKEEAeeerlaELEAKRQAEEEAREAKAEAEqraaELAAEAAKKLAEAekaaaeA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2414 QRK--QELSRDNATLQATLHAARDTLASVFRllhSLDQAKEELERLA------ASLDGARTPLLQRMQTFSPAGSKLRLV 2485
Cdd:COG3064 90 EKKaaAEKAKAAKEAEAAAAAEKAAAAAEKE---KAEEAKRKAEEEAkrkaeeERKAAEAEAAAKAEAEAARAAAAAAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2486 EAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQL 2565
Cdd:COG3064 167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2566 LANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQA--MLAMDTDETSKKIAHAKAVAAEAQDTA 2643
Cdd:COG3064 247 GAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLddSAALAAELLGAVAAEEAVLAAAAAAGA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 2644 TRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELI 2723
Cdd:COG3064 327 LVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLD 406
|
....*..
gi 317373598 2724 AQARGAA 2730
Cdd:COG3064 407 LGAALLE 413
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3555-3622 |
9.60e-03 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 40.03 E-value: 9.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373598 3555 TGLIFHLGQARTPPYLQLQVT--EKQVLLRADDGAGEFSTSVTRPSVLCDGQWHRLAVMKSGNVLRLEVD 3622
Cdd:smart00210 67 RGVLFAIYDAQNVRQFGLEVDgrANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVD 136
|
|
| |
