|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
45-298 |
6.39e-98 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 315.68 E-value: 6.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 45 LHPPYFNLAEGARIAASATCGEEAPargsprpteDLYCKLVGGPvaggdpnqtiRGQYCDICTAANSNKAHPASNAIDGT 124
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP---------ERYCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 125 ER----WWQSPPLSrgLEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSMDFGRTYQPWQFFASskrDCLERFG 200
Cdd:pfam00055 62 NGtnetWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 201 -PQTLERITRDDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLmgkaLR 279
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 2217335166 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 ... |
2146-2404 |
4.67e-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: 4.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2146 LRGINASSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEAT 2225
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2226 LGHAKTLLAAIRAVDRTLSELMSQTGHLGLaNASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLAR 2305
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE-NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2306 VQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLH 2385
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 2217335166 2386 AARDTLASVFRLLHSLDQA 2404
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-298 |
5.35e-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: 305.05 E-value: 5.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 44 SLHPPYFNLAEGARIAASATCGEEAPARgsprptedlYCKLVGGpvaggdpnqTIRGQYCDICTAANSNKAHPASNAIDG 123
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 124 TE----RWWQSPPLSRGLEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSmDFGRTYQPWQFFASskrDCLERF 199
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 200 GPQTLERITR--DDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLMGKA 277
Cdd:smart00136 141 GRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 2217335166 278 lrdPTVTRRYYYSIKDISIGG 298
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1647-1783 |
5.06e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 168.99 E-value: 5.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1647 YWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVfvPMESRPDVVLQGNQMSITFLEPA--YPTPGHVHRGQLQLVEGNFR 1724
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSSPDqpPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 1725 HTeTRNTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASPAGQGALASNVE 1783
Cdd:pfam00052 79 DS-DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1643-1772 |
2.06e-44 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 158.19 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1643 FPELYWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVFVpmeSRPDVVLQGNQMSITFLEPAYPTPGHVHRGQLQLVEGN 1722
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHV---SAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1723 FRHTETRnTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASP 1772
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 ... |
2595-2716 |
2.41e-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: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2595 DTATRVQSQLQAMQENVERWQGQYEGLRGQ---------DLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLa 2665
Cdd:pfam06009 10 ETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 2666 lSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTPRDLADLAAYTAL 2716
Cdd:pfam06009 89 -SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3294-3451 |
4.38e-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: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3294 SYQFGGSlsSHLEFVGiLARHRNWPSLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQR 3373
Cdd:cd00110 1 GVSFSGS--SYVRLPT-LPAPRTRLSISFSFRTTSPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335166 3374 SRPGRWHKVSVRWEKNRILLVTDGARAWSQEGPHRQHQGaehPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLH 3451
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALL---NLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3475-3625 |
1.02e-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: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3475 GLFFPGSGGViTLDLPGATLPDVGLELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGefSTSVTRPSVL 3554
Cdd:cd00110 1 GVSFSGSSYV-RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 3555 CDGQWHRLAVMKSGNVLRLEVD-AQSNHTVGPLLAAAAGAPAPLYLGGLPEPMAV--QPWPPAYCGCMRRLAVN 3625
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSpgLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3319-3453 |
1.76e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 104.34 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3319 SLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQRS-RPGRWHKVSVRWEKNRILLVTDG 3397
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 3398 ARAWSQEGPhRQHQGAEHPQPhtLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3453
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 ... |
3326-3453 |
1.63e-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: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3326 PRSSRGLLLFTARLRpgSPSLALFLSNGHFVAQME-GLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQE 3404
Cdd:pfam02210 3 TRQPNGLLLYAGGGG--SDFLALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217335166 3405 GPHRQHQgaeHPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3453
Cdd:pfam02210 81 PPGESLL---LNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3499-3626 |
1.69e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 92.79 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3499 LELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEFSTSVTRPSVlCDGQWHRLAVMKSGNVLRLEVDAQ 3578
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPL-NDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 3579 SN-HTVGPLLAAAAGAPAPLYLGGLPEPM--AVQPWPPAYCGCMRRLAVNR 3626
Cdd:smart00282 81 NRvSGESPGGLTILNLDGPLYLGGLPEDLklPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3503-3625 |
9.03e-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: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3503 VRPLAVTGLIFHLGQARTPpYLQLQVTEKQVLLRADDGAGEFSTSVTrPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHT 3582
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSS-GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2217335166 3583 VGPLLAAAAGAPAPL-YLGGLPEP--MAVQPWPPAYCGCMRRLAVN 3625
Cdd:pfam02210 79 SLPPGESLLLNLNGPlYLGGLPPLllLPALPVRAGFVGCIRDVRVN 124
|
|
| LamG |
smart00282 |
Laminin G domain; |
2735-2862 |
1.68e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.84 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2735 FVMYMGSRQaTGDYMGVSLRDKKVHWVYQLGeAGPAVLSIDEDI---GeQFAAVSLDRTLQFGHMSVTVERQMIQETkgd 2811
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPTPlndG-QWHRVAVERNGRSVTLSVDGGNRVSGES--- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 2812 tvaPGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIEMDTLNEE 2862
Cdd:smart00282 88 ---PGGLTILNL---DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2301-2573 |
9.46e-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: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATL 2380
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2381 QATLHAARDTLAsvfRLLHSLDQAKEELERLAASLDGARTPLLQRmqtfspAGSKLRLVEAAEAHAQQLGQLALNLSSII 2460
Cdd:COG1196 329 EEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2461 LDVNQDRLTQRAIEASNAysRILQAVQAAEDAAGQALQQADHTwatvvrQGLVDRAQQLLANSTALEEAMLQEQQRLGlv 2540
Cdd:COG1196 400 AQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEE------EEALEEAAEEEAELEEEEEALLELLAELL-- 469
|
250 260 270
....*....|....*....|....*....|...
gi 2217335166 2541 wAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2573
Cdd:COG1196 470 -EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2897-3049 |
3.02e-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: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2897 GSYLDGTGFARISFDSQISTTKRFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGlkkAVPLQPPPPL 2974
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSG---SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2975 -TSASKAIQVFLLGgsrKRVLVRVER---ATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3049
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 ... |
2160-2649 |
8.03e-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: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2160 HRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAV 2239
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2240 DRTLSELMSQTGHL--GLANasapsgEQLLRTLAEVERllwemraRDLGAPQAAAEAELAAAQRLLArVQEQLSSLWEE- 2316
Cdd:pfam01576 263 LKKIRELEAQISELqeDLES------ERAARNKAEKQR-------RDLGEELEALKTELEDTLDTTA-AQQELRSKREQe 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2317 ----NQALATQTRdrlaQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAlqrKQELSRDNATLQATlhaardtla 2392
Cdd:pfam01576 329 vtelKKALEEETR----SHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKA---KQALESENAELQAE--------- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2393 svfrlLHSLDQAKEELERLAASLDGArtplLQRMQTFSPAGSKLRlVEAAEahaqQLGQLALNLSSI--ILDVNQDRLTQ 2470
Cdd:pfam01576 393 -----LRTLQQAKQDSEHKRKKLEGQ----LQELQARLSESERQR-AELAE----KLSKLQSELESVssLLNEAEGKNIK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2471 RAIEASNAYSRiLQAVQaaedaagQALQQadhtwatvvrqglvdRAQQLLANSTALEEAmlqEQQRLGLvwaalqgaRTQ 2550
Cdd:pfam01576 459 LSKDVSSLESQ-LQDTQ-------ELLQE---------------ETRQKLNLSTRLRQL---EDERNSL--------QEQ 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2551 LRDVRAKKDQLEAHIQAAQAMLAmdtdETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRG------Q 2624
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLS----DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtknrlqQ 580
|
490 500 510
....*....|....*....|....*....|.
gi 2217335166 2625 DLGQAVLDAGHS---VSTLEK---TLPQLLA 2649
Cdd:pfam01576 581 ELDDLLVDLDHQrqlVSNLEKkqkKFDQMLA 611
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2127-2690 |
1.81e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.73 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2127 LLLDDLERAGALLPAIHEQLRGINAssmawARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARR 2203
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNL-----KELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2204 LggqavgtrDQASQLLAgteatlghaktLLAAIRAVDRTLSELMSQTghlglanasapsgEQLLRTLAEVERLLWEMRAR 2283
Cdd:COG4717 121 L--------EKLLQLLP-----------LYQELEALEAELAELPERL-------------EELEERLEELRELEEELEEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2284 DlgapqaaaeaelaaaqRLLARVQEQLSSLWEEnqaLATQTRDRLAqheaglmDLREALNRAVDATREAQELNSRNQERL 2363
Cdd:COG4717 169 E----------------AELAELQEELEELLEQ---LSLATEEELQ-------DLAEELEELQQRLAELEEELEEAQEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2364 EEALQRKQELSRD--NATLQATLHAARdTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEA 2441
Cdd:COG4717 223 EELEEELEQLENEleAAALEERLKEAR-LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2442 AEAHAQQLGQLALNLSSIILdvnQDRLTQRAIEASNAYSRILQAVQAAEDAAgQALQQADHTWATVVRQGLVDRAQQLLA 2521
Cdd:COG4717 302 KEAEELQALPALEELEEEEL---EELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIAALLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2522 NSTALEEAMLQEqqrlglvWAALQGARTQLR-DVRAKKDQLEAHIQAAQAMLAMDTDETskkiahakavaaeAQDTATRV 2600
Cdd:COG4717 378 EAGVEDEEELRA-------ALEQAEEYQELKeELEELEEQLEELLGELEELLEALDEEE-------------LEEELEEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2601 QSQLQAMQENVERWQGQYEGLRGQdlgQAVLDAGHSVSTLEKTLPQLLAKLSILENRgvhNASLALsasigrVRELIAQA 2680
Cdd:COG4717 438 EEELEELEEELEELREELAELEAE---LEQLEEDGELAELLQELEELKAELRELAEE---WAALKL------ALELLEEA 505
|
570
....*....|
gi 2217335166 2681 RGAASKVKVP 2690
Cdd:COG4717 506 REEYREERLP 515
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1392-1440 |
2.36e-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: 2.36e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 1392 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFPNCRPCDC 1440
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1531-1579 |
3.67e-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: 66.22 E-value: 3.67e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 1531 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSLDAANPKGC 1579
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2919-3053 |
4.51e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 68.91 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2919 RFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGLKKAVPlQPPPPLTSASKAIQVFLLGgsrKRVLVR 2996
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNDGQWHRVAVERNG---RSVTLS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2997 V---ERATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIKALGK 3053
Cdd:smart00282 77 VdggNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
540-583 |
3.25e-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: 63.53 E-value: 3.25e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217335166 540 PCQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPL 583
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1530-1580 |
9.08e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 9.08e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 1530 PCDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSlDAANPKGCT 1580
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2023-2069 |
9.17e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 9.17e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2023 PCAC-GPAAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQ--GCR 2069
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
587-634 |
9.30e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 9.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFPNCQACTC 634
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2129-2577 |
1.45e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2129 LDDLERAGALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARRLG 2205
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2206 GQ-AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRT----LAEVERLLWEM 2280
Cdd:COG4717 184 EQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2281 RARDLGAPQAAAEAELAAAQRLLA-----RVQEQLSSLWEENQALATQTRDRLAQHEagLMDLREALNRAVDATREAQEL 2355
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLAllfllLAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2356 NSRNQERLEEALQRKQELSRdnatlQATLHAARDTLASVFRLLHSLDqaKEELERLAAsldgartpLLQRMQtfspagsk 2435
Cdd:COG4717 342 LLDRIEELQELLREAEELEE-----ELQLEELEQEIAALLAEAGVED--EEELRAALE--------QAEEYQ-------- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2436 lRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAysriLQAVQAAEDAAGQALQQADHTWATVVRQGLVDR 2515
Cdd:COG4717 399 -ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE----LEELEEELEELREELAELEAELEQLEEDGELAE 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217335166 2516 AQQllanstalEEAMLQEQ-QRLGLVWAALQGARTQLRDVR--AKKDQLEAHIQAAQAMLAMDTD 2577
Cdd:COG4717 474 LLQ--------ELEELKAElRELAEEWAALKLALELLEEAReeYREERLPPVLERASEYFSRLTD 530
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1391-1433 |
1.78e-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: 61.60 E-value: 1.78e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217335166 1391 PCGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFP 1433
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2024-2068 |
1.87e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.87e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 2024 CACGPA-AEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGC 2068
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
541-582 |
2.41e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217335166 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFP 582
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3078-3221 |
2.90e-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: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3078 AMTFHGHGFLRLALSNVAPLTGNVysGFGFHSAQDSALLYYrASPDGLC---QVSLQQGRVSLQL----LRTEVKTQAGF 3150
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSI--SFSFRTTSPNGLLLY-AGSQNGGdflALELEDGRLVLRYdlgsGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 3151 ADGAPHYVAFYSNATGVWLYVDD--QLQQMKPHRGPPPELqpqpegPPRLLLGGLPESG------TIYNFSGCISNVFV 3221
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGerVVESGSPGGSALLNL------DGPLYLGGLPEDLkspglpVSPGFVGCIRDLKV 150
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
541-589 |
3.31e-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: 60.83 E-value: 3.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPLCQLCGC 589
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1977-2021 |
3.56e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.56e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217335166 1977 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGcGGC 2021
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP-PGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1482-1533 |
3.62e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217335166 1482 CNCSGPGIqelTDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYPRCRPCDC 1533
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1531-1579 |
4.29e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 4.29e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 1531 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFsldAANPKGC 1579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1922-1975 |
4.51e-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: 60.45 E-value: 4.51e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 1922 PCDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGNCT 1975
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1976-2022 |
5.12e-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: 5.12e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1976 RCDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCG-GCR 2022
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1977-2021 |
6.38e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 6.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217335166 1977 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCGGC 2021
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
494-541 |
7.56e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 7.56e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217335166 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPC 541
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1482-1526 |
8.59e-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: 8.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 1482 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1526
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. |
2024-2071 |
9.16e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 9.16e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 2024 CACGP-AAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGCRRC 2071
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1482-1526 |
1.44e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 1.44e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 1482 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1526
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1392-1435 |
2.11e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 2.11e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 1392 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWG--FPNC 1435
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2157-2688 |
2.36e-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: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGgqavgtrDQASQLLAGTEATLGHAKTLLAAI 2236
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE-------EKLEELKEELESLEAELEELEAEL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2237 RAVDRTLSELmsQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLWEE 2316
Cdd:TIGR02168 368 EELESRLEEL--EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2317 NQALAtQTRDRLAQHEAGLMDLREALNRA----VDATREAQELNSRnQERLEEALQRKQELSRDNATL---QATLHAARD 2389
Cdd:TIGR02168 446 EEELE-ELQEELERLEEALEELREELEEAeqalDAAERELAQLQAR-LDSLERLQENLEGFSEGVKALlknQSGLSGILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2390 TLASVFR--------------------LLHSLDQAKEELERLAASLDGARTPLL---------------QRMQTFSPAGS 2434
Cdd:TIGR02168 524 VLSELISvdegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndreILKNIEGFLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2435 KLRLVEAAEAhAQQLGQLALNLSSIILDVNQ----------------------------------------------DRL 2468
Cdd:TIGR02168 604 AKDLVKFDPK-LRKALSYLLGGVLVVDDLDNalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrreiEEL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2469 TQRAIEASNAYSRILQAVQAAE---DAAGQALQQADHTWATVVRQglVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQ 2545
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQ--ISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2546 GARTQLRDVRAK----KDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDT---ATRVQSQLQAMQENVERWQGQY 2618
Cdd:TIGR02168 761 AEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRL 840
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 2619 EGLRGQ--DLGQAVLDAGHSVSTLEKTLPQLLAKLSILEN-RGVHNASLALSASigRVRELIAQARGAASKVK 2688
Cdd:TIGR02168 841 EDLEEQieELSEDIESLAAEIEELEELIEELESELEALLNeRASLEEALALLRS--ELEELSEELRELESKRS 911
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
494-543 |
4.38e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.36 E-value: 4.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 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 |
6.20e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 6.20e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPCQC 543
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
632-679 |
7.57e-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: 56.98 E-value: 7.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHGFPSCVPGSC 679
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
587-627 |
7.68e-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: 7.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217335166 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFP 627
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2128-2568 |
1.01e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2128 LLDDLERAGALlpaihEQLRGiNASSmawARL--HRLNASIADLQSQLRSPLGPRHETA--QQLEVLEQQSTSLGQDARR 2203
Cdd:PRK02224 154 MIDDLLQLGKL-----EEYRE-RASD---ARLgvERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2204 LGGQ---AVGTRDQASQLLAGTEATLGHAKTLLAAIRAV---------------------DRTLSELMSQTGHL----GL 2255
Cdd:PRK02224 225 YEEQreqARETRDEADEVLEEHEERREELETLEAEIEDLretiaeterereelaeevrdlRERLEELEEERDDLlaeaGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2256 ANASAPSGEQLLRTL----AEVERLLWEMRArDLGAPQAAAEAELAAAQRLLAR---VQEQLSSLWEENQALATQTRDR- 2327
Cdd:PRK02224 305 DDADAEAVEARREELedrdEELRDRLEECRV-AAQAHNEEAESLREDADDLEERaeeLREEAAELESELEEAREAVEDRr 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2328 --LAQHEAGLMDLREALNRAVDATREAQElnsrnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLL------- 2398
Cdd:PRK02224 384 eeIEELEEEIEELRERFGDAPVDLGNAED-------FLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2399 ---------H--SLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSklrLVEaAEAHAQQLGQLALNLSSIILD----V 2463
Cdd:PRK02224 457 cgqpvegspHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED---LVE-AEDRIERLEERREDLEELIAErretI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2464 NQDRLtqrAIEASNAYSRILQA-VQAAEDAAGQALQQADHTWATVV-----RQGLVDRAQQL--LANSTALEEAMLQEQQ 2535
Cdd:PRK02224 533 EEKRE---RAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnskLAELKERIESLerIRTLLAAIADAEDEIE 609
|
490 500 510
....*....|....*....|....*....|....*..
gi 2217335166 2536 RLGLVWAALQG----ARTQLRDVRAKKDQLEAHIQAA 2568
Cdd:PRK02224 610 RLREKREALAElndeRRERLAEKRERKRELEAEFDEA 646
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
729-781 |
2.80e-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: 2.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 729 RCSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGlDQADYFGCR 781
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2690-2855 |
3.03e-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: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2690 PMKFNGRSGVQLRTPRDLADlaaYTALKFYLQGPEPEpgqGtedrFVMYMGSrQATGDYMGVSLRDKKVHWVYQLGEaGP 2769
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPN---G----LLLYAGS-QNGGDFLALELEDGRLVLRYDLGS-GS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2770 AVLSIDEDIGE-QFAAVSLDRTLQFGHMSVTVERQMiqetkgDTVAPGAEGLLNLRPDdfvFYVGGYPSTFTPPPLLRFP 2848
Cdd:cd00110 69 LVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPVSP 139
|
....*..
gi 2217335166 2849 GYRGCIE 2855
Cdd:cd00110 140 GFVGCIR 146
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
587-629 |
3.97e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 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. |
1923-1973 |
4.67e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.67e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 1923 CDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGN 1973
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| LamG |
smart00282 |
Laminin G domain; |
3105-3223 |
4.74e-09 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 57.35 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3105 FGFHSAQDSALLYYRASPDG---LcQVSLQQGRVSLQLLR--TEVKTQAG---FADGAPHYVAFYSNATGVWLYVDDQLQ 3176
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGgdyL-ALELRDGRLVLRYDLgsGPARLTSDptpLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 3177 QMKPHRGPPPELQPqpegPPRLLLGGLPESG------TIYNFSGCISNVFVQR 3223
Cdd:smart00282 83 VSGESPGGLTILNL----DGPLYLGGLPEDLklpplpVTPGFRGCIRNLKVNG 131
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2157-2650 |
7.28e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.15 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRSPLGPRHEtaQQLEVLEQQSTSLGQDARRLGGQAvgtRDQASQLL-------AGTEATLgHA 2229
Cdd:NF041483 50 AKLHEARRSLASRPAYDGADIGYQAE--QLLRNAQIQADQLRADAERELRDA---RAQTQRILqehaehqARLQAEL-HT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2230 KTLLAAIRaVDRTLSElMSQT--GHLglaNASAPSGEQL-LRTLAEVERLLWEMRARdlgaPQAAAEAELAAAQRLLARV 2306
Cdd:NF041483 124 EAVQRRQQ-LDQELAE-RRQTveSHV---NENVAWAEQLrARTESQARRLLDESRAE----AEQALAAARAEAERLAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEENQALATQTRDRlAQHEAGLMdLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRD-NATLQATLH 2385
Cdd:NF041483 195 RQRLGSEAESARAEAEAILRR-ARKDAERL-LNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAaEQRMQEAEE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2386 AARDTLASVFRLlhsLDQAKEELERLAASLDGARTpllQRMQTfspAGSKL-RLV-------EAAEAHAQQLGQLAlnls 2457
Cdd:NF041483 273 ALREARAEAEKV---VAEAKEAAAKQLASAESANE---QRTRT---AKEEIaRLVgeatkeaEALKAEAEQALADA---- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2458 siilDVNQDRLTQRAIEASNAysrilqavQAAEDAAGQaLQQADHTwatvvrqglvdrAQQLLanSTALEEAmlQEQQRl 2537
Cdd:NF041483 340 ----RAEAEKLVAEAAEKART--------VAAEDTAAQ-LAKAART------------AEEVL--TKASEDA--KATTR- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2538 glvwAALQGARTQLRDVRAKKDQL--EAHIQAAQAMLAM--DTDETSKKIahakavaaeaqdtatrVQsqlqaMQENVER 2613
Cdd:NF041483 390 ----AAAEEAERIRREAEAEADRLrgEAADQAEQLKGAAkdDTKEYRAKT----------------VE-----LQEEARR 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2217335166 2614 WQGQYEGLRGQDL-------GQAVLDAGHSVSTLEKTLPQLLAK 2650
Cdd:NF041483 445 LRGEAEQLRAEAVaegerirGEARREAVQQIEEAARTAEELLTK 488
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2924-3049 |
1.05e-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: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2924 LRLVSYSGVLFFLK-QQSQFLCLAVQEGSLVLLYDFGAGlkkavplqpPPPLTSASKAiqvfLLGGSRKRVLVRVERATV 3002
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3003 ySVEQDND-------------LELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3049
Cdd:pfam02210 68 -TLSVDGQtvvsslppgesllLNLNGPLYLGGLPPLLLLPAL----PVRAGFVGCIRDVR 122
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2181-2609 |
1.65e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.00 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2181 HETAQQLEVLEQQST--------SLGQDARRLGGQAVGTRDQAsqlLAGTEATLGHA-KTLLAAIRAVDRTLSELmsqtg 2251
Cdd:NF041483 414 ADQAEQLKGAAKDDTkeyraktvELQEEARRLRGEAEQLRAEA---VAEGERIRGEArREAVQQIEEAARTAEEL----- 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2252 hlgLANASAPSGEqlLRTLA--EVERLLWEM--RARDLgapqaaaeaeLAAAQRLLARVQEQLSSLWEENQALATQTRdr 2327
Cdd:NF041483 486 ---LTKAKADADE--LRSTAtaESERVRTEAieRATTL----------RRQAEETLERTRAEAERLRAEAEEQAEEVR-- 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2328 lAQHEAGLMDLREALNRAV-----DATREAQELNSRNQERL---EEAL----QRKQELSRDNATLQATLhaaRDTLASVF 2395
Cdd:NF041483 549 -AAAERAARELREETERAIaarqaEAAEELTRLHTEAEERLtaaEEALadarAEAERIRREAAEETERL---RTEAAERI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2396 RLLHSldQAKEELERL--AASLDGARTpllqRMQTFSPAgskLRLVEAAEAHAQQLGQLALNlssiildvNQDRLtqRAi 2473
Cdd:NF041483 625 RTLQA--QAEQEAERLrtEAAADASAA----RAEGENVA---VRLRSEAAAEAERLKSEAQE--------SADRV--RA- 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2474 EASNAYSRI-------LQAVQ--------AAEDAAGQALQQADHTwatvvRQGLVDRAQQLLANS-TALEEAMlQEQQRL 2537
Cdd:NF041483 685 EAAAAAERVgteaaeaLAAAQeeaarrrrEAEETLGSARAEADQE-----RERAREQSEELLASArKRVEEAQ-AEAQRL 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2538 ---------GLVWAALQGARtQLRD-VRAKKDQLEAHIQAAQAMLAMDTDETSKKiahakavaaeAQDTATRVQSQLQAM 2607
Cdd:NF041483 759 veeadrratELVSAAEQTAQ-QVRDsVAGLQEQAEEEIAGLRSAAEHAAERTRTE----------AQEEADRVRSDAYAE 827
|
..
gi 2217335166 2608 QE 2609
Cdd:NF041483 828 RE 829
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
730-780 |
1.73e-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: 53.13 E-value: 1.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 730 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGLDQADYFGC 780
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2301-2613 |
2.65e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQEQLSSLWEENQALatqtRDRLA-------------QHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL 2367
Cdd:PRK04863 314 RELAELNEAESDLEQDYQAA----SDHLNlvqtalrqqekieRYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2368 QRKQELSRDNATLQATL----------HAARDTLASVFRLLH----SLDQAKEELERLAASLDGARTPLLQrmqtfspAG 2433
Cdd:PRK04863 390 EEVDELKSQLADYQQALdvqqtraiqyQQAVQALERAKQLCGlpdlTADNAEDWLEEFQAKEQEATEELLS-------LE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2434 SKLRLveaAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYS--RILQAVQAAEDAAGQALQQADHTWATVVRqg 2511
Cdd:PRK04863 463 QKLSV---AQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLReqRHLAEQLQQLRMRLSELEQRLRQQQRAER-- 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2512 LVDRAQQLLANSTALEEAMLQEQQRLGlvwAALQGARTQLRDV-------RAKKDQLEAHIQ----------AAQAMLAM 2574
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELE---ARLESLSESVSEArerrmalRQQLEQLQARIQrlaarapawlAAQDALAR 614
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2217335166 2575 ------DTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVER 2613
Cdd:PRK04863 615 lreqsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
730-771 |
2.65e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.65e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217335166 730 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFG 771
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. |
1867-1920 |
2.94e-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: 52.36 E-value: 2.94e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 1867 CPCPLSVPSNnfaEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVLGSSC 1920
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1817-1853 |
6.29e-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: 51.59 E-value: 6.29e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2217335166 1817 PCQCHGH---SDRCLPGSGVCVdCQHNTEGAHCERCQAGF 1853
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1818-1867 |
8.40e-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: 51.20 E-value: 8.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 1818 CQCHGH---SDRCLPGSGVCvDCQHNTEGAHCERCQAGFVssrDDPSAPCVSC 1867
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYY---GLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2737-2855 |
9.71e-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: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2737 MYMGSRQatGDYMGVSLRDKKVHWVYQLGEAGPAVLSIDEDI--GeQFAAVSLDRTLQFGHMSVTverqmiQETKGDTVA 2814
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGNTLTLSVD------GQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2217335166 2815 PGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIE 2855
Cdd:pfam02210 82 PGESLLLNL---NGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1867-1913 |
9.76e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.76e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217335166 1867 CPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNP 1913
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
782-821 |
1.55e-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: 50.43 E-value: 1.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2217335166 782 SCRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 821
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 |
2.26e-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: 2.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 429 CNC-ESDFTDGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPSCYP 473
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-680 |
2.43e-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: 49.66 E-value: 2.43e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 631 ACTCDPRGALDQLCGAG-GLCRCRPGYTGTACQECSPGFHGFPScVPGSCH 680
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-347 |
2.55e-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: 49.66 E-value: 2.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 299 RCVCHGHADACDAKDPTDpfrLQCTCQHNTCGGTCDRCCPGFNQQPWKP 347
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
428-470 |
2.68e-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: 49.66 E-value: 2.68e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217335166 428 RCNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPS 470
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
429-471 |
6.73e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 6.73e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 429 CNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTG--FPSC 471
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| TorS_sensor_domain |
cd16172 |
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide ... |
2241-2532 |
7.37e-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: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2241 RTLSELMSQTGHLG--LANAsapsgeqllRTLAEverllWEMRARDLGapqaaaeaelaaaqRLLARVQEQLSSLweENQ 2318
Cdd:cd16172 2 RQLSELSSRIIASAqlLANA---------DSEAE-----RQQQGRQLT--------------AQLEALLRLLKAL--GQD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2319 ALATQTRDRLAQHEAGLMDLREALNRAVdatREAQELNSRNQERLEEALQRKQE---LSR---DNATLQATlhaARdtLA 2392
Cdd:cd16172 52 SFDSFLLSRLEQTVQEIIDNLAQLGELV---GQRLQLRQQFQQLFERLRAAAGElaqLARtqvANASTIAV---AN--VS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2393 SVFRLL--HSLDQAKEELERLAA-SLDgartpLLQRMqtfspagSKLRLveaaeaHAQQLGQLALNLSSIildVNQDRLt 2469
Cdd:cd16172 124 GLYDLIeqNDKEAAYQALDRLIEvDLD-----LLERM-------HELRL------LALQLGNLINELRTA---SDIARL- 181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2470 QRAIEASNAYSRILQA-VQAAED-----AAGQALQQADHtwatvvRQGLVDRAQQLLANSTALEEAMLQ 2532
Cdd:cd16172 182 AELRQQFNANLAILQRrVQAVEDpgrraQMAQLLSDLEQ------GQGLFALRRQLLALEQRLQALMQN 244
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
783-821 |
7.42e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 7.42e-07
10 20 30
....*....|....*....|....*....|....*....
gi 2217335166 783 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 821
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
698-727 |
9.55e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 9.55e-07
10 20 30
....*....|....*....|....*....|
gi 2217335166 698 CMCRAHVEGPSCDRCKPGFWGLSPSNPEGC 727
Cdd:pfam00053 20 CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1866-1921 |
9.69e-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: 48.12 E-value: 9.69e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 1866 SCPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVlGSSCQ 1921
Cdd:cd00055 1 PCDCN---GHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1923-1967 |
1.96e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.96e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 1923 CDCSGNGDpnlLFSDCDPLTGACRgCLRHTTGPRCEICAPGFYGN 1967
Cdd:smart00180 1 CDCDPGGS---ASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
632-674 |
3.67e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHG--FPSC 674
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2157-2416 |
4.27e-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: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRsplgpRHETAQQLevLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTL---- 2232
Cdd:TIGR02168 719 KELEELSRQISALRKDLA-----RLEAEVEQ--LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqi 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2233 ---LAAIRAVDRTLSELMSQTGHLGLANASAPSG-EQLLRTLAEVERLLWEM--RARDLGAPQAAAEAELAAAQRLLARV 2306
Cdd:TIGR02168 792 eqlKEELKALREALDELRAELTLLNEEAANLRERlESLERRIAATERRLEDLeeQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEE----NQALATQtRDRLAQHEAglmDLREALNRAVDATREAQELNSRN---QERLEEALQRKQEL-SRDNA 2378
Cdd:TIGR02168 872 ESELEALLNEraslEEALALL-RSELEELSE---ELRELESKRSELRRELEELREKLaqlELRLEGLEVRIDNLqERLSE 947
|
250 260 270
....*....|....*....|....*....|....*...
gi 2217335166 2379 TLQATLHAArdtLASVFRLLHSLDQAKEELERLAASLD 2416
Cdd:TIGR02168 948 EYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIK 982
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
698-728 |
1.32e-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: 45.04 E-value: 1.32e-05
10 20 30
....*....|....*....|....*....|.
gi 2217335166 698 CMCRAHVEGPSCDRCKPGFWGLsPSNPEGCT 728
Cdd:cd00055 21 CECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3107-3221 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3107 FHSAQDSALLYYRAS--PDGLCqVSLQQGRVSLQL-----LRTEVKTQAGFADGAPHYVAF-YSNATGVwLYVDDQlqqm 3178
Cdd:pfam02210 1 FRTRQPNGLLLYAGGggSDFLA-LELVNGRLVLRYdlgsgPESLLSSGKNLNDGQWHSVRVeRNGNTLT-LSVDGQ---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217335166 3179 KPHRGPPPELQPQPEGPPRLLLGGLPESGTIY------NFSGCISNVFV 3221
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPalpvraGFVGCIRDVRV 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1818-1853 |
2.19e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 2.19e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2217335166 1818 CQCHG---HSDRCLPGSGVCvDCQHNTEGAHCERCQAGF 1853
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. |
783-821 |
2.71e-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: 2.71e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2217335166 783 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 821
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
358-421 |
4.08e-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: 43.50 E-value: 4.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217335166 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 |
7.53e-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: 42.73 E-value: 7.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335166 359 CNCYGHATdcyydpevdrrrasqSLDGTYQGGGVCiDCQHHTTGVNCERCLPGFYRSPNhplDSPHVC 426
Cdd:pfam00053 1 CDCNPHGS---------------LSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
698-727 |
9.85e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 9.85e-05
10 20 30
....*....|....*....|....*....|
gi 2217335166 698 CMCRAHVEGPSCDRCKPGFWGlspSNPEGC 727
Cdd:smart00180 20 CECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2071-2099 |
2.20e-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: 2.20e-04
10 20 30
....*....|....*....|....*....|....
gi 2217335166 2071 CQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2099
Cdd:pfam00053 1 CDCNPhgslsDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2070-2099 |
3.37e-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: 3.37e-04
10 20 30
....*....|....*....|....*....|....*
gi 2217335166 2070 RCQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2099
Cdd:cd00055 1 PCDCNGhgslsGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2071-2099 |
3.75e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.75e-04
10 20 30
....*....|....*....|....*....|....
gi 2217335166 2071 CQCP-----GGRCDPHTGRCNCPPGLSGERCDTC 2099
Cdd:smart00180 1 CDCDpggsaSGTCDPDTGQCECKPNVTGRRCDRC 34
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
300-345 |
3.90e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217335166 300 CVCH--GHADacdakDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQPW 345
Cdd:smart00180 1 CDCDpgGSAS-----GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
387-416 |
4.39e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 4.39e-04
10 20 30
....*....|....*....|....*....|
gi 2217335166 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 |
1.33e-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: 39.26 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 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 |
6.39e-98 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 315.68 E-value: 6.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 45 LHPPYFNLAEGARIAASATCGEEAPargsprpteDLYCKLVGGPvaggdpnqtiRGQYCDICTAANSNKAHPASNAIDGT 124
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGP---------ERYCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 125 ER----WWQSPPLSrgLEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSMDFGRTYQPWQFFASskrDCLERFG 200
Cdd:pfam00055 62 NGtnetWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 201 -PQTLERITRDDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLmgkaLR 279
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 2217335166 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 ... |
2146-2404 |
4.67e-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: 4.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2146 LRGINASSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEAT 2225
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2226 LGHAKTLLAAIRAVDRTLSELMSQTGHLGLaNASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLAR 2305
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE-NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2306 VQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLH 2385
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 2217335166 2386 AARDTLASVFRLLHSLDQA 2404
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-298 |
5.35e-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: 305.05 E-value: 5.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 44 SLHPPYFNLAEGARIAASATCGEEAPARgsprptedlYCKLVGGpvaggdpnqTIRGQYCDICTAANSNKAHPASNAIDG 123
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 124 TE----RWWQSPPLSRGLEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSmDFGRTYQPWQFFASskrDCLERF 199
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 200 GPQTLERITR--DDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLMGKA 277
Cdd:smart00136 141 GRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 2217335166 278 lrdPTVTRRYYYSIKDISIGG 298
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1647-1783 |
5.06e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 168.99 E-value: 5.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1647 YWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVfvPMESRPDVVLQGNQMSITFLEPA--YPTPGHVHRGQLQLVEGNFR 1724
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSSPDqpPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 1725 HTeTRNTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASPAGQGALASNVE 1783
Cdd:pfam00052 79 DS-DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1643-1772 |
2.06e-44 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 158.19 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1643 FPELYWQAPPSYLGDRVSSYGGTLRYELHSETQRGDVFVpmeSRPDVVLQGNQMSITFLEPAYPTPGHVHRGQLQLVEGN 1722
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHV---SAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1723 FRHTETRnTVSREELMMVLASLEQLQIRALFSQISSAVFLRRVALEVASP 1772
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 ... |
2595-2716 |
2.41e-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: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2595 DTATRVQSQLQAMQENVERWQGQYEGLRGQ---------DLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLa 2665
Cdd:pfam06009 10 ETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 2666 lSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTPRDLADLAAYTAL 2716
Cdd:pfam06009 89 -SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3294-3451 |
4.38e-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: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3294 SYQFGGSlsSHLEFVGiLARHRNWPSLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQR 3373
Cdd:cd00110 1 GVSFSGS--SYVRLPT-LPAPRTRLSISFSFRTTSPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335166 3374 SRPGRWHKVSVRWEKNRILLVTDGARAWSQEGPHRQHQGaehPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLH 3451
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALL---NLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3475-3625 |
1.02e-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: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3475 GLFFPGSGGViTLDLPGATLPDVGLELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGefSTSVTRPSVL 3554
Cdd:cd00110 1 GVSFSGSSYV-RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 3555 CDGQWHRLAVMKSGNVLRLEVD-AQSNHTVGPLLAAAAGAPAPLYLGGLPEPMAV--QPWPPAYCGCMRRLAVN 3625
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSpgLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3319-3453 |
1.76e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 104.34 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3319 SLSMHVLPRSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQRS-RPGRWHKVSVRWEKNRILLVTDG 3397
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 3398 ARAWSQEGPhRQHQGAEHPQPhtLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3453
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 ... |
3326-3453 |
1.63e-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: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3326 PRSSRGLLLFTARLRpgSPSLALFLSNGHFVAQME-GLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQE 3404
Cdd:pfam02210 3 TRQPNGLLLYAGGGG--SDFLALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217335166 3405 GPHRQHQgaeHPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGR 3453
Cdd:pfam02210 81 PPGESLL---LNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3499-3626 |
1.69e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 92.79 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3499 LELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEFSTSVTRPSVlCDGQWHRLAVMKSGNVLRLEVDAQ 3578
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPL-NDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 3579 SN-HTVGPLLAAAAGAPAPLYLGGLPEPM--AVQPWPPAYCGCMRRLAVNR 3626
Cdd:smart00282 81 NRvSGESPGGLTILNLDGPLYLGGLPEDLklPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3503-3625 |
9.03e-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: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3503 VRPLAVTGLIFHLGQARTPpYLQLQVTEKQVLLRADDGAGEFSTSVTrPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHT 3582
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSS-GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2217335166 3583 VGPLLAAAAGAPAPL-YLGGLPEP--MAVQPWPPAYCGCMRRLAVN 3625
Cdd:pfam02210 79 SLPPGESLLLNLNGPlYLGGLPPLllLPALPVRAGFVGCIRDVRVN 124
|
|
| LamG |
smart00282 |
Laminin G domain; |
2735-2862 |
1.68e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.84 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2735 FVMYMGSRQaTGDYMGVSLRDKKVHWVYQLGeAGPAVLSIDEDI---GeQFAAVSLDRTLQFGHMSVTVERQMIQETkgd 2811
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPTPlndG-QWHRVAVERNGRSVTLSVDGGNRVSGES--- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 2812 tvaPGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIEMDTLNEE 2862
Cdd:smart00282 88 ---PGGLTILNL---DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2301-2573 |
9.46e-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: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATL 2380
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2381 QATLHAARDTLAsvfRLLHSLDQAKEELERLAASLDGARTPLLQRmqtfspAGSKLRLVEAAEAHAQQLGQLALNLSSII 2460
Cdd:COG1196 329 EEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2461 LDVNQDRLTQRAIEASNAysRILQAVQAAEDAAGQALQQADHTwatvvrQGLVDRAQQLLANSTALEEAMLQEQQRLGlv 2540
Cdd:COG1196 400 AQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEE------EEALEEAAEEEAELEEEEEALLELLAELL-- 469
|
250 260 270
....*....|....*....|....*....|...
gi 2217335166 2541 wAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2573
Cdd:COG1196 470 -EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2897-3049 |
3.02e-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: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2897 GSYLDGTGFARISFDSQISTTKRFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGlkkAVPLQPPPPL 2974
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSG---SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2975 -TSASKAIQVFLLGgsrKRVLVRVER---ATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3049
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 ... |
2160-2649 |
8.03e-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: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2160 HRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAV 2239
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2240 DRTLSELMSQTGHL--GLANasapsgEQLLRTLAEVERllwemraRDLGAPQAAAEAELAAAQRLLArVQEQLSSLWEE- 2316
Cdd:pfam01576 263 LKKIRELEAQISELqeDLES------ERAARNKAEKQR-------RDLGEELEALKTELEDTLDTTA-AQQELRSKREQe 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2317 ----NQALATQTRdrlaQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAlqrKQELSRDNATLQATlhaardtla 2392
Cdd:pfam01576 329 vtelKKALEEETR----SHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKA---KQALESENAELQAE--------- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2393 svfrlLHSLDQAKEELERLAASLDGArtplLQRMQTFSPAGSKLRlVEAAEahaqQLGQLALNLSSI--ILDVNQDRLTQ 2470
Cdd:pfam01576 393 -----LRTLQQAKQDSEHKRKKLEGQ----LQELQARLSESERQR-AELAE----KLSKLQSELESVssLLNEAEGKNIK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2471 RAIEASNAYSRiLQAVQaaedaagQALQQadhtwatvvrqglvdRAQQLLANSTALEEAmlqEQQRLGLvwaalqgaRTQ 2550
Cdd:pfam01576 459 LSKDVSSLESQ-LQDTQ-------ELLQE---------------ETRQKLNLSTRLRQL---EDERNSL--------QEQ 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2551 LRDVRAKKDQLEAHIQAAQAMLAmdtdETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRG------Q 2624
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLS----DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtknrlqQ 580
|
490 500 510
....*....|....*....|....*....|.
gi 2217335166 2625 DLGQAVLDAGHS---VSTLEK---TLPQLLA 2649
Cdd:pfam01576 581 ELDDLLVDLDHQrqlVSNLEKkqkKFDQMLA 611
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2127-2690 |
1.81e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.73 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2127 LLLDDLERAGALLPAIHEQLRGINAssmawARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARR 2203
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNL-----KELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2204 LggqavgtrDQASQLLAgteatlghaktLLAAIRAVDRTLSELMSQTghlglanasapsgEQLLRTLAEVERLLWEMRAR 2283
Cdd:COG4717 121 L--------EKLLQLLP-----------LYQELEALEAELAELPERL-------------EELEERLEELRELEEELEEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2284 DlgapqaaaeaelaaaqRLLARVQEQLSSLWEEnqaLATQTRDRLAqheaglmDLREALNRAVDATREAQELNSRNQERL 2363
Cdd:COG4717 169 E----------------AELAELQEELEELLEQ---LSLATEEELQ-------DLAEELEELQQRLAELEEELEEAQEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2364 EEALQRKQELSRD--NATLQATLHAARdTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEA 2441
Cdd:COG4717 223 EELEEELEQLENEleAAALEERLKEAR-LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2442 AEAHAQQLGQLALNLSSIILdvnQDRLTQRAIEASNAYSRILQAVQAAEDAAgQALQQADHTWATVVRQGLVDRAQQLLA 2521
Cdd:COG4717 302 KEAEELQALPALEELEEEEL---EELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIAALLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2522 NSTALEEAMLQEqqrlglvWAALQGARTQLR-DVRAKKDQLEAHIQAAQAMLAMDTDETskkiahakavaaeAQDTATRV 2600
Cdd:COG4717 378 EAGVEDEEELRA-------ALEQAEEYQELKeELEELEEQLEELLGELEELLEALDEEE-------------LEEELEEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2601 QSQLQAMQENVERWQGQYEGLRGQdlgQAVLDAGHSVSTLEKTLPQLLAKLSILENRgvhNASLALsasigrVRELIAQA 2680
Cdd:COG4717 438 EEELEELEEELEELREELAELEAE---LEQLEEDGELAELLQELEELKAELRELAEE---WAALKL------ALELLEEA 505
|
570
....*....|
gi 2217335166 2681 RGAASKVKVP 2690
Cdd:COG4717 506 REEYREERLP 515
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1392-1440 |
2.36e-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: 2.36e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 1392 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFPNCRPCDC 1440
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1531-1579 |
3.67e-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: 66.22 E-value: 3.67e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 1531 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSLDAANPKGC 1579
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2919-3053 |
4.51e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 68.91 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2919 RFEQELRLVSYSGVLFFL--KQQSQFLCLAVQEGSLVLLYDFGAGLKKAVPlQPPPPLTSASKAIQVFLLGgsrKRVLVR 2996
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNDGQWHRVAVERNG---RSVTLS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2997 V---ERATVYSVEQDNDLELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIKALGK 3053
Cdd:smart00282 77 VdggNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3503-3629 |
9.68e-13 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 67.73 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3503 VRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEfsTSVTRPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHT 3582
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGA--AVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 3583 VGPLLAAAAG--APAPLYLGGLPEpMAVQPWP----PAYCGCMRRLAVNRSPV 3629
Cdd:pfam00054 79 GESPLGATTDldVDGPLYVGGLPS-LGVKKRRlaisPSFDGCIRDVIVNGKPL 130
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2157-2681 |
2.42e-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: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRsPLGPRHETAQ-------QLEVLEQQSTSL-----GQDARRLGGQAVGTRDQASQL---LAG 2221
Cdd:COG1196 186 ENLERLEDILGELERQLE-PLERQAEKAEryrelkeELKELEAELLLLklrelEAELEELEAELEELEAELEELeaeLAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2222 TEATLGHAKTLLAAIR-AVDRTLSELMSQTGHLG-LANASAPSGEQLLRTLAEVERLLWEMRArdlgapqaaaeaelaaa 2299
Cdd:COG1196 265 LEAELEELRLELEELElELEEAQAEEYELLAELArLEQDIARLEERRRELEERLEELEEELAE----------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2300 qrLLARVQEQLSSLwEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNAT 2379
Cdd:COG1196 328 --LEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2380 LQATLHAARDTLAsvfRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFspAGSKLRLVEAAEAHAQQLGQLALNLSSI 2459
Cdd:COG1196 405 LEEAEEALLERLE---RLEEELEELEEALAELEEEEEEEEEALEEAAEEE--AELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2460 I-LDVNQDRLTQRA---IEASNAYSRILQAVQAAEDAAGQALQQADH----TWATVVRQGLVDRAQQLLAN------STA 2525
Cdd:COG1196 480 AeLLEELAEAAARLlllLEAEADYEGFLEGVKAALLLAGLRGLAGAVavliGVEAAYEAALEAALAAALQNivveddEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2526 LEEAMLQEQQRLGLVwAALQGARTQLRDVRAKKDQLEAhIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQ 2605
Cdd:COG1196 560 AAAIEYLKAAKAGRA-TFLPLDKIRARAALAAALARGA-IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 2606 AMQENVERWQGqyEGLRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQAR 2681
Cdd:COG1196 638 RAVTLAGRLRE--VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
540-583 |
3.25e-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: 63.53 E-value: 3.25e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217335166 540 PCQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPL 583
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1530-1580 |
9.08e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 9.08e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 1530 PCDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFSlDAANPKGCT 1580
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2023-2069 |
9.17e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 9.17e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2023 PCAC-GPAAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQ--GCR 2069
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
587-634 |
9.30e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 9.30e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFPNCQACTC 634
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2129-2577 |
1.45e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2129 LDDLERAGALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQ---LRSPLGPRHETAQQLEVLEQQSTSLGQDARRLG 2205
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2206 GQ-AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRT----LAEVERLLWEM 2280
Cdd:COG4717 184 EQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2281 RARDLGAPQAAAEAELAAAQRLLA-----RVQEQLSSLWEENQALATQTRDRLAQHEagLMDLREALNRAVDATREAQEL 2355
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLAllfllLAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2356 NSRNQERLEEALQRKQELSRdnatlQATLHAARDTLASVFRLLHSLDqaKEELERLAAsldgartpLLQRMQtfspagsk 2435
Cdd:COG4717 342 LLDRIEELQELLREAEELEE-----ELQLEELEQEIAALLAEAGVED--EEELRAALE--------QAEEYQ-------- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2436 lRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAysriLQAVQAAEDAAGQALQQADHTWATVVRQGLVDR 2515
Cdd:COG4717 399 -ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE----LEELEEELEELREELAELEAELEQLEEDGELAE 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217335166 2516 AQQllanstalEEAMLQEQ-QRLGLVWAALQGARTQLRDVR--AKKDQLEAHIQAAQAMLAMDTD 2577
Cdd:COG4717 474 LLQ--------ELEELKAElRELAEEWAALKLALELLEEAReeYREERLPPVLERASEYFSRLTD 530
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1391-1433 |
1.78e-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: 61.60 E-value: 1.78e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217335166 1391 PCGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWGFP 1433
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2024-2068 |
1.87e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.87e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 2024 CACGPA-AEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGC 2068
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
541-582 |
2.41e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217335166 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFP 582
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3078-3221 |
2.90e-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: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3078 AMTFHGHGFLRLALSNVAPLTGNVysGFGFHSAQDSALLYYrASPDGLC---QVSLQQGRVSLQL----LRTEVKTQAGF 3150
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSI--SFSFRTTSPNGLLLY-AGSQNGGdflALELEDGRLVLRYdlgsGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 3151 ADGAPHYVAFYSNATGVWLYVDD--QLQQMKPHRGPPPELqpqpegPPRLLLGGLPESG------TIYNFSGCISNVFV 3221
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGerVVESGSPGGSALLNL------DGPLYLGGLPEDLkspglpVSPGFVGCIRDLKV 150
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2339-2680 |
3.12e-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: 69.98 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2339 REALNRAVDATRE---AQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASV---FRLLHSLDQAKEELERLA 2412
Cdd:COG3096 281 RELSERALELRRElfgARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVqtaLRQQEKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2413 ASLdgartpllqRMQTFSPAGSKLRLVEA-AEAHAQQL------GQLAlnlssiilDVNQ--DRLTQRAIeasnAYSril 2483
Cdd:COG3096 361 ERL---------EEQEEVVEEAAEQLAEAeARLEAAEEevdslkSQLA--------DYQQalDVQQTRAI----QYQ--- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2484 QAVQAAEDAAGQaLQQADHTWAtvvrqGLVDRAQQLLANSTALEEAMLQEQQRLGLVWA--------------------- 2542
Cdd:COG3096 417 QAVQALEKARAL-CGLPDLTPE-----NAEDYLAAFRAKEQQATEEVLELEQKLSVADAarrqfekayelvckiagever 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2543 --ALQGARTQLRDVRakkdQLEAHIQAAQAmLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAmQENVERWQGQYEG 2620
Cdd:COG3096 491 sqAWQTARELLRRYR----SQQALAQRLQQ-LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEA 564
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2621 LRgQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGvhNASLALSASIGRVRELIAQA 2680
Cdd:COG3096 565 QL-EELEEQAAEAVEQRSELRQQLEQLRARIKELAARA--PAWLAAQDALERLREQSGEA 621
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
541-589 |
3.31e-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: 60.83 E-value: 3.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 541 CQCSSPGVADDRCDPDTGQCRCRVGFEGATCDRCAPGYFHFPLCQLCGC 589
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1977-2021 |
3.56e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.56e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217335166 1977 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGcGGC 2021
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP-PGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1482-1533 |
3.62e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217335166 1482 CNCSGPGIqelTDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYPRCRPCDC 1533
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1531-1579 |
4.29e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 4.29e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 1531 CDCHEAGTAPGVCDPLTGQCYCKENVQGPKCDQCSLGTFsldAANPKGC 1579
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1922-1975 |
4.51e-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: 60.45 E-value: 4.51e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 1922 PCDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGNCT 1975
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1976-2022 |
5.12e-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: 5.12e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1976 RCDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCG-GCR 2022
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1977-2021 |
6.38e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 6.38e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217335166 1977 CDCTPCGT--EACDPHSGHCLCKAGVTGRRCDRCQEGHFGFDGCGGC 2021
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
494-541 |
7.56e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 7.56e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217335166 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPC 541
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1482-1526 |
8.59e-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: 8.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 1482 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1526
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. |
2024-2071 |
9.16e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 9.16e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 2024 CACGP-AAEGSECHPQSGQCHCRPGTMGPQCRECAPGYWGLPEQGCRRC 2071
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2128-2501 |
1.13e-10 |
|
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: 68.06 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2128 LLDDLERAGALLPAIHEQLrginasSMAWARLHRLNASIADLQSQLrsplgprhetAQQLEVLEQQSTSLGQDArrlggQ 2207
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQL------AEAEARLEAAEEEVDSLKSQL----------ADYQQALDVQQTRAIQYQ-----Q 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2208 AVGTRDQASQLLAGTEATLGHAKTLLAAIRA-VDRTLSELMSQTGHLGLANASAPSGE---QLLRTLA-EVERL-LWEmR 2281
Cdd:COG3096 418 AVQALEKARALCGLPDLTPENAEDYLAAFRAkEQQATEEVLELEQKLSVADAARRQFEkayELVCKIAgEVERSqAWQ-T 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2282 ARDLgapqaaaeaelaaaqrlLARvqeqlsslWEENQALAtqtrDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQE 2361
Cdd:COG3096 497 AREL-----------------LRR--------YRSQQALA----QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2362 RLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASldgartpllqrmqtfSPAGSKLRlvEA 2441
Cdd:COG3096 548 QLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR---------------APAWLAAQ--DA 610
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2442 AEAHAQQLGQlALNLSSIILDVNQdRLTQRAIEASNAYSRILQAVQAAEDAAGQaLQQAD 2501
Cdd:COG3096 611 LERLREQSGE-ALADSQEVTAAMQ-QLLEREREATVERDELAARKQALESQIER-LSQPG 667
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1482-1526 |
1.44e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 1.44e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 1482 CNCSGPGIQeltDPTCDTDSGQCKCRPNVTGRRCDTCSPGFHGYP 1526
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1392-1435 |
2.11e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 2.11e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 1392 CGCHEVGATGPTCEPFGGQCPCHAHVIGRDCSRCATGYWG--FPNC 1435
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2157-2688 |
2.36e-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: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGgqavgtrDQASQLLAGTEATLGHAKTLLAAI 2236
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE-------EKLEELKEELESLEAELEELEAEL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2237 RAVDRTLSELmsQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLWEE 2316
Cdd:TIGR02168 368 EELESRLEEL--EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2317 NQALAtQTRDRLAQHEAGLMDLREALNRA----VDATREAQELNSRnQERLEEALQRKQELSRDNATL---QATLHAARD 2389
Cdd:TIGR02168 446 EEELE-ELQEELERLEEALEELREELEEAeqalDAAERELAQLQAR-LDSLERLQENLEGFSEGVKALlknQSGLSGILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2390 TLASVFR--------------------LLHSLDQAKEELERLAASLDGARTPLL---------------QRMQTFSPAGS 2434
Cdd:TIGR02168 524 VLSELISvdegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndreILKNIEGFLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2435 KLRLVEAAEAhAQQLGQLALNLSSIILDVNQ----------------------------------------------DRL 2468
Cdd:TIGR02168 604 AKDLVKFDPK-LRKALSYLLGGVLVVDDLDNalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrreiEEL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2469 TQRAIEASNAYSRILQAVQAAE---DAAGQALQQADHTWATVVRQglVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQ 2545
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQ--ISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2546 GARTQLRDVRAK----KDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDT---ATRVQSQLQAMQENVERWQGQY 2618
Cdd:TIGR02168 761 AEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRL 840
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 2619 EGLRGQ--DLGQAVLDAGHSVSTLEKTLPQLLAKLSILEN-RGVHNASLALSASigRVRELIAQARGAASKVK 2688
Cdd:TIGR02168 841 EDLEEQieELSEDIESLAAEIEELEELIEELESELEALLNeRASLEEALALLRS--ELEELSEELRELESKRS 911
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3327-3456 |
2.41e-10 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 60.79 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3327 RSSRGLLLFTARlRPGSPSLALFLSNGHFVAQMEGLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQEGP 3406
Cdd:pfam00054 4 TEPSGLLLYNGT-QTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGESP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2217335166 3407 HRQHQgaeHPQ-PHTLFVGGLP-ASSHSSKLPVTVGFSGCVKRLRLHGRPLG 3456
Cdd:pfam00054 83 LGATT---DLDvDGPLYVGGLPsLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
494-543 |
4.38e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.36 E-value: 4.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYG-PGCQPCQC 543
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPETGQCLCKPGVTGRHCDRCKPGYYGlPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2128-2607 |
5.77e-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: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2128 LLDDLERAGALLPAIHEQLRGINAssmawaRLHRLNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGQDARRLGGQ 2207
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEE------ELEELEEELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2208 AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASApSGEQLLRTLAEVERLLWEMRARDLga 2287
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEALEEAAEEEAELEEE-- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2288 pqaaaeaelaaAQRLLARVQEQLSS--LWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELnsRNQERLEE 2365
Cdd:COG1196 458 -----------EEALLELLAELLEEaaLLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--AGLRGLAG 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2366 ALQrkqELSRDNATLQATLhAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPL-LQRMQTFSPAGSKLRLVEAAEA 2444
Cdd:COG1196 525 AVA---VLIGVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpLDKIRARAALAAALARGAIGAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2445 HAqqLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQG------------- 2511
Cdd:COG1196 601 VD--LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGsrrellaalleae 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2512 -----LVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHA 2586
Cdd:COG1196 679 aeleeLAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
490 500
....*....|....*....|.
gi 2217335166 2587 KAVAAEAQDTATRVQSQLQAM 2607
Cdd:COG1196 759 PPDLEELERELERLEREIEAL 779
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
494-543 |
6.20e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 6.20e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 494 CDCSAAGTQGNACrkDPRVGRCLCKPNFQGTHCELCAPGFYGPGCQPCQC 543
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2315-2622 |
6.53e-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: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2315 EENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLAsv 2394
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2395 fRLLHSLDQAKEELERLAASLDGARTPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSIildvnQDRLTQRAIE 2474
Cdd:TIGR02168 299 -RLEQQKQILRERLANLERQLEELEAQLEELES------KLDELAEELAELEEKLEELKEELESL-----EAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2475 ASNAYSRILQAVQAAEDAAG---QALQQADHTWATVVR-----QGLVDRAQQLLAN----STALEEAMLQE-QQRLGLVW 2541
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSkvaQLELQIASLNNEIERlearlERLEDRRERLQQEieelLKKLEEAELKElQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2542 AALQGARTQLRDVRAKKDQLEAHIQAAQAMLamdtdetskkiahakavaAEAQDTATRVQSQLQAMQENVERWQGQYEGL 2621
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQAL------------------DAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
.
gi 2217335166 2622 R 2622
Cdd:TIGR02168 509 K 509
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
632-679 |
7.57e-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: 56.98 E-value: 7.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHGFPSCVPGSC 679
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
587-627 |
7.68e-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: 7.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217335166 587 CGCSPAGTLPEGCD-EAGRCLCQPEFAGPHCDRCRPGYHGFP 627
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2130-2684 |
9.35e-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: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2130 DDLERAGALLPAIHEQ---LRGINAssmAWARLHRLNASIADLQsQLRSPLgpRHETAQQ-LEVLEQQSTSLGQDARRLG 2205
Cdd:COG4913 235 DDLERAHEALEDAREQielLEPIRE---LAERYAAARERLAELE-YLRAAL--RLWFAQRrLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2206 GQAVGTRDQASQLLAgteatlgHAKTLLAAIRAVDrtlselmsqtghlglanasapsGEQLLRTLAEVERLLWEMRARdl 2285
Cdd:COG4913 309 AELERLEARLDALRE-------ELDELEAQIRGNG----------------------GDRLEQLEREIERLERELEER-- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2286 gapqaaaeaelaaaQRLLARVQEQLSSL----------WEENQALATQTRDRLAQHEAglmDLREALNRAVDATREAQEl 2355
Cdd:COG4913 358 --------------ERRRARLEALLAALglplpasaeeFAALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRR- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2356 nsrnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHS--------LDQAKEELE-RLAAS--LDGARTPLLQ 2424
Cdd:COG4913 420 ------ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgelIEVRPEEERwRGAIErvLGGFALTLLV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2425 RMQTFSPAGS-------KLRLV-EAAEAHAQQLGQLALNLSSIIldvnqDRLTQRAIEASNAYSRILQ---AVQAAEDAa 2493
Cdd:COG4913 494 PPEHYAAALRwvnrlhlRGRLVyERVRTGLPDPERPRLDPDSLA-----GKLDFKPHPFRAWLEAELGrrfDYVCVDSP- 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2494 gQALQQadHTWAtVVRQGLV---------------DRAQQLLANSTALEEAMLQEQQRLGlvwAALQGARTQLRDVRAKK 2558
Cdd:COG4913 568 -EELRR--HPRA-ITRAGQVkgngtrhekddrrriRSRYVLGFDNRAKLAALEAELAELE---EELAEAEERLEALEAEL 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2559 DQLEAHIQAAQAMLAM-----DTDETSKKIahakavaAEAQDTATRV---QSQLQAMQENVERWQGQYEGLRGQ--DLGQ 2628
Cdd:COG4913 641 DALQERREALQRLAEYswdeiDVASAEREI-------AELEAELERLdasSDDLAALEEQLEELEAELEELEEEldELKG 713
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 2629 AVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSAsigRVRELIAQARGAA 2684
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE---RFAAALGDAVERE 766
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2128-2568 |
1.01e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2128 LLDDLERAGALlpaihEQLRGiNASSmawARL--HRLNASIADLQSQLRSPLGPRHETA--QQLEVLEQQSTSLGQDARR 2203
Cdd:PRK02224 154 MIDDLLQLGKL-----EEYRE-RASD---ARLgvERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2204 LGGQ---AVGTRDQASQLLAGTEATLGHAKTLLAAIRAV---------------------DRTLSELMSQTGHL----GL 2255
Cdd:PRK02224 225 YEEQreqARETRDEADEVLEEHEERREELETLEAEIEDLretiaeterereelaeevrdlRERLEELEEERDDLlaeaGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2256 ANASAPSGEQLLRTL----AEVERLLWEMRArDLGAPQAAAEAELAAAQRLLAR---VQEQLSSLWEENQALATQTRDR- 2327
Cdd:PRK02224 305 DDADAEAVEARREELedrdEELRDRLEECRV-AAQAHNEEAESLREDADDLEERaeeLREEAAELESELEEAREAVEDRr 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2328 --LAQHEAGLMDLREALNRAVDATREAQElnsrnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLL------- 2398
Cdd:PRK02224 384 eeIEELEEEIEELRERFGDAPVDLGNAED-------FLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2399 ---------H--SLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSklrLVEaAEAHAQQLGQLALNLSSIILD----V 2463
Cdd:PRK02224 457 cgqpvegspHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAED---LVE-AEDRIERLEERREDLEELIAErretI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2464 NQDRLtqrAIEASNAYSRILQA-VQAAEDAAGQALQQADHTWATVV-----RQGLVDRAQQL--LANSTALEEAMLQEQQ 2535
Cdd:PRK02224 533 EEKRE---RAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnskLAELKERIESLerIRTLLAAIADAEDEIE 609
|
490 500 510
....*....|....*....|....*....|....*..
gi 2217335166 2536 RLGLVWAALQG----ARTQLRDVRAKKDQLEAHIQAA 2568
Cdd:PRK02224 610 RLREKREALAElndeRRERLAEKRERKRELEAEFDEA 646
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
2127-2555 |
1.59e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 64.27 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2127 LLLDDLERAGALLPAIHEQLRginaSSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGG 2206
Cdd:COG3903 509 LRGPDQLAWLARLDAEHDNLR----AALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAA 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2207 QAVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLG 2286
Cdd:COG3903 585 AAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2287 APQAAAEAELAAAQRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEA 2366
Cdd:COG3903 665 ALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAA 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2367 LQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHA 2446
Cdd:COG3903 745 LALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAA 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2447 QQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTAL 2526
Cdd:COG3903 825 AAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAA 904
|
410 420
....*....|....*....|....*....
gi 2217335166 2527 EEAMLQEQQRLGLVWAALQGARTQLRDVR 2555
Cdd:COG3903 905 LAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2169-2578 |
2.08e-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: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2169 LQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRlggqavgTRDQASQLLAGTEATLGHAKTLLAAIRavdRTLSELMS 2248
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKR-------DREQWERQRRELESRVAELKEELRQSR---EKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2249 QtgHLGLANASApsgeqllrTLAEVERLLWEMRARDlgapqaaaeaelaaaqrlLARVQEqlssLWEENQALATQTRDRl 2328
Cdd:pfam07888 102 K--YKELSASSE--------ELSEEKDALLAQRAAH------------------EARIRE----LEEDIKTLTQRVLER- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2329 aqhEAGLMDLREALNRAVDATREAQELNSRNQERLEealQRKQELSRDNATLQA--TLHAARDTLA-----SVFRLLHSL 2401
Cdd:pfam07888 149 ---ETELERMKERAKKAGAQRKEEEAERKQLQAKLQ---QTEEELRSLSKEFQElrNSLAQRDTQVlqlqdTITTLTQKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2402 DQAKE---ELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQ--------QLGQLALNLSSIILDVNQDRLT- 2469
Cdd:pfam07888 223 TTAHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQaelhqarlQAAQLTLQLADASLALREGRARw 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2470 -------QRAIEASNaySRIL---QAVQAAEdaagQALQQadhtwATVVRQGL-VDRAQQLLANSTALEEAM--LQEQQr 2536
Cdd:pfam07888 303 aqeretlQQSAEADK--DRIEklsAELQRLE----ERLQE-----ERMEREKLeVELGREKDCNRVQLSESRreLQELK- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2217335166 2537 lglvwAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDE 2578
Cdd:pfam07888 371 -----ASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
729-781 |
2.80e-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: 2.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 729 RCSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGlDQADYFGCR 781
Cdd:cd00055 1 PCDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2690-2855 |
3.03e-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: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2690 PMKFNGRSGVQLRTPRDLADlaaYTALKFYLQGPEPEpgqGtedrFVMYMGSrQATGDYMGVSLRDKKVHWVYQLGEaGP 2769
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSPN---G----LLLYAGS-QNGGDFLALELEDGRLVLRYDLGS-GS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2770 AVLSIDEDIGE-QFAAVSLDRTLQFGHMSVTVERQMiqetkgDTVAPGAEGLLNLRPDdfvFYVGGYPSTFTPPPLLRFP 2848
Cdd:cd00110 69 LVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPVSP 139
|
....*..
gi 2217335166 2849 GYRGCIE 2855
Cdd:cd00110 140 GFVGCIR 146
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
587-629 |
3.97e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 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. |
1923-1973 |
4.67e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.67e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 1923 CDCSGNGDPNllfSDCDPLTGACRgCLRHTTGPRCEICAPGFYGNALLPGN 1973
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| LamG |
smart00282 |
Laminin G domain; |
3105-3223 |
4.74e-09 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 57.35 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3105 FGFHSAQDSALLYYRASPDG---LcQVSLQQGRVSLQLLR--TEVKTQAG---FADGAPHYVAFYSNATGVWLYVDDQLQ 3176
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGgdyL-ALELRDGRLVLRYDLgsGPARLTSDptpLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 3177 QMKPHRGPPPELQPqpegPPRLLLGGLPESG------TIYNFSGCISNVFVQR 3223
Cdd:smart00282 83 VSGESPGGLTILNL----DGPLYLGGLPEDLklpplpVTPGFRGCIRNLKVNG 131
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2308-2643 |
5.74e-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: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2308 EQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAA 2387
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2388 RDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMqtfspAGSKLRLVEAAEAHAQQLGQLALNLSSII-LDVNQD 2466
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRI-----AATERRLEDLEEQIEELSEDIESLAAEIEeLEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2467 RLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADhtwatvvrqglvdraqqllanstALEEAMLQEQQrlglvwaALQG 2546
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELR-----------------------ELESKRSELRR-------ELEE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2547 ARTQLRDVRAKKDQLEAHIQAAQAMLA----MDTDETSKKIAHAKAVAAEAQDTATRVQSQLQ--------AMQEnVERW 2614
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaAIEE-YEEL 998
|
330 340 350
....*....|....*....|....*....|.
gi 2217335166 2615 QGQYEGLRGQ--DLGQAvldaghsVSTLEKT 2643
Cdd:TIGR02168 999 KERYDFLTAQkeDLTEA-------KETLEEA 1022
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2157-2650 |
7.28e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.15 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRSPLGPRHEtaQQLEVLEQQSTSLGQDARRLGGQAvgtRDQASQLL-------AGTEATLgHA 2229
Cdd:NF041483 50 AKLHEARRSLASRPAYDGADIGYQAE--QLLRNAQIQADQLRADAERELRDA---RAQTQRILqehaehqARLQAEL-HT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2230 KTLLAAIRaVDRTLSElMSQT--GHLglaNASAPSGEQL-LRTLAEVERLLWEMRARdlgaPQAAAEAELAAAQRLLARV 2306
Cdd:NF041483 124 EAVQRRQQ-LDQELAE-RRQTveSHV---NENVAWAEQLrARTESQARRLLDESRAE----AEQALAAARAEAERLAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEENQALATQTRDRlAQHEAGLMdLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRD-NATLQATLH 2385
Cdd:NF041483 195 RQRLGSEAESARAEAEAILRR-ARKDAERL-LNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAaEQRMQEAEE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2386 AARDTLASVFRLlhsLDQAKEELERLAASLDGARTpllQRMQTfspAGSKL-RLV-------EAAEAHAQQLGQLAlnls 2457
Cdd:NF041483 273 ALREARAEAEKV---VAEAKEAAAKQLASAESANE---QRTRT---AKEEIaRLVgeatkeaEALKAEAEQALADA---- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2458 siilDVNQDRLTQRAIEASNAysrilqavQAAEDAAGQaLQQADHTwatvvrqglvdrAQQLLanSTALEEAmlQEQQRl 2537
Cdd:NF041483 340 ----RAEAEKLVAEAAEKART--------VAAEDTAAQ-LAKAART------------AEEVL--TKASEDA--KATTR- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2538 glvwAALQGARTQLRDVRAKKDQL--EAHIQAAQAMLAM--DTDETSKKIahakavaaeaqdtatrVQsqlqaMQENVER 2613
Cdd:NF041483 390 ----AAAEEAERIRREAEAEADRLrgEAADQAEQLKGAAkdDTKEYRAKT----------------VE-----LQEEARR 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2217335166 2614 WQGQYEGLRGQDL-------GQAVLDAGHSVSTLEKTLPQLLAK 2650
Cdd:NF041483 445 LRGEAEQLRAEAVaegerirGEARREAVQQIEEAARTAEELLTK 488
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2307-2684 |
8.36e-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: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL---------QRKQELSRD- 2376
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHgafldadieTAAADQEQLp 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2377 ---------NATLQATLHAARDTLASVFRL--------------LHS-LDQAKEELERLAAS----LDGARTPLLQRMQt 2428
Cdd:pfam12128 351 swqselenlEERLKALTGKHQDVTAKYNRRrskikeqnnrdiagIKDkLAKIREARDRQLAVaeddLQALESELREQLE- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2429 fspaGSKLRLVEAAEAHAQQLGQLALNLSSII--------LDVNQDRL--TQRAIEASNAYSRILQ----AVQAAEDAAG 2494
Cdd:pfam12128 430 ----AGKLEFNEEEYRLKSRLGELKLRLNQATatpelllqLENFDERIerAREEQEAANAEVERLQselrQARKRRDQAS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2495 QALQQAdHTWATVVRQGLVDRAQQLLANSTALEEAMLQE----QQRLGLVWAALQGARTQL------------------- 2551
Cdd:pfam12128 506 EALRQA-SRRLEERQSALDELELQLFPQAGTLLHFLRKEapdwEQSIGKVISPELLHRTDLdpevwdgsvggelnlygvk 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2552 ---------------RDVRAKKDQLEAHIQAAQAMLAmdtdETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQG 2616
Cdd:pfam12128 585 ldlkridvpewaaseEELRERLDKAEEALQSAREKQA----AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2617 QYEGLR---GQDLGQAVLDAGHSVSTLEKTLPQLLAKL---------SILENRGVHNASL-----ALSASIGRVRELIAQ 2679
Cdd:pfam12128 661 EKQSEKdkkNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkeQKREARTEKQAYWqvvegALDAQLALLKAAIAA 740
|
....*
gi 2217335166 2680 ARGAA 2684
Cdd:pfam12128 741 RRSGA 745
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2303-2570 |
9.28e-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: 61.89 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEqlsslweenqalATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQA 2382
Cdd:COG3096 336 LNLVQT------------ALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2383 TL----------HAARDTLASVFRLLH----SLDQAKEELERLAASLDGARTPLLQRMQtfspagsKLRLveaAEAHAQQ 2448
Cdd:COG3096 404 ALdvqqtraiqyQQAVQALEKARALCGlpdlTPENAEDYLAAFRAKEQQATEEVLELEQ-------KLSV---ADAARRQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2449 LGQ-LALnLSSIILDVNQDRLTQRAIEASNAYsRILQAVQAAEDAAGQAL---QQADHTWATVVRQ--GLVDRAQQLLAN 2522
Cdd:COG3096 474 FEKaYEL-VCKIAGEVERSQAWQTARELLRRY-RSQQALAQRLQQLRAQLaelEQRLRQQQNAERLleEFCQRIGQQLDA 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2523 STALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQ--AAQA 2570
Cdd:COG3096 552 AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelAARA 601
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2924-3049 |
1.05e-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: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2924 LRLVSYSGVLFFLK-QQSQFLCLAVQEGSLVLLYDFGAGlkkavplqpPPPLTSASKAiqvfLLGGSRKRVLVRVERATV 3002
Cdd:pfam02210 1 FRTRQPNGLLLYAGgGGSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3003 ySVEQDND-------------LELADAYYLGGVPPDQLPPSLrrlfPTGGSVRGCVKGIK 3049
Cdd:pfam02210 68 -TLSVDGQtvvsslppgesllLNLNGPLYLGGLPPLLLLPAL----PVRAGFVGCIRDVR 122
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2181-2609 |
1.65e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.00 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2181 HETAQQLEVLEQQST--------SLGQDARRLGGQAVGTRDQAsqlLAGTEATLGHA-KTLLAAIRAVDRTLSELmsqtg 2251
Cdd:NF041483 414 ADQAEQLKGAAKDDTkeyraktvELQEEARRLRGEAEQLRAEA---VAEGERIRGEArREAVQQIEEAARTAEEL----- 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2252 hlgLANASAPSGEqlLRTLA--EVERLLWEM--RARDLgapqaaaeaeLAAAQRLLARVQEQLSSLWEENQALATQTRdr 2327
Cdd:NF041483 486 ---LTKAKADADE--LRSTAtaESERVRTEAieRATTL----------RRQAEETLERTRAEAERLRAEAEEQAEEVR-- 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2328 lAQHEAGLMDLREALNRAV-----DATREAQELNSRNQERL---EEAL----QRKQELSRDNATLQATLhaaRDTLASVF 2395
Cdd:NF041483 549 -AAAERAARELREETERAIaarqaEAAEELTRLHTEAEERLtaaEEALadarAEAERIRREAAEETERL---RTEAAERI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2396 RLLHSldQAKEELERL--AASLDGARTpllqRMQTFSPAgskLRLVEAAEAHAQQLGQLALNlssiildvNQDRLtqRAi 2473
Cdd:NF041483 625 RTLQA--QAEQEAERLrtEAAADASAA----RAEGENVA---VRLRSEAAAEAERLKSEAQE--------SADRV--RA- 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2474 EASNAYSRI-------LQAVQ--------AAEDAAGQALQQADHTwatvvRQGLVDRAQQLLANS-TALEEAMlQEQQRL 2537
Cdd:NF041483 685 EAAAAAERVgteaaeaLAAAQeeaarrrrEAEETLGSARAEADQE-----RERAREQSEELLASArKRVEEAQ-AEAQRL 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2538 ---------GLVWAALQGARtQLRD-VRAKKDQLEAHIQAAQAMLAMDTDETSKKiahakavaaeAQDTATRVQSQLQAM 2607
Cdd:NF041483 759 veeadrratELVSAAEQTAQ-QVRDsVAGLQEQAEEEIAGLRSAAEHAAERTRTE----------AQEEADRVRSDAYAE 827
|
..
gi 2217335166 2608 QE 2609
Cdd:NF041483 828 RE 829
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
730-780 |
1.73e-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: 53.13 E-value: 1.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 730 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFGLDQADYFGC 780
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2129-2573 |
2.30e-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: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2129 LDDLERAGALLPAIHEQLRGINASsmawARLHRLNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGQDARRLGGQA 2208
Cdd:COG4913 271 LAELEYLRAALRLWFAQRRLELLE----AELEELRAELARLEAELE-------RLEARLDALREELDELEAQIRGNGGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2209 VgtrDQASQLLAGTEATLghaktllaaiRAVDRTLSELMSQTGHLGLANASapSGEQLLRTLAEVERLLwemraRDLGAP 2288
Cdd:COG4913 340 L---EQLEREIERLEREL----------EERERRRARLEALLAALGLPLPA--SAEEFAALRAEAAALL-----EALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2289 QAAAEAELAAAQRLLARVQEQLSSLWEENQALAT----------QTRDRLAQHeAG-----------LMDLRE------- 2340
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERrksniparllALRDALAEA-LGldeaelpfvgeLIEVRPeeerwrg 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2341 ---------------------ALNRAVDATREAQELNSrnqERLEEALQRKQELSRDNATLQATL----HAARDTLASvf 2395
Cdd:COG4913 479 aiervlggfaltllvppehyaAALRWVNRLHLRGRLVY---ERVRTGLPDPERPRLDPDSLAGKLdfkpHPFRAWLEA-- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2396 RLLHSLDQAK----EELERL--AASLDG------------ARTPLLQRMQT-FSPAgsklRLVEAAEAHAQQLGQLALNL 2456
Cdd:COG4913 554 ELGRRFDYVCvdspEELRRHprAITRAGqvkgngtrhekdDRRRIRSRYVLgFDNR----AKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2457 SSIILDVNQ--DRLTQRAieasNAYSRILQAVQAAEDAAGQALQQADHTwatvvrqglvDRAQQLLANSTALEEAmlqeQ 2534
Cdd:COG4913 630 EERLEALEAelDALQERR----EALQRLAEYSWDEIDVASAEREIAELE----------AELERLDASSDDLAAL----E 691
|
490 500 510
....*....|....*....|....*....|....*....
gi 2217335166 2535 QRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2573
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2331-2657 |
2.45e-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: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2331 HEAG--LMDLREALNRAVDATREaqeLNsRNQERLE---EALQRKQELSRDNATLQATLHAARdtlasvfrllhsLDQAK 2405
Cdd:TIGR02168 175 KETErkLERTRENLDRLEDILNE---LE-RQLKSLErqaEKAERYKELKAELRELELALLVLR------------LEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2406 EELERLAASLDGAR------TPLLQRMQTfSPAGSKLRLVEAAEAHAQQLGQLaLNLSSIIldvnqDRLTQRAIEASNAY 2479
Cdd:TIGR02168 239 EELEELQEELKEAEeeleelTAELQELEE-KLEELRLEVSELEEEIEELQKEL-YALANEI-----SRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2480 SRILQAVQAAEDAAGQALQQADHTWATVVRqgLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKD 2559
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAE--LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2560 QLEAHIQAAQAMLamdtdetskkiahakavaaeaqdtaTRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVST 2639
Cdd:TIGR02168 390 QLELQIASLNNEI-------------------------ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330
....*....|....*...
gi 2217335166 2640 LEKTLPQLLAKLSILENR 2657
Cdd:TIGR02168 445 LEEELEELQEELERLEEA 462
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2301-2613 |
2.65e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQEQLSSLWEENQALatqtRDRLA-------------QHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL 2367
Cdd:PRK04863 314 RELAELNEAESDLEQDYQAA----SDHLNlvqtalrqqekieRYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2368 QRKQELSRDNATLQATL----------HAARDTLASVFRLLH----SLDQAKEELERLAASLDGARTPLLQrmqtfspAG 2433
Cdd:PRK04863 390 EEVDELKSQLADYQQALdvqqtraiqyQQAVQALERAKQLCGlpdlTADNAEDWLEEFQAKEQEATEELLS-------LE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2434 SKLRLveaAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYS--RILQAVQAAEDAAGQALQQADHTWATVVRqg 2511
Cdd:PRK04863 463 QKLSV---AQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLReqRHLAEQLQQLRMRLSELEQRLRQQQRAER-- 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2512 LVDRAQQLLANSTALEEAMLQEQQRLGlvwAALQGARTQLRDV-------RAKKDQLEAHIQ----------AAQAMLAM 2574
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELE---ARLESLSESVSEArerrmalRQQLEQLQARIQrlaarapawlAAQDALAR 614
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2217335166 2575 ------DTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVER 2613
Cdd:PRK04863 615 lreqsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
730-771 |
2.65e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.65e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217335166 730 CSCDLRGTLGGvaECQPGTGQCFCKPHVCGQACASCKDGFFG 771
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. |
1867-1920 |
2.94e-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: 52.36 E-value: 2.94e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 1867 CPCPLSVPSNnfaEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVLGSSC 1920
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2303-2573 |
3.84e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEQLSSLWEENQALATQ---TRDRLAQHEAGLMDLREALNRAVDATREAQ-ELNSRNQErLEEALQRKQELSRDNA 2378
Cdd:COG4372 47 LEQLREELEQAREELEQLEEEleqARSELEQLEEELEELNEQLQAAQAELAQAQeELESLQEE-AEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2379 TLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSS 2458
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2459 IILDVNQDRLTQRAIEA----SNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQ 2534
Cdd:COG4372 206 EKLIESLPRELAEELLEakdsLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
250 260 270
....*....|....*....|....*....|....*....
gi 2217335166 2535 QRLGlvwaaLQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2573
Cdd:COG4372 286 EALE-----EAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1817-1853 |
6.29e-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: 51.59 E-value: 6.29e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2217335166 1817 PCQCHGH---SDRCLPGSGVCVdCQHNTEGAHCERCQAGF 1853
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2107-2556 |
7.21e-08 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 58.67 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2107 VPGGPVGHSIHCEVCDHCVVLLLDDLERAGALLPAIHEQLRGINASSMAWARLH---RLNASIAdLQSQLRSPLGPRHET 2183
Cdd:COG2203 253 LGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLvdgRLIGVLA-LYSKEPRAFTEEDLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2184 -----AQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANA 2258
Cdd:COG2203 332 llealADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAAD 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2259 SAPSGEQLLRTLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDL 2338
Cdd:COG2203 412 LSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2339 REALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGA 2418
Cdd:COG2203 492 LLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2419 RTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQ 2498
Cdd:COG2203 572 LSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALA 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335166 2499 QADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRA 2556
Cdd:COG2203 652 SLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSV 709
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1818-1867 |
8.40e-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: 51.20 E-value: 8.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 1818 CQCHGH---SDRCLPGSGVCvDCQHNTEGAHCERCQAGFVssrDDPSAPCVSC 1867
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYY---GLPSDPPQGC 49
|
|
| DAHL |
pfam19443 |
DAHL domain; The DAHL (Double All-Helical Ligand-binding) domain is a novel periplasmic ... |
2301-2502 |
9.28e-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: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQeQLSSLWEENqALATQTR-----DRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELS- 2374
Cdd:pfam19443 11 SALRQLK-QLDAELNRD-VLKARAGllrnyDPLVAALAELRRLLERLELPSFLLAGDSAELDAALAALRAALQEKEELVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2375 ---RDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAAS-LDGARTP---------LLQRMQTFSPAGSKLR-LVE 2440
Cdd:pfam19443 89 rfkSQNALLRNSLAYFPTLVDELLAASPAEPALAAALNELLRAvLLYNLSSdpalaeieaLLERLEALAESAPALRaALQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 2441 AAEAHAQQLgqlaLNLSSIIldvnqDRLTQRAIEASNAYSriLQAVQAA-EDAAGQALQQADH 2502
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 ... |
2737-2855 |
9.71e-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: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2737 MYMGSRQatGDYMGVSLRDKKVHWVYQLGEAGPAVLSIDEDI--GeQFAAVSLDRTLQFGHMSVTverqmiQETKGDTVA 2814
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGNTLTLSVD------GQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2217335166 2815 PGAEGLLNLrpdDFVFYVGGYPSTFTPPPLLRFPGYRGCIE 2855
Cdd:pfam02210 82 PGESLLLNL---NGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1867-1913 |
9.76e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 9.76e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217335166 1867 CPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNP 1913
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 ... |
2157-2689 |
1.35e-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: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLG---------------QDARR--LGGQAVGTRDQ----- 2214
Cdd:TIGR00618 358 RDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkeldilqreqatidtRTSAFrdLQGQLAHAKKQqelqq 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2215 --ASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTG-----HLGLANASAPSGEQLLRtLAEVERLLwEMRARDLGA 2287
Cdd:TIGR00618 438 ryAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeqiHLQETRKKAVVLARLLE-LQEEPCPL-CGSCIHPNP 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2288 PQAAAEAELAAAQRLLARVQE-------------QLSSLWEENQALATQTRdRLAQHEAGLMDLREALNRAVDATR-EAQ 2353
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTyaqletseedvyhQLTSERKQRASLKEQMQ-EIQQSFSILTQCDNRSKEDIPNLQnITV 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2354 ELNSRNQERLEEALQRKQELSRDNATLQATLHAardtlasvFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAG 2433
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL--------QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2434 SK---LRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEAS-NAYSRILQAVQAAEDAAGQALQQADHTWATVVR 2509
Cdd:TIGR00618 667 IRvlpKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHiEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2510 QGlvdRAQQllanSTALEEAMLQEQQRLGLVWAALQgARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAV 2589
Cdd:TIGR00618 747 EL---MHQA----RTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2590 AAEAQDT-ATRVQSQLQAMQEN------VERWQGQYEGLRGQ---------DLGQAVLDAGH----SVSTLEKTLPQLLA 2649
Cdd:TIGR00618 819 LNLQCETlVQEEEQFLSRLEEKsatlgeITHQLLKYEECSKQlaqltqeqaKIIQLSDKLNGinqiKIQFDGDALIKFLH 898
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2217335166 2650 KLSILENrgVHNASLALSASIGRVRELIAQARGAASKVKV 2689
Cdd:TIGR00618 899 EITLYAN--VRLANQSEGRFHGRYADSHVNARKYQGLALL 936
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
782-821 |
1.55e-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: 50.43 E-value: 1.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2217335166 782 SCRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 821
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2188-2684 |
1.57e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 57.95 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2188 EVLEQQ-STSLGQDARRLGGQ--AVGTRDQASQLL--AGTEATLGHAktLLAAIRAVDRTLSELMSQTG-------HLGL 2255
Cdd:COG3899 674 RALEARgPEPLEERLFELAHHlnRAGERDRAARLLlrAARRALARGA--YAEALRYLERALELLPPDPEeeyrlalLLEL 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2256 ANASAPSG-----EQLLRTLAEvERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSsLWEENQALATQTRDRLAQ 2330
Cdd:COG3899 752 AEALYLAGrfeeaEALLERALA-ARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYE-FGELALALAERLGDRRLE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2331 HEAGLM---------DLREALNRAVDATREAQELNSRnqeRLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSL 2401
Cdd:COG3899 830 ARALFNlgfilhwlgPLREALELLREALEAGLETGDA---ALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAA 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2402 DQAKEELERLAASLDGARTPLLQRMQtfspagskLRLVEAAEAHAQQLGQLALN-----------LSSIILDVNQDRLTQ 2470
Cdd:COG3899 907 AAAAAALAAAELARLAAAAAAAAALA--------LAAAAAAAAAAALAAAAAAAalaaalalaaaAAAAAAAALAAAAAA 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2471 RAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQ 2550
Cdd:COG3899 979 AAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAA 1058
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2551 LRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAV 2630
Cdd:COG3899 1059 AAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLL 1138
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2631 LDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAA 2684
Cdd:COG3899 1139 AAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAA 1192
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2157-2392 |
1.85e-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: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQL---LAGTEATLGHAKTLL 2233
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2234 AA-IRAVDRtlselMSQTGHLGLAnASAPSGEQLLRTLAEVERLLWEMRARdlgapqaaaeaelaaaQRLLARVQEQLss 2312
Cdd:COG4942 107 AElLRALYR-----LGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARREQ----------------AEELRADLAEL-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2313 lwEENQALATQTRDRLAQHEAGLMDLREALNRAVDatrEAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLA 2392
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 |
2.26e-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: 2.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 429 CNC-ESDFTDGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPSCYP 473
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
631-680 |
2.43e-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: 49.66 E-value: 2.43e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217335166 631 ACTCDPRGALDQLCGAG-GLCRCRPGYTGTACQECSPGFHGFPScVPGSCH 680
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
299-347 |
2.55e-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: 49.66 E-value: 2.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217335166 299 RCVCHGHADACDAKDPTDpfrLQCTCQHNTCGGTCDRCCPGFNQQPWKP 347
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
428-470 |
2.68e-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: 49.66 E-value: 2.68e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217335166 428 RCNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTGFPS 470
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2129-2497 |
3.98e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2129 LDDLERAGALLPAIHEQLRGINASSMAWAR----LHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRL 2204
Cdd:PRK04863 316 LAELNEAESDLEQDYQAASDHLNLVQTALRqqekIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2205 GGQ--------------------AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGH-LGLANASAPSG 2263
Cdd:PRK04863 396 KSQladyqqaldvqqtraiqyqqAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQkLSVAQAAHSQF 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2264 E---QLLRTLA-EVERL-LWEMrARDlgapqaaaeaelaaaqrLLARvqeqlsslWEENQALAtqtrDRLAQHEAGLMDL 2338
Cdd:PRK04863 476 EqayQLVRKIAgEVSRSeAWDV-ARE-----------------LLRR--------LREQRHLA----EQLQQLRMRLSEL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2339 REALNRAVDATREAQELNSRNQERLE-----EALQRKQELSRDNATLQ-ATLHAARDTLAsvfrllHSLDQAKEELERLA 2412
Cdd:PRK04863 526 EQRLRQQQRAERLLAEFCKRLGKNLDdedelEQLQEELEARLESLSESvSEARERRMALR------QQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2413 asldgARTPllqRMQTFSPAGSKLR-----LVEAAEAHAQQLGQLALNLSSiiLDVNQDRLTQRaIEASNAYSRILQAVQ 2487
Cdd:PRK04863 600 -----ARAP---AWLAAQDALARLReqsgeEFEDSQDVTEYMQQLLERERE--LTVERDELAAR-KQALDEEIERLSQPG 668
|
410
....*....|
gi 2217335166 2488 AAEDAAGQAL 2497
Cdd:PRK04863 669 GSEDPRLNAL 678
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
429-471 |
6.73e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 6.73e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 429 CNCESDFT-DGTCEDLTGRCYCRPNFSGERCDVCAEGFTG--FPSC 471
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2301-2665 |
7.08e-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: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQEQLSSLWEENQALATQ----------TRDRLAQHEAGLMDLREALN--RAVDATREAQelnSRNQER-LEEAL 2367
Cdd:pfam19220 55 ALLAQERAAYGKLRRELAGLTRRlsaaegeleeLVARLAKLEAALREAEAAKEelRIELRDKTAQ---AEALERqLAAET 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2368 QRKQELSRDNATLQATLHAARDTLAsvfRLLHSLDQAKEELERLAAslDGARtplLQ-RMQTFSPAGSKL--RLVE---A 2441
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQ---RAEGELATARERLALLEQ--ENRR---LQaLSEEQAAELAELtrRLAEletQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2442 AEAHAQQLGQLALNLssiildVNQDRLTQRAieasnaysrilqavQAAEDAAGQALQqadhtwatvvrqglVDRAQQLLA 2521
Cdd:pfam19220 204 LDATRARLRALEGQL------AAEQAERERA--------------EAQLEEAVEAHR--------------AERASLRMK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2522 NSTALEEAMLQEQqrlglvwaALQGARTQLRDvrakkdqLEAHIQAAQAMLAmdtdETSKkiahakavaaeAQDTATRVQ 2601
Cdd:pfam19220 250 LEALTARAAATEQ--------LLAEARNQLRD-------RDEAIRAAERRLK----EASI-----------ERDTLERRL 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2602 SQLQAMQENVERwqgqyeglRGQDLGQAVLDAGHSVSTLEKTLPqllAKLSILENRGVHNASLA 2665
Cdd:pfam19220 300 AGLEADLERRTQ--------QFQEMQRARAELEERAEMLTKALA---AKDAALERAEERIASLS 352
|
|
| TorS_sensor_domain |
cd16172 |
sensor domain of the sensor histidine kinase TorS; TorS is part of the trimethylamine-N-oxide ... |
2241-2532 |
7.37e-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: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2241 RTLSELMSQTGHLG--LANAsapsgeqllRTLAEverllWEMRARDLGapqaaaeaelaaaqRLLARVQEQLSSLweENQ 2318
Cdd:cd16172 2 RQLSELSSRIIASAqlLANA---------DSEAE-----RQQQGRQLT--------------AQLEALLRLLKAL--GQD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2319 ALATQTRDRLAQHEAGLMDLREALNRAVdatREAQELNSRNQERLEEALQRKQE---LSR---DNATLQATlhaARdtLA 2392
Cdd:cd16172 52 SFDSFLLSRLEQTVQEIIDNLAQLGELV---GQRLQLRQQFQQLFERLRAAAGElaqLARtqvANASTIAV---AN--VS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2393 SVFRLL--HSLDQAKEELERLAA-SLDgartpLLQRMqtfspagSKLRLveaaeaHAQQLGQLALNLSSIildVNQDRLt 2469
Cdd:cd16172 124 GLYDLIeqNDKEAAYQALDRLIEvDLD-----LLERM-------HELRL------LALQLGNLINELRTA---SDIARL- 181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2470 QRAIEASNAYSRILQA-VQAAED-----AAGQALQQADHtwatvvRQGLVDRAQQLLANSTALEEAMLQ 2532
Cdd:cd16172 182 AELRQQFNANLAILQRrVQAVEDpgrraQMAQLLSDLEQ------GQGLFALRRQLLALEQRLQALMQN 244
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
783-821 |
7.42e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 7.42e-07
10 20 30
....*....|....*....|....*....|....*....
gi 2217335166 783 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 821
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2243-2566 |
8.78e-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: 55.34 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2243 LSELMSQtgHLGLANASAPsgEQLLRTLA----EVERllwemrardlgapqaaaeaELAAAQRLLARVQEQLSSLWEENQ 2318
Cdd:COG3096 818 FSQFVGG--HLAVAFAPDP--EAELAALRqrrsELER-------------------ELAQHRAQEQQLRQQLDQLKEQLQ 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2319 ALatqtrDRLAQH-----EAGLMDLREALNRAVDATREAQELNSRNQERLEealqrkqELSRDNATLQATlHAARDTLAs 2393
Cdd:COG3096 875 LL-----NKLLPQanllaDETLADRLEELREELDAAQEAQAFIQQHGKALA-------QLEPLVAVLQSD-PEQFEQLQ- 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2394 vfrllHSLDQAKEELERLAASLDgARTPLLQRMQTFSPAGSKLRLVEAAEahaqqlgqlaLNlssiildvnqDRLTQRai 2473
Cdd:COG3096 941 -----ADYLQAKEQQRRLKQQIF-ALSEVVQRRPHFSYEDAVGLLGENSD----------LN----------EKLRAR-- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2474 easnaysriLQAVQAAEDAAGQALQQAD--HTWATVVRQGLV---DRAQQLLAnstaleeAMLQEQQRLGLVWA--ALQG 2546
Cdd:COG3096 993 ---------LEQAEEARREAREQLRQAQaqYSQYNQVLASLKssrDAKQQTLQ-------ELEQELEELGVQADaeAEER 1056
|
330 340
....*....|....*....|....*..
gi 2217335166 2547 ART-------QLRDVRAKKDQLEAHIQ 2566
Cdd:COG3096 1057 ARIrrdelheELSQNRSRRSQLEKQLT 1083
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2736-2860 |
9.35e-07 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 50.78 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2736 VMYMGSrQATGDYMGVSLRDKKVHWVYQLGeAGPAVLSIDEDIGE-QFAAVSLDRTLQFGHMSVT-VERQMIQETKGDTV 2813
Cdd:pfam00054 10 LLYNGT-QTERDFLALELRDGRLEVSYDLG-SGAAVVRSGDKLNDgKWHSVELERNGRSGTLSVDgEARPTGESPLGATT 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217335166 2814 APGAEGLLnlrpddfvfYVGGYPSTFTPPPLLRF-PGYRGCIEMDTLN 2860
Cdd:pfam00054 88 DLDVDGPL---------YVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
698-727 |
9.55e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 9.55e-07
10 20 30
....*....|....*....|....*....|
gi 2217335166 698 CMCRAHVEGPSCDRCKPGFWGLSPSNPEGC 727
Cdd:pfam00053 20 CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2186-2425 |
9.62e-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: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2186 QLEVLEQQSTSLGQDArrlggQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLG----------L 2255
Cdd:pfam12795 1 KLDELEKAKLDEAAKK-----KLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQakaeaapkeiL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2256 ANASAPSGEQLL-----------RTLAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARVQEQLSslweENQALATQT 2324
Cdd:pfam12795 76 ASLSLEELEQRLlqtsaqlqelqNQLAQLNSQLIELQTR-------------------PERAQQQLS----EARQRLQQI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2325 RDRLAQHEAGLMDLREALNRAVDAtrEAQELNSRNQErLEEALQ---RKQELS---RDNATLQ-ATLHAARDTLASV--F 2395
Cdd:pfam12795 133 RNRLNGPAPPGEPLSEAQRWALQA--ELAALKAQIDM-LEQELLsnnNRQDLLkarRDLLTLRiQRLEQQLQALQELlnE 209
|
250 260 270
....*....|....*....|....*....|
gi 2217335166 2396 RLLHSLDQAKEELERLAASLDGArTPLLQR 2425
Cdd:pfam12795 210 KRLQEAEQAVAQTEQLAEEAAGD-HPLVQQ 238
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1866-1921 |
9.69e-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: 48.12 E-value: 9.69e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 1866 SCPCPlsvPSNNFAEGCVLRGGrtQCLCKPGYAGASCERCAPGFFGNPLVlGSSCQ 1921
Cdd:cd00055 1 PCDCN---GHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1923-1967 |
1.96e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.96e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 1923 CDCSGNGDpnlLFSDCDPLTGACRgCLRHTTGPRCEICAPGFYGN 1967
Cdd:smart00180 1 CDCDPGGS---ASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2316-2575 |
2.14e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 53.54 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2316 ENQAL---ATQTR--DRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEA-LQRKQ--ELsrDNATLQA----T 2383
Cdd:COG0497 133 EHQSLldpDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELdLLRFQleEL--EAAALQPgeeeE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2384 LHAARDTLASVFRLLHSLDQAkeeLERLAASLDGArTPLLQRMqtfspagskLRLVEAAEAHAQQLGQLALNLSSIILDV 2463
Cdd:COG0497 211 LEEERRRLSNAEKLREALQEA---LEALSGGEGGA-LDLLGQA---------LRALERLAEYDPSLAELAERLESALIEL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2464 NqdrltqraiEASNAYSRILQAVQAaeDAagQALQQAD---HTWATVVR------QGLVDRAQQL---LANSTALEEAML 2531
Cdd:COG0497 278 E---------EAASELRRYLDSLEF--DP--ERLEEVEerlALLRRLARkygvtvEELLAYAEELraeLAELENSDERLE 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2217335166 2532 QEQQRLGLVWAALQGARTQLRDVRAKK-DQLEAHIQAAQAMLAMD 2575
Cdd:COG0497 345 ELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTAELADLGMP 389
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2302-2610 |
2.83e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2302 LLARVQEQLSSLWEENQALATQTRDRLAQHEaglmDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQ 2381
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELE----QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2382 ATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSIIL 2461
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA------EREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2462 DVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVW 2541
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2542 AALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQEN 2610
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2337-2712 |
3.28e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2337 DLREALNRAVDATRE---AQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASV---FRLLHSLDQAKEELER 2410
Cdd:PRK04863 280 ERRVHLEEALELRRElytSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVqtaLRQQEKIERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2411 LAASLDGartpllqrmQTFSPAGSKLRlVEAAEAHAQQLGQLALNLSSIILDVNQ--DRLTQRAIeasnAYSrilQAVQA 2488
Cdd:PRK04863 360 LEERLEE---------QNEVVEEADEQ-QEENEARAEAAEEEVDELKSQLADYQQalDVQQTRAI----QYQ---QAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2489 AEDAAGQaLQQADHTWAtvvrqGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALqgartqlrdvrakkdqlEAHIQAA 2568
Cdd:PRK04863 423 LERAKQL-CGLPDLTAD-----NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH-----------------SQFEQAY 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2569 QAMLAMdTDETSkkiahakavaaeaqdtatRVQSQLQAMQenVERwqgQYEGLRGQDlgqavldaghsvstleKTLPQLL 2648
Cdd:PRK04863 480 QLVRKI-AGEVS------------------RSEAWDVARE--LLR---RLREQRHLA----------------EQLQQLR 519
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2649 AKLSILENRgvhnasLALSAsigRVRELIAQargaaskvkvpmkFNGRSGVQLRTPRDLADLAA 2712
Cdd:PRK04863 520 MRLSELEQR------LRQQQ---RAERLLAE-------------FCKRLGKNLDDEDELEQLQE 561
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2366-2657 |
3.55e-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: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2366 ALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPL-LQRMQtfspagsKLRLVEAAEA 2444
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsALRKD-------LARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2445 HAQQLGQLALNLSSiiLDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADhtwatVVRQGLVDRAQQLlansT 2524
Cdd:TIGR02168 745 LEERIAQLSKELTE--LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-----ALREALDELRAEL----T 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2525 ALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAmDTDETSKKIahakavaaeaQDTATRVQSQL 2604
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEEL----------ESELEALLNER 882
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2217335166 2605 QAMQENVERWQGQYEGLRGQ--DLGQAVLDAGHSVSTLEKTLPQLLAKLSILENR 2657
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEElrELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
632-674 |
3.67e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217335166 632 CTCDPRGALDQLC-GAGGLCRCRPGYTGTACQECSPGFHG--FPSC 674
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2157-2416 |
4.27e-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: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRsplgpRHETAQQLevLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTL---- 2232
Cdd:TIGR02168 719 KELEELSRQISALRKDLA-----RLEAEVEQ--LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqi 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2233 ---LAAIRAVDRTLSELMSQTGHLGLANASAPSG-EQLLRTLAEVERLLWEM--RARDLGAPQAAAEAELAAAQRLLARV 2306
Cdd:TIGR02168 792 eqlKEELKALREALDELRAELTLLNEEAANLRERlESLERRIAATERRLEDLeeQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEE----NQALATQtRDRLAQHEAglmDLREALNRAVDATREAQELNSRN---QERLEEALQRKQEL-SRDNA 2378
Cdd:TIGR02168 872 ESELEALLNEraslEEALALL-RSELEELSE---ELRELESKRSELRRELEELREKLaqlELRLEGLEVRIDNLqERLSE 947
|
250 260 270
....*....|....*....|....*....|....*...
gi 2217335166 2379 TLQATLHAArdtLASVFRLLHSLDQAKEELERLAASLD 2416
Cdd:TIGR02168 948 EYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2128-2573 |
4.44e-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: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2128 LLDDLERAGALLPAIHEQLRGINASSMA--WARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLG 2205
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2206 GQAVGTRDQASQLLAGTEATLGHAKT----LLAAIRAVDRTLSELMSQTG---------------HLGLANASAP----- 2261
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAalrdLRRELRELEAEIASLERRKSniparllalrdalaeALGLDEAELPfvgel 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2262 ------------SGEQLLRTLA---------------EVERLLWEMRAR--DLGAPQAAAEAELAAAQRLLARVQeqlss 2312
Cdd:COG4913 467 ievrpeeerwrgAIERVLGGFAltllvppehyaaalrWVNRLHLRGRLVyeRVRTGLPDPERPRLDPDSLAGKLD----- 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2313 lWEENQAlatqtRDRLAQHEAGLMDLR-----EALNRAVDA-TREAQ--------ELNSR------------NQERLEEA 2366
Cdd:COG4913 542 -FKPHPF-----RAWLEAELGRRFDYVcvdspEELRRHPRAiTRAGQvkgngtrhEKDDRrrirsryvlgfdNRAKLAAL 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2367 LQRKQElsrdnatLQATLHAARDTLAsvfrllhsldQAKEELERLAASLDgartpLLQRMQTFSPAGSKLRLVEAAEAHA 2446
Cdd:COG4913 616 EAELAE-------LEEELAEAEERLE----------ALEAELDALQERRE-----ALQRLAEYSWDEIDVASAEREIAEL 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2447 QQlgQLA-LNLSSIILDVNQDRLTQRAIEasnaysriLQAVQAAEDAAGQALQQADHTWATVVRQglVDRAQQLLANstA 2525
Cdd:COG4913 674 EA--ELErLDASSDDLAALEEQLEELEAE--------LEELEEELDELKGEIGRLEKELEQAEEE--LDELQDRLEA--A 739
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2217335166 2526 LEEAMLQEQQRLGLVWAALQGARtQLRDVRAkkdQLEAHIQAAQAMLA 2573
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDA-VERELRE---NLEERIDALRARLN 783
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1798-1867 |
5.45e-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: 49.22 E-value: 5.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1798 ECAPGFYRDVKGlflGRCVPCQchghsdRCLPGSGVCVDCQHNTEgAHCERCQAGFVSSRDDPSAPCVSC 1867
Cdd:cd13416 79 ECAYGYYLDEDS---GTCEPCT------VCPPGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDPCLPC 138
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2325-2564 |
6.16e-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: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2325 RDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLeEALQRKQELS---RDNATLQATLHAARDTLAsvfrllhSL 2401
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSwdeIDVASAEREIAELEAELE-------RL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2402 DQAKEELERLAASLDGARtpllQRMQtfspagsklRLVEAAEAHAQQLGQLALNLSSI--ILDVNQDRLTQRAIEASNAY 2479
Cdd:COG4913 681 DASSDDLAALEEQLEELE----AELE---------ELEEELDELKGEIGRLEKELEQAeeELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2480 SRILQAV--QAAEDAAGQALQQadhtWATVVRQGLVDRAQQLlanSTALEEAMLQEQQRlglvW-AALQGARTQL---RD 2553
Cdd:COG4913 748 RALLEERfaAALGDAVERELRE----NLEERIDALRARLNRA---EEELERAMRAFNRE----WpAETADLDADLeslPE 816
|
250
....*....|.
gi 2217335166 2554 VRAKKDQLEAH 2564
Cdd:COG4913 817 YLALLDRLEED 827
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2165-2459 |
6.43e-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: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2165 SIADLQSQLRSPLGPRHETAQQLevleqqstsLgqdARRLGGQAVGT-----RDQ---ASQLLAGTEATLGHAKTLLAAI 2236
Cdd:COG4913 174 SFSAYLARLRRRLGIGSEKALRL---------L---HKTQSFKPIGDlddfvREYmleEPDTFEAADALVEHFDDLERAH 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2237 RAVDRTLSelmsQTGHLGLANASAPSGEQLLRTLAEVERL-----LWEMRARDlgapqaaaeaelaaaqRLLARVQEQLS 2311
Cdd:COG4913 242 EALEDARE----QIELLEPIRELAERYAAARERLAELEYLraalrLWFAQRRL----------------ELLEAELEELR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2312 SLWEENQALATQTRDRLAQHEAGLMDLREALNRAvdATREAQELNSRnQERLEEALQRKQELSRDNATLQATLHAARDTL 2391
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLERE-IERLERELEERERRRARLEALLAALGLPLPAS 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2392 ASVF-RLLHSLDQAKEELERLAASLDGARTPLLQRmqtfspagsKLRLVEAAEAHAQQLGQLALNLSSI 2459
Cdd:COG4913 379 AEEFaALRAEAAALLEALEEELEALEEALAEAEAA---------LRDLRRELRELEAEIASLERRKSNI 438
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2360-2573 |
8.51e-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: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2360 QERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTfspagSKLRLV 2439
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-----LEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2440 EAAEAHAQQLGQLALNLSSIILDVNQDRLT--------QRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVV--R 2509
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2510 QGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2573
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2355-2684 |
1.26e-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: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2355 LNSRNQER---LEEA------LQRKQE-LSRdnatlqatlhaardtlasvfrllhsLDQAKEELERL---AASLDGARTP 2421
Cdd:COG1196 150 IEAKPEERraiIEEAagiskyKERKEEaERK-------------------------LEATEENLERLediLGELERQLEP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2422 L------LQRMQTFSpagSKLRLVEAA------EAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRI-LQAVQA 2488
Cdd:COG1196 205 LerqaekAERYRELK---EELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeLEELEL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2489 AEDAAGQALQQADHTWATVVRQG--LVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQ 2566
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2567 AAQAMLAMDT---DETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVSTLEKT 2643
Cdd:COG1196 362 EAEEALLEAEaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217335166 2644 LPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAA 2684
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
698-728 |
1.32e-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: 45.04 E-value: 1.32e-05
10 20 30
....*....|....*....|....*....|.
gi 2217335166 698 CMCRAHVEGPSCDRCKPGFWGLsPSNPEGCT 728
Cdd:cd00055 21 CECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3107-3221 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3107 FHSAQDSALLYYRAS--PDGLCqVSLQQGRVSLQL-----LRTEVKTQAGFADGAPHYVAF-YSNATGVwLYVDDQlqqm 3178
Cdd:pfam02210 1 FRTRQPNGLLLYAGGggSDFLA-LELVNGRLVLRYdlgsgPESLLSSGKNLNDGQWHSVRVeRNGNTLT-LSVDGQ---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217335166 3179 KPHRGPPPELQPQPEGPPRLLLGGLPESGTIY------NFSGCISNVFV 3221
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPalpvraGFVGCIRDVRV 123
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2303-2500 |
1.60e-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: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEQLSSLWEE--------NQALA--TQTRDRLAQHEAGLMDLREALNRAVDA----TREAQE-------------- 2354
Cdd:COG3883 32 LEAAQAELDALQAEleelneeyNELQAelEALQAEIDKLQAEIAEAEAEIEERREElgerARALYRsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2355 ---------------LNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGAR 2419
Cdd:COG3883 112 esfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2420 TPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQ 2499
Cdd:COG3883 192 AAAEAQLA------ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
.
gi 2217335166 2500 A 2500
Cdd:COG3883 266 G 266
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2162-2388 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2162 LNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGqdarrLGGQAvgtrDQASQLLAGTEATLGHAKTLLAAIRAVDR 2241
Cdd:COG3206 180 LEEQLPELRKELE-------EAEAALEEFRQKNGLVD-----LSEEA----KLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2242 TLSELMSQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRAR------DLgapqaaaeaelaaaQRLLARVQEQLSSLWE 2315
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpDV--------------IALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2316 ENQALATQTRDRLAQHEAGLMDLREALNRavdATREAQELNSRNQERLEeaLQRKQELSRDN-ATLQATLHAAR 2388
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQ---LEARLAELPELEAELRR--LEREVEVARELyESLLQRLEEAR 378
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2389-2649 |
2.02e-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: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2389 DTLASVFR-LLHSLDQAKEELERLaasLDGArtplLQRMQtfspagskLRLVEAAEAHAQQLGQLALNlssiildvnQDR 2467
Cdd:pfam04012 3 KRLGRLVRaNIHEGLDKAEDPEKM---LEQA----IRDMQ--------SELVKARQALAQTIARQKQL---------ERR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2468 LTQRAIEASNAYSRILQAV-QAAEDAAGQALQQAdhtwatvvrqglvdraqQLLANSTALEEAMLQEQQRLGL-VWAALQ 2545
Cdd:pfam04012 59 LEQQTEQAKKLEEKAQAALtKGNEELAREALAEK-----------------KSLEKQAEALETQLAQQRSAVEqLRKQLA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2546 GARTQLRDVRAKKDQLEAHIQAAQAMLAMDTdeTSKKIahakavaaeaqDTATRVqSQLQAMQENVERWQGQ---YEGLR 2622
Cdd:pfam04012 122 ALETKIQQLKAKKNLLKARLKAAKAQEAVQT--SLGSL-----------STSSAT-DSFERIEEKIEEREARadaAAELA 187
|
250 260
....*....|....*....|....*...
gi 2217335166 2623 G-QDLGQAVLDAGHSVSTLEKTLPQLLA 2649
Cdd:pfam04012 188 SaVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2329-2639 |
2.11e-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: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2329 AQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLAsvfRLLHSLDQAKEEL 2408
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2409 ERLAASL--DGARTPLLQRM---QTFSPAGSKLRLVEAAEAHAQQlgqlalnlssIILDVNQDRltQRAIEASNAYSRIL 2483
Cdd:COG3883 89 GERARALyrSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADAD----------LLEELKADK--AELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2484 QAVQAAEDAAGQALQQAdhtwatvvrQGLVDRAQQLLANSTAlEEAMLQEQ-QRLGLVWAALQGARTQLRDvrAKKDQLE 2562
Cdd:COG3883 157 AELEALKAELEAAKAEL---------EAQQAEQEALLAQLSA-EEAAAEAQlAELEAELAAAEAAAAAAAA--AAAAAAA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217335166 2563 AHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVST 2639
Cdd:COG3883 225 AAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASG 301
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1818-1853 |
2.19e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 2.19e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2217335166 1818 CQCHG---HSDRCLPGSGVCvDCQHNTEGAHCERCQAGF 1853
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. |
783-821 |
2.71e-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: 2.71e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2217335166 783 CRCDIGGALGQSCEPRTGVCRCRPNTQGPTCSEPARDHY 821
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2184-2396 |
2.74e-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: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2184 AQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAI--RAVDRTLSELMSQtghlgLANASAP 2261
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAE-----LERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2262 SGEqllrtLAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARVQEQLSSLWEEnqalATQTRDRLAQHEAGLMDLREA 2341
Cdd:COG4913 684 SDD-----LAALEEQLEELEAE-------------------LEELEEELDELKGE----IGRLEKELEQAEEELDELQDR 735
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2342 LNRAVDATREAQ--ELNSRNQERLEEALQRK--QELSRDNATLQATLHAARDTLASVFR 2396
Cdd:COG4913 736 LEAAEDLARLELraLLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELERAMR 794
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
2303-2410 |
2.82e-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: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEQLSSLWEENQALATQTR-----------------DRLAQHEAGLMDLREALNRAVDATREA-QELNSRNQE--R 2362
Cdd:pfam15619 20 LAELQSKLEELRKENRLLKRLQKrqekalgkyegteselpQLIARHNEEVRVLRERLRRLQEKERDLeRKLKEKEAEllR 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217335166 2363 LEEALQRKQELSRDnATLqatlhAARDTLAsvfrllHSLDQAKEELER 2410
Cdd:pfam15619 100 LRDQLKRLEKLSED-KNL-----AEREELQ------KKLEQLEAKLED 135
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2318-2572 |
2.99e-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: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2318 QALATQTRDRLAQHEAgLMDLREALNRaVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAA---RDTLASV 2394
Cdd:pfam12795 3 DELEKAKLDEAAKKKL-LQDLQQALSL-LDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAApkeILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2395 FRLLHSLDQAKEELERLAASLDGARTpLLQRMQTfSPAGSKLRLVEAAeahaQQLGQLALNLSSiiLDVNQDRLTQraie 2474
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNS-QLIELQT-RPERAQQQLSEAR----QRLQQIRNRLNG--PAPPGEPLSE---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2475 asnaysrilqavqaAEDAAGQALQQAdhtwatvvRQGLVDRAQQLLANSTALEEAmlqeqqrlglvwaalqgARTQLRDV 2554
Cdd:pfam12795 149 --------------AQRWALQAELAA--------LKAQIDMLEQELLSNNNRQDL-----------------LKARRDLL 189
|
250
....*....|....*...
gi 2217335166 2555 RAKKDQLEAHIQAAQAML 2572
Cdd:pfam12795 190 TLRIQRLEQQLQALQELL 207
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2930-3056 |
3.25e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 46.16 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2930 SGVLFFLKQQSQ--FLCLAVQEGSLVLLYDFGAGLKkavpLQPPPPLTSASKAIQVFLLGgSRKRVLVRVERATVYSVEQ 3007
Cdd:pfam00054 7 SGLLLYNGTQTErdFLALELRDGRLEVSYDLGSGAA----VVRSGDKLNDGKWHSVELER-NGRSGTLSVDGEARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217335166 3008 ----DNDLELADAYYLGGVPPDQLppsLRRLFPTGGSVRGCVKGIKALGKYVD 3056
Cdd:pfam00054 82 plgaTTDLDVDGPLYVGGLPSLGV---KKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2318-2684 |
3.32e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 49.81 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2318 QALATQTRDRL--AQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVF 2395
Cdd:COG2203 334 EALADQAAIAIerARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2396 RLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEA 2475
Cdd:COG2203 414 GLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2476 SNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVR 2555
Cdd:COG2203 494 LLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLS 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2556 AKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGH 2635
Cdd:COG2203 574 VLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASL 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217335166 2636 SVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAA 2684
Cdd:COG2203 654 VLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVA 702
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
358-421 |
4.08e-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: 43.50 E-value: 4.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217335166 358 SCNCYGHAtdcyydpevdrrrasqSLDGT-YQGGGVCIdCQHHTTGVNCERCLPGFYRSPNHPLD 421
Cdd:cd00055 1 PCDCNGHG----------------SLSGQcDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2128-2563 |
4.33e-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: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2128 LLDDLERAGALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLGQDARRLGGQ 2207
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2208 AVGTRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLRTLAEVERLLWEMRARDLGA 2287
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2288 PQAAAeaelaaaQRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEAL 2367
Cdd:COG1196 541 EAALA-------AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2368 QRKQelsRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTpllqrmqtfspAGSKLRLVEAAEAHAQ 2447
Cdd:COG1196 614 RYYV---LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-----------GGSRRELLAALLEAEA 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2448 QLGQLALNLSSIILDVNQDRLTQRAIEasnaysriLQAVQAAEDAAGQALQQADhtwatvVRQGLVDRAQQLLANSTALE 2527
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEE--------RELAEAEEERLEEELEEEA------LEEQLEAEREELLEELLEEE 745
|
410 420 430
....*....|....*....|....*....|....*.
gi 2217335166 2528 EAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEA 2563
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2301-2689 |
5.65e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 49.04 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQEQLsslweenqALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRKQELSRDNATL 2380
Cdd:COG2203 331 ELLEALADQA--------AIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAEL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2381 QATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSII 2460
Cdd:COG2203 403 LLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2461 LDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLV 2540
Cdd:COG2203 483 LLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLT 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2541 WAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEG 2620
Cdd:COG2203 563 LVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSAL 642
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2621 LRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAASKVKV 2689
Cdd:COG2203 643 LLRLALALASLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLE 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2120-2416 |
5.72e-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: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2120 VCDHCVVLLLDDLERAGALLPAIHEQLRGINASSMAWARlhrlnASIADLQSQLRSPLgprheTAQQLEVLEQQSTSLGQ 2199
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA-----AAIEYLKAAKAGRA-----TFLPLDKIRARAALAAA 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2200 DARRLGGQAVGTRDQASQLLAGTEATLGhaKTLLAAIRAVDRTLSelmsqtghlGLANASAPSGEQLLRTLAEVERLLWE 2279
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLG--DTLLGRTLVAARLEA---------ALRRAVTLAGRLREVTLEGEGGSAGG 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2280 MRARdlgapqaaaeaelaaaqrllARVQEQLSSLwEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRN 2359
Cdd:COG1196 661 SLTG--------------------GSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335166 2360 QERLEEALQRKQELSRDNATLQATLHAA-RDTLASVFRLLHSLDQAKEELERLAASLD 2416
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELlEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
359-426 |
7.53e-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: 42.73 E-value: 7.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335166 359 CNCYGHATdcyydpevdrrrasqSLDGTYQGGGVCiDCQHHTTGVNCERCLPGFYRSPNhplDSPHVC 426
Cdd:pfam00053 1 CDCNPHGS---------------LSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2166-2564 |
8.96e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2166 IADLQSQLRSPLGPRHETAQQLEVLEQQstslgqdarrlggqavgtRDQASQLLAGTEATLGHAKTLLAAIRavdrtlSE 2245
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREE------------------LEQAREELEQLEEELEQARSELEQLE------EE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2246 LmsqtghlglanasapsgEQLLRTLAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARVQEQLSSLWEENQALATQtR 2325
Cdd:COG4372 82 L-----------------EELNEQLQAAQAELAQAQEE-------------------LESLQEEAEELQEELEELQKE-R 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2326 DRLAQHEAGLMDLREALNRAVDA-TREAQELNSR---NQERLEEALQRKQELSRDNAT--LQATLHAARDTLASVFRLLH 2399
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAErEEELKELEEQlesLQEELAALEQELQALSEAEAEqaLDELLKEANRNAEKEEELAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2400 SLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEAsNAY 2479
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI-AAL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2480 SRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQEQQRlGLVWAALQGARTQLRDVRAKKD 2559
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA-DLLQLLLVGLLDNDVLELLSKG 362
|
....*
gi 2217335166 2560 QLEAH 2564
Cdd:COG4372 363 AEAGV 367
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2157-2426 |
9.65e-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: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2157 ARLHRLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSLgqdaRRLGGQAVGTRDQ-ASQLLAGTEATLGHAKTLLAA 2235
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLL----NKLLPQANLLADEtLADRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2236 IRAVDRTLSELMSQTGHLglanASAP-SGEQLLRTLAEVERLLWEMRARdlgapqaaaeaeLAAAQRLLARVQ----EQL 2310
Cdd:COG3096 912 IQQHGKALAQLEPLVAVL----QSDPeQFEQLQADYLQAKEQQRRLKQQ------------IFALSEVVQRRPhfsyEDA 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2311 SSLWEENQALATQTRDRLAQHEAGLMDLREAL----NRAVDATREAQELNSR---NQERLEEALQRKQELS-RDNATLQA 2382
Cdd:COG3096 976 VGLLGENSDLNEKLRARLEQAEEARREAREQLrqaqAQYSQYNQVLASLKSSrdaKQQTLQELEQELEELGvQADAEAEE 1055
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2217335166 2383 TLHAARDTLASvfrLLHSLDQAKEELERLAASLDGARTPLLQRM 2426
Cdd:COG3096 1056 RARIRRDELHE---ELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
698-727 |
9.85e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 9.85e-05
10 20 30
....*....|....*....|....*....|
gi 2217335166 698 CMCRAHVEGPSCDRCKPGFWGlspSNPEGC 727
Cdd:smart00180 20 CECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1937-2023 |
1.09e-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: 45.08 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 1937 DCDPLTGACRGClRHTTGPRCEICAPGFYGNAL---LPGNCTRCDCTPCGTE--ACDPHSG-HCLCKAGVT-------GR 2003
Cdd:cd13406 17 ECPPGEGMESRC-TGTQDTVCSPCEPGFYNEAVnyePCKPCTQCNQRSGSEEkqKCTKTSDtVCRCRPGTQpldsykpGV 95
|
90 100
....*....|....*....|
gi 2217335166 2004 RCDRCQEGHFGFDGCGGCRP 2023
Cdd:cd13406 96 DCVPCPPGHFSRGDNQACKP 115
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2438-2651 |
1.69e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2438 LVEAAEAHAQQLGqlalnlssiildvNQDRLTQRAIEASNA----YSRILQAVQAA-EDAAGQALQQ-ADHtwatvvrQG 2511
Cdd:COG1842 39 LVEARQALAQVIA-------------NQKRLERQLEELEAEaekwEEKARLALEKGrEDLAREALERkAEL-------EA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2512 LVDRAQQLLANSTALEEAMLQEQQRLglvwaalqgaRTQLRDVRAKKDQLEAHIQAAQAMLAMdtDETSKKIahakavaa 2591
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQL----------ESKLEELKAKKDTLKARAKAAKAQEKV--NEALSGI-------- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 2592 eaqdTATRVQSQLQAMQENVERWQGQYEGL----RGQDLGQ--AVLDAGHSVstlEKTLPQLLAKL 2651
Cdd:COG1842 159 ----DSDDATSALERMEEKIEEMEARAEAAaelaAGDSLDDelAELEADSEV---EDELAALKAKM 217
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2161-2573 |
1.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2161 RLNASIADLQSQLRSPLGPRHETAQQLEVLEQQSTSL---------GQDA-RRLG---GQAVGTRDQASQLLAGT---EA 2224
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawlaAQDAlARLReqsGEEFEDSQDVTEYMQQLlerER 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2225 TLGHAKTLLAA-IRAVDRTLSELmsqtghlglanaSAPSGEQL--LRTLAE---------------------VERLLWEM 2280
Cdd:PRK04863 642 ELTVERDELAArKQALDEEIERL------------SQPGGSEDprLNALAErfggvllseiyddvsledapyFSALYGPA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2281 R----ARDLGapqaaaeaelaaaqrllaRVQEQLSSLWE--ENQALATQTRDRLAQ--HEAglmdlrEALNRAV------ 2346
Cdd:PRK04863 710 RhaivVPDLS------------------DAAEQLAGLEDcpEDLYLIEGDPDSFDDsvFSV------EELEKAVvvkiad 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2347 ---------------DATREAQeLNSRNQERlEEALQRKQELSRDNATLQATLHAARDTLAS----VFR-----LLHSLD 2402
Cdd:PRK04863 766 rqwrysrfpevplfgRAAREKR-IEQLRAER-EELAERYATLSFDVQKLQRLHQAFSRFIGShlavAFEadpeaELRQLN 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2403 QAKEELERLAASLDGARtpLLQRMQtfspagsklrlVEAAEAHAQQLGQLALNLSsiILDVN--QDRLTQ------RAIE 2474
Cdd:PRK04863 844 RRRVELERALADHESQE--QQQRSQ-----------LEQAKEGLSALNRLLPRLN--LLADEtlADRVEEireqldEAEE 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2475 A-------SNAYSRI------LQAVQAAEDAAGQALQQADHTWATVVRQG-----LVDR--------AQQLLANSTALEE 2528
Cdd:PRK04863 909 AkrfvqqhGNALAQLepivsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfalteVVQRrahfsyedAAEMLAKNSDLNE 988
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2217335166 2529 AMlqeQQRLGLVWAALQGARTQLRDVRAKKDQ-------LEAHIQAAQAMLA 2573
Cdd:PRK04863 989 KL---RQRLEQAEQERTRAREQLRQAQAQLAQynqvlasLKSSYDAKRQMLQ 1037
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2435-2657 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2435 KLRLVEAAEAHAQQLGQLALNLSSIiLDVNQDRLT------------QRAIEASNAYSR--ILQAVQAAEDAAGQALQQa 2500
Cdd:COG3206 102 KLNLDEDPLGEEASREAAIERLRKN-LTVEPVKGSnvieisytspdpELAAAVANALAEayLEQNLELRREEARKALEF- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2501 dhtwatvvrqgLVDRAQQLLANSTALEEAMLQEQQRLGLVWAA---------LQGARTQLRDVRAKKDQLEAHIQAAQAM 2571
Cdd:COG3206 180 -----------LEEQLPELRKELEEAEAALEEFRQKNGLVDLSeeaklllqqLSELESQLAEARAELAEAEARLAALRAQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2572 LAMDTDETSKKIAHAKAVAAEAQdtATRVQSQLQAMQEN-------VERWQGQYEGLRGQ---DLGQAVLDAGHSVSTLE 2641
Cdd:COG3206 249 LGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARytpnhpdVIALRAQIAALRAQlqqEAQRILASLEAELEALQ 326
|
250
....*....|....*.
gi 2217335166 2642 KTLPQLLAKLSILENR 2657
Cdd:COG3206 327 AREASLQAQLAQLEAR 342
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2071-2099 |
2.20e-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: 2.20e-04
10 20 30
....*....|....*....|....*....|....
gi 2217335166 2071 CQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2099
Cdd:pfam00053 1 CDCNPhgslsDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2070-2099 |
3.37e-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: 3.37e-04
10 20 30
....*....|....*....|....*....|....*
gi 2217335166 2070 RCQCPG-----GRCDPHTGRCNCPPGLSGERCDTC 2099
Cdd:cd00055 1 PCDCNGhgslsGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2071-2099 |
3.75e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.75e-04
10 20 30
....*....|....*....|....*....|....
gi 2217335166 2071 CQCP-----GGRCDPHTGRCNCPPGLSGERCDTC 2099
Cdd:smart00180 1 CDCDpggsaSGTCDPDTGQCECKPNVTGRRCDRC 34
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
2307-2411 |
3.80e-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: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEENQAL-------ATQTrDRLAQHEAGLM---------------DLREALNRAVDATREAQELNSRNQERLE 2364
Cdd:pfam04849 170 QEKLRGLEEENLKLrseashlKTET-DTYEEKEQQLMsdcveqlseanqqmaELSEELARKMEENLRQQEEITSLLAQIV 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217335166 2365 EALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELERL 2411
Cdd:pfam04849 249 DLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGM 295
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
300-345 |
3.90e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217335166 300 CVCH--GHADacdakDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQPW 345
Cdd:smart00180 1 CDCDpgGSAS-----GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
2303-2575 |
3.91e-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: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEQLSslweenqalatQTRDRLAQHEAGLMDLREAlnRAVDATREAQELNSRNQerLEEALQRKQELSRDNATLQA 2382
Cdd:TIGR01844 136 LAALKEQLD-----------LARARFDVGLGTRTDVLQA--EARYASARAQLIQAQNN--LDDAKAQLRRLVGQPELAPL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2383 TLHAARDtlasvfRLLHSLDQAKEELER-----LAA--SLDGARTPLLQR----MQTFSPAGSKLRLVEAAEAHAQQLGQ 2451
Cdd:TIGR01844 201 AVPSFPA------ELPEPLDQLLEIAEAsnpllLAAqaAVDAARYQVEQAraghLPTLSLTASTGNSDTSSGGSGNSDSD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2452 LAlnlsSIILDVN----QDRLTQRAIEAsnAYSRILQAVQAAEDAAGQALQQADHTWATVV--RQGLVDRAQQLLANSTA 2525
Cdd:TIGR01844 275 TY----SVGLNVSiplyQGGATSAQVRQ--AAHQLNQSRSTLESQKRTVRQQVRNAWSNLNaaAASVQAYEQQVASAQKA 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217335166 2526 LeEAMLQEQQ---R--LGLVWA--ALQGARTQLrdVRAKKDQLEAHIQAAQAMLAMD 2575
Cdd:TIGR01844 349 L-DAYRQEYQvgtRtlLDVLNAeqELYQARQEL--ANARYDYLQAQLNLLSATGTLN 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2118-2410 |
4.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2118 CEVCDHcvvlLLDDLERAGaLLPAIHEQLRGINAssmawaRLHRLNASIADLQSQLR---------SPLGPRHETAQQLE 2188
Cdd:PRK03918 438 CPVCGR----ELTEEHRKE-LLEEYTAELKRIEK------ELKEIEEKERKLRKELRelekvlkkeSELIKLKELAEQLK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2189 VLEQQSTSLG--------QDARRLGGQAVGTRDQASQL---LAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLAn 2257
Cdd:PRK03918 507 ELEEKLKKYNleelekkaEEYEKLKEKLIKLKGEIKSLkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE- 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2258 asapSGEQLLRTLAEVERLLWE-MRARDlgapqaaaeaelaaAQRLLARVQEQLSSLWEEnqalATQTRDRLAQHEAGLM 2336
Cdd:PRK03918 586 ----SVEELEERLKELEPFYNEyLELKD--------------AEKELEREEKELKKLEEE----LDKAFEELAETEKRLE 643
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217335166 2337 DLREALNravdatreaqELNSR-NQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHSLDQAKEELER 2410
Cdd:PRK03918 644 ELRKELE----------ELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
387-416 |
4.39e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 4.39e-04
10 20 30
....*....|....*....|....*....|
gi 2217335166 387 YQGGGVCiDCQHHTTGVNCERCLPGFYRSP 416
Cdd:smart00180 14 DPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2129-2609 |
5.09e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2129 LDDLERAgalLPAihEQLRGinassmAWARLHRLNASIAD-----------LQSQLRSPLGPRHETAQQLEVLEQQSTSL 2197
Cdd:PRK10246 280 LAALSLA---QPA--RQLRP------HWERIQEQSAALAHtrqqieevntrLQSTMALRARIRHHAAKQSAELQAQQQSL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2198 GQ-----DARRLGGQAV-GTRDQASQL------LAGTEATLGHAKTLLAAIRAVDRTLSelmsqtghlglANASAPSGEQ 2265
Cdd:PRK10246 349 NTwlaehDRFRQWNNELaGWRAQFSQQtsdreqLRQWQQQLTHAEQKLNALPAITLTLT-----------ADEVAAALAQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2266 LLRTLAEVERLLwemrardlgapqaaaeaelaaaqRLLARVQEQLSSLwEENQALATQTRDRLAQHEAGLMDLRealnra 2345
Cdd:PRK10246 418 HAEQRPLRQRLV-----------------------ALHGQIVPQQKRL-AQLQVAIQNVTQEQTQRNAALNEMR------ 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2346 vdatreaQELNSRNQERLE-----EALQRKQELSRDNATLQA---------TLHAARDTLASVF-----RLLHSLDQAKE 2406
Cdd:PRK10246 468 -------QRYKEKTQQLADvkticEQEARIKDLEAQRAQLQAgqpcplcgsTSHPAVEAYQALEpgvnqSRLDALEKEVK 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2407 ELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRLTqraieASNAYSRIL--- 2483
Cdd:PRK10246 541 KLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLD-----AQEEHERQLrll 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2484 ---QAVQAAEDAAGQALQQADHTWATvVRQGLVDraqQLLANSTAL-----EEAMLQEQQRLGLVWAALQgarTQLRDVR 2555
Cdd:PRK10246 616 sqrHELQGQIAAHNQQIIQYQQQIEQ-RQQQLLT---ALAGYALTLpqedeEASWLATRQQEAQSWQQRQ---NELTALQ 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2556 AKKDQLEAHIQAAQAMLAMDTDETSkkiaHAKAVAAEAQDTATRVQSQLQAMQE 2609
Cdd:PRK10246 689 NRIQQLTPLLETLPQSDDLPHSEET----VALDNWRQVHEQCLSLHSQLQTLQQ 738
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2302-2449 |
5.57e-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: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2302 LLARVQEQLSSLweenqalatqtRDRLAQHEAglmDLREALNRAVD--------ATREAQELNSRNQERLEEALQRKQEL 2373
Cdd:pfam01442 38 LRERLQKDLEEV-----------RAKLEPYLE---ELQAKLGQNVEelrqrlepYTEELRKRLNADAEELQEKLAPYGEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2374 SRDNA-----TLQATLHAARDtlasvfRLLHSLDQAKEEL-ERLAASLDGARTPLLQRMQtfspagsklRLVEAAEAHAQ 2447
Cdd:pfam01442 104 LRERLeqnvdALRARLAPYAE------ELRQKLAERLEELkESLAPYAEEVQAQLSQRLQ---------ELREKLEPQAE 168
|
..
gi 2217335166 2448 QL 2449
Cdd:pfam01442 169 DL 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2303-2582 |
5.69e-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: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEQLSSLWEENQALAtQTRDRLAQHEAGLMD-LREALNRAVDATREAQELN---SRNQERLEEALQRKQELSRDNA 2378
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQ-SELRRIENRLDELSQeLSDASRKIGEIEKEIEQLEqeeEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2379 TLQATLHAARDTLASVFRLLHSLdqaKEELERLAASLDGARTPLLQRM-----QTFSPAGSKLRLVEAAEAHAQQLGQLA 2453
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSRIPEIQAElskleEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2454 ----LNLSSIILDV-NQDRLTQRAIEASNAYSRILQAV----QAAE-----------------DAAGQALQQADHTWATV 2507
Cdd:TIGR02169 832 ekeiQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEleelEAALrdlesrlgdlkkerdelEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2508 vrqglVDRAQQLLANSTALEEAMLQEQQRLGLVWAALQ---GARTQLRDVRAKKDQLEAHIQAAQA--MLAMDTDETSKK 2582
Cdd:TIGR02169 912 -----IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALEPvnMLAIQEYEEVLK 986
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2303-2537 |
7.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEQLSSLWEENQALATQTRDRL--AQHEAGLMDLREALNRAVDATREAQELNSR---NQERLEEALQRKQELSRDN 2377
Cdd:COG4913 636 LEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLAALEEQleeLEAELEELEEELDELKGEI 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2378 ATLQATLHAARDtlasvfrllhSLDQAKEELERLAASLDGARTPLLQRMqtfspagsklRLVEAAEAHAQQLGQlalNLS 2457
Cdd:COG4913 716 GRLEKELEQAEE----------ELDELQDRLEAAEDLARLELRALLEER----------FAAALGDAVERELRE---NLE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2458 SII--LDVNQDRLTQRAIEASNAYSR----ILQAVQAAEDAAGQALQQADhtwaTVVRQGLVDRAQQLLAnstALEEAML 2531
Cdd:COG4913 773 ERIdaLRARLNRAEEELERAMRAFNRewpaETADLDADLESLPEYLALLD----RLEEDGLPEYEERFKE---LLNENSI 845
|
....*.
gi 2217335166 2532 QEQQRL 2537
Cdd:COG4913 846 EFVADL 851
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
2338-2578 |
7.52e-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: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2338 LREALNRAVDATREAQELNS-------------RNQERLEEALQ-RKQELSRDNATLQATLHaardtLASVFRLLHSLDQ 2403
Cdd:COG2956 20 LNGQPDKAIDLLEEALELDPetveahlalgnlyRRRGEYDRAIRiHQKLLERDPDRAEALLE-----LAQDYLKAGLLDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2404 AKEELERLAASLDGARTPLLQRMQTFspagSKLRLVEAAEAHAQQLgqLALNLSSIILDVNQDRLTQRAIEASNAYSRIL 2483
Cdd:COG2956 95 AEELLEKLLELDPDDAEALRLLAEIY----EQEGDWEKAIEVLERL--LKLGPENAHAYCELAELYLEQGDYDEAIEALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2484 QAVQAAEDAAGQALQQADhtwaTVVRQGLVDRAQQLLANSTALEEAMLQEQQRLGLVWAAL---QGARTQLRDVRAKKDQ 2560
Cdd:COG2956 169 KALKLDPDCARALLLLAE----LYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLgdpEEALELLRKALELDPS 244
|
250
....*....|....*...
gi 2217335166 2561 LEAHIQAAQAMLAMDTDE 2578
Cdd:COG2956 245 DDLLLALADLLERKEGLE 262
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2307-2626 |
7.63e-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: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRavdaTREAQELNSRNQERLEEALQRKQELSRdnatLQATLHA 2386
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQEEQLKKQQLLKQ----LRARIEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2387 ARDTLASVFRLLHSLDQAK------EELERLaASLDGARTPLLQRMQtfspagSKLRLVEAAEAHAQQLGQLALNLSSii 2460
Cdd:TIGR00618 272 LRAQEAVLEETQERINRARkaaplaAHIKAV-TQIEQQAQRIHTELQ------SKMRSRAKLLMKRAAHVKQQSSIEE-- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2461 ldvnQDRLTQraieasnaysRILQAVQAAEDAAGQALQQADH-TWATVVRQGLVDRAQQL-----LANSTALEEAMLQEQ 2534
Cdd:TIGR00618 343 ----QRRLLQ----------TLHSQEIHIRDAHEVATSIREIsCQQHTLTQHIHTLQQQKttltqKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2535 QrlglvwaALQGARTQ-LRDVRAKKDQLEAHIQAAQAMLAMD----TDETSKKIAHAKAVAAEAQDTATRVQ--SQLQAM 2607
Cdd:TIGR00618 409 Q-------ATIDTRTSaFRDLQGQLAHAKKQQELQQRYAELCaaaiTCTAQCEKLEKIHLQESAQSLKEREQqlQTKEQI 481
|
330
....*....|....*....
gi 2217335166 2608 QENVERwQGQYEGLRGQDL 2626
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 ... |
2421-2574 |
9.60e-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: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2421 PLLQrmqtFSPAGSKLRLVEAAEAHAQQLGQLALNLSSI----ILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQA 2496
Cdd:pfam00529 47 VLFQ----LDPTDYQAALDSAEAQLAKAQAQVARLQAELdrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2497 LQQADHTWAT-----VVRQGLVDRAQQLLANSTALeeamLQEQQRLGLVWA-ALQGARTQLRDVRAKKDQLEAHIQAAQA 2570
Cdd:pfam00529 123 QIDLARRRVLapiggISRESLVTAGALVAQAQANL----LATVAQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
....
gi 2217335166 2571 MLAM 2574
Cdd:pfam00529 199 ELKL 202
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2230-2444 |
9.83e-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: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2230 KTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQL--LRT-LAEVERLLWEMRARdlgapqaaaeaelaaaqrlLARV 2306
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLseLESqLAEARAELAEAEAR-------------------LAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLWEENQALAT-----QTRDRLAQHEAGLMDLREALN----RAVDATREAQELNSRNQERLEEALQrkqELSRDN 2377
Cdd:COG3206 246 RAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILA---SLEAEL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2378 ATLQATLHAARDTLASVFRLLHSLDQAKEELERLAASLDGAR---TPLLQRMQ----TFSPAGSKLRLVEAAEA 2444
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARelyESLLQRLEearlAEALTVGNVRVIDPAVV 396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2475-2630 |
1.15e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2475 ASNAYSRILQAVQAAEDAAGQALQQADHTWATV--VRQGLVDRAQQLLANSTALEEAMLQEQQRLglvwAALQGARTQLR 2552
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELeqLEEELEQARSELEQLEEELEELNEQLQAAQ----AELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2553 DVRAKKDQLEAHIQAAQA---MLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQA 2629
Cdd:COG4372 105 SLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
.
gi 2217335166 2630 V 2630
Cdd:COG4372 185 L 185
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2307-2537 |
1.29e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2307 QEQLSSLweenQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQElnsrNQERLEEALQ--RKQELS-RDNA-TLQA 2382
Cdd:PRK04778 354 EKQLESL----EKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK----EQEKLSEMLQglRKDELEaREKLeRYRN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2383 TLHAARDTLASVfRL-------LHSLDQAKEELERLAASLDgaRTPLlqRMQTFSpagsklRLVEAAEAHAQQLGQLALN 2455
Cdd:PRK04778 426 KLHEIKRYLEKS-NLpglpedyLEMFFEVSDEIEALAEELE--EKPI--NMEAVN------RLLEEATEDVETLEEETEE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2456 LssiildVNQDRLTQRAIEASNAY----SRILQAVQAAE------------DAAGQALQQADhtwatvvrQGLVDRaqql 2519
Cdd:PRK04778 495 L------VENATLTEQLIQYANRYrsdnEEVAEALNEAErlfreydykaalEIIATALEKVE--------PGVTKR---- 556
|
250
....*....|....*...
gi 2217335166 2520 lanstaLEEAMLQEQQRL 2537
Cdd:PRK04778 557 ------IEDSYEKEKETI 568
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
300-344 |
1.33e-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: 39.26 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217335166 300 CVCHGHADAcdaKDPTDPFRLQCTCQHNTCGGTCDRCCPGFNQQP 344
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2350-2519 |
1.43e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2350 REAQELNSRNQErLEEAL----QRKQELSRDNATLQATLHAARdtlasvfrllhsldQAKEELERLAASLDGARTPLLQR 2425
Cdd:PRK09039 53 SALDRLNSQIAE-LADLLslerQGNQDLQDSVANLRASLSAAE--------------AERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2426 MQTFSPAgsklrLVEAAEAHAQQLGQLALnlssiildVNQDrltqraIEASNaysRILQAVQAAEDAAGQALQQADHTWA 2505
Cdd:PRK09039 118 AGELAQE-----LDSEKQVSARALAQVEL--------LNQQ------IAALR---RQLAALEAALDASEKRDRESQAKIA 175
|
170
....*....|....*..
gi 2217335166 2506 TVVRQ---GLVDRAQQL 2519
Cdd:PRK09039 176 DLGRRlnvALAQRVQEL 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2345-2573 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2345 AVDATREAQELNSRNQERLEEALQRKQELSRDNATLQATLHAARDTLASvfrllhsLDQAKEELERLAASLDGARTPLLQ 2424
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-------LEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2425 RMQTFspagsklrlveAAEAHAQQLGQLALNLSSIILDVNqdrltqraiEASNAYSRiLQAVQAAEDAAGQALQQADHTw 2504
Cdd:COG3883 84 RREEL-----------GERARALYRSGGSVSYLDVLLGSE---------SFSDFLDR-LSALSKIADADADLLEELKAD- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2505 atvvrQGLVDRAQQLLANSTALEEAMLQEQQrlglvwAALQGARTQLRDVRAKKDQLEAHIQAAQAMLA 2573
Cdd:COG3883 142 -----KAELEAKKAELEAKLAELEALKAELE------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2155-2451 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2155 AWARLHRLNASIADLQSQLRsplgprhETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEATlghaktlla 2234
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIER-------QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE--------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2235 aIRAVDRTLSELMSQTghlglanasapsgEQLLRTLAEVERLLWEMRARdlgapqaaAEAELAAAQRLLARVqEQLSSLW 2314
Cdd:TIGR02169 289 -QLRVKEKIGELEAEI-------------ASLERSIAEKERELEDAEER--------LAKLEAEIDKLLAEI-EELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2315 EENQALATQTRDRLAQHEAGLMDLR---EALNRAVDATREaqELNSRnQERLEEA--------------LQRKQELSRDN 2377
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRaelEEVDKEFAETRD--ELKDY-REKLEKLkreinelkreldrlQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2378 ATLQATLHAARDTLASVFRLLHSLD----QAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVE----AAEAHAQQL 2449
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKAleikKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelaEAEAQARAS 502
|
..
gi 2217335166 2450 GQ 2451
Cdd:TIGR02169 503 EE 504
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2339-2474 |
2.08e-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: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2339 REALNRAVDATREAQELNSRNQERLEEALQRKQELsRDNATLQATLHAARdtlasvfrllhSLDQAKEELERLAASldgA 2418
Cdd:COG0711 37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEI-IAEARKEAEAIAEE-----------AKAEAEAEAERIIAQ---A 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217335166 2419 RtpllqrmqtfspagsklRLVEAAEAHA-----QQLGQLALNLSSIILDVN-----QDRLTQRAIE 2474
Cdd:COG0711 102 E-----------------AEIEQERAKAlaelrAEVADLAVAIAEKILGKEldaaaQAALVDRFIA 150
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2314-2789 |
2.10e-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: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2314 WEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELNSRNQERLEE-ALQRKQELSRDNATLQAtlHAARDTLA 2392
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEeAREAKAEAEQRAAELAA--EAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2393 SVFRLLHSLDQAKEELERLA----ASLDGARTPLLQRMQTFSPAgsKLRLVEAAEAHAQQLGQLALNLSSIILDVNQDRL 2468
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAkeaeAAAAAEKAAAAAEKEKAEEA--KRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2469 TQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRA--QQLLANSTALEEAMLQEQQRLGLVWAALQG 2546
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAaaAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2547 ARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEGLRGQDL 2626
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2627 GQAVLDAGHSVSTLEKTL--PQLLAKLSILENRGVHNASLALSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTP 2704
Cdd:COG3064 320 AAAAAGALVVRGGGAASLeaALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2705 RDLADLAAYTALKFYLQGPEPEPGQGTED-RFVMYMGSRQATGDYMGVSLRDKKVHWVYQLGEAGPAVLSIDEDIGEQFA 2783
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGaAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 2217335166 2784 AVSLDR 2789
Cdd:COG3064 480 LLLLGG 485
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2306-2453 |
2.64e-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: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2306 VQEQLSSLWEENQALATQtrdrLAQHEAGLMDLREALNRAVDATREAQELNSRNQERL-EEALQRKQELSRDNATLQATL 2384
Cdd:pfam04012 31 IRDMQSELVKARQALAQT----IARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELaREALAEKKSLEKQAEALETQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2385 HAARDTLASVFRLLHSLD----QAKEELERLAASLDGAR-----------------TPLLQRMQTfspagsklrLVEAAE 2443
Cdd:pfam04012 107 AQQRSAVEQLRKQLAALEtkiqQLKAKKNLLKARLKAAKaqeavqtslgslstssaTDSFERIEE---------KIEERE 177
|
170
....*....|
gi 2217335166 2444 AHAQQLGQLA 2453
Cdd:pfam04012 178 ARADAAAELA 187
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2352-2572 |
2.74e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2352 AQELNSRN--QERLEEALQRKQeLSRDNATLQATLhaaRDTLAsvfrLLHSLDQAKEELERLAASLDGArtPllQRMQTF 2429
Cdd:PRK11281 32 NGDLPTEAdvQAQLDALNKQKL-LEAEDKLVQQDL---EQTLA----LLDKIDRQKEETEQLKQQLAQA--P--AKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2430 SPAGSKLRLVEAAEAhAQQLGQLAL-NLSSIILDVNQD-RLTQRAIEASNAYSRILQA----VQAAEDAAGQALQQADHT 2503
Cdd:PRK11281 100 QAELEALKDDNDEET-RETLSTLSLrQLESRLAQTLDQlQNAQNDLAEYNSQLVSLQTqperAQAALYANSQRLQQIRNL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217335166 2504 WATVVRQGLVDRA--QQLLANSTALEEAMLQEQQRLglvwaaLQGArTQLRD--------VRAKKDQLEAHIQAAQAML 2572
Cdd:PRK11281 179 LKGGKVGGKALRPsqRVLLQAEQALLNAQNDLQRKS------LEGN-TQLQDllqkqrdyLTARIQRLEHQLQLLQEAI 250
|
|
| NIT |
pfam08376 |
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ... |
2321-2566 |
2.77e-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: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2321 ATQTRDRLAQHeaglmdlREALNRAVDATREAQ---ELNSRNQERLEEALQRKQELS--RDNATLQATlhAARDTLASVF 2395
Cdd:pfam08376 20 GGRFAAELAAQ-------RAATDAALAALRAALaelALPARLADRLAALLRALDQLPalRRQVDAGAL--SALEALAAYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2396 RLLHSLdqakeeLERLAASLDGARTP-LLQRMQTFSPagsklrLVEAAEAHAQQLGQLALNLSSiildvnqDRLTQraie 2474
Cdd:pfam08376 91 ELIAAL------LDLVDELAAGSPDPeLARQLRALAA------LLRAKEAAGQERALLAAALAA-------GRFTA---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2475 asNAYSRILQAVQAAEDAAGQALQQADHTWATvvrqglvdRAQQLLANSTALEEAMLQEQQRLGLVWAALQGAR-TQLRD 2553
Cdd:pfam08376 148 --AEYRRFLSLVAAQRAALAEFRAAATPEQRA--------LYDATVTGPAVAAAERLRDRLVDAAAWFAASTARiDLLRE 217
|
250
....*....|...
gi 2217335166 2554 VRakkDQLEAHIQ 2566
Cdd:pfam08376 218 VE---DRLADDLA 227
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2180-2502 |
2.77e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2180 RHETAQ-QLEVLEQQSTslgqdarrlgGQAVGTRDQASQLLAGTEATLGHAKTLLAAiravdrtlselmsqtghlglana 2258
Cdd:PRK10246 192 QHKSARtELEKLQAQAS----------GVALLTPEQVQSLTASLQVLTDEEKQLLTA----------------------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2259 sapsgEQLLRtlaevERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSSLweENQALATQTR---DRLAQHEAGL 2335
Cdd:PRK10246 239 -----QQQQQ-----QSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAAL--SLAQPARQLRphwERIQEQSAAL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2336 MDLRealnravdatREAQELNSrnqeRLEEALQRKQELSRDNATLQATLHAARDTLAS------VFRLLHS--------- 2400
Cdd:PRK10246 307 AHTR----------QQIEEVNT----RLQSTMALRARIRHHAAKQSAELQAQQQSLNTwlaehdRFRQWNNelagwraqf 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2401 --LDQAKEELERLAASLDGARtpllQRMQTFSPAGSKLRLVEAAEAHAQQ-----LGQLALNLSSIILDVnQDRLTQRAI 2473
Cdd:PRK10246 373 sqQTSDREQLRQWQQQLTHAE----QKLNALPAITLTLTADEVAAALAQHaeqrpLRQRLVALHGQIVPQ-QKRLAQLQV 447
|
330 340
....*....|....*....|....*....
gi 2217335166 2474 EASNAYSRILQAVQAAEDAAGQALQQADH 2502
Cdd:PRK10246 448 AIQNVTQEQTQRNAALNEMRQRYKEKTQQ 476
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2128-2439 |
2.77e-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: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2128 LLDDLERAGALLPAIHEQLRGINASSMAWARLHRLN----------ASIADLQSQLRSPLgprhETAQQLEVLEQQSTSL 2197
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaeREIAELEAELERLD----ASSDDLAALEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2198 GQDARRLGGQavgtRDQASQLLAGTEATLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANA-SAPSGEQLLRTLAEverl 2276
Cdd:COG4913 698 EAELEELEEE----LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfAAALGDAVERELRE---- 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2277 lwemrardlgapqaaaeaelaaaqRLLARVQEQLSSLWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELN 2356
Cdd:COG4913 770 ------------------------NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2357 S----RNQERLEEALQRKQElsRDNATLQATLHAARDTlasvfrllhsldqAKEELERLAASLdgARTPllqrmqtFSPa 2432
Cdd:COG4913 826 EdglpEYEERFKELLNENSI--EFVADLLSKLRRAIRE-------------IKERIDPLNDSL--KRIP-------FGP- 880
|
....*..
gi 2217335166 2433 GSKLRLV 2439
Cdd:COG4913 881 GRYLRLE 887
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2483-2573 |
2.80e-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: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2483 LQAVQAAEDAAGQALQQADHTWATVvrQGLVDRAQQLLANSTAleEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLE 2562
Cdd:TIGR04320 270 LAAAQTALNTAQAALTSAQTAYAAA--QAALATAQKELANAQA--QALQTAQNNLATAQAALANAEARLAKAKEALANLN 345
|
90
....*....|.
gi 2217335166 2563 AHIQAAQAMLA 2573
Cdd:TIGR04320 346 ADLAKKQAALD 356
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
2315-2448 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2315 EENQALaTQTRDRLAQHEAGLMDLREALNRAVDATRE----------------------AQELN---SRNQERLEEALQR 2369
Cdd:cd07596 1 EEDQEF-EEAKDYILKLEEQLKKLSKQAQRLVKRRRElgsalgefgkaliklakceeevGGELGealSKLGKAAEELSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2370 KQELSR-DNATLQATLH-------AARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEA 2441
Cdd:cd07596 80 SEAQANqELVKLLEPLKeylrycqAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAES 159
|
....*..
gi 2217335166 2442 AEAHAQQ 2448
Cdd:cd07596 160 ALEEARK 166
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2308-2681 |
3.72e-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: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2308 EQLSSLWEENQALATQTRdrlaqheagLMDLREALNRAVDATREAQELNSRNQERLE--EALQRKQELSRDNAT--LQAT 2383
Cdd:COG3206 71 SGLSSLSASDSPLETQIE---------ILKSRPVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSnvIEIS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2384 L------HAAR--DTLASVFrLLHSLDQAKEELERLAASLDGaRTPLLQRmqtfspagsKLRLVEAA-EAHAQQLGQLAL 2454
Cdd:COG3206 142 YtspdpeLAAAvaNALAEAY-LEQNLELRREEARKALEFLEE-QLPELRK---------ELEEAEAAlEEFRQKNGLVDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2455 NLSSIILDVNQDRLTQRAIEASNAysriLQAVQAAEDAAGQALQQADHTWATVVRQGLVdraQQLLANSTALEEAMLQEQ 2534
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEARAE----LAEAEARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2535 QRLGlvwaalqgarTQLRDVRAKKDQleahIQAAQAMLAMDTDETSKKIahakavaaeaQDTATRVQSQLQAMQENVERW 2614
Cdd:COG3206 284 ARYT----------PNHPDVIALRAQ----IAALRAQLQQEAQRILASL----------EAELEALQAREASLQAQLAQL 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217335166 2615 QGQYEGLRGQDLGQAVLDagHSVSTLEKTLPQLLAKLSilenrgvhNASLALSASIGRVReLIAQAR 2681
Cdd:COG3206 340 EARLAELPELEAELRRLE--REVEVARELYESLLQRLE--------EARLAEALTVGNVR-VIDPAV 395
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2122-2684 |
4.12e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.31 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2122 DHCVVLLLDDLERA-GALLPAIHEQLRGINASSMAW---------ARLHRLNASIADLQSQLRS----PLGP--RHETAQ 2185
Cdd:COG3899 432 ERPLVLVLDDLHWAdPASLELLEFLLRRLRDLPLLLvgtyrpeevPPAHPLRLLLAELRRAGAGvtrlELGPlsREEVAA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2186 QL-EVLEQQSTS-----------------LGQDARRLGGQAVGTRDQASQLLAGTEATLGHAKTLLAAIRAvdRtLSELM 2247
Cdd:COG3899 512 LVaDLLGAAELPaelaellvertggnpffLEELLRALLEEGLLRFDGGGWRWDAALAALALPDTVVDLLAA--R-LDRLP 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2248 SQTGHLgLANASA---PSGEQLLRTL-----AEVERLLWEMRARDLgapQAAAEAELAAAQRLL-ARVQEQL-SSLWEEN 2317
Cdd:COG3899 589 PAARRV-LRLAAVlgrRFDLELLAAVlglseAELAAALEELVAAGL---LVPRGDAGGGRYRFRhDLVREAAyASLPPEE 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2318 ---------QALATQTRD-------RLAQH--EAGlmDLREALNRAVDATREAQELNSrnqerLEEA---LQRKQELSRD 2376
Cdd:COG3899 665 rralhrriaRALEARGPEpleerlfELAHHlnRAG--ERDRAARLLLRAARRALARGA-----YAEAlryLERALELLPP 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2377 NATLQATLhAARDTLASVFRLLHSLDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAE---AHAQQLGQLA 2453
Cdd:COG3899 738 DPEEEYRL-ALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLgdyEEAYEFGELA 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2454 LNLSSIILDVNQ---------------------DRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGL 2512
Cdd:COG3899 817 LALAERLGDRRLearalfnlgfilhwlgplreaLELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2513 VDRAQQLLANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDTDETSKKIAHAKAVAAE 2592
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2593 AQDTATRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGR 2672
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
650
....*....|..
gi 2217335166 2673 VRELIAQARGAA 2684
Cdd:COG3899 1057 AAAAALAAAAAL 1068
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
2309-2672 |
4.38e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2309 QLSSLWEenQALATQTRdrLAQHEAGLMDLREALNRAVDATREAQEL----NSRNQERLEEALQRKQELSRDNATLQATL 2384
Cdd:COG1538 1 TLDELIE--RALANNPD--LRAARARVEAARAQLRQARAGLLPSQELdlggKRRARIEAAKAQAEAAEADLRAARLDLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2385 HAARdTLASVFRLLHSLDQAKEELERLAASLD--------GARTPL-LQRMQTFSpAGSKLRLVEAAEAHAQQLGQLALN 2455
Cdd:COG1538 77 EVAQ-AYFDLLAAQEQLALAEENLALAEELLElararyeaGLASRLdVLQAEAQL-AQARAQLAQAEAQLAQARNALALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2456 L-----SSIILDVNQDRLTQRAIEASNAYSRILQ---AVQAAEDAAGQALQQADHTWA------TVVRQGLVDRAQQLLA 2521
Cdd:COG1538 155 LglpppAPLDLPDPLPPLPPLPPSLPGLPSEALErrpDLRAAEAQLEAAEAEIGVARAaflpslSLSASYGYSSSDDLFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2522 NSTALEEAMLQEQQRL---GLVWAALQGARTQLRDVRAKKDQ--LEAHIQAAQAMLAMDTDetskkiahakavaaeaQDT 2596
Cdd:COG1538 235 GGSDTWSVGLSLSLPLfdgGRNRARVRAAKAQLEQAEAQYEQtvLQALQEVEDALAALRAA----------------REQ 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217335166 2597 ATRVQSQLQAMQENVERWQGQYE-GLRGQdlgQAVLDAghsvstlEKTLpqLLAKLSILENRG-VHNASLALSASIGR 2672
Cdd:COG1538 299 LEALEEALEAAEEALELARARYRaGLASL---LDVLDA-------QREL--LQAQLNLIQARYdYLLALVQLYRALGG 364
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2330-2629 |
4.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2330 QHEAG---LMD-LREALNRAVDatREAQELNSRNQERLEEALQRKQELSRDnatlqatLHAARDTLASVFRLLHSLDQAK 2405
Cdd:COG4717 31 PNEAGkstLLAfIRAMLLERLE--KEADELFKPQGRKPELNLKELKELEEE-------LKEAEEKEEEYAELQEELEELE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2406 EELERLAASLDGARtpllQRMQtfspagsKLRLVEAAEAHAQQLGQLALNLSSIildvnQDRLtqraieasnaysrilqa 2485
Cdd:COG4717 102 EELEELEAELEELR----EELE-------KLEKLLQLLPLYQELEALEAELAEL-----PERL----------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2486 vqaaedaagQALQQADHTWATVVRQgLVDRAQQLLANSTALEEAMLQEQQRlglVWAALQGARTQLRDVRAKKDQLEAHI 2565
Cdd:COG4717 149 ---------EELEERLEELRELEEE-LEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEEL 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217335166 2566 QAAQamlamdtdetskkiahakavaaeaqdtatrvqsqlqamqENVERWQGQYEGLRGQDLGQA 2629
Cdd:COG4717 216 EEAQ---------------------------------------EELEELEEELEQLENELEAAA 240
|
|
| FlgL |
COG1344 |
Flagellin and related hook-associated protein FlgL [Cell motility]; |
2303-2500 |
4.82e-03 |
|
Flagellin and related hook-associated protein FlgL [Cell motility];
Pssm-ID: 440955 [Multi-domain] Cd Length: 245 Bit Score: 41.77 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2303 LARVQEQLSSLWEENQA--LATQTrdrlaqheAGLMDLREALNRAVDATREAQELNSRNQ------ERLEEALQRKQELs 2374
Cdd:COG1344 23 LAKLQEQLSSGKRINSAsdDPAGA--------AIALRLRSQIRGLEQYQRNANDAISRLQtaegalGEITDILQRAREL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2375 rdnaTLQA---TLHAA-RDTLASvfrllhSLDQAKEELERLAASLDGARTPLLQRMQTFSP---------AGSKLRLVEA 2441
Cdd:COG1344 94 ----AVQAangTLSDEdRAAIAA------ELEQLLDQLLSIANTTDFNGRYLFAGTATDTPpfqvdyqgdAGQRTAALGA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217335166 2442 AEAHAQQLGQLALNLSSII--LDVNQDRLTQRAIEASNAYSRI-----------LQAVQAAEDAAGQALQQA 2500
Cdd:COG1344 164 LDAALDNVSSARAELGARQnrLESAINNLSDLSENLTAALSRLedadmaeaitrLTKLQTLLQAALAALAQA 235
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2301-2419 |
5.19e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2301 RLLARVQEQLSSLweENQALA--TQTRDRLA--------QHEAGLMDLREALNRAVDATREAQELNSRNQERLEEALQRK 2370
Cdd:COG1842 58 RQLEELEAEAEKW--EEKARLalEKGREDLArealerkaELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKK 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2217335166 2371 QEL-SRDNA-----TLQATLHAARDTLAsvfrlLHSLDQAKEELERLAASLDGAR 2419
Cdd:COG1842 136 DTLkARAKAakaqeKVNEALSGIDSDDA-----TSALERMEEKIEEMEARAEAAA 185
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
2214-2583 |
5.95e-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: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2214 QASQLLAGTEATLGH---AKTLLAAIRAVDRTLSELMSQtghLGLANASAPSGEQLLRTLAEVErllweMRARDLgapqa 2290
Cdd:TIGR02917 313 QAYQYLNQILKYAPNshqARRLLASIQLRLGRVDEAIAT---LSPALGLDPDDPAALSLLGEAY-----LALGDF----- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2291 aaeaelAAAQRLLARVQEQLSslweENQALATQT-RDRLAQ--HEAGLMDLREALNRAVDATR----------EAQELNS 2357
Cdd:TIGR02917 380 ------EKAAEYLAKATELDP----ENAAARTQLgISKLSQgdPSEAIADLETAAQLDPELGRadlllilsylRSGQFDK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2358 RN--QERLEE--------------ALQRKQELSRDNATLQATLHAARDTLASVFRLLH------SLDQAKEELERLAASL 2415
Cdd:TIGR02917 450 ALaaAKKLEKkqpdnaslhnllgaIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARidiqegNPDDAIQRFEKVLTID 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2416 DGARTPLLQ----RMQTFSPAGSKLRLVEAAEAHAQQLgQLALNLSSIILDVNQdrlTQRAIEASNAYSRILQAVQAAED 2491
Cdd:TIGR02917 530 PKNLRAILAlaglYLRTGNEEEAVAWLEKAAELNPQEI-EPALALAQYYLGKGQ---LKKALAILNEAADAAPDSPEAWL 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2492 AAGQA-LQQADHTWATVVRQGLVDRAQQllaNSTALEE-AMLQEQQRlglvwaALQGARTQLRdvRA---KKDQLEAHIQ 2566
Cdd:TIGR02917 606 MLGRAqLAAGDLNKAVSSFKKLLALQPD---SALALLLlADAYAVMK------NYAKAITSLK--RAlelKPDNTEAQIG 674
|
410
....*....|....*..
gi 2217335166 2567 AAQAMLAMDTDETSKKI 2583
Cdd:TIGR02917 675 LAQLLLAAKRTESAKKI 691
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2304-2684 |
6.66e-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: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2304 ARVQEQLSSLweENQALATQTRDRLAQHEA------GLMDLREALNRAVDATREAQ----ELNSRNQERLEEA------L 2367
Cdd:COG3064 12 AAAQERLEQA--EAEKRAAAEAEQKAKEEAeeerlaELEAKRQAEEEAREAKAEAEqraaELAAEAAKKLAEAekaaaeA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2368 QRK--QELSRDNATLQATLHAARDTLASVFRllhSLDQAKEELERLA------ASLDGARTPLLQRMQTFSPAGSKLRLV 2439
Cdd:COG3064 90 EKKaaAEKAKAAKEAEAAAAAEKAAAAAEKE---KAEEAKRKAEEEAkrkaeeERKAAEAEAAAKAEAEAARAAAAAAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2440 EAAEAHAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQAAEDAAGQALQQADHTWATVVRQGLVDRAQQL 2519
Cdd:COG3064 167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2520 LANSTALEEAMLQEQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQA--MLAMDTDETSKKIAHAKAVAAEAQDTA 2597
Cdd:COG3064 247 GAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLddSAALAAELLGAVAAEEAVLAAAAAAGA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 2598 TRVQSQLQAMQENVERWQGQYEGLRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASLALSASIGRVRELI 2677
Cdd:COG3064 327 LVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLD 406
|
....*..
gi 2217335166 2678 AQARGAA 2684
Cdd:COG3064 407 LGAALLE 413
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
3509-3576 |
9.47e-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: 9.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217335166 3509 TGLIFHLGQARTPPYLQLQVT--EKQVLLRADDGAGEFSTSVTRPSVLCDGQWHRLAVMKSGNVLRLEVD 3576
Cdd:smart00210 67 RGVLFAIYDAQNVRQFGLEVDgrANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVD 136
|
|
| |
