|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1-1213 |
0e+00 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 1634.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1 MVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEI 80
Cdd:TIGR00606 99 MVCTQKTKKTEFKTLEGVITRYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 81 FSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIE 160
Cdd:TIGR00606 179 FSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 161 HNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLL 240
Cdd:TIGR00606 259 HNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 241 NQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVRERQEGEAKTANQLMNDFA 320
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 321 EKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVET 400
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTET 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 401 LKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDW 480
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDW 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 481 LHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAML 560
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAML 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 561 AGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSI 640
Cdd:TIGR00606 659 AGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 641 IDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGI 720
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 721 DLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQ 800
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 801 SLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETE 880
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE 978
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 881 LNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQK 960
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK 1058
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 961 LEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMK 1040
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMK 1138
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1041 MEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAE 1120
Cdd:TIGR00606 1139 MEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAE 1218
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1121 TFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRIKKNIDQCSEI 1200
Cdd:TIGR00606 1219 TFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRLKKNEDQCSEI 1298
|
1210
....*....|...
gi 1099267288 1201 VKCSVSSLGFNVH 1213
Cdd:TIGR00606 1299 VKCSPSSLGKRVH 1311
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1096-1198 |
8.96e-43 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 155.07 E-value: 8.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1096 LDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIEslaHALVEIIKSRSQQRNFQLLVITHDEDFV 1175
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIE---ESLAEIIEERKSQKNFQLIVITHDEELV 186
|
90 100
....*....|....*....|...
gi 1099267288 1176 ELLGrseyveKFYRIKKNIDQCS 1198
Cdd:cd03240 187 DAAD------HIYRVEKDGRQKS 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-913 |
2.12e-17 |
|
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: 88.19 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 91 ETLRQVRQTQG--QKV----KEYQMELKYLKQYKEKA---CEIRDQItsKEAQLTSSKEIVKSYENELDPLKNRLKEIEH 161
Cdd:TIGR02168 176 ETERKLERTREnlDRLedilNELERQLKSLERQAEKAeryKELKAEL--RELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 162 nlsKIMKLDNEIKALDSRKKQMEKDNSELEEKMEkvfqgtdeQLNDLYHNHQRTVREKERklvdchrELEKLNKESRLLN 241
Cdd:TIGR02168 254 ---ELEELTAELQELEEKLEELRLEVSELEEEIE--------ELQKELYALANEISRLEQ-------QKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 242 QEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLEldgfergpfserqiknfhklvreRQEGEAKTANQLMNDFAE 321
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-----------------------SLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 322 KETLKQKQIDEIRDKktglgrIIELKSEILSKkQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETL 401
Cdd:TIGR02168 373 RLEELEEQLETLRSK------VAQLELQIASL-NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 402 KMEVISLQNEKADLDRTLRKLDQEMEQLNhhtttrtqmEMLTKDKADKDEQIRKIKSRHSDElTSLLGYFPNKKQLEDWl 481
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAE---------QALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKN- 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 482 hskSKEINQTRDRLAKLnkeLASSEQNKNHINNELkrkEEQLSSYEDKlfdvcGSQDFESDLDRLKeeieKSSKQRAMLA 561
Cdd:TIGR02168 515 ---QSGLSGILGVLSEL---ISVDEGYEAAIEAAL---GGRLQAVVVE-----NLNAAKKAIAFLK----QNELGRVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 562 GATAVYSQFIT----QLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTEselKKKEKRRDEML------ 631
Cdd:TIGR02168 577 PLDSIKGTEIQgndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALE---LAKKLRPGYRIvtldgd 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 632 ----------GLVPMRQSIIDlKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQ 700
Cdd:TIGR02168 654 lvrpggvitgGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALR 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 701 MELKDVERKIAQQAAKLQGIDLDRTVQQV-----NQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSE- 774
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAeieelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEl 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 775 ---KLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELinkkntsnkiaQDKLNDIKEK 851
Cdd:TIGR02168 813 tllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----------ESELEALLNE 881
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1099267288 852 VKNIHGYMKDIENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQK 913
Cdd:TIGR02168 882 RASLEEALALLRSELEE-LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1098-1199 |
3.13e-16 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 77.40 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1098 MRGRCSAGQKVLASLIIRLALAEtfCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNfQLLVITHDEDFVEL 1177
Cdd:cd03227 74 TRLQLSGGEKELSALALILALAS--LKPRPLYILDEIDRGLDPRD----GQALAEAILEHLVKGA-QVIVITHLPELAEL 146
|
90 100
....*....|....*....|..
gi 1099267288 1178 LgrseyvEKFYRIKKNIDQCSE 1199
Cdd:cd03227 147 A------DKLIHIKKVITGVYK 162
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
318-853 |
2.05e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 318 DFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKaeknsn 397
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 398 VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLlgyfpnKKQL 477
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI------EERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 478 EDwLHSKSKEINQTRDRLAKLNKELASSEQnKNHINNELKRKEEQLSSYEDKLFDVcGSQDFESDLDRLKEEIEKSSKQR 557
Cdd:PRK03918 331 KE-LEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 558 AMLAGATAVYSQFITQLTD------ENQSCCPVCQRVFqTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEML 631
Cdd:PRK03918 408 SKITARIGELKKEIKELKKaieelkKAKGKCPVCGREL-TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 632 GLVPMRQSIIDLKE--KEIPELRNKLQNVNrdIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERK 709
Cdd:PRK03918 487 KVLKKESELIKLKElaEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 710 IAQQAAKLQGI-------------DLDRTVQQ-------------VNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQH 763
Cdd:PRK03918 565 LDELEEELAELlkeleelgfesveELEERLKElepfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 764 LKSTTNELKSEklqisTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKI--A 841
Cdd:PRK03918 645 LRKELEELEKK-----YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekA 719
|
570
....*....|..
gi 1099267288 842 QDKLNDIKEKVK 853
Cdd:PRK03918 720 LERVEELREKVK 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
79-711 |
6.05e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 79 EIFSATRYIKALETLRQVRqtqgqkvKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKE 158
Cdd:PRK03918 153 QILGLDDYENAYKNLGEVI-------KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 159 IEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMekvfQGTDEQLNDLyHNHQRTVREKERKLvdchRELEKLNKESR 238
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI----RELEERIEEL-KKEIEELEEKVKEL----KELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 239 LLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKnfhklvRERQEGEAKTANQLMND 318
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR------LEELEERHELYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 319 FAEKETLKQKQIDEIRDKktgLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAE-------RELSK 391
Cdd:PRK03918 371 KEELERLKKRLTGLTPEK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 392 AEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNhhtTTRTQMEMLTKDKaDKDEQIRKIKSRHS----DELTSL 467
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE---KVLKKESELIKLK-ELAEQLKELEEKLKkynlEELEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 468 LGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASseqnknhINNELKRKEEQLSSYEDKLFDVcGSQDFESDLDRLK 547
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-------LEKKLDELEEELAELLKELEEL-GFESVEELEERLK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 548 eEIEKsskqramlagataVYSQFITQLTDEnqsccpvcqrvfQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRR 627
Cdd:PRK03918 596 -ELEP-------------FYNEYLELKDAE------------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 628 DEMLGLvpmrqsiidLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKvclTDVTIMERFQMELKDVE 707
Cdd:PRK03918 650 EELEKK---------YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK---EELEEREKAKKELEKLE 717
|
....
gi 1099267288 708 RKIA 711
Cdd:PRK03918 718 KALE 721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
294-969 |
1.64e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 294 IKNFHKLVRERQEGEAKTANQL-MNDFAEKETLKQKQIDEiRDKKTGLGRIIELkseilskkQSELKNVKYELQQLEGSS 372
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKeKREYEGYELLKEKEALE-RQKEAIERQLASL--------EEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 373 DRILELDQELIKAERELSKAEKNsnveTLKMEVISLQNEKADLDRTLRKLDQEMEQLNhhtttrtqmemltKDKADKDEQ 452
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERELEDAE-------------ERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 453 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQnknhinnELKRKEEQLSSYEDKLFD 532
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 533 VCGSQDfeSDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAEL---QEVISDLQSKLRLA 609
Cdd:TIGR02169 404 LKRELD--RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLskyEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 610 PDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIP----------------------ELRNKLQNV--------N 659
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataievAAGNRLNNVvveddavaK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 660 RDIQRLK------------NDIEEQETLLGTIMPE----------------EESAKVCLTDVTIMERF--------QMEL 703
Cdd:TIGR02169 562 EAIELLKrrkagratflplNKMRDERRDLSILSEDgvigfavdlvefdpkyEPAFKYVFGDTLVVEDIeaarrlmgKYRM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 704 KDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKqhKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKseklqistnlQ 783
Cdd:TIGR02169 642 VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPA--ELQRLRERLEGLKRELSSLQSELRRIENRLDELS----------Q 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 784 RRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQD---KLNDIKEKVKNIhgYMK 860
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEleeDLHKLEEALNDL--EAR 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 861 DIENYIQDGKDDYKKQKEtELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERK 940
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEE-EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
730 740
....*....|....*....|....*....
gi 1099267288 941 QHLKEMGQMQVLQMKSEHQKLEENIDNIK 969
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELE 895
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-830 |
3.40e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 88 KALETLRQVRQTQGQ---KVKEYQMELKYLKQYKEKAceIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLS 164
Cdd:TIGR02169 174 KALEELEEVEENIERldlIIDEKRQQLERLRREREKA--ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 165 KIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEK 244
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 245 SELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELdgfergpfserqiknfhkLVRERQEgEAKTANQLMNDFAEKET 324
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED------------------LRAELEE-VDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 325 LKQKQIDEIRDKKTGLGRIIELKSEiLSKKQSELKNvkyelqQLEGSSDRILELDQELIKAERELSKAEKN--SNVETLK 402
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQR-LSEELADLNA------AIAGIEAKINELEEEKEDKALEIKKQEWKleQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 403 MEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIR--------------KIKSRHSDELTSLL 468
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvaqlgSVGERYATAIEVAA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 469 GYFPNKKQLEDWLHSKS-----KEINQTRDRLAKLNKeLASSEQNKNHI------------------------------- 512
Cdd:TIGR02169 546 GNRLNNVVVEDDAVAKEaiellKRRKAGRATFLPLNK-MRDERRDLSILsedgvigfavdlvefdpkyepafkyvfgdtl 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 513 ---NNELKRK---EEQLSSYEDKLFDVCGS---------------QDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFI 571
Cdd:TIGR02169 625 vveDIEAARRlmgKYRMVTLEGELFEKSGAmtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 572 TQLTDENQSCCPVC-------QRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEM-LGLVPMRQSIIDL 643
Cdd:TIGR02169 705 DELSQELSDASRKIgeiekeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELeEDLHKLEEALNDL 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 644 KEK----EIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKvclTDVTIMERFQMELKDVERKIAQQAAKLQG 719
Cdd:TIGR02169 785 EARlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE---KEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 720 idldrTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSeklQISTNLQRRQQLEEQTVELSTEV 799
Cdd:TIGR02169 862 -----KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA---QIEKKRKRLSELKAKLEALEEEL 933
|
810 820 830
....*....|....*....|....*....|.
gi 1099267288 800 QSLYREIKDAKEqVSPLETTLEKFQQEKEEL 830
Cdd:TIGR02169 934 SEIEDPKGEDEE-IPEEELSLEDVQAELQRV 963
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1103-1184 |
7.75e-10 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 58.80 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVELLGRSE 1182
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-----AEEGRTVIIVTHDPELAELAADRV 150
|
..
gi 1099267288 1183 YV 1184
Cdd:cd00267 151 IV 152
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
297-1019 |
1.61e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 297 FHKLVRERQEGEAKT-ANQLMNDFAEKETLkQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLegSSDRI 375
Cdd:TIGR02169 213 YQALLKEKREYEGYElLKEKEALERQKEAI-ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL--GEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 376 LELDQELIKAERELSKAEknSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTT-RTQMEMLTKDKADKDEQIR 454
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLE--RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEEYAELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 455 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSsyedklfdvc 534
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN---------- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 535 gsqDFESDLDRLKEEIEKSSKQRamlagatavySQFITQLTDENQSccpvcqrvfqteaelqevISDLQSKLRLAPDKLK 614
Cdd:TIGR02169 438 ---ELEEEKEDKALEIKKQEWKL----------EQLAADLSKYEQE------------------LYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 615 STESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIP----------------------ELRNKLQNV--------NRDIQR 664
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataievAAGNRLNNVvveddavaKEAIEL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 665 LK------------NDIEEQETLLGTIMPE----------------EESAKVCLTDVTIMERFQM--------------- 701
Cdd:TIGR02169 567 LKrrkagratflplNKMRDERRDLSILSEDgvigfavdlvefdpkyEPAFKYVFGDTLVVEDIEAarrlmgkyrmvtleg 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 702 ELKDVERKIAQQAAKLQGIDLDRT-----VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKL 776
Cdd:TIGR02169 647 ELFEKSGAMTGGSRAPRGGILFSRsepaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 777 QI----STNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSN-KIAQDKLNDIKEK 851
Cdd:TIGR02169 727 QLeqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 852 VKNIHGYMKDIENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRIMRQDI-DTQKIQERWLQDNLTLRKRNE 930
Cdd:TIGR02169 807 VSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKeELEEELEELEAALRDLESRLG 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 931 ELKEVEEERKQHLKEMgQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELRE-PQFRDAEEKYREMM 1009
Cdd:TIGR02169 886 DLKKERDELEAQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEeLSLEDVQAELQRVE 964
|
810
....*....|
gi 1099267288 1010 IVMRTTELVN 1019
Cdd:TIGR02169 965 EEIRALEPVN 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
374-1072 |
5.76e-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: 60.84 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 374 RILELDQELIKAERELSKAEKNS---NVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNH-HTTTRTQMEMLTK----- 444
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEElreELEELQEELKEAEEELEELTAELQELEEKLEELRLeVSELEEEIEELQKelyal 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 445 --DKADKDEQIRKIKSRhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQ 522
Cdd:TIGR02168 294 anEISRLEQQKQILRER--------------LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 523 LSSYEDKLFD-VCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfqteaELQEVISD 601
Cdd:TIGR02168 360 LEELEAELEElESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE--------------RLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 602 LQSKLRLApdKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMP 681
Cdd:TIGR02168 426 LLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 682 EEESAK--------------VCLTDVTIMERFQMELKDVERKIAQ------QAAKLQGIDLDR----------------- 724
Cdd:TIGR02168 504 FSEGVKallknqsglsgilgVLSELISVDEGYEAAIEAALGGRLQavvvenLNAAKKAIAFLKqnelgrvtflpldsikg 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 725 TVQQVNQEKQEKQHK--------LDTVSSKIE------LNRKLIQDQQEQIQHLKSTTNEL------------------K 772
Cdd:TIGR02168 584 TEIQGNDREILKNIEgflgvakdLVKFDPKLRkalsylLGGVLVVDDLDNALELAKKLRPGyrivtldgdlvrpggvitG 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 773 SEKLQISTNLQRRQ---QLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEElinkKNTSNKIAQDKLNDIK 849
Cdd:TIGR02168 664 GSAKTNSSILERRReieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 850 EKVKNIHGYMKDIENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLTLRKRN 929
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 930 EELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELR--EPQFRDAEEKYRE 1007
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAslEEALALLRSELEE 898
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1099267288 1008 MMIVMRTTELVNKDLDIYYKTLDQAIMKFH------SMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADE 1072
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1103-1176 |
5.80e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.92 E-value: 5.80e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1176
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYFLD 131
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
71-580 |
1.10e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 71 KALKQKFDEIFSAT-----RYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSY 145
Cdd:COG4717 49 ERLEKEADELFKPQgrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 146 E--NELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKL 223
Cdd:COG4717 129 PlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 224 VDCHRELEKLNKESRLLNQEksellVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSerqiknfhklVRE 303
Cdd:COG4717 209 AELEEELEEAQEELEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS----------LIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 304 RQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELK-NVKYELQQLEGSSDRILELDQEL 382
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 383 IKAERELSKAEKNSNVETLKmevISLQNEKADLDRTLRKLDQEMEQLnhhtttrtqmEMLTKDKADKDEQIRkiksRHSD 462
Cdd:COG4717 354 REAEELEEELQLEELEQEIA---ALLAEAGVEDEEELRAALEQAEEY----------QELKEELEELEEQLE----ELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 463 ELTSLLGYFpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASseqnknhINNELKRKEEQlSSYEDKlfdvcgsqdfESD 542
Cdd:COG4717 417 ELEELLEAL-DEEELEEELEELEEELEELEEELEELREELAE-------LEAELEQLEED-GELAEL----------LQE 477
|
490 500 510
....*....|....*....|....*....|....*...
gi 1099267288 543 LDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQS 580
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1102-1174 |
1.22e-08 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 56.50 E-value: 1.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099267288 1102 CSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAhalvEIIKSRSQQRNfQLLVITHDEDF 1174
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG----ELIRELAAQGK-AVIVITHDYEF 188
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1103-1192 |
2.63e-08 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 55.55 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIEslahALVEIIKsRSQQRNFQLLVITHDEDFVEllgrsE 1182
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDPAGRR----ELLELLK-KLKAEGKTIIIVTHDLDLLL-----E 199
|
90
....*....|
gi 1099267288 1183 YVEKFYRIKK 1192
Cdd:cd03225 200 LADRVIVLED 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
596-838 |
2.81e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 596 QEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETL 675
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 676 LGTImpEEESAKVcltdvtIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQ 755
Cdd:COG4942 99 LEAQ--KEELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 756 DQQEQIQHLKsttNELKSEKLQISTNLQRRQQLEEQtveLSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKN 835
Cdd:COG4942 171 AERAELEALL---AELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 1099267288 836 TSN 838
Cdd:COG4942 245 AAG 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
87-917 |
3.37e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 87 IKALETLRQVRQtQGQKVKEYQMELKYLKQYkEKACEIRDQITSK---EAQLTSSKEIVKSYENELDPLKNRLKEIEHNL 163
Cdd:TIGR02169 197 RQQLERLRRERE-KAERYQALLKEKREYEGY-ELLKEKEALERQKeaiERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 164 SKIMKldnEIKALDsrkkqmEKDNSELEEKMEKVfQGTDEQLndlyhnhQRTVREKERKLVDCHRELEKLNKESRLLNQE 243
Cdd:TIGR02169 275 EELNK---KIKDLG------EEEQLRVKEKIGEL-EAEIASL-------ERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 244 KSELLVEQGRLQLQADRHQEHirardslIQSLATQLELdgfergpfserqiknfhkLVRERQEgEAKTANQLMNDFAEKE 323
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEE-------YAELKEELED------------------LRAELEE-VDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 324 TLKQKQIDEIRDKKTGLGRIIELKSEiLSKKQSELKNvkyelqQLEGSSDRILELDQELIKAERELSKAEKN--SNVETL 401
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQR-LSEELADLNA------AIAGIEAKINELEEEKEDKALEIKKQEWKleQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 402 KMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIR--------------KIKSRHSDELTSL 467
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvaqlgSVGERYATAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 468 LGYFPNKKQLEDWLHSKS-----KEINQTRDRLAKLNKeLASSEQNKNHINNE--------LKRKEEQlssYEDKLFDVC 534
Cdd:TIGR02169 545 AGNRLNNVVVEDDAVAKEaiellKRRKAGRATFLPLNK-MRDERRDLSILSEDgvigfavdLVEFDPK---YEPAFKYVF 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 535 GSQDFESDLDRLKE----------EIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpvcqrvfqtEAELQEVISDLQS 604
Cdd:TIGR02169 621 GDTLVVEDIEAARRlmgkyrmvtlEGELFEKSGAMTGGSRAPRGGILFSRSE---------------PAELQRLRERLEG 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 605 KLRLapdkLKSTESELKKKEKRRDEMlglvpmrQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEE 684
Cdd:TIGR02169 686 LKRE----LSSLQSELRRIENRLDEL-------SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 685 SAKvcltdvtimerfqMELKDVERKIAQQAAKLQGIDLdrtvQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHL 764
Cdd:TIGR02169 755 NVK-------------SELKELEARIEELEEDLHKLEE----ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 765 KSTTNELKSEKLQIStnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELInkkntsnkiaqDK 844
Cdd:TIGR02169 818 EQKLNRLTLEKEYLE---KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-----------SR 883
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1099267288 845 LNDIKEKVKNIHGYMKDIENYIQDGKDDY--KKQKETELNKVIAQLSECEKHKEK-INEDMRIMRQDIDTQKIQER 917
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIekKRKRLSELKAKLEALEEELSEIEDpKGEDEEIPEEELSLEDVQAE 959
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
650-1012 |
3.84e-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: 58.14 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 650 ELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtimERFQmELKDVERKIAQQAAKLQGIDLDRTVQQV 729
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----------ERYK-ELKAELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 730 NQEKQEKQHK-------LDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQ----RRQQLEEQTVELSTE 798
Cdd:TIGR02168 245 QEELKEAEEEleeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 799 VQSLYREIKDAKEQVSPLETTLEKFQQEKEELinkkntsnkiaQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYkKQKE 878
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESL-----------EAELEELEAELEELESRLEELEEQLETLRSKV-AQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 879 TELNKVIAQLSECEKHKEkinedmrimrqdiDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEH 958
Cdd:TIGR02168 393 LQIASLNNEIERLEARLE-------------RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1099267288 959 QKLEENIDNIKRNHNLALgRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVM 1012
Cdd:TIGR02168 460 EEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-830 |
4.07e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 257 QADRHQEhIRARDSLIQSLATQLELDGFERgpfserQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKQI---DEI 333
Cdd:COG1196 211 KAERYRE-LKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELEAELEELRLELEeleLEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 334 RDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNsnVETLKMEVISLQNEKA 413
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE--LEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 414 DLDRTLRKLDQEMEQLNHHTTTRTQMEM-LTKDKADKDEQIRKIKSRHSDELTSLLgyfpnkkQLEDWLHSKSKEINQTR 492
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLeALRAAAELAAQLEELEEAEEALLERLE-------RLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 493 DRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFI- 571
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA------ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLe 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 572 ----TQLTDENQSCCPVCQRVFQTEAELQEVISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSiid 642
Cdd:COG1196 509 gvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR--- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 643 lKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIDL 722
Cdd:COG1196 586 -AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 723 DRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSL 802
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580
....*....|....*....|....*...
gi 1099267288 803 YREIKDAKEQVSPLETTLEKFQQEKEEL 830
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERL 772
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
328-870 |
4.46e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 328 KQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSN---------- 397
Cdd:PRK01156 204 KQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNyykeleerhm 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 398 ----------------VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHS 461
Cdd:PRK01156 284 kiindpvyknrnyindYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 462 DeltsLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLfdvcgsqdfES 541
Cdd:PRK01156 364 D----YNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSL---------NQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 542 DLDRLKEEIEKSSKQRAMLAGatavysqfitqltdenQSCCPVCQRVFQTEaELQEVISDLQSKLRLAPDKLKSTESELK 621
Cdd:PRK01156 431 RIRALRENLDELSRNMEMLNG----------------QSVCPVCGTTLGEE-KSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 622 K-KEKRRDemlgLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKND---IEEQETLLGTIMPEEESAKV--------- 688
Cdd:PRK01156 494 DiDEKIVD----LKKRKEYLESEEINKSINEYNKIESARADLEDIKIKineLKDKHDKYEEIKNRYKSLKLedldskrts 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 689 -----CLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDrtVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQH 763
Cdd:PRK01156 570 wlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIG--FPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 764 LKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELinkkntsnkiaQD 843
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL-----------SD 716
|
570 580
....*....|....*....|....*..
gi 1099267288 844 KLNDIKEKVKNihgyMKDIENYIQDGK 870
Cdd:PRK01156 717 RINDINETLES----MKKIKKAIGDLK 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
487-985 |
4.63e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.42 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 487 EINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKlfdvcgSQDFESDLDRLKEEIEKSSKQRAMLAGATAV 566
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK------KDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 567 YSQFITQLTDENQSCCP-----------VCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVP 635
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEelnkakaahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 636 MRQsiIDLKE-KEIPELRNKLQNVNRDIQRLKNDIEEQET----LLGTIMPEEESAKVCLTDVTIMERFQM-ELKDVERK 709
Cdd:pfam05483 402 NKE--VELEElKKILAEDEKLLDEKKQFEKIAEELKGKEQelifLLQAREKEIHDLEIQLTAIKTSEEHYLkEVEDLKTE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 710 IAQQaaKLQGIDLDRTVQQVNQEkqekqhkldtvsskielNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLE 789
Cdd:pfam05483 480 LEKE--KLKNIELTAHCDKLLLE-----------------NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 790 EQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIEN---YI 866
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkAL 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 867 QDGKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLtlrKRNEELKEVEEERKQHLKEM 946
Cdd:pfam05483 621 KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV---EKAKAIADEAVKLQKEIDKR 697
|
490 500 510
....*....|....*....|....*....|....*....
gi 1099267288 947 GQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEE 985
Cdd:pfam05483 698 CQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-985 |
1.00e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 702 ELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQhkLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSeklQISTN 781
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQ---DIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 782 LQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKD 861
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 862 IENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQ 941
Cdd:COG1196 388 LLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1099267288 942 HLKEmgqmQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEE 985
Cdd:COG1196 467 ELLE----EAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-499 |
1.15e-07 |
|
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: 56.60 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 164 SKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVfQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQE 243
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 244 KSELLVEQGRLQLQ-ADRHQEHIRARDSLIQSLATQLELDGfergpfSERQIKNFHKLVRERQEGEAKTANQLMNDFAEK 322
Cdd:TIGR02168 749 IAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEA------QIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 323 ETLKQKQIDEIRDKKTGLGRIIELKsEILSKKQSELKnvkyelQQLEGSSDRILELDQELIKAERElsKAEKNSNVETLK 402
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQI-EELSEDIESLA------AEIEELEELIEELESELEALLNE--RASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 403 MEVISLQNEKADLDRTLRKLDQEMEQLNHHtttRTQMEM-LTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 481
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREK---LAQLELrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330
....*....|....*...
gi 1099267288 482 HSKSKEINQTRDRLAKLN 499
Cdd:TIGR02168 971 RRRLKRLENKIKELGPVN 988
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
293-905 |
1.63e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 293 QIKNFHKLVRERQEGEAKTANQLMNDFAEKETlkqkQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQ------ 366
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVIDLQT----KLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEaakclk 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 367 --QLEGSSDRILELDQELIKAER----------ELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHT- 433
Cdd:pfam15921 162 edMLEDSNTQIEQLRKMMLSHEGvlqeirsilvDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIf 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 434 TTRTQMEMLTKDKADKDE--------QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEIN-QTRDRLAKLNKELAS 504
Cdd:pfam15921 242 PVEDQLEALKSESQNKIElllqqhqdRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQeQARNQNSMYMRQLSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 505 SEQNKNHINNELKrkeEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEKSSKQRAMlagatavYSQFITQLTDEnqsccpv 584
Cdd:pfam15921 322 LESTVSQLRSELR---EAKRMYEDKI------EELEKQLVLANSELTEARTERDQ-------FSQESGNLDDQ------- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 585 cqrvfqteaeLQEVISDLQSKlrlapDKLKSTESELKKKEKRRDemlglvpMRQSIIdlkekeIPELRNKLQNVNRDIQR 664
Cdd:pfam15921 379 ----------LQKLLADLHKR-----EKELSLEKEQNKRLWDRD-------TGNSIT------IDHLRRELDDRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 665 L-------KNDIEEQ-ETLLGTIMPEEESakvcLTDVTIMERFQMELKDVERKIAQQ--AAKLQGIDLDRTVQQVNQEKQ 734
Cdd:pfam15921 431 LeallkamKSECQGQmERQMAAIQGKNES----LEKVSSLTAQLESTKEMLRKVVEEltAKKMTLESSERTVSDLTASLQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 735 EKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSE-------KLQISTNLQ----RRQQLEEQT----------- 792
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqtecealKLQMAEKDKvieiLRQQIENMTqlvgqhgrtag 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 793 ------VELSTEVQSLYREIKDAK-------EQVSPLETTLEKFQQEKEELINKKNTSNKiaqdKLNDIKEKVKNIHGYM 859
Cdd:pfam15921 587 amqvekAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLR----AVKDIKQERDQLLNEV 662
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1099267288 860 KDIENYIQDGKDDYK----------KQKETELNKVIAQLSECEKHKEKINEDMRIM 905
Cdd:pfam15921 663 KTSRNELNSLSEDYEvlkrnfrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
590-815 |
1.70e-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: 54.77 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 590 QTEAELQEV---ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLK 666
Cdd:COG4942 24 EAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 667 NDIEEQETLLGTiMPEEESAKVCL--TDVTIMERFQMELKDVERKIAQQAAKLQGI--DLDRTVQQVNQEKQEKQHKLDT 742
Cdd:COG4942 104 EELAELLRALYR-LGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADlaELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099267288 743 VSSKIELNRKLIQDQQEQIQHLKSTTNELKseklqistnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSP 815
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELA----------AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
228-1199 |
2.20e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 228 RELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVRERQEG 307
Cdd:pfam02463 201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 308 EAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEIlSKKQSELKNVKYELQQLEGSSDrILELDQELIKAER 387
Cdd:pfam02463 281 KKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK-KKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 388 ELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSL 467
Cdd:pfam02463 359 EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEES 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 468 LGYFPNKKQLEDwlhskskeiNQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLK 547
Cdd:pfam02463 439 IELKQGKLTEEK---------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 548 EEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKL----KSTESELKKK 623
Cdd:pfam02463 510 KVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgarkLRLLIPKLKL 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 624 EKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIM----PEEESAKVCLTDVTIMERF 699
Cdd:pfam02463 590 PLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESglrkGVSLEEGLAEKSEVKASLS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 700 QMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQIS 779
Cdd:pfam02463 670 ELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 780 TNLQ--RRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKN-TSNKIAQDKLNDIKEKVKNIH 856
Cdd:pfam02463 750 EEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEeELKEEAELLEEEQLLIEQEEK 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 857 GYMKDIENYIQD----GKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLTLRKRNEEL 932
Cdd:pfam02463 830 IKEEELEELALElkeeQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 933 KEVEEERKQHLKEMGQMQVLQMK--SEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMI 1010
Cdd:pfam02463 910 NLLEEKENEIEERIKEEAEILLKyeEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1011 VmRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDlwRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRV-VM 1089
Cdd:pfam02463 990 Y-NKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS--INKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIsAR 1066
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1090 LKGDTALDMRgRCSAGQKVLASLIIRLALAE----TFCLncgiiaLDEPTTNLDRENIESLAHALveiiksRSQQRNFQL 1165
Cdd:pfam02463 1067 PPGKGVKNLD-LLSGGEKTLVALALIFAIQKykpaPFYL------LDEIDAALDDQNVSRVANLL------KELSKNAQF 1133
|
970 980 990
....*....|....*....|....*....|....
gi 1099267288 1166 LVITHDEDFVELlgrseyVEKFYRIKKNIDQCSE 1199
Cdd:pfam02463 1134 IVISLREEMLEK------ADKLVGVTMVENGVST 1161
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1093-1176 |
7.86e-07 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 53.22 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1093 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITHD 1171
Cdd:COG4988 464 DTPLGEGGRGlSGGQAQ------RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT------VILITHR 531
|
....*
gi 1099267288 1172 EDFVE 1176
Cdd:COG4988 532 LALLA 536
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-741 |
1.37e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 163 LSKIMK-LDNEIKALDSR----KKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKES 237
Cdd:pfam15921 222 ISKILReLDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 238 RLLNQEKS-------------ELLVEQGRLQLqadrhQEHIRARDSLIQSLATQLELDG-------FERGPFS------- 290
Cdd:pfam15921 302 EIIQEQARnqnsmymrqlsdlESTVSQLRSEL-----REAKRMYEDKIEELEKQLVLANseltearTERDQFSqesgnld 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 291 ---ERQIKNFHKLVRE-------------RQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKK 354
Cdd:pfam15921 377 dqlQKLLADLHKREKElslekeqnkrlwdRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 355 QSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSN--VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHH 432
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 433 TT-------TRTQMEMLTKDKADKDEQIrKIKSRHSDELTSLLGYFP--------NKKQLEdwlhsksKEINQTRDRLak 497
Cdd:pfam15921 537 KNegdhlrnVQTECEALKLQMAEKDKVI-EILRQQIENMTQLVGQHGrtagamqvEKAQLE-------KEINDRRLEL-- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 498 lnKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVcGSQ------DFESDLDRLKEEIEKSSKQramlagatavysqfI 571
Cdd:pfam15921 607 --QEFKILKDKKDAKIRELEARVSDLELEKVKLVNA-GSErlravkDIKQERDQLLNEVKTSRNE--------------L 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 572 TQLTDENQsccpVCQRVFQTEAELQEVISD-LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPE 650
Cdd:pfam15921 670 NSLSEDYE----VLKRNFRNKSEEMETTTNkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDA 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 651 LRNKLQ-------NVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGIDLD 723
Cdd:pfam15921 746 LQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER-RLKEKVANMEVALDKASLQFAECQ 824
|
650 660
....*....|....*....|
gi 1099267288 724 RTVQQVNQE--KQEKQHKLD 741
Cdd:pfam15921 825 DIIQRQEQEsvRLKLQHTLD 844
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-646 |
1.50e-06 |
|
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: 52.76 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 302 RERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGssdRILELDQE 381
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 382 LIKAERELSKAEKNSNVETLKmeviSLQNEKADLDRTLRKLDQEMEQLNhhtttrtqmemltkdkadkdeqiRKIKSRHs 461
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIP----EIQAELSKLEEEVSRIEARLREIE-----------------------QKLNRLT- 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 462 deltsllgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQD--- 538
Cdd:TIGR02169 826 ----------LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDele 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 539 -----FESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTD------ENQSCCPVCQRVFQTEAELQEVISDLQSKLR 607
Cdd:TIGR02169 896 aqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
|
330 340 350
....*....|....*....|....*....|....*....
gi 1099267288 608 LAPDKLKSTESELKKKEKRRDEmlgLVPMRQSIIDLKEK 646
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAK---LEEERKAILERIEE 1011
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1093-1180 |
2.72e-06 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 51.52 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1093 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDREniesLAHALVEIIKSRSQQRNfqLLVITHD 1171
Cdd:TIGR02857 449 DTPIGEGGAgLSGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAE----TEAEVLEALRALAQGRT--VLLVTHR 516
|
....*....
gi 1099267288 1172 EDFVELLGR 1180
Cdd:TIGR02857 517 LALAALADR 525
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1078-1152 |
3.16e-06 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 46.46 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1078 DKRRNYNYRVVMLKGDTA----LDMRGRCSAGQK-VLASLIIRLALAETFCLN------CGIIALDEPTTNLDRENIESL 1146
Cdd:pfam13558 5 DYRNWLSFEVEVRDEDGSevetYRRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTA 84
|
....*.
gi 1099267288 1147 AHALVE 1152
Cdd:pfam13558 85 LELLRA 90
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1100-1176 |
3.74e-06 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 49.01 E-value: 3.74e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 1100 GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIEslahALVEIIKSRSQQRnfQLLVI-THDEDFVE 1176
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGVA----LLAELIAAHLARG--GAVLLtTHQPLELA 195
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-845 |
3.95e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 105 KEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMK-LDNEIKALDSRKKQM 183
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKhLREALQQTQQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 184 EKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQE 263
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 264 HIRARDSLIQSLATQLELDGFERGPFSErqiknfHKLVRERQEGEAKTANQLMNDFAEKETLKQKQIDeirdkKTGLGRI 343
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQ------EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-----KTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 344 IELKSEILSKKQSELKNVKYELQqlegsSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLD 423
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTS-----AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 424 QEMEQLNhhtttrtQMEMLTKDKADKDEQIRKIKSRHSDELTSLLG---YFPNKKQLEDWLHSKSKEINQTRDRLAKLNK 500
Cdd:TIGR00618 470 EREQQLQ-------TKEQIHLQETRKKAVVLARLLELQEEPCPLCGsciHPNPARQDIDNPGPLTRRMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 501 ELASSEQNKNHINNELKRKEEQLSSYEDKLFDV--------CGSQDFESDLDRLKEEIEKSSKQRAMLAGAtavySQFIT 572
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACE----QHALL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 573 QLTDENQSCCPVCQRVFQTEAELQEVISDL-QSKLRLAPDK-----LKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEk 646
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLTALhALQLTLTQERvrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKE- 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 647 EIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDRTV 726
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 727 QQVNQEKQEKQHKLDTVSskiELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREI 806
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLRE---EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKY 854
|
730 740 750
....*....|....*....|....*....|....*....
gi 1099267288 807 KDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKL 845
Cdd:TIGR00618 855 EECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDAL 893
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-762 |
4.90e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 344 IELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLD 423
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 424 QEMEQLNHhttTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWlhskSKEINQTRDRLAKLNKELA 503
Cdd:COG4717 153 ERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEEL----QQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 504 SSEQNKNHINNEL--KRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSC 581
Cdd:COG4717 224 ELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 582 CPVCQRVFQ----TEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLvpMRQSIIDLKEKEIPELRNKLQN 657
Cdd:COG4717 304 AEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL--EEELQLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 658 VNRD-----------IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQ----------MELKDVERKIAQQAAK 716
Cdd:COG4717 382 EDEEelraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEeleeeleeleEELEELREELAELEAE 461
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1099267288 717 LQGIDLDRTVQQVNQEKQEKQHKLDTVS---SKIELNRKLIQDQQEQIQ 762
Cdd:COG4717 462 LEQLEEDGELAELLQELEELKAELRELAeewAALKLALELLEEAREEYR 510
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
397-1173 |
5.58e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 397 NVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQ 476
Cdd:PRK01156 167 NYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 477 LEDWLHSKSKEINQTRDRLA----KLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVcgsQDFESDLDRLKEEIEK 552
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSmeleKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDI---ENKKQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 553 SSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLG 632
Cdd:PRK01156 324 YHAIIKKLSVLQKDYNDYIKKKSRYDD--------LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 633 LVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDI------EEQETLLGTIMPEEESAKVCLTDV------TIMERFQ 700
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIralrenLDELSRNMEMLNGQSVCPVCGTTLgeeksnHIINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 701 MELKDVERKIAQqaaklqgidLDRTVQQVNQEKQEKQHKLDTVSSKiELNRKLIQDQQeqiqhLKSTTNELKSEKLQIST 780
Cdd:PRK01156 476 EKKSRLEEKIRE---------IEIEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNK-----IESARADLEDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 781 NLQRRQQLEEqtveLSTEVQSLYREIKDAKEQvSPLETTLEKFQQEKEELINKKNTSNKiaqdKLNDIKEKVKNIHGYMK 860
Cdd:PRK01156 541 LKDKHDKYEE----IKNRYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKK----QLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 861 DIENYIqdgkDDYKKQKETELNKVIAQLSECEKHKEKINEdmriMRQDIDTQKIQerwlqdnltlrkrneelKEVEEERK 940
Cdd:PRK01156 612 DDKSYI----DKSIREIENEANNLNNKYNEIQENKILIEK----LRGKIDNYKKQ-----------------IAEIDSII 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 941 QHLKEMgQMQVLQMKSEHQKLEENIDNIKRNHnlalgrqkgYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNK 1020
Cdd:PRK01156 667 PDLKEI-TSRINDIEDNLKKSRKALDDAKANR---------ARLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1021 DLDIYYKTLDQAIMKfhSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSAsdkrrnynYRVVMLKGDTALdmrg 1100
Cdd:PRK01156 737 DLKRLREAFDKSGVP--AMIRKSASQAMTSLTRKYLFEFNLDFDDIDVDQDFNITV--------SRGGMVEGIDSL---- 802
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099267288 1101 rcSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRnfQLLVITHDED 1173
Cdd:PRK01156 803 --SGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIP--QVIMISHHRE 871
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
109-680 |
1.01e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 109 MELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSY--ENELDPLKNRLKEIEhnlSKIMKLDNEIKALDSRKKQMEKD 186
Cdd:PRK02224 159 LQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQieEKEEKDLHERLNGLE---SELAELDEEIERYEEQREQARET 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 187 NSELEEKMEKvFQGTDEQLNDLyhnhQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIR 266
Cdd:PRK02224 236 RDEADEVLEE-HEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 267 ARDSLIQSLATQLELdgfergpfserqiknfhklVRERQEgEAKTANQLMNDFAEKETLKQKQID----EIRDKKTGLGR 342
Cdd:PRK02224 311 AVEARREELEDRDEE-------------------LRDRLE-ECRVAAQAHNEEAESLREDADDLEeraeELREEAAELES 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 343 IIELKSEILSKKQSELKNVKYELQQLEGSSDRIlELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKL 422
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDA-PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 423 D--------QEMEQLNHHTTT---RTQMEMLTKDKADKDEQIRKIKSRH---------SDELTSLLgyfPNKKQLEDWLH 482
Cdd:PRK02224 450 EagkcpecgQPVEGSPHVETIeedRERVEELEAELEDLEEEVEEVEERLeraedlveaEDRIERLE---ERREDLEELIA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 483 SKSKEINQTRDRLAKLNKELASSEqnknhinNELKRKEEQLSSYEDKLFDVCGS-QDFESDLDRLKEEIEKSSKQRAMLA 561
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELE-------AEAEEKREAAAEAEEEAEEAREEvAELNSKLAELKERIESLERIRTLLA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 562 gATAVYSQFITQLTDENQSCCPV-----------CQRVFQTEAELQEV-ISDLQSKLRLAPDKLKSTESELKKKEKRRDE 629
Cdd:PRK02224 600 -AIADAEDEIERLREKREALAELnderrerlaekRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1099267288 630 MLGLVPMRQSIIdlkeKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIM 680
Cdd:PRK02224 679 LQAEIGAVENEL----EELEELRERREALENRVEALEALYDEAEELESMYG 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-718 |
1.32e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 375 ILELDQELIKAERELSKAEKNSN-----VETLKMEVISLQNEKADLDR--TLRKLDQEMEQ---LNHHTTTRTQMEMLTK 444
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIErldliIDEKRQQLERLRREREKAERyqALLKEKREYEGyelLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 445 DKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSK-SKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQL 523
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 524 ssyedklfdvcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQ 603
Cdd:TIGR02169 325 -------------AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 604 SKLrlapDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRlknDIEEQETLLGTIMPEE 683
Cdd:TIGR02169 392 EKL----EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL---EIKKQEWKLEQLAADL 464
|
330 340 350
....*....|....*....|....*....|....*.
gi 1099267288 684 ESAKVCLTDVTI-MERFQMELKDVERKIAQQAAKLQ 718
Cdd:TIGR02169 465 SKYEQELYDLKEeYDRVEKELSKLQRELAEAEAQAR 500
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
322-560 |
1.42e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 322 KETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKyeLQQLEGSSDRILELDQELIKAERELSkaEKNSNVETL 401
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEEELEKIEKEIK--ELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 402 KMEVISLQNEKADLDRtLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKI-------------------KSRHSD 462
Cdd:PRK05771 113 ENEIKELEQEIERLEP-WGNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVenveyistdkgyvyvvvvvLKELSD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 463 ELTSLL---GY----FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSeqnKNHINNELKRKEEQLSSYEDKlFDVC- 534
Cdd:PRK05771 192 EVEEELkklGFerleLEEEGTPSELIREIKEELEEIEKERESLLEELKEL---AKKYLEELLALYEYLEIELER-AEALs 267
|
250 260 270
....*....|....*....|....*....|....*..
gi 1099267288 535 ---GSQDF--------ESDLDRLKEEIEKSSKQRAML 560
Cdd:PRK05771 268 kflKTDKTfaiegwvpEDRVKKLKELIDKATGGSAYV 304
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
321-865 |
1.43e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 321 EKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSK--AEKNSNV 398
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkiKELEKQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 399 ETLKMEVISLQNEK-ADLDRTLRklDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSrhsdeltsllgyfpNKKQL 477
Cdd:TIGR04523 291 NQLKSEISDLNNQKeQDWNKELK--SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK--------------ELTNS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 478 EDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKlfdvcgSQDFESDLDRLKEEIEKSSKQR 557
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL------NQQKDEQIKKLQQEKELLEKEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 558 AMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpmR 637
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL------N 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 638 QSIIDLKEKeIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTdvtimerfQMELKDVERKIAQQAAKL 717
Cdd:TIGR04523 503 EEKKELEEK-VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--------KENLEKEIDEKNKEIEEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 718 Q--GIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVEL 795
Cdd:TIGR04523 574 KqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099267288 796 STEVQS----LYREIKDAKEQVSPLETTLEKFQQEKEeLINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENY 865
Cdd:TIGR04523 654 IKEIRNkwpeIIKKIKESKTKIDDIIELMKDWLKELS-LHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEF 726
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
171-396 |
1.49e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 171 NEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLyhnhqrtvREKERKLVDCHRELEKLNKESRLLNQEKSELLVE 250
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--------AALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 251 QGRLQLQADRHQEHIRARDSLIQSLATQLEL------DGFERgpfSERQIKNFHKLVRERQE------GEAKTANQLMND 318
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLalllspEDFLD---AVRRLQYLKYLAPARREqaeelrADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 319 FAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRileLDQELIKAERELSKAEKNS 396
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAERT 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
347-1003 |
1.49e-05 |
|
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: 49.58 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 347 KSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEM 426
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 427 EQLNH--------HTTTRTQMEMLTKDKAdKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKL 498
Cdd:TIGR00618 300 KAVTQieqqaqriHTELQSKMRSRAKLLM-KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-HEVATSIREISCQQHTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 499 NKELASSEQNKNHinneLKRKEEQLSSYEDKLFDVCGSQDFES--------DLDRLKEEIEKSSKQRAMLAGATAVYSQF 570
Cdd:TIGR00618 378 TQHIHTLQQQKTT----LTQKLQSLCKELDILQREQATIDTRTsafrdlqgQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 571 IT----------QLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSI 640
Cdd:TIGR00618 454 EKlekihlqesaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 641 ID---LKEKEIPELRNKLQNVNRDIQRLKNDIEE--QETLLGTIMPEEESAkvcltdvtIMERFQMELKDVERKIAQQAA 715
Cdd:TIGR00618 534 EQtyaQLETSEEDVYHQLTSERKQRASLKEQMQEiqQSFSILTQCDNRSKE--------DIPNLQNITVRLQDLTEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 716 KLQGIDLDRTVQQVnqEKQEKQHKLDtvssKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEeqtveL 795
Cdd:TIGR00618 606 AEDMLACEQHALLR--KLQPEQDLQD----VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE-----L 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 796 STEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDgkddYKK 875
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE----LMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 876 QKETELnkviaQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLtLRKRNEELKEVEEERKQHLKEMGQMQVLQMK 955
Cdd:TIGR00618 751 QARTVL-----KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL-REEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1099267288 956 SEHQKLEENIDNIKRNHNL--ALGRQKGYEEEIIHFKKELREPQFRDAEE 1003
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-1173 |
1.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 348 SEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSkaEKNSNVETLKMEVISLQNEKADLDrtlrKLDQEME 427
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN--EISSELPELREELEKLEKEVKELE----ELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 428 QLnhhtttRTQMEMLTKDKADKDEQIRKIKSR------HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE 501
Cdd:PRK03918 242 EL------EKELESLEGSKRKLEEKIRELEERieelkkEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 502 LASSEQnknhinnELKRKEEQLSSYEDKlfdvcgsqdfESDLDRLKEEIEKSSKQRAMLAGATAVYsqfitqltdenqsc 581
Cdd:PRK03918 316 LSRLEE-------EINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELY-------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 582 cpvcQRVFQTEAELQEVisdlqsKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrqsiidlkEKEIPELRNKLQNVNRD 661
Cdd:PRK03918 365 ----EEAKAKKEELERL------KKRLTGLTPEKLEKELEELEKAKEEI--------------EEEISKITARIGELKKE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 662 IQRLKNDIEEQET------LLGTIMPEEESAKvcltdvtIMERFQMELKDVERKIAQQAAKLQgidldrtvqqvnqekqE 735
Cdd:PRK03918 421 IKELKKAIEELKKakgkcpVCGRELTEEHRKE-------LLEEYTAELKRIEKELKEIEEKER----------------K 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 736 KQHKLDTVSSKIELNRKLIQDQQ--EQIQHLKSTTNELKSEKLQISTNLQRRqqLEEQTVELSTEVQSLYREIKDAKEQV 813
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEK--LKEKLIKLKGEIKSLKKELEKLEELK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 814 SPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGY------MKDIENYIQDGKDDYKKQkETELNKVIAQ 887
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneyleLKDAEKELEREEKELKKL-EEELDKAFEE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 888 LSECEKHKEKINedmrimrqdidtqkiqerwlqdnltlrkrneelkeveeerkqhlKEMGQMQVLQMKSEHQKLEENIDN 967
Cdd:PRK03918 635 LAETEKRLEELR--------------------------------------------KELEELEKKYSEEEYEELREEYLE 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 968 IKRNHNLALGRQKGYEEEIIHFKKELrepqfRDAEEKYREMMIVMRTTELVNKDLDiyyktldqaimkfhsmKMEEINKI 1047
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTL-----EKLKEELEEREKAKKELEKLEKALE----------------RVEELREK 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1048 IRDLWRSTYRGQDIEYIEIRSD-----ADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETF 1122
Cdd:PRK03918 730 VKKYKALLKERALSKVGEIASEifeelTEGKYSGVRVKAEENKVKLFVVYQGKERPLTFLSGGERIALGLAFRLALSLYL 809
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1099267288 1123 CLNCGIIALDEPTTNLDRENieslAHALVEIIkSRSQQRNFQLLVITHDED 1173
Cdd:PRK03918 810 AGNIPLLILDEPTPFLDEER----RRKLVDIM-ERYLRKIPQVIIVSHDEE 855
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1128-1181 |
1.89e-05 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 47.10 E-value: 1.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1099267288 1128 IIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRS 1181
Cdd:cd03255 161 IILADEPTGNLDSET----GKEVMELLRELNKEAGTTIVVVTHDPELAEYADRI 210
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
112-671 |
2.21e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 112 KYLKQYKEKACEIRDQITSKEAQLTSS-------KEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQME 184
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLnnkyndlKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 185 KDNSELEEKMEKvfqgtdeqLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEH 264
Cdd:TIGR04523 211 QKNKSLESQISE--------LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 265 IRARDSLIQSLATQLELDGFERgpfSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQkQIDEIRDKKTGLGRII 344
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQK---EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE-QISQLKKELTNSESEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 345 ELKSEILSKKQSELKNVKYE----LQQLEGSSDRILELDQELIKAERElsKAEKNSNVETLKMEVISLQNEKADLDRTLR 420
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKEnqsyKQEIKNLESQINDLESKIQNQEKL--NQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 421 KLDQEMEQL-NHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN 499
Cdd:TIGR04523 437 KNNSEIKDLtNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 500 KELASSEQNKNHINNELKRKEEQLSSYEDKLFdvcgSQDFESDLDRLKEEIEKSSKQRAMLagatavySQFITQLTDENQ 579
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELN----KDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 580 SccpVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKE---KEIPELRNKLQ 656
Cdd:TIGR04523 586 E---KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKqikETIKEIRNKWP 662
|
570
....*....|....*
gi 1099267288 657 NVNRDIQRLKNDIEE 671
Cdd:TIGR04523 663 EIIKKIKESKTKIDD 677
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1103-1179 |
2.94e-05 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 46.03 E-value: 2.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDREniesLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLG 1179
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALDPI----TRREVRALLKSLQAQLGITVVLVTHDLDEAARLA 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
435-634 |
3.94e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 435 TRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINN 514
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 515 ELKRKEEQLS------------SYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 582
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1099267288 583 PVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLV 634
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
697-874 |
5.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 697 ERFQMELKDVERKIAQQAAKLQgiDLDRTVQQVNQEKQEKQHKLDTVSSKIELN--RKLIQDQQEQIQHLKSTTNELKSE 774
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE--ALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 775 KLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEEL-----------INKKNTSNKIAQD 843
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralleerfaaALGDAVERELREN 770
|
170 180 190
....*....|....*....|....*....|.
gi 1099267288 844 KLNDIKEKVKNIHGYMKDIENYIQDGKDDYK 874
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFNREWP 801
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
715-926 |
6.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 715 AKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKsttNELKSEKLQISTNlqrRQQLEEQTVE 794
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEA---EAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 795 LSTEVQSLYReikdAKEQVSPLETTLEkfQQEKEELINKKNTSNKIA---QDKLNDIKEKVKNIHGYMKDIENYIQDgKD 871
Cdd:COG3883 88 LGERARALYR----SGGSVSYLDVLLG--SESFSDFLDRLSALSKIAdadADLLEELKADKAELEAKKAELEAKLAE-LE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1099267288 872 DYKKQKETELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLTLR 926
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
474-879 |
6.85e-05 |
|
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: 47.53 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 474 KKQLEDWLHSKSKEINQTRDRLaklNKELASSEQNKNHINNELKRKEEQLSSYED-KLFDVCGSQD----FESDLDRLKE 548
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDEL---NGELSAADAAVAKDRSELEALEDQHGAFLDaDIETAAADQEqlpsWQSELENLEE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 549 EIE-----KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRlapDKLKSTESELKKK 623
Cdd:pfam12128 362 RLKaltgkHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR---EQLEAGKLEFNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 624 EKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRdiqrlkndieEQETLlgtimpEEESAKVcltdvtimERFQMEL 703
Cdd:pfam12128 439 EYRLKSRLGELKLRLNQATATPELLLQLENFDERIER----------AREEQ------EAANAEV--------ERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 704 KDVERKIAQQAAKLQgiDLDRTVQQVNQEKQEKQHKLDTVS-SKIELNRKLIQDQQEQIQHLKST--------------- 767
Cdd:pfam12128 495 RQARKRRDQASEALR--QASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVISPellhrtdldpevwdg 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 768 --------------------------TNELKSEKLQISTNLQ----RRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLE 817
Cdd:pfam12128 573 svggelnlygvkldlkridvpewaasEEELRERLDKAEEALQsareKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1099267288 818 TTLEKFQQEKEELINKKNTSNKIAQDKLNdikEKVKNIHGYMKDIENYIQDGKDDYKKQKET 879
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALAERKDSAN---ERLNSLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
120-901 |
7.51e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 120 KACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDneikalDSRKKQMEKDNSELEEKMEKVFQ 199
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE------EAKKDAEEAKKAEEERNNEEIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 200 GTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSEllVEQGRLQLQADRHQEHIRARDSLIQSLATQL 279
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 280 ELDGFERGPFSERQIKNFHKLVRERQEGEAKTanqlmnDFAEKETLKQKQIDEIRDKKTGLGRiielKSEILSKKQSELK 359
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA------EAAEKKKEEAKKKADAAKKKAEEKK----KADEAKKKAEEDK 1404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 360 NVKYELQQLEGSSDRILELD---QELIKAERELSKAEKNSNVETLKmevislqnEKADLDRTLRKLDQEMEQLNHHTTTR 436
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAK--------KKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 437 TQMEmlTKDKADKDEQIRKIKSRHSDELtsllgyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASSEQNKnhinNEL 516
Cdd:PTZ00121 1477 KKAE--EAKKADEAKKKAEEAKKKADEA------------------KKAAEAKKKADEAKKAEEAKKADEAKK----AEE 1532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 517 KRKEEQLSSYEDKLfdvcgsqdfESDLDRLKEEIEKSSKQRAMlagatavySQFITQLTDENQSCCPVCQRVFQTEAELQ 596
Cdd:PTZ00121 1533 AKKADEAKKAEEKK---------KADELKKAEELKKAEEKKKA--------EEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 597 EVISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQET 674
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 675 LLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIdldRTVQQVNQEKQEKQHKLDTVSSKIELNRKLI 754
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL---KKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 755 QDQQEQIQHLKStTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKD--------AKEQVSPLETTLEKFQQE 826
Cdd:PTZ00121 1753 EEEKKKIAHLKK-EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDnfaniiegGKEGNLVINDSKEMEDSA 1831
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1099267288 827 KEELINKKNTsnkiaqdKLNDIKEKVKniHGYMKDIENYiQDGKDDYKKQKETELNKVIAQLSECEKHKEKINED 901
Cdd:PTZ00121 1832 IKEVADSKNM-------QLEEADAFEK--HKFNKNNENG-EDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKD 1896
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-577 |
8.26e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 327 QKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEgssDRILELDQELIKAERELSKAEKnsNVETLKMEVI 406
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEA--ELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 407 SLQNEKADLDRTLRKLDQEMEQLNHHTTtrtqMEMLtkdkadkdeqirkIKSRHSDELTSLLGYFpnkKQLEDWLHSKSK 486
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPP----LALL-------------LSPEDFLDAVRRLQYL---KYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 487 EINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEdklfdvcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAV 566
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALK---------AERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|.
gi 1099267288 567 YSQFITQLTDE 577
Cdd:COG4942 225 LEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
641-822 |
8.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 641 IDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVtimerfqmELKDVERKIAQQAAKLQGI 720
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAL---QRLAEYSWDEI--------DVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 721 D--------LDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNEL-KSEKLQISTNLQRRQQLEEQ 791
Cdd:COG4913 681 DassddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|.
gi 1099267288 792 TVELSTEVQSLYREIKDAKEQVSPLETTLEK 822
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
593-841 |
8.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 593 AELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsiidlKEKEIPELRNKLQNVNRDIQRLKNDIEEQ 672
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 673 ETLLGTIMpeeesakvcltdvtimerfqmelkdverkiaqQAAKLQGIDLDRTVQQVNQEkqekqhKLDTVSSKIELNRK 752
Cdd:COG3883 85 REELGERA--------------------------------RALYRSGGSVSYLDVLLGSE------SFSDFLDRLSALSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 753 LIQDQQEQIQHLKSTTNELKSEKLQIStnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELIN 832
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELE---AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
....*....
gi 1099267288 833 KKNTSNKIA 841
Cdd:COG3883 204 ELAAAEAAA 212
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-421 |
8.69e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 71 KALKQKFDEIFSATRYIK-ALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEirdQITSKEAQLTSSKEIVKSYENEL 149
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE---RLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 150 DPLKNRLKEIEHNLSKIMKLDNEIKA--LDSRKKQMEKDNSELEEkmekvfqgtdeqlndlyhnhqrTVREKERKLVDCH 227
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEE----------------------EVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 228 RELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQL-ELDGFERGPFSE-----RQIKNFHKLV 301
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeELEAALRDLESRlgdlkKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 302 RERQEG------EAKTANQLMNDFAEKETLKQKQIDEIRDKKtglGRIIELKSEILS--KKQSELKNVKYELQQLEGSSD 373
Cdd:TIGR02169 899 RELERKieeleaQIEKKRKRLSELKAKLEALEEELSEIEDPK---GEDEEIPEEELSleDVQAELQRVEEEIRALEPVNM 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1099267288 374 RILELDQELIKAERELSKAEknsnvETLKMEVISLQNEKADLDRTLRK 421
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKR-----AKLEEERKAILERIEEYEKKKRE 1018
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1103-1170 |
9.09e-05 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 44.30 E-value: 9.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNfqLLVITH 1170
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPET----EALILEALRALAKGKT--VIVIAH 153
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
128-861 |
1.14e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 128 ITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLskiMKLDNEIKALDSRKKQMEKDNSELEEKMEKvfqgtdeqlnd 207
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNL---NKDEEKINNSNNKIKILEQQIKDLNDKLKK----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 208 lyhnhqrtvreKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLEL------ 281
Cdd:TIGR04523 94 -----------NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnnkyn 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 282 DGFERGPFSERQIKNFHKLVRERQEGEAKTANQLMND---------FAEKETLKQKQIDEIRDKKTGLGRIIELKSEILS 352
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 353 KKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSK--AEKNSNVETLKMEVISLQNEK-ADLDRTLRklDQEMEQL 429
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkiKELEKQLNQLKSEISDLNNQKeQDWNKELK--SELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 430 NHHTTTRTQMEMLTKDKADKDEQIRKIKSrhsdeltsllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNK 509
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKK--------------ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 510 NHINNELKRKEEQLSSYEDKlfdvcgSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVF 589
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKL------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 590 QTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrqsiidlkEKEIPELRNKLQNVNRDIQRLKNDI 669
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--------------NEEKKELEEKVKDLTKKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 670 EEQETllgtimpeeesakvcltdvtimerfqmELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLdtvsSKIEL 749
Cdd:TIGR04523 527 EKLES---------------------------EKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI----EELKQ 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 750 NRKLIQDQQEQIQHL-KSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKE 828
Cdd:TIGR04523 576 TQKSLKKKQEEKQELiDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
730 740 750
....*....|....*....|....*....|...
gi 1099267288 829 ELINKKNTSNKiaqdKLNDIKEKVKNIHGYMKD 861
Cdd:TIGR04523 656 EIRNKWPEIIK----KIKESKTKIDDIIELMKD 684
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
302-529 |
1.26e-04 |
|
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: 45.91 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 302 RERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQE 381
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 382 LIKAerelskAEKNSNVETLKmeVISLQNEKADLDRTLRKLDQEMEQLnhhtttRTQMEMLTKDKADKDEQIRKIKSRHS 461
Cdd:COG4942 109 LLRA------LYRLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 462 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDK 529
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
87-550 |
1.29e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 87 IKALETLRQVRQTQGQKVKEYQMELKYLKQykekacEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKI 166
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKN------ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 167 MkldneiKALDSRKKQMEKDNSELEEKMEKVfqgtDEQLNDLYHnhqrtVREKERKLVDCHRELEKLnkesrllnqekse 246
Cdd:pfam15921 502 T------ASLQEKERAIEATNAEITKLRSRV----DLKLQELQH-----LKNEGDHLRNVQTECEAL------------- 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 247 llveqgRLQLQadrhqehirARDSLIQSLatqleldgfergpfsERQIKNFHKLVreRQEGEAKTANQLmndfaEKETLK 326
Cdd:pfam15921 554 ------KLQMA---------EKDKVIEIL---------------RQQIENMTQLV--GQHGRTAGAMQV-----EKAQLE 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 327 QkqidEIRDKKTGLGRIIELKseilSKKQSELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKN--SNVETLKME 404
Cdd:pfam15921 597 K----EINDRRLELQEFKILK----DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQllNEVKTSRNE 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 405 VISLQNEKADLDRTLRKLDQEMEqlnhhtTTRTQMEMLTKDKADKDEQIRK-IKSRHSDELTSLLGYFPNKKQLEdwlhS 483
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEME------TTTNKLKMQLKSAQSELEQTRNtLKSMEGSDGHAMKVAMGMQKQIT----A 738
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 484 KSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQD-FESDLDRLKEEI 550
Cdd:pfam15921 739 KRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEvLRSQERRLKEKV 806
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
560-613 |
1.63e-04 |
|
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. The Rad50 coiled-coil region contains a dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn ion. This alignment includes the zinc hook motif and a short stretch of coiled-coil on either side.
Pssm-ID: 427940 [Multi-domain] Cd Length: 52 Bit Score: 40.64 E-value: 1.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1099267288 560 LAGATAVYSQFITQLTDENQsCCPVCQRVFQTEaELQEVISDLQSKLRLAPDKL 613
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEG-CCPLCGRPLDEE-HRSELIKELQSKLERLPEEL 52
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
119-518 |
1.88e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.88 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 119 EKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKldNEIKALDSRKKQmEKDNSELEEKMEKVF 198
Cdd:COG4694 99 EENIELEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIK--DDLKKLFASSGR-NYRKANLEKKLSALK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 199 QGTDEQLNDLYhnhqRTVREKERKLVDCHRELEKLnkesRLLNQEKSELLVEQgrlqlqadrhqehirARDSLIQSLATQ 278
Cdd:COG4694 176 SSSEDELKEKL----KLLKEEEPEPIAPITPLPDL----KALLSEAETLLEKS---------------AVSSAIEELAAL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 279 LELDGfergpfSERQIKNFHKLVRERQEG-----EAKTANQLMNDFAEK-----ETLKQKQIDEIRDKKTGLGRIIELKS 348
Cdd:COG4694 233 IQNPG------NSDWVEQGLAYHKEEEDDtcpfcQQELAAERIEALEAYfddeyEKLLAALKDLLEELESAINALSALLL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 349 EILskkQSELKNVKYELQQLEGSSDRILELDQELIKAerelsKAEKNSNVETLKMEVI--SLQNEKADLDRTLRKLDQEM 426
Cdd:COG4694 307 EIL---RTLLPSAKEDLKAALEALNALLETLLAALEE-----KIANPSTSIDLDDQELldELNDLIAALNALIEEHNAKI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 427 EQLnhhtttrtqmemltkdKADKDEQIRKIKSRHSDELTSLL-GYFPNKKQLED---WLHSKSKEINQTRDRLAKLNKEL 502
Cdd:COG4694 379 ANL----------------KAEKEEARKKLEAHELAELKEDLsRYKAEVEELIEelkTIKALKKALEDLKTEISELEAEL 442
|
410
....*....|....*.
gi 1099267288 503 ASSEQNKNHINNELKR 518
Cdd:COG4694 443 SSVDEAADEINEELKA 458
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-630 |
2.04e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 88 KALETLRQVRQTQGQKVKEYQMELKylkqykekacEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKim 167
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 168 kLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQeksel 247
Cdd:COG1196 335 -LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA----- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 248 lvEQGRLQLQADRHQEHIRARDSLIQSLATQLEldgfERGPFSERQIKnfhklvRERQEGEAKTANQLMNDFAEKETLKQ 327
Cdd:COG1196 409 --EEALLERLERLEEELEELEEALAELEEEEEE----EEEALEEAAEE------EAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 328 KQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKyeLQQLEGSSDRILELDQELIKAERELSKAEKNSnvetlkmEVIS 407
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVK--AALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-------LAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 408 LQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQL---------- 477
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtllgrtl 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 478 -EDWLHSKSKEINQTRDRLAK-------LNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDvcGSQDFESDLDRLKEE 549
Cdd:COG1196 628 vAARLEAALRRAVTLAGRLREvtlegegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE--EELELEEALLAEEEE 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 550 IEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDE 629
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAER-------EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
.
gi 1099267288 630 M 630
Cdd:COG1196 779 L 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-802 |
2.32e-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: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 542 DLDRLKEEIEKSSKQRAMLAGATAVYSQFitqltdenqsccpvcQRVFQTEAELQEVISDL-----QSKLRLAPDKLKST 616
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERY---------------AAARERLAELEYLRAALrlwfaQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 617 ESELKKKEKRRDEmlglvpmRQSIIDLKEKEIPELRNKLQNV-NRDIQRLKNDIEEQETllgtimpeeesakvcltdvti 695
Cdd:COG4913 301 RAELARLEAELER-------LEARLDALREELDELEAQIRGNgGDRLEQLEREIERLER--------------------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 696 merfqmELKDVERKIAQQAAKLQGIDLdrtvqqvnqekqekqhkldtvssKIELNRKLIQDQQEQIQHLKSTTNELKSE- 774
Cdd:COG4913 353 ------ELEERERRRARLEALLAALGL-----------------------PLPASAEEFAALRAEAAALLEALEEELEAl 403
|
250 260
....*....|....*....|....*...
gi 1099267288 775 KLQISTNLQRRQQLEEQTVELSTEVQSL 802
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1093-1171 |
2.67e-04 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 45.12 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1093 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHD 1171
Cdd:COG4618 458 DTRIGEGGARlSGGQRQ------RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-----KARGATVVVITHR 526
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
71-529 |
2.86e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 71 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEyQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELD 150
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN-QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 151 PLKNRLKEIEHNLSKImklDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEqLNDLYHNHQRTVREKERKLVDCHREL 230
Cdd:TIGR04523 346 QLKKELTNSESENSEK---QRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEKLNQQKDEQIKKLQQEK 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 231 EKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELdgfergpfSERQIKNFHKLVRERQEGEAK 310
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV--------LSRSINKIKQNLEQKQKELKS 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 311 TANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEIlSKKQSELKNVKyelqqlegssDRILELDQELIKAERELS 390
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK-KEKESKISDLE----------DELNKDDFELKKENLEKE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 391 KAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLnhhtttRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGY 470
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL------IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1099267288 471 FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDK 529
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
702-853 |
2.87e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 702 ELKDVERKIAQQAAKLQgiDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNE----------- 770
Cdd:COG3883 24 ELSELQAELEAAQAELD--ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 771 -------LKSEKLQ-ISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQ 842
Cdd:COG3883 102 vsyldvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170
....*....|.
gi 1099267288 843 DKLNDIKEKVK 853
Cdd:COG3883 182 ALLAQLSAEEA 192
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
72-185 |
3.01e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 72 ALKQKFDEIFSATRYIKALE---TLRQVRQTQGQKVKEYQMELK----YLKQYKEKACEIRDqiTSKEAQLTSSKEIVKS 144
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHiedLKEELSNERLRKLRSLLTKLSealdKLRSYLPKLNPLRE--EKKKVSVKSLEELIKD 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1099267288 145 YENELDPLKNRLKEIEhnlSKIMKLDNEIKALDSRKKQMEK 185
Cdd:PRK05771 91 VEEELEKIEKEIKELE---EEISELENEIKELEQEIERLEP 128
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
89-282 |
3.04e-04 |
|
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: 44.75 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 89 ALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMK 168
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 169 -LDNEIKALDSRKKQMEKdNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSEL 247
Cdd:COG4942 98 eLEAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1099267288 248 LVEQGRLQLQADRHQEHIRARDSLIQSLATQLELD 282
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
45-645 |
3.22e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 45 LGVSKAVLNNVIFCHQEDSNWPLSEGKALKQK-FDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACE 123
Cdd:PRK01156 122 LGISKDVFLNSIFVGQGEMDSLISGDPAQRKKiLDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELEN 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 124 IRDQITSKEAQLT-------SSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEK 196
Cdd:PRK01156 202 IKKQIADDEKSHSitlkeieRLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEER 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 197 VFQGTD-------EQLNDLYHNHQRTVREKE---------RKLVDCHRELEKLNK---ESRLLNQEKSELLVEQGRLQLQ 257
Cdd:PRK01156 282 HMKIINdpvyknrNYINDYFKYKNDIENKKQilsnidaeiNKYHAIIKKLSVLQKdynDYIKKKSRYDDLNNQILELEGY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 258 ADRHQEHIRARDSL---IQSLATQLELDGFERGPFSERQIKNFHKLVRERQEgeaktANQLMNDFAEKETLKQKQIDEIR 334
Cdd:PRK01156 362 EMDYNSYLKSIESLkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE-----INVKLQDISSKVSSLNQRIRALR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 335 DKKTGLGRIIELKSeilskKQSELKNVKYELQQlEGSSDRILELDQELIKAERELSKAEKN-SNVETLKMEVISLQN--E 411
Cdd:PRK01156 437 ENLDELSRNMEMLN-----GQSVCPVCGTTLGE-EKSNHIINHYNEKKSRLEEKIREIEIEvKDIDEKIVDLKKRKEylE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 412 KADLDRTLRKlDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIR-KIKSRHSDEL----TSLLGYFPNKKQLE-DWLHSKS 485
Cdd:PRK01156 511 SEEINKSINE-YNKIESARADLEDIKIKINELKDKHDKYEEIKnRYKSLKLEDLdskrTSWLNALAVISLIDiETNRSRS 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 486 KEIN-QTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVcgsQDFESDLDRLKEEIEKSSKQRAMLAGAT 564
Cdd:PRK01156 590 NEIKkQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI---QENKILIEKLRGKIDNYKKQIAEIDSII 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 565 AVYSQFITQLTDENqsccpvcQRVFQTEAELQEVISDlQSKLRLAPDKLKSTESELKKKEKRRDEML-GLVPMRQSIIDL 643
Cdd:PRK01156 667 PDLKEITSRINDIE-------DNLKKSRKALDDAKAN-RARLESTIEILRTRINELSDRINDINETLeSMKKIKKAIGDL 738
|
..
gi 1099267288 644 KE 645
Cdd:PRK01156 739 KR 740
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1128-1180 |
3.75e-04 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 43.49 E-value: 3.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1099267288 1128 IIAlDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGR 1180
Cdd:COG1136 166 ILA-DEPTGNLDSKT----GEEVLELLRELNRELGTTIVMVTHDPELAARADR 213
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
509-669 |
4.43e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 509 KNHINNELKRKEEQLSSYEDKLFD-VCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSC------ 581
Cdd:PHA02562 201 NKNIEEQRKKNGENIARKQNKYDElVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkvikm 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 582 ------CPVCQRVFQTEaelQEVISDLQsklrlapDKLKSTESELKKKEKRRDEMLGLVPMRQSIIdlkeKEIPELRNKL 655
Cdd:PHA02562 281 yekggvCPTCTQQISEG---PDRITKIK-------DKLKELQHSLEKLDTAIDELEEIMDEFNEQS----KKLLELKNKI 346
|
170
....*....|....
gi 1099267288 656 QNVNRDIQRLKNDI 669
Cdd:PHA02562 347 STNKQSLITLVDKA 360
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1115-1171 |
4.68e-04 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 43.26 E-value: 4.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1099267288 1115 RLALAETFCLNCGIIALDEPTTNLDRenieSLAHALVEIIKSRSQQRNFQLLVITHD 1171
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDV----SVQAQILDLLKKLQEELGLTLLFITHD 205
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
586-901 |
4.92e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 586 QRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvPMRQsiiDLKEKEIPELRNKLQNVNRDIQRL 665
Cdd:PRK11281 69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE-----ETRE---TLSTLSLRQLESRLAQTLDQLQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 666 KNDIEEQETLLGTIMPEEESAKVCLT-----------------------DVTIMERFQMELKDVERKIAQQAAKLQGIDL 722
Cdd:PRK11281 141 QNDLAEYNSQLVSLQTQPERAQAALYansqrlqqirnllkggkvggkalRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 723 ---------DRTVQQVNQEKQEKQHKLDTVSSK-IELNRKLIQDQQEQIQHLKSTTNELKSEKLQIstNLQRRQQLEEQT 792
Cdd:PRK11281 221 lqdllqkqrDYLTARIQRLEHQLQLLQEAINSKrLTLSEKTVQEAQSQDEAARIQANPLVAQELEI--NLQLSQRLLKAT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 793 VELSTEVQ----------SLYREIKDAKEQVSPLETTL---EKFQQEKEEL---INKKNTSNKIA-----QDKLNDIKEK 851
Cdd:PRK11281 299 EKLNTLTQqnlrvknwldRLTQSERNIKEQISVLKGSLllsRILYQQQQALpsaDLIEGLADRIAdlrleQFEINQQRDA 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1099267288 852 VKNIHGYMKDIEnyiqdgkddyKKQKETELNKVIAQLSECEKHKEKINED 901
Cdd:PRK11281 379 LFQPDAYIDKLE----------AGHKSEVTDEVRDALLQLLDERRELLDQ 418
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
473-969 |
5.14e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 473 NKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEK 552
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL------NLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 553 SSKQRAMLAGATAV---YSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDE 629
Cdd:TIGR04523 192 IKNKLLKLELLLSNlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 630 mlglvpmRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQ--ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVE 707
Cdd:TIGR04523 272 -------KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 708 RKIAQQAAKLQG------IDLDRTVQQVNQEKQEKQHKLDTV----SSKIELNRKlIQDQQEQIQHLKSTTNELKSEKLQ 777
Cdd:TIGR04523 345 SQLKKELTNSESensekqRELEEKQNEIEKLKKENQSYKQEIknleSQINDLESK-IQNQEKLNQQKDEQIKKLQQEKEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 778 ISTNLQRRQQ-----------LEEQTVELSTEVQSLYREIKDAKEQVSPLE-------TTLEKFQQE---KEELINKKNT 836
Cdd:TIGR04523 424 LEKEIERLKEtiiknnseikdLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKElksKEKELKKLNE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 837 SNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDgKDDYKKQKETELNKVIAQL--SECEKHKEKINEDMRIMRQDIDTQKI 914
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKE-KESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKK 582
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1099267288 915 QERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIK 969
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
322-1079 |
5.54e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 322 KETLKQKqIDEIRDKKTGLGRIIELKSEILSKKQ--SEL-KNVKYELQQLEGSSDRILE-LDQELIKAERELSKAEKNSN 397
Cdd:TIGR01612 602 KLELKEK-IKNISDKNEYIKKAIDLKKIIENNNAyiDELaKISPYQVPEHLKNKDKIYStIKSELSKIYEDDIDALYNEL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 398 VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTkdkadkdeqIRKIKSRHSDELTsllgyfpnkkQL 477
Cdd:TIGR01612 681 SSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSN---------IENKKNELLDIIV----------EI 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 478 EDWLHSK-SKEINQTRDRLAKLNKELAsseqnkNHINNELKRKEeQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQ 556
Cdd:TIGR01612 742 KKHIHGEiNKDLNKILEDFKNKEKELS------NKINDYAKEKD-ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 557 RamlagaTAVYSQFITQLTDEnqsccpvcqrVFQTEAELQEVISDLQSKLRlapdklKSTESELKKKEKRRDEMLGLVPM 636
Cdd:TIGR01612 815 K------SKEYIKTISIKEDE----------IFKIINEMKFMKDDFLNKVD------KFINFENNCKEKIDSEHEQFAEL 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 637 RQSI-IDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAa 715
Cdd:TIGR01612 873 TNKIkAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNI- 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 716 klqgidldRTVQQVNQ-EKQEKQHKLDTVSSKIELNRKLIQDQqeQIQHLKSTTNELKSEKLQISTNL--QRRQQLEEQT 792
Cdd:TIGR01612 952 --------DTIKESNLiEKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAKNNELIKYFNDLKANLgkNKENMLYHQF 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 793 VELSTEVQSLYREIKDAKEQVSPLE----TTLEKFQQEKEELINK------KNTSNK--IAQDKLNDIKEKVK--NIHGY 858
Cdd:TIGR01612 1022 DEKEKATNDIEQKIEDANKNIPNIEiaihTSIYNIIDEIEKEIGKniellnKEILEEaeINITNFNEIKEKLKhyNFDDF 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 859 MKD----IENYIQDGKDD-----------------YKKQKETELNKVIAQLSECEKHKEKI--NEDMRIMR---QDIDTQ 912
Cdd:TIGR01612 1102 GKEenikYADEINKIKDDiknldqkidhhikaleeIKKKSENYIDEIKAQINDLEDVADKAisNDDPEEIEkkiENIVTK 1181
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 913 KIQERWLQDNLtlrKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKe 992
Cdd:TIGR01612 1182 IDKKKNIYDEI---KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKE- 1257
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 993 lREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYktldqAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEyiEIRSDADE 1072
Cdd:TIGR01612 1258 -KSPEIENEMGIEMDIKAEMETFNISHDDDKDHH-----IISKKHDENISDIREKSLKIIEDFSEESDIN--DIKKELQK 1329
|
....*..
gi 1099267288 1073 NVSASDK 1079
Cdd:TIGR01612 1330 NLLDAQK 1336
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1096-1180 |
5.67e-04 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 42.58 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1096 LDM----RGR-CSAGQKVLasliirLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1170
Cdd:cd03245 130 LDLqigeRGRgLSGGQRQA------VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT------LIIITH 197
|
90
....*....|
gi 1099267288 1171 DEDFVELLGR 1180
Cdd:cd03245 198 RPSLLDLVDR 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
472-673 |
5.70e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 472 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIE 551
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI------AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 552 K--SSKQR--------AMLAGATAVySQFITQLTdenqsccpVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELK 621
Cdd:COG3883 90 EraRALYRsggsvsylDVLLGSESF-SDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1099267288 622 KKEKRRDEMLGLVpmrQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQE 673
Cdd:COG3883 161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1093-1170 |
6.69e-04 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 43.88 E-value: 6.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1099267288 1093 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITH 1170
Cdd:TIGR01842 445 DTVIGPGGAtLSGGQRQ------RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-----KARGITVVVITH 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
165-457 |
6.98e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 165 KIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKErklvdchRELEKLNKESRLLNQEK 244
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERE-------RELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 245 ---SELLVEQGRL----QLQADRHQEHIRARDSLiqSLATQLELDGFERGPFSERQIKNFHKLVRERQEGEAKTANQL-- 315
Cdd:pfam17380 365 irqEEIAMEISRMreleRLQMERQQKNERVRQEL--EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLee 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 316 -----MNDFAEKETLKQKQIDEIRDKKTGLGR-IIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAEREL 389
Cdd:pfam17380 443 erareMERVRLEEQERQQQVERLRQQEEERKRkKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 390 SKAEKNSNVETLKMEVislqNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKadkdEQIRKIK 457
Cdd:pfam17380 523 EERQKAIYEEERRREA----EEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER----EMMRQIV 582
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1100-1176 |
7.15e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.52 E-value: 7.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1099267288 1100 GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1176
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL----------DDFPgtVLLVSHDRYFLD 493
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
102-548 |
7.22e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 102 QKVKEYQMELKY--LKQYKEKACEIRDQITSKEAQLTSSkEIVKSYENELDplkNRLKEIEHNLSKIMKLDNEIK-ALDS 178
Cdd:COG5022 856 KAKKRFSLLKKEtiYLQSAQRVELAERQLQELKIDVKSI-SSLKLVNLELE---SEIIELKKSLSSDLIENLEFKtELIA 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 179 RKKQMeKDNSELEEKMEKVFQGTDEQLNdlYHNHQRTVREKERKLVDCH-------RELEKLNKESRLLNQEKSELLVEQ 251
Cdd:COG5022 932 RLKKL-LNNIDLEEGPSIEYVKLPELNK--LHEVESKLKETSEEYEDLLkkstilvREGNKANSELKNFKKELAELSKQY 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 252 GRLQLQADRHQEhiraRDSLIQSLATQLELDGFErgPFSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKQID 331
Cdd:COG5022 1009 GALQESTKQLKE----LPVEVAELQSASKIISSE--STELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 332 EIRDKKT-GLGRIIELKSEILSKKQSELKnvKYELQQLEGSSDRILELDQElikaerelskaeknsnVETLKMEVISLQN 410
Cdd:COG5022 1083 LYQLESTeNLLKTINVKDLEVTNRNLVKP--ANVLQFIVAQMIKLNLLQEI----------------SKFLSQLVNTLEP 1144
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 411 EKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTsllgyfpnkKQLEDWLHSKSKEINQ 490
Cdd:COG5022 1145 VFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEV---------NDLKNELIALFSKIFS 1215
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 491 TrDRLAKLNKELASSEQNKNHINNELKRkeeqlSSYEDKLFDVCGSQDFESDLDRLKE 548
Cdd:COG5022 1216 G-WPRGDKLKKLISEGWVPTEYSTSLKG-----FNNLNKKFDTPASMSNEKLLSLLNS 1267
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
696-830 |
7.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 696 MERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEK 775
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1099267288 776 LQIS-TNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEEL 830
Cdd:COG4717 184 EQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
102-196 |
7.84e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 102 QKVKEYQMELKYLKQYKEkacEIRDQITSKEAQLtsskeivKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKK 181
Cdd:COG2433 413 EEIRRLEEQVERLEAEVE---ELEAELEEKDERI-------ERLERELSEARSEERREIRKDREISRLDREIERLERELE 482
|
90
....*....|....*
gi 1099267288 182 QMEKDNSELEEKMEK 196
Cdd:COG2433 483 EERERIEELKRKLER 497
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1103-1170 |
7.97e-04 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 41.82 E-value: 7.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEiIKSRSQQRnfqlLVITH 1170
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGATR----IVIAH 154
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1103-1176 |
8.41e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 42.26 E-value: 8.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 1103 SAGQKVLASLIIRLALAETFCLNCGI----IALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVE 1176
Cdd:cd03279 125 SGGETFLASLSLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALELI-----RTENRMVGVISHVEELKE 197
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-993 |
8.98e-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: 43.52 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 726 VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTN------ELKSEK--LQISTNLQRRQQLEEQTVELST 797
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKreYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 798 EVQSLYREIKDAKEQVSPLETTLEKFQQEKEElINKKntSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDgkddykkqK 877
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEE-LNKK--IKDLGEEEQLRVKEKIGELEAEIASLERSIAE--------K 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 878 ETELNKVIAQLSECEKHKEKINEDMRIMRQDIDTQKIQERWLQDNLTLRKrneELKEVEEERKQHLKEMGQMQVLQMKSE 957
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---EELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270
....*....|....*....|....*....|....*....
gi 1099267288 958 HQKLE---ENIDNIKRNHNLALGRQKGYEEEIIHFKKEL 993
Cdd:TIGR02169 391 REKLEklkREINELKRELDRLQEELQRLSEELADLNAAI 429
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
696-862 |
9.32e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 696 MERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELkSEK 775
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 776 LQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQvspLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNI 855
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
....*..
gi 1099267288 856 HGYMKDI 862
Cdd:COG3206 340 EARLAEL 346
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
594-885 |
1.06e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 594 ELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEqe 673
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE----------NIARKQNKYDELVEEAKTIKAEIEELTDELLN-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 674 tllgTIMPEEE--SAKVCLTDVTI-----MERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSK 746
Cdd:PHA02562 246 ----LVMDIEDpsAALNKLNTAAAkikskIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 747 IElNRKLIQDqqeQIQHLKSTTNELKSeklQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQvsplettLEKFQQE 826
Cdd:PHA02562 322 ID-ELEEIMD---EFNEQSKKLLELKN---KISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE-------LAKLQDE 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1099267288 827 KEELINKKNTSNK------IAQDKLNDIKEKVKNIHGYM----KDIENYIQDGKDDYKKQKETELNKVI 885
Cdd:PHA02562 388 LDKIVKTKSELVKekyhrgIVTDLLKDSGIKASIIKKYIpyfnKQINHYLQIMEADYNFTLDEEFNETI 456
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
387-531 |
1.18e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 387 RELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTttrtqmEMLTKDKADKDEQIRKIKSRHSDElts 466
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV------EELEAELEEKDERIERLERELSEA--- 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1099267288 467 llgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNknhiNNELKRKEEQLSSYEDKLF 531
Cdd:COG2433 454 --------RSEERREIRKDREISRLDREIERLERELEEERER----IEELKRKLERLKELWKLEH 506
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
301-929 |
1.27e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 301 VRERQEGEAKTANQLMNDFAEKETLKQkqidEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLegssdrILELDQ 380
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHF----GYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 381 ELIKAERELSKAEknSNVETLkmEVISLQNEKADLDRtlRKLDQEMEQLnhhttTRTQMEMLTKDKADKDEQIRKIkSRH 460
Cdd:pfam12128 309 ELSAADAAVAKDR--SELEAL--EDQHGAFLDADIET--AAADQEQLPS-----WQSELENLEERLKALTGKHQDV-TAK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 461 SDELTSLLGYfPNKKQLEDwLHSKSKEINQTRDRLA--------KLNKELASS-EQNKNHINNELKRKEEQLSSYEDKLF 531
Cdd:pfam12128 377 YNRRRSKIKE-QNNRDIAG-IKDKLAKIREARDRQLavaeddlqALESELREQlEAGKLEFNEEEYRLKSRLGELKLRLN 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 532 DVCGSQD-------FESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCpvcQRVFQTEAELQEVisdlqs 604
Cdd:pfam12128 455 QATATPElllqlenFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS---RRLEERQSALDEL------ 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 605 klrlapdklksteselkkkekrrdeMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEqETLLGTIMPEEE 684
Cdd:pfam12128 526 -------------------------ELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDP-EVWDGSVGGELN 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 685 --SAKVCLTDVTIMERFQMElKDVERKIAQQAAKLQGidldrtvQQVNQEKQEKQ-----HKLDTVSSKIELNRKLIQDQ 757
Cdd:pfam12128 580 lyGVKLDLKRIDVPEWAASE-EELRERLDKAEEALQS-------AREKQAAAEEQlvqanGELEKASREETFARTALKNA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 758 QEQIQHLkstTNELKSEKLQISTNLQRRQQL-EEQTVELSTEVQSLYREIKDAKEQV--SPLETTLEKFQQEKEELINKK 834
Cdd:pfam12128 652 RLDLRRL---FDEKQSEKDKKNKALAERKDSaNERLNSLEAQLKQLDKKHQAWLEEQkeQKREARTEKQAYWQVVEGALD 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 835 NTSNKIAQDKL---NDIKEKVKNIHGYMK-DIENYIQDGKDDYKKqkETELNKVIAQLSECEKHKEKINEDMRIMrqdid 910
Cdd:pfam12128 729 AQLALLKAAIAarrSGAKAELKALETWYKrDLASLGVDPDVIAKL--KREIRTLERKIERIAVRRQEVLRYFDWY----- 801
|
650 660
....*....|....*....|.
gi 1099267288 911 tqkiQERWLQ--DNLTLRKRN 929
Cdd:pfam12128 802 ----QETWLQrrPRLATQLSN 818
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
73-509 |
1.41e-03 |
|
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: 43.03 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 73 LKQKFDEIFSATRYIKALETLRQVRQTQGQKVKE-YQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEI------VKSY 145
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPgpltrrMQRG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 146 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVD 225
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 226 CHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEhirardsliqslatQLELdGFERGPFSERQIKNFHKLVRERQ 305
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL--------------QLTL-TQERVREHALSIRVLPKELLASR 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 306 EGEAKTANQLMNDFA-EKETLKQKQIdeirdkktgLGRIIELKSEILSKKQSELKNVKYELQQ-LEGSSDRILELDQELI 383
Cdd:TIGR00618 679 QLALQKMQSEKEQLTyWKEMLAQCQT---------LLRELETHIEEYDREFNEIENASSSLGSdLAAREDALNQSLKELM 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 384 KAERELSKAEKNSNVETLKMEVISLQ--NEKADLDRTLRKLDQEMEQLNHHTTTR----------------TQMEMLTKD 445
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLeaeigqeipsdedilnLQCETLVQE 829
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099267288 446 KADKDEQIRKiKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNK 509
Cdd:TIGR00618 830 EEQFLSRLEE-KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDA 892
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1115-1171 |
1.81e-03 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 40.50 E-value: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1099267288 1115 RLALAETFCLNCGIIALDEPTTNLDreniesLAH--ALVEIIKSRSQQRNFQLLVITHD 1171
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLD------IAHqiELLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1091-1171 |
2.41e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.59 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 1091 KGDTALDMRG------RC----SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIEslahALVEIIKsRSQQ 1160
Cdd:cd03235 112 KVDEALERVGlseladRQigelSGGQQQ------RVLLARALVQDPDLLLLDEPFAGVDPKTQE----DIYELLR-ELRR 180
|
90
....*....|.
gi 1099267288 1161 RNFQLLVITHD 1171
Cdd:cd03235 181 EGMTILVVTHD 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1103-1175 |
2.48e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 41.81 E-value: 2.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDreniESLAHALVEIIKSRSQQRNFQLLVITHDEDFV 1175
Cdd:COG1123 144 SGGQRQ------RVAIAMALALDPDLLIADEPTTALD----VTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
115-994 |
2.52e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 115 KQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKM 194
Cdd:TIGR01612 537 KLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKN 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 195 EKVfqgtdeqlndlyhnhqrtvrekeRKLVDCHRELEKlnkesrllNQEKSELLVEQGRLQLqadrhQEHIRARDSLIQS 274
Cdd:TIGR01612 617 EYI-----------------------KKAIDLKKIIEN--------NNAYIDELAKISPYQV-----PEHLKNKDKIYST 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 275 LATQLeldgfergpfSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKqIDEIRDKKTGL-GRIIELKSEILSK 353
Cdd:TIGR01612 661 IKSEL----------SKIYEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSK-IDKEYDKIQNMeTATVELHLSNIEN 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 354 KQSELKNVKYELQQLEGSsdrilELDQELIKAERELSKAEKNsnvetLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHT 433
Cdd:TIGR01612 730 KKNELLDIIVEIKKHIHG-----EINKDLNKILEDFKNKEKE-----LSNKINDYAKEKDELNKYKSKISEIKNHYNDQI 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 434 TTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKqlEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHIN 513
Cdd:TIGR01612 800 NIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMK--DDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIK 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 514 NELkrKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEKSskqramlagatavySQFITQLTDENQScCPVCQRVFQTEA 593
Cdd:TIGR01612 878 AEI--SDDKLNDYEKKF------NDSKSLINEINKSIEEE--------------YQNINTLKKVDEY-IKICENTKESIE 934
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 594 ELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLglvpmrQSIIDLKEKEIPELR-NKLQNVNRDIQRLKNDIEEQ 672
Cdd:TIGR01612 935 KFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTL------IDKINELDKAFKDASlNDYEAKNNELIKYFNDLKAN 1008
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 673 etlLGTimPEEEsakvcltdvTIMERFQMELK---DVERKIAQQAAKLQGIDLDRTVQQVN-QEKQEKQhkldtVSSKIE 748
Cdd:TIGR01612 1009 ---LGK--NKEN---------MLYHQFDEKEKatnDIEQKIEDANKNIPNIEIAIHTSIYNiIDEIEKE-----IGKNIE 1069
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 749 -LNRKLIQDQQEQIQHLksttNELKsEKLQIstnLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEK 827
Cdd:TIGR01612 1070 lLNKEILEEAEINITNF----NEIK-EKLKH---YNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKS 1141
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 828 EELINKKntsnKIAQDKLNDIKEKV---KNIHGYMKDIENYIQdgKDDYKKQKETELNKVIAQLSECEKHK--------- 895
Cdd:TIGR01612 1142 ENYIDEI----KAQINDLEDVADKAisnDDPEEIEKKIENIVT--KIDKKKNIYDEIKKLLNEIAEIEKDKtsleevkgi 1215
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 896 -------------EKINEDMRIMRQDIdtqKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSE----- 957
Cdd:TIGR01612 1216 nlsygknlgklflEKIDEEKKKSEHMI---KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKdhhii 1292
|
890 900 910
....*....|....*....|....*....|....*..
gi 1099267288 958 HQKLEENIDNIkRNHNLALGRQKGYEEEIIHFKKELR 994
Cdd:TIGR01612 1293 SKKHDENISDI-REKSLKIIEDFSEESDINDIKKELQ 1328
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1103-1174 |
2.79e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.59 E-value: 2.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099267288 1103 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDF 1174
Cdd:COG0488 154 SGGWRR------RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----------KNYPgtVLVVSHDRYF 211
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
726-888 |
3.19e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 726 VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQeqiqhlKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYRE 805
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR------KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 806 IKDakeqvspLETTLEKFQQEKEELINKKNTSNKIA-------------------QDKLNDIKEKVKNIHGYMKDIENYI 866
Cdd:PHA02562 250 IED-------PSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptctqqisegPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180
....*....|....*....|....*..
gi 1099267288 867 QDGK---DDYKKQ--KETELNKVIAQL 888
Cdd:PHA02562 323 DELEeimDEFNEQskKLLELKNKISTN 349
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1115-1182 |
3.34e-03 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 40.49 E-value: 3.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 1115 RLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEdfvELLGRSE 1182
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAAT----GEQIIDLLFELNRERGTTLVLVTHDP---ALAARCD 214
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
262-556 |
4.34e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 41.32 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 262 QEHIRARDSLIQSLATQLEldgFERGPFSERQIKNFHKLVRERQEGEAKTANQLMNdfAEKETLKQKQ-IDEIRDKKTGL 340
Cdd:COG5391 221 EERRQSLQNFLRRVSTHPL---LSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLD--LTSTTQELDMeRKELNESTSKA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 341 GRIIELKSEILSKKQSELKNVKYELQQLEgsSDRILELDQELIKAERELSKAEKNSN--VETLKMEVISLQNEKADLDRT 418
Cdd:COG5391 296 IHNILSIFSLFEKILIQLESEEESLTRLL--ESLNNLLLLVLNFSGVFAKRLEQNQNsiLNEGVVQAETLRSSLKELLTQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 419 LRKLDQEMEQLNHhtttrtQMEMLTKDKADKDEQIRKI------KSRHSDELTS--LLGYFPNKKQ--LEDWLH--SKSK 486
Cdd:COG5391 374 LQDEIKSRESLIL------TDSNLEKLTDQNLEDVEELsrslrkNSSQRAVVSQqpEGLTSFSKLSykLRDFVQekSRSK 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 487 EINQTRDRLAKLNKELASSEQNKNHINNELKrkeeqlssYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQ 556
Cdd:COG5391 448 SIESLQQDKEKLEEQLAIAEKDAQEINEELK--------NELKFFFSVRNSDLEKILKSVADSHIEWAEE 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
126-280 |
4.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 126 DQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQL 205
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 206 NDLYHNHQ------------------------RTVREKERKLVDCHREL-EKLNKESRLLNQEKSELLVEQGRLQLQADR 260
Cdd:COG3883 93 RALYRSGGsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADkAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180
....*....|....*....|
gi 1099267288 261 HQEHIRARDSLIQSLATQLE 280
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEA 192
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-673 |
5.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 74 KQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITS--KEAQLTSSKEIVKSYENELDP 151
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAakKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 152 LKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNS-ELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHREL 230
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 231 EKLNKESRLLNQEKSEllVEQGRLQLQADRHQEHIRARDSLiqslatqleldgfergpfserqiknfhklvrERQEGEAK 310
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKKADEA-------------------------------KKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 311 TANQLmndfAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQSELKNVKYELQQLEGSSDRILELDQELIKAErELS 390
Cdd:PTZ00121 1484 KADEA----KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 391 KAEKNSNVETLKMEvislQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGY 470
Cdd:PTZ00121 1559 KAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 471 FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDvcgSQDFESDLDRLKEEI 550
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 551 EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEm 630
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE- 1790
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1099267288 631 lglvpMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQE 673
Cdd:PTZ00121 1791 -----KRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
50-67 |
6.28e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 6.28e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-429 |
6.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 302 RERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKK--QSELKNVKYELQQLEGSSDRILELD 379
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1099267288 380 QELIKAERELSKAEKnsNVETLKMEVISLQNEKADLDRTLRKLDQEMEQL 429
Cdd:COG4913 692 EQLEELEAELEELEE--ELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
696-852 |
6.74e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 696 MERFQMELKDVERKIAQQAAKLQGidLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKsTTNELKSEK 775
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAA--LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1099267288 776 LQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKV 852
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1093-1170 |
8.25e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 40.15 E-value: 8.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1099267288 1093 DTALDMRG-RCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1170
Cdd:COG1132 467 DTVVGERGvNLSGGQRQ------RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT------TIVIAH 533
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1101-1178 |
8.66e-03 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 38.53 E-value: 8.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099267288 1101 RCSAGQKvlasliIRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSqQRNFQLLVITHDEDFVELL 1178
Cdd:cd03230 95 KLSGGMK------QRLALAQALLHDPELLILDEPTSGLDPES----RREFWELLRELK-KEGKTILLSSHILEEAERL 161
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
799-918 |
9.61e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.66 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099267288 799 VQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHgyMKDIENYIQDGKDDYKKQKE 878
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKE--IKDLQKELEKLNEEYAAKLK 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1099267288 879 TELNKV---IAQLSECEKHKEKINEDMRIMRQDIDT------------QKIQERW 918
Cdd:cd22656 201 AKIDELkalIADDEAKLAAALRLIADLTAADTDLDNllaligpaipalEKLQGAW 255
|
|
| |
