|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-1312 |
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: 1832.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 2 SRIEKMSILGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 81
Cdd:TIGR00606 1 AKFLKMSILGVRSFGIEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 82 IRLQFRDVNGELIAVQRSMVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQED 161
Cdd:TIGR00606 81 IRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 162 SNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIV 241
Cdd:TIGR00606 161 SNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 242 KSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERK 321
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 322 LVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVR 401
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 402 ERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQEL 481
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 482 IKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSD 561
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 562 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESD 641
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 642 LDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKK 721
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 722 KEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME 801
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 802 LKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNL 881
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 882 QRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDI 961
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 962 ENYIQDGKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQH 1041
Cdd:TIGR00606 961 ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQH 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1042 LKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1121
Cdd:TIGR00606 1041 LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1122 DIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRC 1201
Cdd:TIGR00606 1121 DIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRC 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1202 SAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSE 1281
Cdd:TIGR00606 1201 SAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSE 1280
|
1290 1300 1310
....*....|....*....|....*....|.
gi 19924129 1282 YVEKFYRIKKNIDQCSEIVKCSVSSLGFNVH 1312
Cdd:TIGR00606 1281 YVEKFYRLKKNEDQCSEIVKCSPSSLGKRVH 1311
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1195-1297 |
9.23e-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: 9.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1195 LDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIEslaHALVEIIKSRSQQRNFQLLVITHDEDFV 1274
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIE---ESLAEIIEERKSQKNFQLIVITHDEELV 186
|
90 100
....*....|....*....|...
gi 19924129 1275 ELLGrseyveKFYRIKKNIDQCS 1297
Cdd:cd03240 187 DAAD------HIYRVEKDGRQKS 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-166 |
7.23e-37 |
|
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: 138.12 E-value: 7.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 4 IEKMSILGVRSFgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNtfVHDPKVAQETDVRAQIR 83
Cdd:cd03240 1 IDKLSIRNIRSF----HERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGG--AHDPKLIREGEVRAQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 84 LQFRDVNGELIAVQRSMvctqkskktefktlegvitrtkhgekvslsskcaeidremisslgvskAVLNNVIFCHQEDSN 163
Cdd:cd03240 75 LAFENANGKKYTITRSL------------------------------------------------AILENVIFCHQGESN 106
|
...
gi 19924129 164 WPL 166
Cdd:cd03240 107 WPL 109
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-215 |
1.13e-19 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 88.32 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 7 MSILGVRSFgiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFP---PGTKGNTFVHDPKVAQETDVRAQIR 83
Cdd:pfam13476 1 LTIENFRSF-----RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSrlkRKSGGGFVKGDIRIGLEGKGKAYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 84 LQFRDVNGELI-AVQRSMVCTQKSKKTEFKTLEGVITRtkhgekvslsskcaEIDREMISSLGVSKAVLNNVIFCHQEDS 162
Cdd:pfam13476 76 ITFENNDGRYTyAIERSRELSKKKGKTKKKEILEILEI--------------DELQQFISELLKSDKIILPLLVFLGQER 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19924129 163 NWPLSEgkalKQKFDEIFSATRYIKALETLRQVRQTQgQKVKEYQMELKYLKQ 215
Cdd:pfam13476 142 EEEFER----KEKKERLEELEKALEEKEDEKKLLEKL-LQLKEKKKELEELKE 189
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-1012 |
6.34e-19 |
|
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: 93.58 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 190 ETLRQVRQTQG--QKV----KEYQMELKYLKQYKEKA---CEIRDQItsKEAQLTSSKEIVKSYENELDPLKNRLKEIEH 260
Cdd:TIGR02168 176 ETERKLERTREnlDRLedilNELERQLKSLERQAEKAeryKELKAEL--RELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 261 nlsKIMKLDNEIKALDSRKKQMEKDNSELEEKMEkvfqgtdeQLNDLYHNHQRTVREKERklvdchrELEKLNKESRLLN 340
Cdd:TIGR02168 254 ---ELEELTAELQELEEKLEELRLEVSELEEEIE--------ELQKELYALANEISRLEQ-------QKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 341 QEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLEldgfergpfserqiknfhklvreRQEGEAKTANQLMNDFAE 420
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-----------------------SLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 421 KETLKQKQIDEIRDKktglgrIIELKSEILSKkQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETL 500
Cdd:TIGR02168 373 RLEELEEQLETLRSK------VAQLELQIASL-NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 501 KMEVISLQNEKADLDRTLRKLDQEMEQLNhhtttrtqmEMLTKDKADKDEQIRKIKSRHSDElTSLLGYFPNKKQLEDWl 580
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAE---------QALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKN- 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 581 hskSKEINQTRDRLAKLnkeLASSEQNKNHINNELkrkEEQLSSYEDKlfdvcGSQDFESDLDRLKeeieKSSKQRAMLA 660
Cdd:TIGR02168 515 ---QSGLSGILGVLSEL---ISVDEGYEAAIEAAL---GGRLQAVVVE-----NLNAAKKAIAFLK----QNELGRVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 661 GATAVYSQFIT----QLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTEselKKKEKRRDEML------ 730
Cdd:TIGR02168 577 PLDSIKGTEIQgndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALE---LAKKLRPGYRIvtldgd 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 731 ----------GLVPMRQSIIDlKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQ 799
Cdd:TIGR02168 654 lvrpggvitgGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALR 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 800 MELKDVERKIAQQAAKLQGIDLDRTVQQV-----NQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSE- 873
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAeieelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEl 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 874 ---KLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELinkkntsnkiaQDKLNDIKEK 950
Cdd:TIGR02168 813 tllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----------ESELEALLNE 881
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19924129 951 VKNIHGYMKDIENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQK 1012
Cdd:TIGR02168 882 RASLEEALALLRSELEE-LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1197-1298 |
3.41e-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: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1197 MRGRCSAGQKVLASLIIRLALAEtfCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNfQLLVITHDEDFVEL 1276
Cdd:cd03227 74 TRLQLSGGEKELSALALILALAS--LKPRPLYILDEIDRGLDPRD----GQALAEAILEHLVKGA-QVIVITHLPELAEL 146
|
90 100
....*....|....*....|..
gi 19924129 1277 LgrseyvEKFYRIKKNIDQCSE 1298
Cdd:cd03227 147 A------DKLIHIKKVITGVYK 162
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
417-952 |
1.42e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.42 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 417 DFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKaeknsn 496
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 497 VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLlgyfpnKKQL 576
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI------EERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 577 EDwLHSKSKEINQTRDRLAKLNKELASSEQnKNHINNELKRKEEQLSSYEDKLFDVcGSQDFESDLDRLKEEIEKSSKQR 656
Cdd:PRK03918 331 KE-LEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 657 AMLAGATAVYSQFITQLTD------ENQSCCPVCQRVFqTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEML 730
Cdd:PRK03918 408 SKITARIGELKKEIKELKKaieelkKAKGKCPVCGREL-TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 731 GLVPMRQSIIDLKE--KEIPELRNKLQNVNrdIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERK 808
Cdd:PRK03918 487 KVLKKESELIKLKElaEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 809 IAQQAAKLQGI-------------DLDRTVQQ-------------VNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQH 862
Cdd:PRK03918 565 LDELEEELAELlkeleelgfesveELEERLKElepfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 863 LKSTTNELKSEklqisTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKI--A 940
Cdd:PRK03918 645 LRKELEELEKK-----YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekA 719
|
570
....*....|..
gi 19924129 941 QDKLNDIKEKVK 952
Cdd:PRK03918 720 LERVEELREKVK 731
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-1016 |
1.94e-15 |
|
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: 82.04 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 4 IEKMSILGVRSFGiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKyictgdFPPGTKGNT---------FVHDPKVAQ 74
Cdd:TIGR02169 2 IERIELENFKSFG----KKKVIPFSKGFTVISGPNGSGKSNIGDAIL------FALGLSSSKamraerlsdLISNGKNGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 75 ETDvRAQIRLQFRD---VNGELIAVQRSMVCTQKSKKTEFKTlegvitrtkHGEKVSLSskcaEIDrEMISSLGVSKAVL 151
Cdd:TIGR02169 72 SGN-EAYVTVTFKNddgKFPDELEVVRRLKVTDDGKYSYYYL---------NGQRVRLS----EIH-DFLAAAGIYPEGY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 152 NNVIfchQEDSNWPLS-EGKALKQKFDEIFSATRY----IKALETLRQVRQTQGQ---KVKEYQMELKYLKQYKEKAceI 223
Cdd:TIGR02169 137 NVVL---QGDVTDFISmSPVERRKIIDEIAGVAEFdrkkEKALEELEEVEENIERldlIIDEKRQQLERLRREREKA--E 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 224 RDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQ 303
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 304 LNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELdgf 383
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 384 ergpfserqiknfhkLVRERQEgEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEiLSKKQNELKNvkye 463
Cdd:TIGR02169 369 ---------------LRAELEE-VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR-LSEELADLNA---- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 464 lqQLEGSSDRILELDQELIKAERELSKAEKN--SNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEML 541
Cdd:TIGR02169 428 --AIAGIEAKINELEEEKEDKALEIKKQEWKleQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 542 TKDKADKDEQIR--------------KIKSRHSDELTSLLGYFPNKKQLEDWLHSKS-----KEINQTRDRLAKLNKeLA 602
Cdd:TIGR02169 506 VRGGRAVEEVLKasiqgvhgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEaiellKRRKAGRATFLPLNK-MR 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 603 SSEQNKNHINNE--------LKRKEEQlssYEDKLFDVCGSQDFESDLDRLKE----------EIEKSSKQRAMLAGATA 664
Cdd:TIGR02169 585 DERRDLSILSEDgvigfavdLVEFDPK---YEPAFKYVFGDTLVVEDIEAARRlmgkyrmvtlEGELFEKSGAMTGGSRA 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 665 VYSQFITQLTDenqsccpvcqrvfqtEAELQEVISDLQSKLRLapdkLKSTESELKKKEKRRDEMlglvpmrQSIIDLKE 744
Cdd:TIGR02169 662 PRGGILFSRSE---------------PAELQRLRERLEGLKRE----LSSLQSELRRIENRLDEL-------SQELSDAS 715
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 745 KEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimerfqMELKDVERKIAQQAAKLQGIDLdrt 824
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK-------------SELKELEARIEELEEDLHKLEE--- 779
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 825 vQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQIStnlQRRQQLEEQTVELSTEVQSLYRE 904
Cdd:TIGR02169 780 -ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE---KEIQELQEQRIDLKEQIKSIEKE 855
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 905 IKDAKEQVSPLETTLEKFQQEKEELInkkntsnkiaqDKLNDIKEKVKNIHGYMKDIENYIQDGKDDY--KKQKETELNK 982
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLE-----------SRLGDLKKERDELEAQLRELERKIEELEAQIekKRKRLSELKA 924
|
1050 1060 1070
....*....|....*....|....*....|....*
gi 19924129 983 VIAQLSECEKHKEK-INEDMRLMRQDIDTQKIQER 1016
Cdd:TIGR02169 925 KLEALEEELSEIEDpKGEDEEIPEEELSLEDVQAE 959
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-810 |
5.58e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 3 RIEKMSILGVRSfgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLK---YICTGDFPPGTKGNTFVHDPKVaqetdvR 79
Cdd:PRK03918 2 KIEELKIKNFRS-----HKSSVVEFDDGINLIIGQNGSGKSSILEAILvglYWGHGSKPKGLKKDDFTRIGGS------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 80 AQIRLQFrDVNGELIAVQRsmvctqkskktefKTLEGVITRTKHGEKVSLSSKCAEIDREMISSlgVSKAVLNNVIFCHQ 159
Cdd:PRK03918 71 TEIELKF-EKNGRKYRIVR-------------SFNRGESYLKYLDGSEVLEEGDSSVREWVERL--IPYHVFLNAIYIRQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 160 EDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRqtqgqkvKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKE 239
Cdd:PRK03918 135 GEIDAILESDESREKVVRQILGLDDYENAYKNLGEVI-------KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 240 IVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMekvfQGTDEQLNDLyHNHQRTVREKE 319
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI----RELEERIEEL-KKEIEELEEKV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 320 RKLvdchRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRArdslIQSLATQLELDGFERGPFSERQIKNFHKL 399
Cdd:PRK03918 283 KEL----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----IEERIKELEEKEERLEELKKKLKELEKRL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 400 vrERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKktgLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQ 479
Cdd:PRK03918 355 --EELEERHELYEEAKAKKEELERLKKRLTGLTPEK---LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 480 ELIKAE-------RELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNhhtTTRTQMEMLTKDKaDKDEQI 552
Cdd:PRK03918 430 ELKKAKgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE---KVLKKESELIKLK-ELAEQL 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 553 RKIKSRHS----DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASseqnknhINNELKRKEEQLSSYEDK 628
Cdd:PRK03918 506 KELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-------LEKKLDELEEELAELLKE 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 629 LFDVcGSQDFESDLDRLKeEIEKsskqramlagataVYSQFITQLTDEnqsccpvcqrvfQTEAELQEVISDLQSKLRLA 708
Cdd:PRK03918 579 LEEL-GFESVEELEERLK-ELEP-------------FYNEYLELKDAE------------KELEREEKELKKLEEELDKA 631
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 709 PDKLKSTESELKKKEKRRDEMLGLvpmrqsiidLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKvc 788
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKK---------YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK-- 700
|
810 820
....*....|....*....|..
gi 19924129 789 lTDVTIMERFQMELKDVERKIA 810
Cdd:PRK03918 701 -EELEEREKAKKELEKLEKALE 721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-1068 |
1.03e-11 |
|
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: 69.71 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 393 IKNFHKLVRERQEGEAKTANQL-MNDFAEKETLKQKQIDEiRDKKTGLGRIIELkseilskkQNELKNVKYELQQLEGSS 471
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKeKREYEGYELLKEKEALE-RQKEAIERQLASL--------EEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 472 DRILELDQELIKAERELSKAEKNsnveTLKMEVISLQNEKADLDRTLRKLDQEMEQLNhhtttrtqmemltKDKADKDEQ 551
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERELEDAE-------------ERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 552 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQnknhinnELKRKEEQLSSYEDKLFD 631
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 632 VCGSQDfeSDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAEL---QEVISDLQSKLRLA 708
Cdd:TIGR02169 404 LKRELD--RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLskyEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 709 PDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIP----------------------ELRNKLQNV--------N 758
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataievAAGNRLNNVvveddavaK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 759 RDIQRLK------------NDIEEQETLLGTIMPE----------------EESAKVCLTDVTIMERF--------QMEL 802
Cdd:TIGR02169 562 EAIELLKrrkagratflplNKMRDERRDLSILSEDgvigfavdlvefdpkyEPAFKYVFGDTLVVEDIeaarrlmgKYRM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 803 KDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKqhKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKseklqistnlQ 882
Cdd:TIGR02169 642 VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPA--ELQRLRERLEGLKRELSSLQSELRRIENRLDELS----------Q 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 883 RRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQD---KLNDIKEKVKNIhgYMK 959
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEleeDLHKLEEALNDL--EAR 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 960 DIENYIQDGKDDYKKQKEtELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERK 1039
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEE-EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
730 740
....*....|....*....|....*....
gi 19924129 1040 QHLKEMGQMQVLQMKSEHQKLEENIDNIK 1068
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELE 895
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-85 |
3.59e-11 |
|
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: 62.76 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 6 KMSILGVRSFGIEdkdkQIITFFSP-LTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRL 84
Cdd:cd03227 1 KIVLGRFPSYFVP----NDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRL 76
|
.
gi 19924129 85 Q 85
Cdd:cd03227 77 Q 77
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
396-1118 |
3.88e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 396 FHKLVRERQEGEAKT-ANQLMNDFAEKETLkQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLegSSDRI 474
Cdd:TIGR02169 213 YQALLKEKREYEGYElLKEKEALERQKEAI-ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL--GEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 475 LELDQELIKAERELSKAEknSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTT-RTQMEMLTKDKADKDEQIR 553
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLE--RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEEYAELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 554 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSsyedklfdvc 633
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN---------- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 634 gsqDFESDLDRLKEEIEKSSKQRamlagatavySQFITQLTDENQSccpvcqrvfqteaelqevISDLQSKLRLAPDKLK 713
Cdd:TIGR02169 438 ---ELEEEKEDKALEIKKQEWKL----------EQLAADLSKYEQE------------------LYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 714 STESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIP----------------------ELRNKLQNV--------NRDIQR 763
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataievAAGNRLNNVvveddavaKEAIEL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 764 LK------------NDIEEQETLLGTIMPE----------------EESAKVCLTDVTIMERFQM--------------- 800
Cdd:TIGR02169 567 LKrrkagratflplNKMRDERRDLSILSEDgvigfavdlvefdpkyEPAFKYVFGDTLVVEDIEAarrlmgkyrmvtleg 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 801 ELKDVERKIAQQAAKLQGIDLDRT-----VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKL 875
Cdd:TIGR02169 647 ELFEKSGAMTGGSRAPRGGILFSRsepaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 876 QI----STNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSN-KIAQDKLNDIKEK 950
Cdd:TIGR02169 727 QLeqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 951 VKNIHGYMKDIENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKRNE 1029
Cdd:TIGR02169 807 VSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKeELEEELEELEAALRDLESRLG 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1030 ELKEVEEERKQHLKEMgQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELRE-PQFRDAEEKYREMM 1108
Cdd:TIGR02169 886 DLKKERDELEAQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEeLSLEDVQAELQRVE 964
|
810
....*....|
gi 19924129 1109 IVMRTTELVN 1118
Cdd:TIGR02169 965 EEIRALEPVN 974
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
26-944 |
3.43e-10 |
|
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: 64.60 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 26 TFFSPLTILVGPNGAGKTTIIECLKYICTGDFPpgTKGNTFVHDPKVAQETDVRAQIRLQFrDVNGELIAVQRSMVCTQK 105
Cdd:TIGR00618 23 TALGPIFLICGKTGAGKTTLLDAITYALYGKLP--RRSEVIRSLNSLYAAPSEAAFAELEF-SLGTKIYRVHRTLRCTRS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 106 SKKTEfkTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQ-EDSNWPLSEGKALKQKFDEIFSATR 184
Cdd:TIGR00618 100 HRKTE--QPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQgEFAQFLKAKSKEKKELLMNLFPLDQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 185 Y-IKALETLRQVRQTQGQKVKEyQMELKYLKQYKEKaceirdqitskeaQLTSSKEIVKSYENELDPLKNRLKEIEHNLS 263
Cdd:TIGR00618 178 YtQLALMEFAKKKSLHGKAELL-TLRSQLLTLCTPC-------------MPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 264 KIMKLDNEIKALDSRKKQMEKDNSELEEkmekvfqgtdeqlndlyHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEK 343
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEE-----------------LRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 344 SELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSErqiknfHKLVRERQEGEAKTANQLMNDFAEKET 423
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ------EIHIRDAHEVATSIREISCQQHTLTQH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 424 LKQKQIDeirdkKTGLGRIIELKSEILSKKQNELKNVKYELQqlegsSDRILELDQELIKAERELSKAEKNSNVETLKME 503
Cdd:TIGR00618 381 IHTLQQQ-----KTTLTQKLQSLCKELDILQREQATIDTRTS-----AFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 504 VISLQNEKADLDRTLRKLDQEMEQLNhhtttrtQMEMLTKDKADKDEQIRKIKSRHSDELTSLLG---YFPNKKQLEDWL 580
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQ-------TKEQIHLQETRKKAVVLARLLELQEEPCPLCGsciHPNPARQDIDNP 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 581 HSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDV--------CGSQDFESDLDRLKEEIEKS 652
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrskEDIPNLQNITVRLQDLTEKL 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 653 SKQRAMLAGAtavySQFITQLTDENQSCCPVCQRVFQTEAELQEVISDL-QSKLRLAPDK-----LKSTESELKKKEKRR 726
Cdd:TIGR00618 604 SEAEDMLACE----QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhALQLTLTQERvrehaLSIRVLPKELLASRQ 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 727 DEMLGLVPMRQSIIDLKEkEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVE 806
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKE-MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 807 RKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSskiELNRKLIQDQQEQIQHLKSTTNELkseKLQISTNLQRRQQ 886
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE---EDTHLLKTLEAEIGQEIPSDEDIL---NLQCETLVQEEEQ 832
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19924129 887 LEEQTVELST---EVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKL 944
Cdd:TIGR00618 833 FLSRLEEKSAtlgEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDAL 893
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
473-1171 |
4.98e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 473 RILELDQELIKAERELSKAEKNS---NVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNH-HTTTRTQMEMLTK----- 543
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEElreELEELQEELKEAEEELEELTAELQELEEKLEELRLeVSELEEEIEELQKelyal 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 544 --DKADKDEQIRKIKSRhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQ 621
Cdd:TIGR02168 294 anEISRLEQQKQILRER--------------LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 622 LSSYEDKLFD-VCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfqteaELQEVISD 700
Cdd:TIGR02168 360 LEELEAELEElESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE--------------RLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 701 LQSKLRLApdKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMP 780
Cdd:TIGR02168 426 LLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 781 EEESAK--------------VCLTDVTIMERFQMELKDVERKIAQ------QAAKLQGIDLDR----------------- 823
Cdd:TIGR02168 504 FSEGVKallknqsglsgilgVLSELISVDEGYEAAIEAALGGRLQavvvenLNAAKKAIAFLKqnelgrvtflpldsikg 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 824 TVQQVNQEKQEKQHK--------LDTVSSKIE------LNRKLIQDQQEQIQHLKSTTNEL------------------K 871
Cdd:TIGR02168 584 TEIQGNDREILKNIEgflgvakdLVKFDPKLRkalsylLGGVLVVDDLDNALELAKKLRPGyrivtldgdlvrpggvitG 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 872 SEKLQISTNLQRRQ---QLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEElinkKNTSNKIAQDKLNDIK 948
Cdd:TIGR02168 664 GSAKTNSSILERRReieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 949 EKVKNIHGYMKDIENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRN 1028
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1029 EELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELR--EPQFRDAEEKYRE 1106
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAslEEALALLRSELEE 898
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19924129 1107 MMIVMRTTELVNKDLDIYYKTLDQAIMKFH------SMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADE 1171
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-1298 |
6.92e-10 |
|
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: 63.84 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 251 LKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELE 330
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 331 KLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELdgfergpfserqiKNFHKLVRERQEGEAKT 410
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS-------------ELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 411 ANQLMNDFAEKETLKQKQIDEIRDKktglgriiELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSK 490
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEK--------ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 491 AEKNSNVETLKMEVISLQNEKADLDRTlrkldQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYF 570
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQ-----LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 571 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRkeeqlssyedklfdvcgsqdfesdldrlkeeIE 650
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-------------------------------LL 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 651 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKL----KSTESELKKKEKRR 726
Cdd:pfam02463 514 ALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgarkLRLLIPKLKLPLKS 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 727 DEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIM----PEEESAKVCLTDVTIMERFQMEL 802
Cdd:pfam02463 594 IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESglrkGVSLEEGLAEKSEVKASLSELTK 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 803 KDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQ 882
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 883 --RRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKN-TSNKIAQDKLNDIKEKVKNIHGYMK 959
Cdd:pfam02463 754 ksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEeELKEEAELLEEEQLLIEQEEKIKEE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 960 DIENYIQD----GKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVE 1035
Cdd:pfam02463 834 ELEELALElkeeQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1036 EERKQHLKEMGQMQVLQMK--SEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVmRT 1113
Cdd:pfam02463 914 EKENEIEERIKEEAEILLKyeEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY-NK 992
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1114 TELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDlwRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRV-VMLKGD 1192
Cdd:pfam02463 993 DELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS--INKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIsARPPGK 1070
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1193 TALDMRgRCSAGQKVLASLIIRLALAE----TFCLncgiiaLDEPTTNLDRENIESLAHALveiiksRSQQRNFQLLVIT 1268
Cdd:pfam02463 1071 GVKNLD-LLSGGEKTLVALALIFAIQKykpaPFYL------LDEIDAALDDQNVSRVANLL------KELSKNAQFIVIS 1137
|
1050 1060 1070
....*....|....*....|....*....|
gi 19924129 1269 HDEDFVELlgrseyVEKFYRIKKNIDQCSE 1298
Cdd:pfam02463 1138 LREEMLEK------ADKLVGVTMVENGVST 1161
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1202-1283 |
9.38e-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: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVELLGRSE 1281
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-----AEEGRTVIIVTHDPELAELAADRV 150
|
..
gi 19924129 1282 YV 1283
Cdd:cd00267 151 IV 152
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
392-1004 |
9.42e-10 |
|
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: 63.21 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 392 QIKNFHKLVRERQEGEAKTANQLMNDFAEKETlkqkQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQ------ 465
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVIDLQT----KLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEaakclk 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 466 --QLEGSSDRILELDQELIKAER----------ELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHT- 532
Cdd:pfam15921 162 edMLEDSNTQIEQLRKMMLSHEGvlqeirsilvDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIf 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 533 TTRTQMEMLTKDKADKDE--------QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEIN-QTRDRLAKLNKELAS 603
Cdd:pfam15921 242 PVEDQLEALKSESQNKIElllqqhqdRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQeQARNQNSMYMRQLSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 604 SEQNKNHINNELKrkeEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEKSSKQRAMlagatavYSQFITQLTDEnqsccpv 683
Cdd:pfam15921 322 LESTVSQLRSELR---EAKRMYEDKI------EELEKQLVLANSELTEARTERDQ-------FSQESGNLDDQ------- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 684 cqrvfqteaeLQEVISDLQSKlrlapDKLKSTESELKKKEKRRDemlglvpMRQSIIdlkekeIPELRNKLQNVNRDIQR 763
Cdd:pfam15921 379 ----------LQKLLADLHKR-----EKELSLEKEQNKRLWDRD-------TGNSIT------IDHLRRELDDRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 764 L-------KNDIEEQ-ETLLGTIMPEEESakvcLTDVTIMERFQMELKDVERKIAQQ--AAKLQGIDLDRTVQQVNQEKQ 833
Cdd:pfam15921 431 LeallkamKSECQGQmERQMAAIQGKNES----LEKVSSLTAQLESTKEMLRKVVEEltAKKMTLESSERTVSDLTASLQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 834 EKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSE-------KLQISTNLQ----RRQQLEEQT----------- 891
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqtecealKLQMAEKDKvieiLRQQIENMTqlvgqhgrtag 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 892 ------VELSTEVQSLYREIKDAK-------EQVSPLETTLEKFQQEKEELINKKNTSNKiaqdKLNDIKEKVKNIHGYM 958
Cdd:pfam15921 587 amqvekAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLR----AVKDIKQERDQLLNEV 662
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 19924129 959 KDIENYIQDGKDDYK----------KQKETELNKVIAQLSECEKHKEKINEDMRLM 1004
Cdd:pfam15921 663 KTSRNELNSLSEDYEvlkrnfrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
402-1084 |
1.29e-09 |
|
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: 62.82 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 402 ERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLG---RIIELKSEILSKKQNELKNVKYELQQ-LEGSSDRILEL 477
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEeIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 478 DQ-----ELIKaERELSKAEKNSNVETLKMEVislQNEKADLDRTLRKLDQEMEQLNHHTTTrTQMEMLTKDKADKdEQI 552
Cdd:pfam05483 151 NAtrhlcNLLK-ETCARSAEKTKKYEYEREET---RQVYMDLNNNIEKMILAFEELRVQAEN-ARLEMHFKLKEDH-EKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 553 RKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTRDrlakLNKELASSEQNKNHINNELKRKEEQLSSYEDKlfdv 632
Cdd:pfam05483 225 QHLEEEYKKEIND------KEKQVSLLLIQITEKENKMKD----LTFLLEESRDKANQLEEKTKLQDENLKELIEK---- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 633 cgSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCP-----------VCQRVFQTEAELQEVISDL 701
Cdd:pfam05483 291 --KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnkakaahsfVVTEFEATTCSLEELLRTE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 702 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQsiIDLKE-KEIPELRNKLQNVNRDIQRLKNDIEEQET----LLG 776
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE--VELEElKKILAEDEKLLDEKKQFEKIAEELKGKEQelifLLQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 777 TIMPEEESAKVCLTDVTIMERFQM-ELKDVERKIAQQaaKLQGIDLDRTVQQVNQEkqekqhkldtvsskielNRKLIQD 855
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYLkEVEDLKTELEKE--KLKNIELTAHCDKLLLE-----------------NKELTQE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 856 QQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNT 935
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 936 SNKIAQDKLNDIKEKVKNIHgymKDIENYIQDGKDDYKK--QKETELN----KVIAQLSECEKHKEKINEDMRLMRQDID 1009
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKN---KNIEELHQENKALKKKgsAENKQLNayeiKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19924129 1010 TQKIQERWLQDNLtlrKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEE 1084
Cdd:pfam05483 665 DKKISEEKLLEEV---EKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
170-679 |
1.80e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 170 KALKQKFDEIFSAT-----RYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSY 244
Cdd:COG4717 49 ERLEKEADELFKPQgrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 245 E--NELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKL 322
Cdd:COG4717 129 PlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 323 VDCHRELEKLNKESRLLNQEksellVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSerqiknfhklVRE 402
Cdd:COG4717 209 AELEEELEEAQEELEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS----------LIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 403 RQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELK-NVKYELQQLEGSSDRILELDQEL 481
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 482 IKAERELSKAEKNSNVETLKmevISLQNEKADLDRTLRKLDQEMEQLnhhtttrtqmEMLTKDKADKDEQIRkiksRHSD 561
Cdd:COG4717 354 REAEELEEELQLEELEQEIA---ALLAEAGVEDEEELRAALEQAEEY----------QELKEELEELEEQLE----ELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 562 ELTSLLGYFpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASseqnknhINNELKRKEEQlSSYEDKlfdvcgsqdfESD 641
Cdd:COG4717 417 ELEELLEAL-DEEELEEELEELEEELEELEEELEELREELAE-------LEAELEQLEED-GELAEL----------LQE 477
|
490 500 510
....*....|....*....|....*....|....*...
gi 19924129 642 LDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQS 679
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
427-969 |
2.07e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.23 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 427 KQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSN---------- 496
Cdd:PRK01156 204 KQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNyykeleerhm 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 497 ----------------VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHS 560
Cdd:PRK01156 284 kiindpvyknrnyindYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 561 DeltsLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLfdvcgsqdfES 640
Cdd:PRK01156 364 D----YNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSL---------NQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 641 DLDRLKEEIEKSSKQRAMLAGatavysqfitqltdenQSCCPVCQRVFQTEaELQEVISDLQSKLRLAPDKLKSTESELK 720
Cdd:PRK01156 431 RIRALRENLDELSRNMEMLNG----------------QSVCPVCGTTLGEE-KSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 721 K-KEKRRDemlgLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKND---IEEQETLLGTIMPEEESAKV--------- 787
Cdd:PRK01156 494 DiDEKIVD----LKKRKEYLESEEINKSINEYNKIESARADLEDIKIKineLKDKHDKYEEIKNRYKSLKLedldskrts 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 788 -----CLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDrtVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQH 862
Cdd:PRK01156 570 wlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIG--FPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 863 LKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELinkkntsnkiaQD 942
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL-----------SD 716
|
570 580
....*....|....*....|....*..
gi 19924129 943 KLNDIKEKVKNihgyMKDIENYIQDGK 969
Cdd:PRK01156 717 RINDINETLES----MKKIKKAIGDLK 739
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1202-1275 |
5.79e-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: 5.79e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1275
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYFLD 131
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
749-1111 |
9.22e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 749 ELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtimERFQmELKDVERKIAQQAAKLQGIDLDRTVQQV 828
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----------ERYK-ELKAELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 829 NQEKQEKQHK-------LDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQ----RRQQLEEQTVELSTE 897
Cdd:TIGR02168 245 QEELKEAEEEleeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 898 VQSLYREIKDAKEQVSPLETTLEKFQQEKEELinkkntsnkiaQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYkKQKE 977
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESL-----------EAELEELEAELEELESRLEELEEQLETLRSKV-AQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 978 TELNKVIAQLSECEKHKEkinedmrlmrqdiDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEH 1057
Cdd:TIGR02168 393 LQIASLNNEIERLEARLE-------------RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 19924129 1058 QKLEENIDNIKRNHNLALgRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVM 1111
Cdd:TIGR02168 460 EEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
313-929 |
1.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 313 RTVREKERKlvdchRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFErgpfSERQ 392
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE----LEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 393 IKNFHKLVRE--RQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGS 470
Cdd:COG1196 287 QAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 471 SDRILELDQELIKAERELSKAEknsnvETLKMEVISLQNEKADLDRTLRKLDQEMEQLnhhtttRTQMEMLTKDKADKDE 550
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEEL-----LEALRAAAELAAQLEELEEAEEALLERLERL------EEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 551 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLf 630
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 631 dvcGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQfitqltdenqsccpvcQRVFQTEAELQEVISDLQSKlRLAPD 710
Cdd:COG1196 515 ---LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ----------------NIVVEDDEVAAAAIEYLKAA-KAGRA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 711 KLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTImpeEESAKVCLT 790
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL---AGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 791 DVTIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQhlksttnel 870
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE--------- 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 19924129 871 kseklqistNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEEL 929
Cdd:COG1196 723 ---------EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1201-1273 |
1.20e-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: 1.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19924129 1201 CSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAhalvEIIKSRSQQRNfQLLVITHDEDF 1273
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG----ELIRELAAQGK-AVIVITHDYEF 188
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
695-937 |
1.21e-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: 58.62 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 695 QEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETL 774
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 775 LGTImpEEESAKVcltdvtIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQ 854
Cdd:COG4942 99 LEAQ--KEELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 855 DQQEQIQHLKsttNELKSEKLQISTNLQRRQQLEEQtveLSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKN 934
Cdd:COG4942 171 AERAELEALL---AELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 19924129 935 TSN 937
Cdd:COG4942 245 AAG 247
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1202-1291 |
2.59e-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: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIEslahALVEIIKsRSQQRNFQLLVITHDEDFVEllgrsE 1281
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDPAGRR----ELLELLK-KLKAEGKTIIIVTHDLDLLL-----E 199
|
90
....*....|
gi 19924129 1282 YVEKFYRIKK 1291
Cdd:cd03225 200 LADRVIVLED 209
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
262-840 |
4.29e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 262 LSKIMK-LDNEIKALDSR----KKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKES 336
Cdd:pfam15921 222 ISKILReLDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 337 RLLNQEKS-------------ELLVEQGRLQLqadrhQEHIRARDSLIQSLATQLELDG-------FERGPFS------- 389
Cdd:pfam15921 302 EIIQEQARnqnsmymrqlsdlESTVSQLRSEL-----REAKRMYEDKIEELEKQLVLANseltearTERDQFSqesgnld 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 390 ---ERQIKNFHKLVRE-------------RQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKK 453
Cdd:pfam15921 377 dqlQKLLADLHKREKElslekeqnkrlwdRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 454 QNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSN--VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHH 531
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 532 TT-------TRTQMEMLTKDKADKDEQIrKIKSRHSDELTSLLGYFP--------NKKQLEdwlhsksKEINQTRDRLak 596
Cdd:pfam15921 537 KNegdhlrnVQTECEALKLQMAEKDKVI-EILRQQIENMTQLVGQHGrtagamqvEKAQLE-------KEINDRRLEL-- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 597 lnKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVcGSQ------DFESDLDRLKEEIEKSSKQramlagatavysqfI 670
Cdd:pfam15921 607 --QEFKILKDKKDAKIRELEARVSDLELEKVKLVNA-GSErlravkDIKQERDQLLNEVKTSRNE--------------L 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 671 TQLTDENQsccpVCQRVFQTEAELQEVISD-LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPE 749
Cdd:pfam15921 670 NSLSEDYE----VLKRNFRNKSEEMETTTNkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDA 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 750 LRNKLQ-------NVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGIDLD 822
Cdd:pfam15921 746 LQSKIQfleeamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER-RLKEKVANMEVALDKASLQFAECQ 824
|
650 660
....*....|....*....|
gi 19924129 823 RTVQQVNQE--KQEKQHKLD 840
Cdd:pfam15921 825 DIIQRQEQEsvRLKLQHTLD 844
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
752-1084 |
4.52e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 752 NKLQNVNRDIQRLKNDIEEQETLLGTImpEEESAKVcltdvtimERFQmELKDVERKIAQQAAKLQGIDLDRTVQQVNQE 831
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPL--ERQAEKA--------ERYR-ELKEELKELEAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 832 KQEKQHK-------LDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNL----QRRQQLEEQTVELSTEVQS 900
Cdd:COG1196 248 LEELEAEleeleaeLAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarleERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 901 LYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDgKDDYKKQKETEL 980
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 981 NKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEmgqmQVLQMKSEHQKL 1060
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE----EAALLEAALAEL 482
|
330 340
....*....|....*....|....
gi 19924129 1061 EENIDNIKRNHNLALGRQKGYEEE 1084
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGF 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
689-914 |
6.91e-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: 56.31 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 689 QTEAELQEV---ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLK 765
Cdd:COG4942 24 EAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 766 NDIEEQETLLGTiMPEEESAKVCL--TDVTIMERFQMELKDVERKIAQQAAKLQGI--DLDRTVQQVNQEKQEKQHKLDT 841
Cdd:COG4942 104 EELAELLRALYR-LGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADlaELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19924129 842 VSSKIELNRKLIQDQQEQIQHLKSTTNELKseklqistnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSP 914
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELA----------AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-598 |
7.71e-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: 56.99 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 263 SKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVfQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQE 342
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 343 KSELLVEQGRLQLQ-ADRHQEHIRARDSLIQSLATQLELDGfergpfSERQIKNFHKLVRERQEGEAKTANQLMNDFAEK 421
Cdd:TIGR02168 749 IAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEA------QIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 422 ETLKQKQIDEIRDKKTGLGRIIELKSEIlskkqnelknvkyeLQQLEGSSDRILELDQELIKAEREL-----SKAEKNSN 496
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEEL--------------SEDIESLAAEIEELEELIEELESELeallnERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 497 VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHtttRTQMEM-LTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQ 575
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
330 340
....*....|....*....|...
gi 19924129 576 LEDWLHSKSKEINQTRDRLAKLN 598
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKELGPVN 988
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-98 |
1.01e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.86 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 3 RIEKMSILGVRSFgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTK-GNTFVHDPkvaqetDVRAQ 81
Cdd:COG0419 1 KLLRLRLENFRSY----RDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKlRSDLINVG------SEEAS 70
|
90
....*....|....*..
gi 19924129 82 IRLQFrDVNGELIAVQR 98
Cdd:COG0419 71 VELEF-EHGGKRYRIER 86
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
447-1040 |
1.42e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 447 SEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSkaEKNSNVETLKMEVISLQNEKADLDrtlrKLDQEME 526
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN--EISSELPELREELEKLEKEVKELE----ELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 527 QLnhhtttRTQMEMLTKDKADKDEQIRKIKSR------HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE 600
Cdd:PRK03918 242 EL------EKELESLEGSKRKLEEKIRELEERieelkkEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 601 LASSEQnknhinnELKRKEEQLSSYEDKlfdvcgsqdfESDLDRLKEEIEKSSKQRAMLAGATAVYsqfitqltdenqsc 680
Cdd:PRK03918 316 LSRLEE-------EINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELY-------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 681 cpvcQRVFQTEAELQEVisdlqsKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrqsiidlkEKEIPELRNKLQNVNRD 760
Cdd:PRK03918 365 ----EEAKAKKEELERL------KKRLTGLTPEKLEKELEELEKAKEEI--------------EEEISKITARIGELKKE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 761 IQRLKNDIEEQET------LLGTIMPEEESAKvcltdvtIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQE 834
Cdd:PRK03918 421 IKELKKAIEELKKakgkcpVCGRELTEEHRKE-------LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 835 KQHKLDTVSSKIE--------LNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIK 906
Cdd:PRK03918 494 ELIKLKELAEQLKeleeklkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 907 DAKEQVSPL----ETTLEKFQQEKEELINKKNTSnKIAQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKEtELNK 982
Cdd:PRK03918 574 ELLKELEELgfesVEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-ELEE 651
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19924129 983 VIAQLSEcEKHKEKINEDMRLMRQ--DIDTQKIQERWLQDNL--TLRKRNEELKEVEEERKQ 1040
Cdd:PRK03918 652 LEKKYSE-EEYEELREEYLELSRElaGLRAELEELEKRREEIkkTLEKLKEELEEREKAKKE 712
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
25-744 |
2.08e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 25 ITFFSPLTILVGPNGAGKTTIIECLKYICTGDfppgtKGNTFVHDpkVAQETDVRAQIRLQFRdVNGELIAVQRSMVCTQ 104
Cdd:PRK01156 19 IEFDTGINIITGKNGAGKSSIVDAIRFALFTD-----KRTEKIED--MIKKGKNNLEVELEFR-IGGHVYQIRRSIERRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 105 KSKKTEFKTLegvitrtKHGEKVSLSSKCAEIDREMiSSLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQK-FDEIFSAT 183
Cdd:PRK01156 91 KGSRREAYIK-------KDGSIIAEGFDDTTKYIEK-NILGISKDVFLNSIFVGQGEMDSLISGDPAQRKKiLDEILEIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 184 RYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLS 263
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 264 KIMKLDNEIKALDSRKKQMEKDNSELEEKMEKvFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEK 343
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 344 SELLVEQGRLQ-LQADRHQEHIRAR--DSLIQSLatqLELDGFERGPFSE-RQIKNFHKLVRE----RQEGEAKTANQLM 415
Cdd:PRK01156 322 NKYHAIIKKLSvLQKDYNDYIKKKSryDDLNNQI---LELEGYEMDYNSYlKSIESLKKKIEEysknIERMSAFISEILK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 416 NDFAEKETLKqKQIDEIRDKKTGL-GRIIELKSEILSKKQNELKnVKYELQQLEGSS-------DRILELDQELIKAERE 487
Cdd:PRK01156 399 IQEIDPDAIK-KELNEINVKLQDIsSKVSSLNQRIRALRENLDE-LSRNMEMLNGQSvcpvcgtTLGEEKSNHIINHYNE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 488 lSKAEKNSNVETLKMEVISLQNEKADLDRTLRKL-----------DQEMEQLNHHTTTRTQMEMLTKDKADKDEQIR-KI 555
Cdd:PRK01156 477 -KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeseeinksineYNKIESARADLEDIKIKINELKDKHDKYEEIKnRY 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 556 KSRHSDEL----TSLLGYFPNKKQLE-DWLHSKSKEIN-QTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKL 629
Cdd:PRK01156 556 KSLKLEDLdskrTSWLNALAVISLIDiETNRSRSNEIKkQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKY 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 630 FDVcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEVISDlQSKLRLAP 709
Cdd:PRK01156 636 NEI---QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIE-------DNLKKSRKALDDAKAN-RARLESTI 704
|
730 740 750
....*....|....*....|....*....|....*.
gi 19924129 710 DKLKSTESELKKKEKRRDEML-GLVPMRQSIIDLKE 744
Cdd:PRK01156 705 EILRTRINELSDRINDINETLeSMKKIKKAIGDLKR 740
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
238-964 |
2.45e-07 |
|
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: 55.41 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 238 KEIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQrtvre 317
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIK---NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKD----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 318 kerKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLEL------DGFERGPFSER 391
Cdd:TIGR04523 97 ---KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnnkynDLKKQKEELEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 392 QIKNFHKLVRERQEGEAKTANQLMND---------FAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKY 462
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 463 ELQQLEGSSDRILEldqELIKAERELSKA-----EKNSNVETLKMEVISLQNEK-ADLDRTLRklDQEMEQLNHHTTTRT 536
Cdd:TIGR04523 254 QLNQLKDEQNKIKK---QLSEKQKELEQNnkkikELEKQLNQLKSEISDLNNQKeQDWNKELK--SELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 537 QMEMLTKDKADKDEQIRKIKSrhsdeltsllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELK 616
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK--------------ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 617 RKEEQLSSYEDKlfdvcgSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE 696
Cdd:TIGR04523 395 DLESKIQNQEKL------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 697 VISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpmRQSIIDLKEKeIPELRNKLQNVNRDIQRLKNDIEEQETLLG 776
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKL------NEEKKELEEK-VKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 777 TIMPEEESAKVCLTdvtimerfQMELKDVERKIAQQAAKLQ--GIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQ 854
Cdd:TIGR04523 542 DLEDELNKDDFELK--------KENLEKEIDEKNKEIEELKqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 855 DQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQS----LYREIKDAKEQVSPLETTLEKFQQEKEeLI 930
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNkwpeIIKKIKESKTKIDDIIELMKDWLKELS-LH 692
|
730 740 750
....*....|....*....|....*....|....
gi 19924129 931 NKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENY 964
Cdd:TIGR04523 693 YKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEF 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
426-861 |
3.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 426 QKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQ----LEGSSDRILELDQELIKAERELSKAEKNSNVETLK 501
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqeeLEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 502 MEVISLQNEKADLDRTLRKLDQEMEQLNHhttTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWlh 581
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEEL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 582 skSKEINQTRDRLAKLNKELASSEQNKNHINNEL--KRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAML 659
Cdd:COG4717 205 --QQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 660 AGATAVYSQFITQLTDENQSCCPVCQRVFQ----TEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLvpM 735
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL--E 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 736 RQSIIDLKEKEIPELRNKLQNVNRD-----------IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQ----- 799
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEelraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEeleee 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 800 -----MELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVS---SKIELNRKLIQDQQEQIQ 861
Cdd:COG4717 441 leeleEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAeewAALKLALELLEEAREEYR 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
401-745 |
3.16e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 401 RERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGssdRILELDQE 480
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 481 LIKAERELSKAEKNSNVETLKmeviSLQNEKADLDRTLRKLDQEMEQLNhhtttrtqmemltkdkadkdeqiRKIKSRHs 560
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIP----EIQAELSKLEEEVSRIEARLREIE-----------------------QKLNRLT- 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 561 deltsllgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQD--- 637
Cdd:TIGR02169 826 ----------LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDele 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 638 -----FESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTD------ENQSCCPVCQRVFQTEAELQEVISDLQSKLR 706
Cdd:TIGR02169 896 aqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
|
330 340 350
....*....|....*....|....*....|....*....
gi 19924129 707 LAPDKLKSTESELKKKEKRRDEmlgLVPMRQSIIDLKEK 745
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAK---LEEERKAILERIEE 1011
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
487-1272 |
3.79e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 487 ELSKAEKNSNVetLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSL 566
Cdd:PRK01156 160 EINSLERNYDK--LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 567 LGYFPNKKQLEDWLHSKSKEINQTRDRLA----KLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVcgsQDFESDL 642
Cdd:PRK01156 238 KSALNELSSLEDMKNRYESEIKTAESDLSmeleKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDI---ENKKQIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 643 DRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKK 722
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDD--------LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 723 EKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDI------EEQETLLGTIMPEEESAKVCLTDV---- 792
Cdd:PRK01156 387 ERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIralrenLDELSRNMEMLNGQSVCPVCGTTLgeek 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 793 --TIMERFQMELKDVERKIAQqaaklqgidLDRTVQQVNQEKQEKQHKLDTVSSKiELNRKLIQDQQeqiqhLKSTTNEL 870
Cdd:PRK01156 467 snHIINHYNEKKSRLEEKIRE---------IEIEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNK-----IESARADL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 871 KSEKLQISTNLQRRQQLEEqtveLSTEVQSLYREIKDAKEQvSPLETTLEKFQQEKEELINKKNTSNKiaqdKLNDIKEK 950
Cdd:PRK01156 532 EDIKIKINELKDKHDKYEE----IKNRYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKK----QLNDLESR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 951 VKNIHGYMKDIENYIqdgkDDYKKQKETELNKVIAQLSECEKHKEKINEdmrlMRQDIDTQKIQerwlqdnltlrkrnee 1030
Cdd:PRK01156 603 LQEIEIGFPDDKSYI----DKSIREIENEANNLNNKYNEIQENKILIEK----LRGKIDNYKKQ---------------- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1031 lKEVEEERKQHLKEMgQMQVLQMKSEHQKLEENIDNIKRNHnlalgrqkgYEEEIIHFKKELREPQFRDAEEKYREMMIV 1110
Cdd:PRK01156 659 -IAEIDSIIPDLKEI-TSRINDIEDNLKKSRKALDDAKANR---------ARLESTIEILRTRINELSDRINDINETLES 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1111 MRTTELVNKDLDIYYKTLDQAIMKfhSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSAsdkrrnynYRVVMLK 1190
Cdd:PRK01156 728 MKKIKKAIGDLKRLREAFDKSGVP--AMIRKSASQAMTSLTRKYLFEFNLDFDDIDVDQDFNITV--------SRGGMVE 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1191 GDTALdmrgrcSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRnfQLLVITHD 1270
Cdd:PRK01156 798 GIDSL------SGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIP--QVIMISHH 869
|
..
gi 19924129 1271 ED 1272
Cdd:PRK01156 870 RE 871
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
211-770 |
4.64e-07 |
|
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: 54.26 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 211 KYLKQYKEKACEIRDQITSKEAQLTSS-------KEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQME 283
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLnnkyndlKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 284 KDNSELEEKMEKvFQGTDEQLNDlyhnhqrTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEH 363
Cdd:TIGR04523 211 QKNKSLESQISE-LKKQNNQLKD-------NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 364 IRARDSLIQSLATQLELDGFERgpfSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQkQIDEIRDKKTGLGRII 443
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQK---EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE-QISQLKKELTNSESEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 444 ELKSEILSKKQNELKNVKYE----LQQLEGSSDRILELDQELIKAERElsKAEKNSNVETLKMEVISLQNEKADLDRTLR 519
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKEnqsyKQEIKNLESQINDLESKIQNQEKL--NQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 520 KLDQEMEQL-NHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN 598
Cdd:TIGR04523 437 KNNSEIKDLtNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 599 KELASSEQNKNHINNELKRKEEQLSSYEDKLFdvcgSQDFESDLDRLKEEIEKSSKQRAMLagatavySQFITQLTDENQ 678
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELN----KDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 679 SccpVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKE---KEIPELRNKLQ 755
Cdd:TIGR04523 586 E---KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKqikETIKEIRNKWP 662
|
570
....*....|....*
gi 19924129 756 NVNRDIQRLKNDIEE 770
Cdd:TIGR04523 663 EIIKKIKESKTKIDD 677
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
446-1102 |
5.54e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 446 KSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEM 525
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 526 EQLNH--------HTTTRTQMEMLTKDKAdKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKL 597
Cdd:TIGR00618 300 KAVTQieqqaqriHTELQSKMRSRAKLLM-KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-HEVATSIREISCQQHTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 598 NKELASSEQNKNHinneLKRKEEQLSSYEDKLFDVCGSQDFES--------DLDRLKEEIEKSSKQRAMLAGATAVYSQF 669
Cdd:TIGR00618 378 TQHIHTLQQQKTT----LTQKLQSLCKELDILQREQATIDTRTsafrdlqgQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 670 IT----------QLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSI 739
Cdd:TIGR00618 454 EKlekihlqesaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 740 ID---LKEKEIPELRNKLQNVNRDIQRLKNDIEE--QETLLGTIMPEEESAkvcltdvtIMERFQMELKDVERKIAQQAA 814
Cdd:TIGR00618 534 EQtyaQLETSEEDVYHQLTSERKQRASLKEQMQEiqQSFSILTQCDNRSKE--------DIPNLQNITVRLQDLTEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 815 KLQGIDLDRTVQQVnqEKQEKQHKLDtvssKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEeqtveL 894
Cdd:TIGR00618 606 AEDMLACEQHALLR--KLQPEQDLQD----VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE-----L 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 895 STEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDgkddYKK 974
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE----LMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 975 QKETELnkviaQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLtLRKRNEELKEVEEERKQHLKEMGQMQVLQMK 1054
Cdd:TIGR00618 751 QARTVL-----KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL-REEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 19924129 1055 SEHQKLEENIDNIKRNHNL--ALGRQKGYEEEIIHFKKELREPQFRDAEE 1102
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-960 |
7.04e-07 |
|
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: 53.87 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 227 ITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLskiMKLDNEIKALDSRKKQMEKDNSELEEKMEKvfqgtdeqlnd 306
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNL---NKDEEKINNSNNKIKILEQQIKDLNDKLKK----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 307 lyhnhqrtvreKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLEL------ 380
Cdd:TIGR04523 94 -----------NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnnkyn 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 381 DGFERGPFSERQIKNFHKLVRERQEGEAKTANQLMND---------FAEKETLKQKQIDEIRDKKTGLGRIIELKSEILS 451
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 452 KKQNELKNVKYELQQLEGSSDRILEldqELIKAERELSKA-----EKNSNVETLKMEVISLQNEK-ADLDRTLRklDQEM 525
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKK---QLSEKQKELEQNnkkikELEKQLNQLKSEISDLNNQKeQDWNKELK--SELK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 526 EQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSrhsdeltsllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSE 605
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKK--------------ELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 606 QNKNHINNELKRKEEQLSSYEDKlfdvcgSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 685
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKL------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 686 RVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglvpmrqsiidlkEKEIPELRNKLQNVNRDIQRLK 765
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--------------NEEKKELEEKVKDLTKKISSLK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 766 NDIEEQETllgtimpeeesakvcltdvtimerfqmELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLdtvsSK 845
Cdd:TIGR04523 524 EKIEKLES---------------------------EKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI----EE 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 846 IELNRKLIQDQQEQIQHL-KSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQ 924
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELiDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
730 740 750
....*....|....*....|....*....|....*.
gi 19924129 925 EKEELINKKNTSNKiaqdKLNDIKEKVKNIHGYMKD 960
Cdd:TIGR04523 653 TIKEIRNKWPEIIK----KIKESKTKIDDIIELMKD 684
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1192-1275 |
8.63e-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: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1192 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITHD 1270
Cdd:COG4988 464 DTPLGEGGRGlSGGQAQ------RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT------VILITHR 531
|
....*
gi 19924129 1271 EDFVE 1275
Cdd:COG4988 532 LALLA 536
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
208-779 |
1.53e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 208 MELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSY--ENELDPLKNRLKEIEhnlSKIMKLDNEIKALDSRKKQMEKD 285
Cdd:PRK02224 159 LQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQieEKEEKDLHERLNGLE---SELAELDEEIERYEEQREQARET 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 286 NSELEEKMEKvFQGTDEQLNDLyhnhQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIR 365
Cdd:PRK02224 236 RDEADEVLEE-HEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 366 ARDSLIQSLATQLELdgfergpfserqiknfhklVRERQEgEAKTANQLMNDFAEKETLKQKQID----EIRDKKTGLGR 441
Cdd:PRK02224 311 AVEARREELEDRDEE-------------------LRDRLE-ECRVAAQAHNEEAESLREDADDLEeraeELREEAAELES 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 442 IIELKSEILSKKQNELKNVKYELQQLEGSSDRIlELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKL 521
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDA-PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 522 D--------QEMEQLNHHTTT---RTQMEMLTKDKADKDEQIRKIKSRH---------SDELTSLLgyfPNKKQLEDWLH 581
Cdd:PRK02224 450 EagkcpecgQPVEGSPHVETIeedRERVEELEAELEDLEEEVEEVEERLeraedlveaEDRIERLE---ERREDLEELIA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 582 SKSKEINQTRDRLAKLNK---ELASSEQNKNhinnelKRKEEQLSSYEDKLFDVcgsQDFESDLDRLKEEIEKSSKQRAM 658
Cdd:PRK02224 527 ERRETIEEKRERAEELREraaELEAEAEEKR------EAAAEAEEEAEEAREEV---AELNSKLAELKERIESLERIRTL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 659 LAgATAVYSQFITQLTDENQSCCPV-----------CQRVFQTEAELQEV-ISDLQSKLRLAPDKLKSTESELKKKEKRR 726
Cdd:PRK02224 598 LA-AIADAEDEIERLREKREALAELnderrerlaekRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 19924129 727 DEMLGLVPMRQSIIdlkeKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIM 779
Cdd:PRK02224 677 DDLQAEIGAVENEL----EELEELRERREALENRVEALEALYDEAEELESMYG 725
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1192-1279 |
2.98e-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: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1192 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDREniesLAHALVEIIKSRSQQRNfqLLVITHD 1270
Cdd:TIGR02857 449 DTPIGEGGAgLSGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAE----TEAEVLEALRALAQGRT--VLLVTHR 516
|
....*....
gi 19924129 1271 EDFVELLGR 1279
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 ... |
1177-1251 |
3.43e-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: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1177 DKRRNYNYRVVMLKGDTA----LDMRGRCSAGQK-VLASLIIRLALAETFCLN------CGIIALDEPTTNLDRENIESL 1245
Cdd:pfam13558 5 DYRNWLSFEVEVRDEDGSevetYRRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTA 84
|
....*.
gi 19924129 1246 AHALVE 1251
Cdd:pfam13558 85 LELLRA 90
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-1001 |
3.87e-06 |
|
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: 51.51 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 4 IEKMSILGVRSFGiedkdKQIITFFSP-LTILVGPNGAGKTTIIECLKY---ICTGDFPPGTKGNTFVHdpKVAQETDVR 79
Cdd:pfam02463 2 LKRIEIEGFKSYA-----KTVILPFSPgFTAIVGPNGSGKSNILDAILFvlgERSAKSLRSERLSDLIH--SKSGAFVNS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 80 AQIRLQFRDVNGEL------IAVQRSMVctqKSKKTEFKTlegvitrtkHGEKVSLSSKcaeidREMISSLGVSKAVLNN 153
Cdd:pfam02463 75 AEVEITFDNEDHELpidkeeVSIRRRVY---RGGDSEYYI---------NGKNVTKKEV-----AELLESQGISPEAYNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 154 VIFCHQEDsNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKE----YQMELKYLKQYKEKACEIRDQITS 229
Cdd:pfam02463 138 LVQGGKIE-IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELiidlEELKLQELKLKEQAKKALEYYQLK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 230 KEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYH 309
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 310 NHQRTVREKERKLVDCHRELEKLNKESRL----LNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGF-- 383
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKaekeLKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEll 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 384 ------ERGPFSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNEL 457
Cdd:pfam02463 377 akkkleSERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 458 KNVKYELQQLEGSSDRILELDQEL-------------IKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQE 524
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVklqeqlelllsrqKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 525 MEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASS 604
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 605 EQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESDLDRL---KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 681
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGlaeKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 682 PVCQRVFQTEAELQEVISDLQSKLRLAPDKL-----KSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQN 756
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVqeaqdKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 757 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQ 836
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 837 HKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLE 916
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 917 TTLEKFQQEKE---ELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETElNKVIAQLSECEKH 993
Cdd:pfam02463 937 PEELLLEEADEkekEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE-EKKKLIRAIIEET 1015
|
....*...
gi 19924129 994 KEKINEDM 1001
Cdd:pfam02463 1016 CQRLKEFL 1023
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1199-1275 |
4.08e-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: 4.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1199 GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIEslahALVEIIKSRSQQRnfQLLVI-THDEDFVE 1275
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGVA----LLAELIAAHLARG--GAVLLtTHQPLELA 195
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-1000 |
4.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 219 KACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDneikalDSRKKQMEKDNSELEEKMEKVFQ 298
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE------EAKKDAEEAKKAEEERNNEEIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 299 GTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSEllVEQGRLQLQADRHQEHIRARDSLIQSLATQL 378
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 379 ELDGFERGPFSERQIKNFHKLVRERQEGEAKTanqlmnDFAEKETLKQKQIDEIRDKKTGLGRiielKSEILSKKQNELK 458
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA------EAAEKKKEEAKKKADAAKKKAEEKK----KADEAKKKAEEDK 1404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 459 NVKYELQQLEGSSDRILELD---QELIKAERELSKAEKNSNVETLKmevislqnEKADLDRTLRKLDQEMEQLNHHTTTR 535
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAK--------KKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 536 TQMEmlTKDKADKDEQIRKIKSRHSDELtsllgyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASSEQNKnhinNEL 615
Cdd:PTZ00121 1477 KKAE--EAKKADEAKKKAEEAKKKADEA------------------KKAAEAKKKADEAKKAEEAKKADEAKK----AEE 1532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 616 KRKEEQLSSYEDKLfdvcgsqdfESDLDRLKEEIEKSSKQRAMlagatavySQFITQLTDENQSCCPVCQRVFQTEAELQ 695
Cdd:PTZ00121 1533 AKKADEAKKAEEKK---------KADELKKAEELKKAEEKKKA--------EEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 696 EVISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQET 773
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 774 LLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIdldRTVQQVNQEKQEKQHKLDTVSSKIELNRKLI 853
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL---KKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 854 QDQQEQIQHLKStTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKD--------AKEQVSPLETTLEKFQQE 925
Cdd:PTZ00121 1753 EEEKKKIAHLKK-EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDnfaniiegGKEGNLVINDSKEMEDSA 1831
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19924129 926 KEELINKKNTsnkiaqdKLNDIKEKVKniHGYMKDIENYiQDGKDDYKKQKETELNKVIAQLSECEKHKEKINED 1000
Cdd:PTZ00121 1832 IKEVADSKNM-------QLEEADAFEK--HKFNKNNENG-EDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKD 1896
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
449-1068 |
6.01e-06 |
|
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: 50.79 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 449 ILSKKQNELKNVKYELQ----QLEGSSDRILELDQELIKaeRELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQE 524
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKtiknELKNKEKELKNLDKNLNK--DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 525 MEQLNHHTTTRTQMEMLTKDKADK-DEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELAS 603
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKlEKQKKENKKNIDKFLTEI-------KKKEKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 604 SEQNKNHINNELKRKEEQLSSYEDKLFDVcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPV 683
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNL---KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 684 CQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELK---------KKEKRRDEMLGLvpmrQSIIDLKEKEIPELRNKL 754
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkseisdlNNQKEQDWNKEL----KSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 755 QNVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimerfqmelkdverkiaqqaaklqgIDLDRTVQQVNQEKQE 834
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSESENSEKQ--------------------------------RELEEKQNEIEKLKKE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 835 KQHKLDTV----SSKIELNRKlIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQ-----------LEEQTVELSTEVQ 899
Cdd:TIGR04523 379 NQSYKQEIknleSQINDLESK-IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnseikdLTNQDSVKELIIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 900 SLYREIKDAKEQVSPLE-------TTLEKFQQE---KEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDgK 969
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSrsinkikQNLEQKQKElksKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE-K 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 970 DDYKKQKETELNKVIAQL--SECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQ 1047
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
650 660
....*....|....*....|.
gi 19924129 1048 MQVLQMKSEHQKLEENIDNIK 1068
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIK 637
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-58 |
8.06e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.23 E-value: 8.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 3 RIEKMSILGVRsfGIEDKDkqiITF--FSPLTILVGPNGAGKTTIIECLKYICTGDFP 58
Cdd:COG3950 2 RIKSLTIENFR--GFEDLE---IDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLS 54
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-56 |
9.28e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 49.62 E-value: 9.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 19924129 3 RIEKMSILGVRSFGiedkdKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGD 56
Cdd:COG3593 2 KLEKIKIKNFRSIK-----DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
573-978 |
1.16e-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: 49.84 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 573 KKQLEDWLHSKSKEINQTRDRLaklNKELASSEQNKNHINNELKRKEEQLSSYED-KLFDVCGSQD----FESDLDRLKE 647
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDEL---NGELSAADAAVAKDRSELEALEDQHGAFLDaDIETAAADQEqlpsWQSELENLEE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 648 EIE-----KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRlapDKLKSTESELKKK 722
Cdd:pfam12128 362 RLKaltgkHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR---EQLEAGKLEFNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 723 EKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRdiqrlkndieEQETLlgtimpEEESAKVcltdvtimERFQMEL 802
Cdd:pfam12128 439 EYRLKSRLGELKLRLNQATATPELLLQLENFDERIER----------AREEQ------EAANAEV--------ERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 803 KDVERKIAQQAAKLQgiDLDRTVQQVNQEKQEKQHKLDTVS-SKIELNRKLIQDQQEQIQHLKST--------------- 866
Cdd:pfam12128 495 RQARKRRDQASEALR--QASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVISPellhrtdldpevwdg 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 867 --------------------------TNELKSEKLQISTNLQ----RRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLE 916
Cdd:pfam12128 573 svggelnlygvkldlkridvpewaasEEELRERLDKAEEALQsareKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19924129 917 TTLEKFQQEKEELINKKNTSNKIAQDKLNdikEKVKNIHGYMKDIENYIQDGKDDYKKQKET 978
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALAERKDSAN---ERLNSLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
814-1025 |
1.53e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 814 AKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKsttNELKSEKLQISTNlqrRQQLEEQTVE 893
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEA---EAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 894 LSTEVQSLYReikdAKEQVSPLETTLEkfQQEKEELINKKNTSNKIA---QDKLNDIKEKVKNIHGYMKDIENYIQDgKD 970
Cdd:COG3883 88 LGERARALYR----SGGSVSYLDVLLG--SESFSDFLDRLSALSKIAdadADLLEELKADKAELEAKKAELEAKLAE-LE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19924129 971 DYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLR 1025
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
214-1149 |
1.86e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 214 KQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKM 293
Cdd:TIGR01612 537 KLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKN 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 294 EKVfqgtdeqlndlyhnhqrtvrekeRKLVDCHRELEKlnkesrllNQEKSELLVEQGRLQLqadrhQEHIRARDSLIQS 373
Cdd:TIGR01612 617 EYI-----------------------KKAIDLKKIIEN--------NNAYIDELAKISPYQV-----PEHLKNKDKIYST 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 374 LATQLeldgfergpfSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKqIDEIRDKKTGL-GRIIELKSEILSK 452
Cdd:TIGR01612 661 IKSEL----------SKIYEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSK-IDKEYDKIQNMeTATVELHLSNIEN 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 453 KQNELKNVKYELQQLEGSsdrilELDQELIKAERELSKAEKNsnvetLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHT 532
Cdd:TIGR01612 730 KKNELLDIIVEIKKHIHG-----EINKDLNKILEDFKNKEKE-----LSNKINDYAKEKDELNKYKSKISEIKNHYNDQI 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 533 TTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKqlEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHIN 612
Cdd:TIGR01612 800 NIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMK--DDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIK 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 613 NELkrKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEKSskqramlagatavySQFITQLTDENQScCPVCQRVFQTEA 692
Cdd:TIGR01612 878 AEI--SDDKLNDYEKKF------NDSKSLINEINKSIEEE--------------YQNINTLKKVDEY-IKICENTKESIE 934
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 693 ELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLglvpmrQSIIDLKEKEIPELR-NKLQNVNRDIQRLKNDIEEQ 771
Cdd:TIGR01612 935 KFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTL------IDKINELDKAFKDASlNDYEAKNNELIKYFNDLKAN 1008
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 772 etlLGTimPEEEsakvcltdvTIMERFQMELK---DVERKIAQQAAKLQGIDLDRTVQQVN-QEKQEKQhkldtVSSKIE 847
Cdd:TIGR01612 1009 ---LGK--NKEN---------MLYHQFDEKEKatnDIEQKIEDANKNIPNIEIAIHTSIYNiIDEIEKE-----IGKNIE 1069
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 848 -LNRKLIQDQQEQIQHLksttNELKsEKLQIstnLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEK 926
Cdd:TIGR01612 1070 lLNKEILEEAEINITNF----NEIK-EKLKH---YNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKS 1141
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 927 EELINKKntsnKIAQDKLNDIKEKV---KNIHGYMKDIENYIQdgKDDYKKQKETELNKVIAQLSECEKHKEKINEDM-- 1001
Cdd:TIGR01612 1142 ENYIDEI----KAQINDLEDVADKAisnDDPEEIEKKIENIVT--KIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKgi 1215
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1002 ---------RLMRQDIDTQKIQ--------ERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSE-----HQK 1059
Cdd:TIGR01612 1216 nlsygknlgKLFLEKIDEEKKKsehmikamEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKdhhiiSKK 1295
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1060 LEENIDNIkRNHNLALGRQKGYEEEIIHFKKELREpQFRDAEEKYREMMIVM-RTTELVN-KDLDIYYKTLDQaiMKFHS 1137
Cdd:TIGR01612 1296 HDENISDI-REKSLKIIEDFSEESDINDIKKELQK-NLLDAQKHNSDINLYLnEIANIYNiLKLNKIKKIIDE--VKEYT 1371
|
970
....*....|..
gi 19924129 1138 MKMEEINKIIRD 1149
Cdd:TIGR01612 1372 KEIEENNKNIKD 1383
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1227-1280 |
1.91e-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: 1.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 19924129 1227 IIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRS 1280
Cdd:cd03255 161 IILADEPTGNLDSET----GKEVMELLRELNKEAGTTIVVVTHDPELAEYADRI 210
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
186-649 |
1.95e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 186 IKALETLRQVRQTQGQKVKEYQMELKYLKQykekacEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKI 265
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKN------ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 266 MkldneiKALDSRKKQMEKDNSELEEKMEKVfqgtDEQLNDLYHnhqrtVREKERKLVDCHRELEKLnkesrllnqekse 345
Cdd:pfam15921 502 T------ASLQEKERAIEATNAEITKLRSRV----DLKLQELQH-----LKNEGDHLRNVQTECEAL------------- 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 346 llveqgRLQLQadrhqehirARDSLIQSLatqleldgfergpfsERQIKNFHKLVreRQEGEAKTANQLmndfaEKETLK 425
Cdd:pfam15921 554 ------KLQMA---------EKDKVIEIL---------------RQQIENMTQLV--GQHGRTAGAMQV-----EKAQLE 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 426 QkqidEIRDKKTGLGRIIELKseilSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELsKAEKN---SNVETLKM 502
Cdd:pfam15921 597 K----EINDRRLELQEFKILK----DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDI-KQERDqllNEVKTSRN 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 503 EVISLQNEKADLDRTLRKLDQEMEqlnhhtTTRTQMEMLTKDKADKDEQIRK-IKSRHSDELTSLLGYFPNKKQLEdwlh 581
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEME------TTTNKLKMQLKSAQSELEQTRNtLKSMEGSDGHAMKVAMGMQKQIT---- 737
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19924129 582 SKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQD-FESDLDRLKEEI 649
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEvLRSQERRLKEKV 806
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
534-733 |
2.01e-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: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 534 TRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINN 613
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 614 ELKRKEEQLS------------SYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 681
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19924129 682 PVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLV 733
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
170-628 |
2.06e-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: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 170 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEyQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELD 249
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN-QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 250 PLKNRLKEIEHNLSKImklDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEqLNDLYHNHQRTVREKERKLVDCHREL 329
Cdd:TIGR04523 346 QLKKELTNSESENSEK---QRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEKLNQQKDEQIKKLQQEK 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 330 EKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELdgfergpfSERQIKNFHKLVRERQEGEAK 409
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV--------LSRSINKIKQNLEQKQKELKS 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 410 TANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEIlSKKQNELKNVKyelqqlegssDRILELDQELIKAERELS 489
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK-KEKESKISDLE----------DELNKDDFELKKENLEKE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 490 KAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLnhhtttRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGY 569
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL------IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 19924129 570 FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDK 628
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK 695
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
421-1178 |
2.11e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.28 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 421 KETLKQKqIDEIRDKKTGLGRIIELKSEILSKKQ--NEL-KNVKYELQQLEGSSDRILE-LDQELIKAERELSKAEKNSN 496
Cdd:TIGR01612 602 KLELKEK-IKNISDKNEYIKKAIDLKKIIENNNAyiDELaKISPYQVPEHLKNKDKIYStIKSELSKIYEDDIDALYNEL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 497 VETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTkdkadkdeqIRKIKSRHSDELTsllgyfpnkkQL 576
Cdd:TIGR01612 681 SSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSN---------IENKKNELLDIIV----------EI 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 577 EDWLHSK-SKEINQTRDRLAKLNKELAsseqnkNHINNELKRKEeQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQ 655
Cdd:TIGR01612 742 KKHIHGEiNKDLNKILEDFKNKEKELS------NKINDYAKEKD-ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 656 RamlagaTAVYSQFITQLTDEnqsccpvcqrVFQTEAELQEVISDLQSKLRlapdklKSTESELKKKEKRRDEMLGLVPM 735
Cdd:TIGR01612 815 K------SKEYIKTISIKEDE----------IFKIINEMKFMKDDFLNKVD------KFINFENNCKEKIDSEHEQFAEL 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 736 RQSI-IDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAa 814
Cdd:TIGR01612 873 TNKIkAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNI- 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 815 klqgidldRTVQQVNQ-EKQEKQHKLDTVSSKIELNRKLIQDQqeQIQHLKSTTNELKSEKLQISTNL--QRRQQLEEQT 891
Cdd:TIGR01612 952 --------DTIKESNLiEKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAKNNELIKYFNDLKANLgkNKENMLYHQF 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 892 VELSTEVQSLYREIKDAKEQVSPLE----TTLEKFQQEKEELINK------KNTSNK--IAQDKLNDIKEKVK--NIHGY 957
Cdd:TIGR01612 1022 DEKEKATNDIEQKIEDANKNIPNIEiaihTSIYNIIDEIEKEIGKniellnKEILEEaeINITNFNEIKEKLKhyNFDDF 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 958 MKD----IENYIQDGKDD-----------------YKKQKETELNKVIAQLSECEKHKEKI--NEDMRLMR---QDIDTQ 1011
Cdd:TIGR01612 1102 GKEenikYADEINKIKDDiknldqkidhhikaleeIKKKSENYIDEIKAQINDLEDVADKAisNDDPEEIEkkiENIVTK 1181
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1012 KIQERWLQDNLtlrKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKe 1091
Cdd:TIGR01612 1182 IDKKKNIYDEI---KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKE- 1257
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1092 lREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYktldqAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEyiEIRSDADE 1171
Cdd:TIGR01612 1258 -KSPEIENEMGIEMDIKAEMETFNISHDDDKDHH-----IISKKHDENISDIREKSLKIIEDFSEESDIN--DIKKELQK 1329
|
....*..
gi 19924129 1172 NVSASDK 1178
Cdd:TIGR01612 1330 NLLDAQK 1336
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
573-1107 |
2.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 573 KKQLEDWLHSKSkeinQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLfdvcgsqdfeSDLDRLKEEIEKS 652
Cdd:PRK03918 178 IERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----------KELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 653 SKQRAMLAGATAVYSQFItqltdenqsccpvcqrvfqteAELQEVISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGL 732
Cdd:PRK03918 244 EKELESLEGSKRKLEEKI---------------------RELEERIEELKKEIE----ELEEKVKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 733 VPMRQSIIDLK---EKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFqMELKDVERKI 809
Cdd:PRK03918 299 SEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 810 AQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQIsTNLQRRQQLEE 889
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-TEEHRKELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 890 QTVELStEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSnkiaqDKLNDIKEKVKNIhgymkDIENYIQDGK 969
Cdd:PRK03918 457 YTAELK-RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-----EQLKELEEKLKKY-----NLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 970 DdYKKQKEtELNKVIAQLSECEKHKEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQM 1048
Cdd:PRK03918 526 E-YEKLKE-KLIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1049 QVLQMKSEHQ---------KLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREM 1107
Cdd:PRK03918 604 YLELKDAEKElereekelkKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-520 |
2.48e-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: 48.91 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 170 KALKQKFDEIFSATRYIK-ALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEirdQITSKEAQLTSSKEIVKSYENEL 248
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE---RLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 249 DPLKNRLKEIEHNLSKIMKLDNEIKA--LDSRKKQMEKDNSELEEkmekvfqgtdeqlndlyhnhqrTVREKERKLVDCH 326
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEE----------------------EVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 327 RELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQL-ELDGFERGPFSE-----RQIKNFHKLV 400
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeELEAALRDLESRlgdlkKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 401 RERQEG------EAKTANQLMNDFAEKETLKQKQIDEIRDKKtglGRIIELKSEILS--KKQNELKNVKYELQQLEGSSD 472
Cdd:TIGR02169 899 RELERKieeleaQIEKKRKRLSELKAKLEALEEELSEIEDPK---GEDEEIPEEELSleDVQAELQRVEEEIRALEPVNM 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 19924129 473 RILELDQELIKAERELSKAEknsnvETLKMEVISLQNEKADLDRTLRK 520
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKR-----AKLEEERKAILERIEEYEKKKRE 1018
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
692-940 |
2.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 692 AELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsiidlKEKEIPELRNKLQNVNRDIQRLKNDIEEQ 771
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 772 ETLLGTIMpeeesakvcltdvtimerfqmelkdverkiaqQAAKLQGIDLDRTVQQVNQEkqekqhKLDTVSSKIELNRK 851
Cdd:COG3883 85 REELGERA--------------------------------RALYRSGGSVSYLDVLLGSE------SFSDFLDRLSALSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 852 LIQDQQEQIQHLKSTTNELKSEKLQIStnlQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELIN 931
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELE---AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
....*....
gi 19924129 932 KKNTSNKIA 940
Cdd:COG3883 204 ELAAAEAAA 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1202-1278 |
3.59e-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: 45.64 E-value: 3.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDREniesLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLG 1278
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALDPI----TRREVRALLKSLQAQLGITVVLVTHDLDEAARLA 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-676 |
3.66e-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: 47.84 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 426 QKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEgssDRILELDQELIKAERELSKAEKnsNVETLKMEVI 505
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEA--ELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 506 SLQNEKADLDRTLRKLDQEMEQLNHHTTtrtqMEMLtkdkadkdeqirkIKSRHSDELTSLLGYFpnkKQLEDWLHSKSK 585
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPP----LALL-------------LSPEDFLDAVRRLQYL---KYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 586 EINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEdklfdvcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAV 665
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALK---------AERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|.
gi 19924129 666 YSQFITQLTDE 676
Cdd:COG4942 225 LEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
796-973 |
3.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 796 ERFQMELKDVERKIAQQAAKLQgiDLDRTVQQVNQEKQEKQHKLDTVSSKIELN--RKLIQDQQEQIQHLKSTTNELKSE 873
Cdd:COG4913 613 AALEAELAELEEELAEAEERLE--ALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 874 KLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEEL-----------INKKNTSNKIAQD 942
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralleerfaaALGDAVERELREN 770
|
170 180 190
....*....|....*....|....*....|.
gi 19924129 943 KLNDIKEKVKNIHGYMKDIENYIQDGKDDYK 973
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFNREWP 801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
740-921 |
4.53e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 740 IDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTImpeeesakvcltdvTIMERFQMELKDV---ERKIAQQAAKL 816
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------------QRLAEYSWDEIDVasaEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 817 QGID--------LDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNEL-KSEKLQISTNLQRRQQL 887
Cdd:COG4913 678 ERLDassddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAA 757
|
170 180 190
....*....|....*....|....*....|....
gi 19924129 888 EEQTVELSTEVQSLYREIKDAKEQVSPLETTLEK 921
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
421-659 |
4.92e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 421 KETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKyeLQQLEGSSDRILELDQELIKAERELSkaEKNSNVETL 500
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEEELEKIEKEIK--ELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 501 KMEVISLQNEKADLDRtLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKI-------------------KSRHSD 561
Cdd:PRK05771 113 ENEIKELEQEIERLEP-WGNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVenveyistdkgyvyvvvvvLKELSD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 562 ELTSLL---GY----FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSeqnKNHINNELKRKEEQLSSYEDKlFDVC- 633
Cdd:PRK05771 192 EVEEELkklGFerleLEEEGTPSELIREIKEELEEIEKERESLLEELKEL---AKKYLEELLALYEYLEIELER-AEALs 267
|
250 260 270
....*....|....*....|....*....|....*..
gi 19924129 634 ---GSQDF--------ESDLDRLKEEIEKSSKQRAML 659
Cdd:PRK05771 268 kflKTDKTfaiegwvpEDRVKKLKELIDKATGGSAYV 304
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
659-712 |
6.23e-05 |
|
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: 41.79 E-value: 6.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 19924129 659 LAGATAVYSQFITQLTDENQsCCPVCQRVFQTEaELQEVISDLQSKLRLAPDKL 712
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEG-CCPLCGRPLDEE-HRSELIKELQSKLERLPEEL 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
187-729 |
6.38e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 187 KALETLRQVRQTQGQKVKEYQMELKylkqykekacEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKim 266
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 267 kLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQeksel 346
Cdd:COG1196 335 -LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA----- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 347 lvEQGRLQLQADRHQEHIRARDSLIQSLATQLEldgfERGPFSERQIKnfhklvRERQEGEAKTANQLMNDFAEKETLKQ 426
Cdd:COG1196 409 --EEALLERLERLEEELEELEEALAELEEEEEE----EEEALEEAAEE------EAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 427 KQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKyeLQQLEGSSDRILELDQELIKAERELSKAEKNSnvetlkmEVIS 506
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVK--AALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-------LAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 507 LQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQL---------- 576
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtllgrtl 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 577 -EDWLHSKSKEINQTRDRLAK-------LNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDvcGSQDFESDLDRLKEE 648
Cdd:COG1196 628 vAARLEAALRRAVTLAGRLREvtlegegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE--EELELEEALLAEEEE 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 649 IEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDE 728
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAER-------EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
.
gi 19924129 729 M 729
Cdd:COG1196 779 L 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
401-628 |
7.21e-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: 46.68 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 401 RERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQE 480
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 481 LIKAerelskAEKNSNVETLKmeVISLQNEKADLDRTLRKLDQEMEQLnhhtttRTQMEMLTKDKADKDEQIRKIKSRHS 560
Cdd:COG4942 109 LLRA------LYRLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 561 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDK 628
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
25-70 |
8.19e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 45.53 E-value: 8.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 19924129 25 ITFFSPLTILVGPNGAGKTTIIECLKYICtgDFPP--GTKGNTFVHDP 70
Cdd:COG3910 33 LEFHPPVTFFVGENGSGKSTLLEAIAVAA--GFNPegGSKNFRFSTRE 78
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
218-617 |
9.59e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 46.65 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 218 EKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKldNEIKALDSRKKQmEKDNSELEEKMEKVF 297
Cdd:COG4694 99 EENIELEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIK--DDLKKLFASSGR-NYRKANLEKKLSALK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 298 QGTDEQLNDLYhnhqRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQAdrHQEHIRARDSLIQSLATQ 377
Cdd:COG4694 176 SSSEDELKEKL----KLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAVSSAIEELAA--LIQNPGNSDWVEQGLAYH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 378 LELDG----FERGPFSERQIKNFHKLVRERQEGEAKTANQLMNDF-AEKETLKQKQIDEIRDKKTGLGRIIELKSEILSK 452
Cdd:COG4694 250 KEEEDdtcpFCQQELAAERIEALEAYFDDEYEKLLAALKDLLEELeSAINALSALLLEILRTLLPSAKEDLKAALEALNA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 453 KQNELKNVkyeLQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEmeqlnhht 532
Cdd:COG4694 330 LLETLLAA---LEEKIANPSTSIDLDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAHELA-------- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 533 ttrTQMEMLTKDKADKDEQIRKIKsrhsdeltsllgyfpnkkqledWLHSKSKEINQTRDRLAKLNKELASSEQNKNHIN 612
Cdd:COG4694 399 ---ELKEDLSRYKAEVEELIEELK----------------------TIKALKKALEDLKTEISELEAELSSVDEAADEIN 453
|
....*
gi 19924129 613 NELKR 617
Cdd:COG4694 454 EELKA 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
641-901 |
9.69e-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: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 641 DLDRLKEEIEKSSKQRAMLAGATAVYSQFitqltdenqsccpvcQRVFQTEAELQEVISDL-----QSKLRLAPDKLKST 715
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERY---------------AAARERLAELEYLRAALrlwfaQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 716 ESELKKKEKRRDEmlglvpmRQSIIDLKEKEIPELRNKLQNV-NRDIQRLKNDIEEQETllgtimpeeesakvcltdvti 794
Cdd:COG4913 301 RAELARLEAELER-------LEARLDALREELDELEAQIRGNgGDRLEQLEREIERLER--------------------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 795 merfqmELKDVERKIAQQAAKLQGIDLdrtvqqvnqekqekqhkldtvssKIELNRKLIQDQQEQIQHLKSTTNELKSE- 873
Cdd:COG4913 353 ------ELEERERRRARLEALLAALGL-----------------------PLPASAEEFAALRAEAAALLEALEEELEAl 403
|
250 260
....*....|....*....|....*...
gi 19924129 874 KLQISTNLQRRQQLEEQTVELSTEVQSL 901
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1202-1269 |
9.90e-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: 9.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNfqLLVITH 1269
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPET----EALILEALRALAKGKT--VIVIAH 153
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
801-952 |
1.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 801 ELKDVERKIAQQAAKLQgiDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNE----------- 869
Cdd:COG3883 24 ELSELQAELEAAQAELD--ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 870 -------LKSEKLQ-ISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQ 941
Cdd:COG3883 102 vsyldvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170
....*....|.
gi 19924129 942 DKLNDIKEKVK 952
Cdd:COG3883 182 ALLAQLSAEEA 192
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
173-647 |
1.19e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 173 KQKFDEIFSATRYIKALETLRQVRQTQgQKVKEYQMELKY--LKQYKEKACEIRDQITSKEAQLTSSkEIVKSYENELDp 250
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSL-KAKKRFSLLKKEtiYLQSAQRVELAERQLQELKIDVKSI-SSLKLVNLELE- 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 251 lkNRLKEIEHNLSKIMKLDNEIK-ALDSRKKQMeKDNSELEEKMEKVFQGTDEQLNdlYHNHQRTVREKERKLVDCH--- 326
Cdd:COG5022 906 --SEIIELKKSLSSDLIENLEFKtELIARLKKL-LNNIDLEEGPSIEYVKLPELNK--LHEVESKLKETSEEYEDLLkks 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 327 ----RELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLiqslatqleldgfergpFSERQIKNFHKLVRE 402
Cdd:COG5022 981 tilvREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAEL-----------------QSASKIISSESTELS 1043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 403 RQEGEAKtanqLMNDFAEKETLKQKQIDEIRDKKTGlGRIIELKSEILSKKQNELKNVKYELQQlegSSDRILELDQELI 482
Cdd:COG5022 1044 ILKPLQK----LKGLLLLENNQLQARYKALKLRREN-SLLDDKQLYQLESTENLLKTINVKDLE---VTNRNLVKPANVL 1115
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 483 KAereLSKAEKNSNVETLKMEVIS-----LQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKS 557
Cdd:COG5022 1116 QF---IVAQMIKLNLLQEISKFLSqlvntLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS 1192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 558 RHSDELTsllgyfpnkKQLEDWLHSKSKEINQTrDRLAKLNKELASSEQNKNHINNELKRkeeqlSSYEDKLFDVCGSQD 637
Cdd:COG5022 1193 KLSSSEV---------NDLKNELIALFSKIFSG-WPRGDKLKKLISEGWVPTEYSTSLKG-----FNNLNKKFDTPASMS 1257
|
490
....*....|
gi 19924129 638 FESDLDRLKE 647
Cdd:COG5022 1258 NEKLLSLLNS 1267
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
405-1028 |
1.69e-04 |
|
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: 46.37 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 405 EGEAKTANQLMNDFAEKETLkqkqIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGS-SDRILELDQELIK 483
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESA----ELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQwKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 484 AERELSKAEknSNVETLkmEVISLQNEKADLDRtlRKLDQEMEQLnhhttTRTQMEMLTKDKADKDEQIRKIkSRHSDEL 563
Cdd:pfam12128 313 ADAAVAKDR--SELEAL--EDQHGAFLDADIET--AAADQEQLPS-----WQSELENLEERLKALTGKHQDV-TAKYNRR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 564 TSLLGYfPNKKQLEDwLHSKSKEINQTRDRLA--------KLNKELASS-EQNKNHINNELKRKEEQLSSYEDKLFDVCG 634
Cdd:pfam12128 381 RSKIKE-QNNRDIAG-IKDKLAKIREARDRQLavaeddlqALESELREQlEAGKLEFNEEEYRLKSRLGELKLRLNQATA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 635 SQD-------FESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCpvcQRVFQTEAELQEVisdlqsklrl 707
Cdd:pfam12128 459 TPElllqlenFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS---RRLEERQSALDEL---------- 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 708 apdklksteselkkkekrrdeMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIE--------EQETLLGTIm 779
Cdd:pfam12128 526 ---------------------ELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDpevwdgsvGGELNLYGV- 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 780 peeesaKVCLTDVTIMERFQMElKDVERKIAQQAAKLQGidldrtvQQVNQEKQEKQ-----HKLDTVSSKIELNRKLIQ 854
Cdd:pfam12128 584 ------KLDLKRIDVPEWAASE-EELRERLDKAEEALQS-------AREKQAAAEEQlvqanGELEKASREETFARTALK 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 855 DQQEQIQHLkstTNELKSEKLQISTNLQRRQQL-EEQTVELSTEVQSLYREIKDAKEQV--SPLETTLEKFQQEKEELIN 931
Cdd:pfam12128 650 NARLDLRRL---FDEKQSEKDKKNKALAERKDSaNERLNSLEAQLKQLDKKHQAWLEEQkeQKREARTEKQAYWQVVEGA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 932 KKNTSNKIAQDKL---NDIKEKVKNIHGYMK-DIENYIQDGKDDYKKqkETELNKVIAQLSECEKHKEKINEDMRLMrqd 1007
Cdd:pfam12128 727 LDAQLALLKAAIAarrSGAKAELKALETWYKrDLASLGVDPDVIAKL--KREIRTLERKIERIAVRRQEVLRYFDWY--- 801
|
650 660
....*....|....*....|...
gi 19924129 1008 idtqkiQERWLQ--DNLTLRKRN 1028
Cdd:pfam12128 802 ------QETWLQrrPRLATQLSN 818
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-381 |
1.70e-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: 45.53 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 188 ALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMK 267
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 268 -LDNEIKALDSRKKQMEKdNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSEL 346
Cdd:COG4942 98 eLEAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 19924129 347 LVEQGRLQLQADRHQEHIRARDSLIQSLATQLELD 381
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
571-772 |
1.87e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 571 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLfdvcgsQDFESDLDRLKEEIE 650
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI------AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 651 K--SSKQR--------AMLAGATAVySQFITQLTdenqsccpVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELK 720
Cdd:COG3883 90 EraRALYRsggsvsylDVLLGSESF-SDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19924129 721 KKEKRRDEMLGLVpmrQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQE 772
Cdd:COG3883 161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
1-461 |
2.32e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.50 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1 MSRIEKMSilGVRSFgiedKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVR- 79
Cdd:COG4694 2 ITKIKKLK--NVGAF----KDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNPSVRv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 80 -----AQIRLQFRD-VNGELIAVQRSmvctqKSKKTEFKTLEGVITRTK---HGEKVSLSSKCAEIDREMISSLGVSKAV 150
Cdd:COG4694 76 fnrdfVEENLRSGEeIKGIFTLGEEN-----IELEEEIEELEKEIEDLKkelDKLEKELKEAKKALEKLLEDLAKSIKDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 151 LNNVIFCHQEDSNWPLSEGKALKQKFDeifSATRYIKALETLRQVRQTQGQKVKEYQmELKYLKQYKEKACE------IR 224
Cdd:COG4694 151 LKKLFASSGRNYRKANLEKKLSALKSS---SEDELKEKLKLLKEEEPEPIAPITPLP-DLKALLSEAETLLEksavssAI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 225 DQITSKEAQLTSS------KEIVKSYENELDPL------KNRLKEIEHnlskimKLDNEIKALdsrKKQMEKDNSELEEK 292
Cdd:COG4694 227 EELAALIQNPGNSdwveqgLAYHKEEEDDTCPFcqqelaAERIEALEA------YFDDEYEKL---LAALKDLLEELESA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 293 MEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQA--DRHQEHIRARDSL 370
Cdd:COG4694 298 INALSALLLEILRTLLPSAKEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELLDELNDliAALNALIEEHNAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 371 IQSLATQLEldgfergpfserqiknfhklvRERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEIl 450
Cdd:COG4694 378 IANLKAEKE---------------------EARKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEI- 435
|
490
....*....|.
gi 19924129 451 SKKQNELKNVK 461
Cdd:COG4694 436 SELEAELSSVD 446
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
34-105 |
2.44e-04 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 44.03 E-value: 2.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19924129 34 LVGPNGAGKTTIIECLkyicTGDFPPgTKGNTFVHDpkvaqetdvraqirlqfRDVNGELIAVQRSM-VCTQK 105
Cdd:cd03263 33 LLGHNGAGKTTTLKML----TGELRP-TSGTAYING-----------------YSIRTDRKAARQSLgYCPQF 83
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-929 |
2.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 736 RQSIIDLKE-KEIPELRNKLQNVNRDIQRLKNDIEEQETLLgtimpeeesakvcltdvtimERFQMELKDVERKIAQQAA 814
Cdd:COG4717 64 RKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEEL--------------------EELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 815 KLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQIS-TNLQRRQQLEEQTVE 893
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 19924129 894 LSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEEL 929
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-50 |
2.80e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.61 E-value: 2.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 19924129 4 IEKMSILGVRSFGiedkDKQIITFFSPLTILVGPNGAGKTTIIECLK 50
Cdd:cd03278 1 LKKLELKGFKSFA----DKTTIPFPPGLTAIVGPNGSGKSNIIDAIR 43
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-50 |
2.82e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.92 E-value: 2.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 19924129 3 RIEKMSILGVRSFGIEDKDkqiitfFSPLTILVGPNGAGKTTIIECLK 50
Cdd:COG4637 1 MITRIRIKNFKSLRDLELP------LGPLTVLIGANGSGKSNLLDALR 42
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1192-1270 |
2.92e-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: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1192 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHD 1270
Cdd:COG4618 458 DTRIGEGGARlSGGQRQ------RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-----KARGATVVVITHR 526
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
608-768 |
2.98e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 608 KNHINNELKRKEEQLSSYEDKLFD-VCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSC------ 680
Cdd:PHA02562 201 NKNIEEQRKKNGENIARKQNKYDElVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkvikm 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 681 ------CPVCQRVFQTEaelQEVISDLQsklrlapDKLKSTESELKKKEKRRDEMLGLVPMRQSIIdlkeKEIPELRNKL 754
Cdd:PHA02562 281 yekggvCPTCTQQISEG---PDRITKIK-------DKLKELQHSLEKLDTAIDELEEIMDEFNEQS----KKLLELKNKI 346
|
170
....*....|....
gi 19924129 755 QNVNRDIQRLKNDI 768
Cdd:PHA02562 347 STNKQSLITLVDKA 360
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
825-1092 |
3.04e-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: 45.44 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 825 VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTN------ELKSEK--LQISTNLQRRQQLEEQTVELST 896
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKreYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 897 EVQSLYREIKDAKEQVSPLETTLEKFQQEKEElINKKntSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDgkddykkqK 976
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEE-LNKK--IKDLGEEEQLRVKEKIGELEAEIASLERSIAE--------K 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 977 ETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKrneELKEVEEERKQHLKEMGQMQVLQMKSE 1056
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---EELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270
....*....|....*....|....*....|....*....
gi 19924129 1057 HQKLE---ENIDNIKRNHNLALGRQKGYEEEIIHFKKEL 1092
Cdd:TIGR02169 391 REKLEklkREINELKRELDRLQEELQRLSEELADLNAAI 429
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
171-284 |
3.38e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 171 ALKQKFDEIFSATRYIKALE---TLRQVRQTQGQKVKEYQMELK----YLKQYKEKACEIRDqiTSKEAQLTSSKEIVKS 243
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHiedLKEELSNERLRKLRSLLTKLSealdKLRSYLPKLNPLRE--EKKKVSVKSLEELIKD 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 19924129 244 YENELDPLKNRLKEIEhnlSKIMKLDNEIKALDSRKKQMEK 284
Cdd:PRK05771 91 VEEELEKIEKEIKELE---EEISELENEIKELEQEIERLEP 128
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
264-556 |
3.46e-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: 45.11 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 264 KIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKErklvdchRELEKLNKESRLLNQEK 343
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERE-------RELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 344 ---SELLVEQGRL----QLQADRHQEHIRARDSLiqSLATQLELDGFERGPFSERQIKNFHKLVRERQEGEAKTANQL-- 414
Cdd:pfam17380 365 irqEEIAMEISRMreleRLQMERQQKNERVRQEL--EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLee 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 415 -----MNDFAEKETLKQKQIDEIRDKKTGLGR-IIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAEREL 488
Cdd:pfam17380 443 erareMERVRLEEQERQQQVERLRQQEEERKRkKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 489 SKAEKNSNVETLKMEVislqNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKadkdEQIRKIK 556
Cdd:pfam17380 523 EERQKAIYEEERRREA----EEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER----EMMRQIV 582
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-55 |
3.73e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.38 E-value: 3.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 19924129 3 RIEKMSILGVRSFgiedkDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTG 55
Cdd:COG1195 1 RLKRLSLTNFRNY-----ESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATG 48
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
685-1000 |
3.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 685 QRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvPMRQsiiDLKEKEIPELRNKLQNVNRDIQRL 764
Cdd:PRK11281 69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE-----ETRE---TLSTLSLRQLESRLAQTLDQLQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 765 KNDIEEQETLLGTIMPEEESAKVCLT-----------------------DVTIMERFQMELKDVERKIAQQAAKLQGIDL 821
Cdd:PRK11281 141 QNDLAEYNSQLVSLQTQPERAQAALYansqrlqqirnllkggkvggkalRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 822 ---------DRTVQQVNQEKQEKQHKLDTVSSK-IELNRKLIQDQQEQIQHLKSTTNELKSEKLQIstNLQRRQQLEEQT 891
Cdd:PRK11281 221 lqdllqkqrDYLTARIQRLEHQLQLLQEAINSKrLTLSEKTVQEAQSQDEAARIQANPLVAQELEI--NLQLSQRLLKAT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 892 VELSTEVQ----------SLYREIKDAKEQVSPLETTL---EKFQQEKEEL---INKKNTSNKIA-----QDKLNDIKEK 950
Cdd:PRK11281 299 EKLNTLTQqnlrvknwldRLTQSERNIKEQISVLKGSLllsRILYQQQQALpsaDLIEGLADRIAdlrleQFEINQQRDA 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 19924129 951 VKNIHGYMKDIEnyiqdgkddyKKQKETELNKVIAQLSECEKHKEKINED 1000
Cdd:PRK11281 379 LFQPDAYIDKLE----------AGHKSEVTDEVRDALLQLLDERRELLDQ 418
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1227-1279 |
3.98e-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: 3.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 19924129 1227 IIAlDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGR 1279
Cdd:COG1136 166 ILA-DEPTGNLDSKT----GEEVLELLRELNRELGTTIVMVTHDPELAARADR 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
799-1022 |
4.24e-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: 44.37 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 799 QMELKDVERKIAQQAAKLQgidldrtvqQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQIs 878
Cdd:COG4942 26 EAELEQLQQEIAELEKELA---------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 879 tnlqrRQQLEEQTVELSTEVQSLYReikdaKEQVSPLETTLEkfQQEKEELINKKNTSNKIA---QDKLNDIKEKVKNIH 955
Cdd:COG4942 96 -----RAELEAQKEELAELLRALYR-----LGRQPPLALLLS--PEDFLDAVRRLQYLKYLAparREQAEELRADLAELA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19924129 956 GYMKDIENYIQDgKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNL 1022
Cdd:COG4942 164 ALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1214-1270 |
5.01e-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: 5.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 19924129 1214 RLALAETFCLNCGIIALDEPTTNLDRenieSLAHALVEIIKSRSQQRNFQLLVITHD 1270
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDV----SVQAQILDLLKKLQEELGLTLLFITHD 205
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
693-994 |
5.70e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 693 ELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglvpmrqsIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEqe 772
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE----------NIARKQNKYDELVEEAKTIKAEIEELTDELLN-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 773 tllgTIMPEEE--SAKVCLTDVTI-----MERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSK 845
Cdd:PHA02562 246 ----LVMDIEDpsAALNKLNTAAAkikskIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 846 IElNRKLIQDqqeQIQHLKSTTNELKSeklQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQvsplettLEKFQQE 925
Cdd:PHA02562 322 ID-ELEEIMD---EFNEQSKKLLELKN---KISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE-------LAKLQDE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 926 KEELINKKNTSNK------IAQDKLNDIKEKVKNIHGYM----KDIENYIQDGKDDYKKQKETELNKVI----------A 985
Cdd:PHA02562 388 LDKIVKTKSELVKekyhrgIVTDLLKDSGIKASIIKKYIpyfnKQINHYLQIMEADYNFTLDEEFNETIksrgredfsyA 467
|
....*....
gi 19924129 986 QLSECEKHK 994
Cdd:PHA02562 468 SFSQGEKAR 476
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
201-295 |
6.21e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 201 QKVKEYQMELKYLKQYKEkacEIRDQITSKEAQLtsskeivKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKK 280
Cdd:COG2433 413 EEIRRLEEQVERLEAEVE---ELEAELEEKDERI-------ERLERELSEARSEERREIRKDREISRLDREIERLERELE 482
|
90
....*....|....*
gi 19924129 281 QMEKDNSELEEKMEK 295
Cdd:COG2433 483 EERERIEELKRKLER 497
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1199-1275 |
6.48e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.90 E-value: 6.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19924129 1199 GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1275
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL----------DDFPgtVLLVSHDRYFLD 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
795-961 |
6.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 795 MERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELkSEK 874
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 875 LQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQvspLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNI 954
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
....*..
gi 19924129 955 HGYMKDI 961
Cdd:COG3206 340 EARLAEL 346
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1195-1279 |
6.77e-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: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1195 LDM----RGR-CSAGQKVLasliirLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1269
Cdd:cd03245 130 LDLqigeRGRgLSGGQRQA------VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT------LIIITH 197
|
90
....*....|
gi 19924129 1270 DEDFVELLGR 1279
Cdd:cd03245 198 RPSLLDLVDR 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1192-1269 |
7.32e-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: 7.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19924129 1192 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITH 1269
Cdd:TIGR01842 445 DTVIGPGGAtLSGGQRQ------RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-----KARGITVVVITH 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
173-772 |
7.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 173 KQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKeivksyeneldplk 252
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK-------------- 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 253 nrlKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEqlndlyhnhQRTVREKERKLVDCHRELEKL 332
Cdd:PTZ00121 1343 ---KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE---------KKKADEAKKKAEEDKKKADEL 1410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 333 NKESRllNQEKSEllveqgrlqlQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVRERQEG------ 406
Cdd:PTZ00121 1411 KKAAA--AKKKAD----------EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeakkk 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 407 --EAKTANQLmndfAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKA 484
Cdd:PTZ00121 1479 aeEAKKADEA----KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 485 ErELSKAEKNSNVETLKMEvislQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELT 564
Cdd:PTZ00121 1555 E-ELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 565 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDvcgSQDFESDLDR 644
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---EAEEAKKAEE 1706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 645 LKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEK 724
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 19924129 725 RRDEmlglvpMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQE 772
Cdd:PTZ00121 1787 EEDE------KRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1202-1269 |
8.68e-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: 8.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEiIKSRSQQRnfqlLVITH 1269
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGATR----IVIAH 154
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
486-630 |
8.96e-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: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 486 RELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTttrtqmEMLTKDKADKDEQIRKIKSRHSDElts 565
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV------EELEAELEEKDERIERLERELSEA--- 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19924129 566 llgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNknhiNNELKRKEEQLSSYEDKLF 630
Cdd:COG2433 454 --------RSEERREIRKDREISRLDREIERLERELEEERER----IEELKRKLERLKELWKLEH 506
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1202-1275 |
9.60e-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: 9.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1202 SAGQKVLASLIIRLALAETFCLNCGI----IALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVE 1275
Cdd:cd03279 125 SGGETFLASLSLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALELI-----RTENRMVGVISHVEELKE 197
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
825-1008 |
1.40e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 825 VQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQeqiqhlKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYRE 904
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR------KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 905 IKDakeqvspLETTLEKFQQEKEELINKKNTSNKIA-------------------QDKLNDIKEKVKNIHGYMKDIENYI 965
Cdd:PHA02562 250 IED-------PSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptctqqisegPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19924129 966 QdgkddykkqketELNKVIAQLSECEKHKEKINEDMRLMRQDI 1008
Cdd:PHA02562 323 D------------ELEEIMDEFNEQSKKLLELKNKISTNKQSL 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
661-1017 |
1.51e-03 |
|
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: 42.80 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 661 GATAVYSQFITQLTDENQSCCPVCQRVFQTEAElqevisdlqsklRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSII 740
Cdd:pfam17380 262 GQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE------------KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 741 DLKEKEIPELRNKLQNVNRDIQRLKndIEEQETLLGTIMPEEESAKVclTDVTIMERFQMEL------------------ 802
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIR--QEERKRELERIRQEEIAMEI--SRMRELERLQMERqqknervrqeleaarkvk 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 803 ---KDVERKIAQQAAKLQGIdldrTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQIST 879
Cdd:pfam17380 406 ileEERQRKIQQQKVEMEQI----RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 880 NLQRRQQLEEQTvelstevqslyREIkdakeqvspLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEkvknihgymk 959
Cdd:pfam17380 482 EKRDRKRAEEQR-----------RKI---------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE---------- 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19924129 960 diENYIQDGKDDYKKQKETELNKVIAQ----LSECEKHKEKINEDMRLMRQDIDTQKIQERW 1017
Cdd:pfam17380 532 --EERRREAEEERRKQQEMEERRRIQEqmrkATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1214-1270 |
1.85e-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: 40.88 E-value: 1.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 19924129 1214 RLALAETFCLNCGIIALDEPTTNLDreniesLAH--ALVEIIKSRSQQRNFQLLVITHD 1270
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLD------IAHqiELLELLRRLARERGKTVVMVLHD 157
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
190-620 |
2.00e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 190 ETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDplknrlkeiehnlskimKLD 269
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE-----------------ELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 270 NEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEqlndlyhnhqrtVREKERKLVDCHRELEKlnkesrllNQEKSELLVE 349
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDE------------LREREAELEATLRTARE--------RVEEAEALLE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 350 QGRL-----QLQADRHQEHIRARDSLIQSLATQLEldgfergpfserQIKNFHKLVRERQEgEAKTANQLmndfaeketl 424
Cdd:PRK02224 451 AGKCpecgqPVEGSPHVETIEEDRERVEELEAELE------------DLEEEVEEVEERLE-RAEDLVEA---------- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 425 kQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQEL-IKAERELSK-AEKNSNVETLKM 502
Cdd:PRK02224 508 -EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAeEEAEEAREEvAELNSKLAELKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 503 EVISLQNEKADLDRtLRKLDQEMEQLNHHTTTRTQMEMLTKDK-ADKDEQIRKIKSRHSDELTSLLGyfPNKKQLEDWLH 581
Cdd:PRK02224 587 RIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERlAEKRERKRELEAEFDEARIEEAR--EDKERAEEYLE 663
|
410 420 430
....*....|....*....|....*....|....*....
gi 19924129 582 SKSKEINQTRDRLAKLNKELASseqnknhINNELKRKEE 620
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGA-------VENELEELEE 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
225-379 |
2.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 225 DQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQL 304
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 305 NDLYHNHQ------------------------RTVREKERKLVDCHREL-EKLNKESRLLNQEKSELLVEQGRLQLQADR 359
Cdd:COG3883 93 RALYRSGGsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADkAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180
....*....|....*....|
gi 19924129 360 HQEHIRARDSLIQSLATQLE 379
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEA 192
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1202-1273 |
2.57e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.97 E-value: 2.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDF 1273
Cdd:COG0488 154 SGGWRR------RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----------KNYPgtVLVVSHDRYF 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1190-1270 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1190 KGDTALDMRG------RC----SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIEslahALVEIIKsRSQQ 1259
Cdd:cd03235 112 KVDEALERVGlseladRQigelSGGQQQ------RVLLARALVQDPDLLLLDEPFAGVDPKTQE----DIYELLR-ELRR 180
|
90
....*....|.
gi 19924129 1260 RNFQLLVITHD 1270
Cdd:cd03235 181 EGMTILVVTHD 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1202-1274 |
2.69e-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: 2.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19924129 1202 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDreniESLAHALVEIIKSRSQQRNFQLLVITHDEDFV 1274
Cdd:COG1123 144 SGGQRQ------RVAIAMALALDPDLLIADEPTTALD----VTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
795-951 |
2.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 795 MERFQMELKDVERKIAQQAAKLQGidLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKsTTNELKSEK 874
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAA--LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19924129 875 LQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKV 951
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
34-91 |
2.97e-03 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 41.18 E-value: 2.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 34 LVGPNGAGKTTIIECLkyicTGDFPPgTKGntfvhdpkvaqetdvraQIRLQFRDVNG 91
Cdd:COG0411 35 LIGPNGAGKTTLFNLI----TGFYRP-TSG-----------------RILFDGRDITG 70
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
898-1017 |
3.19e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 898 VQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHgyMKDIENYIQDGKDDYKKQKE 977
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKE--IKDLQKELEKLNEEYAAKLK 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19924129 978 TELNKV---IAQLSECEKHKEKINEDMRLMRQDIDT------------QKIQERW 1017
Cdd:cd22656 201 AKIDELkalIADDEAKLAAALRLIADLTAADTDLDNllaligpaipalEKLQGAW 255
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
317-662 |
3.23e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 317 EKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQL-----ELDGFERGPFSE- 390
Cdd:pfam19220 52 ELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELrdktaQAEALERQLAAEt 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 391 RQIKNFHKLVRERQEgEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKyelQQLEGS 470
Cdd:pfam19220 132 EQNRALEEENKALRE-EAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE---TQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 471 SDRILELDQELI--KAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQmEMLTKDKADK 548
Cdd:pfam19220 208 RARLRALEGQLAaeQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDE-AIRAAERRLK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 549 DEQI-RKIKSRHSDELtsllgyfpnKKQLEDwLHSKSKEINQTR----DRLAKLNKELASS----EQNKNHINNELKRKE 619
Cdd:pfam19220 287 EASIeRDTLERRLAGL---------EADLER-RTQQFQEMQRARaeleERAEMLTKALAAKdaalERAEERIASLSDRIA 356
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 19924129 620 EQLSSYEDKlfdvcgSQDFESDLDRLKEEIEKSSKQRAMLAGA 662
Cdd:pfam19220 357 ELTKRFEVE------RAALEQANRRLKEELQRERAERALAQGA 393
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
31-61 |
3.60e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 40.87 E-value: 3.60e-03
10 20 30
....*....|....*....|....*....|.
gi 19924129 31 LTILVGPNGAGKTTIIECLkyicTGDFPPGT 61
Cdd:COG4559 29 LTAIIGPNGAGKSTLLKLL----TGELTPSS 55
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1214-1281 |
3.64e-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: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1214 RLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEdfvELLGRSE 1281
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAAT----GEQIIDLLFELNRERGTTLVLVTHDP---ALAARCD 214
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
361-655 |
3.70e-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: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 361 QEHIRARDSLIQSLATQLEldgFERGPFSERQIKNFHKLVRERQEGEAKTANQLMNdfAEKETLKQKQ-IDEIRDKKTGL 439
Cdd:COG5391 221 EERRQSLQNFLRRVSTHPL---LSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLD--LTSTTQELDMeRKELNESTSKA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 440 GRIIELKSEILSKKQNELKNVKYELQQLEgsSDRILELDQELIKAERELSKAEKNSN--VETLKMEVISLQNEKADLDRT 517
Cdd:COG5391 296 IHNILSIFSLFEKILIQLESEEESLTRLL--ESLNNLLLLVLNFSGVFAKRLEQNQNsiLNEGVVQAETLRSSLKELLTQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 518 LRKLDQEMEQLNHhtttrtQMEMLTKDKADKDEQIRKI------KSRHSDELTS--LLGYFPNKKQ--LEDWLH--SKSK 585
Cdd:COG5391 374 LQDEIKSRESLIL------TDSNLEKLTDQNLEDVEELsrslrkNSSQRAVVSQqpEGLTSFSKLSykLRDFVQekSRSK 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 586 EINQTRDRLAKLNKELASSEQNKNHINNELKrkeeqlssYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQ 655
Cdd:COG5391 448 SIESLQQDKEKLEEQLAIAEKDAQEINEELK--------NELKFFFSVRNSDLEKILKSVADSHIEWAEE 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-658 |
4.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 298 QGTDEQLNDLyhnhQRTVREKERKLVDCHRELEKLNKESRLLNQEKSEL--LVEQGRLQLQADRHQEHIRARDSLIQSL- 374
Cdd:COG4913 606 FDNRAKLAAL----EAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERLd 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 375 ATQLELDGFERgpfserQIknfhklvrERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQ 454
Cdd:COG4913 682 ASSDDLAALEE------QL--------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 455 NELKNVKYELQQLEGSSDRILE-LDQELIKAERELSKAEKNsnVETLKMEVISL-QNEKADLDRTLRKLDQEMEQLNHht 532
Cdd:COG4913 748 RALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEE--LERAMRAFNREwPAETADLDADLESLPEYLALLDR-- 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 533 ttrtqmemLTKDK-ADKDEQIRKIKSRHSDEltsllgyfpNKKQLEDWLHSKSKEInqtRDRLAKLNKELASSEQNKNHI 611
Cdd:COG4913 824 --------LEEDGlPEYEERFKELLNENSIE---------FVADLLSKLRRAIREI---KERIDPLNDSLKRIPFGPGRY 883
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19924129 612 ----------------NNELKRKEEQLSSYEDKLfdvcgSQDFESDLDRLKEEIEKSSKQRAM 658
Cdd:COG4913 884 lrlearprpdpevrefRQELRAVTSGASLFDEEL-----SEARFAALKRLIERLRSEEEESDR 941
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-921 |
4.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 302 EQLNDLYHNHQRTvREKERKLVDC---------HRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQ 372
Cdd:COG4913 255 EPIRELAERYAAA-RERLAELEYLraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 373 SLATQlELDGFergpfsERQIKNfHKLVRERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDK-KTGLGRIIELKSEI-- 449
Cdd:COG4913 334 GNGGD-RLEQL------EREIER-LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaAALLEALEEELEALee 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 450 --------LSKKQNELKNVKYELQQLEGSSDRIlelDQELIKAERELSKAEKNSNVEtLK-----MEVISLQN------- 509
Cdd:COG4913 406 alaeaeaaLRDLRRELRELEAEIASLERRKSNI---PARLLALRDALAEALGLDEAE-LPfvgelIEVRPEEErwrgaie 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 510 ------------EKADLDRTLRKLDQemeqlnHHTTTRtqmemLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKkqLE 577
Cdd:COG4913 482 rvlggfaltllvPPEHYAAALRWVNR------LHLRGR-----LVYERVRTGLPDPERPRLDPDSLAGKLDFKPHP--FR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 578 DWLHSkskEINQ--------------------TRDRLAKLNKELAssEQNKNHI---------NNE--LKRKEEQLSSYE 626
Cdd:COG4913 549 AWLEA---ELGRrfdyvcvdspeelrrhpraiTRAGQVKGNGTRH--EKDDRRRirsryvlgfDNRakLAALEAELAELE 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 627 DKLfdvcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFItqltdenqsccpvcqRVFQTEAELQEVISDLQSkLR 706
Cdd:COG4913 624 EEL------AEAEERLEALEAELDALQERREALQRLAEYSWDEI---------------DVASAEREIAELEAELER-LD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 707 LAPDKLKSTESELKKKEKRRDEMlglvpmrQSIIDLKEKEIPELRNKLQNVNRDIQRLK---NDIEEQETLLGTIMPEEE 783
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEEL-------EEELDELKGEIGRLEKELEQAEEELDELQdrlEAAEDLARLELRALLEER 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 784 SAKVCLTDV--TIMERFQMELKDVERKIAQQAAKLQgidldRTVQQVNQEKQEKQHKLDTVsskielnrklIQDQQEQIQ 861
Cdd:COG4913 755 FAAALGDAVerELRENLEERIDALRARLNRAEEELE-----RAMRAFNREWPAETADLDAD----------LESLPEYLA 819
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19924129 862 HLksttNELKSEKLqistnLQRRQQLEEQTVELSTE-----VQSLYREIKDAKEQVSPLETTLEK 921
Cdd:COG4913 820 LL----DRLEEDGL-----PEYEERFKELLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
462-660 |
4.64e-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: 40.29 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 462 YELQQLEgssDRILELDQELIKAERELSKAEKNsnVETLKMEVISLQNEKADLDRTLRKLDQEMEQLnhhtttrtqmeml 541
Cdd:COG1579 10 LDLQELD---SELDRLEHRLKELPAELAELEDE--LAALEARLEAAKTELEDLEKEIKRLELEIEEV------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 542 tKDKADKDE-QIRKIKSrhSDELTSLLgyfpnkKQLEdwlhSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEE 620
Cdd:COG1579 72 -EARIKKYEeQLGNVRN--NKEYEALQ------KEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19924129 621 QLSSYEDKLfdvcgsqdfESDLDRLKEEIEKSSKQRAMLA 660
Cdd:COG1579 139 ELEEKKAEL---------DEELAELEAELEELEAEREELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-1278 |
5.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 691 EAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLvpmrqsiidlkEKEIPELRNKLQNVNRDIQRLKNDIEE 770
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-----------QEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 771 QETLLGTIMPEEEsakvcltdvtiMERFQMELKDVERKIAQQAAKLQGI-DLDRTVQQVNQEKQEKQHKLDTVSSKIEL- 848
Cdd:COG4717 121 LEKLLQLLPLYQE-----------LEALEAELAELPERLEELEERLEELrELEEELEELEAELAELQEELEELLEQLSLa 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 849 NRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQlEEQTVELSTEVQSLYREIKDAKEQ----------------- 911
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLlliaaallallglggsl 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 912 -------------------VSPLETTLEKFQQEKE-ELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKD-IENYIQDGKD 970
Cdd:COG4717 269 lsliltiagvlflvlgllaLLFLLLAREKASLGKEaEELQALPALEELEEEELEELLAALGLPPDLSPEeLLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 971 dyKKQKETELNKVIAQLsECEKHKEKINEDMRLMRQDIDTQ--KIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQM 1048
Cdd:COG4717 349 --LQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1049 QVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELRepqFRDAEEKYREMMIVMRTTELVNKDLDIYYKTL 1128
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---LAELLQELEELKAELRELAEEWAALKLALELL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1129 DQAIMKFHSMKMEEINKIIRDLWRSTYRGqdiEYIEIRSDADENVSASDKRRNYnYRVVMLkgdtaldmrgrcSAGQKVL 1208
Cdd:COG4717 503 EEAREEYREERLPPVLERASEYFSRLTDG---RYRLIRIDEDLSLKVDTEDGRT-RPVEEL------------SRGTREQ 566
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 1209 ASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRsqqrnfQLLVITHDEDFVELLG 1278
Cdd:COG4717 567 LYLALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGR------QVIYFTCHEELVELFQ 630
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
224-944 |
5.67e-03 |
|
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: 41.16 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 224 RDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNL----SKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVfqg 299
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELeklnNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI--- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 300 tdeqlndlyhNHQRtvREKERKLVDchreLEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLE 379
Cdd:TIGR04523 193 ----------KNKL--LKLELLLSN----LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 380 ldgfergPFSERQIKNFHKLvrERQEGEAKTANQLMNDfaeketlKQKQIDEIRDKktglgrIIELKSEilsKKQNELKN 459
Cdd:TIGR04523 257 -------QLKDEQNKIKKQL--SEKQKELEQNNKKIKE-------LEKQLNQLKSE------ISDLNNQ---KEQDWNKE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 460 VKYELQQLEgssDRILELDQELIKAERELSkaEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQ-M 538
Cdd:TIGR04523 312 LKSELKNQE---KKLEEIQNQISQNNKIIS--QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQeI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 539 EMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRK 618
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 619 EEQLSSYEDKLfdvcgsQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrVFQTEAELQEVI 698
Cdd:TIGR04523 467 ETQLKVLSRSI------NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-------LKEKIEKLESEK 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 699 SDLQSKLRLAPDKLKSTESELKKK--EKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLG 776
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 777 TIMPEEESAKvcltdvtimerfqmelkDVERKIAQQAAKLQGiDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQ 856
Cdd:TIGR04523 614 SLEKELEKAK-----------------KENEKLSSIIKNIKS-KKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 857 QEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEqtvelstevqslyreIKDAKEQVSPLettLEKFQQEKEELINKKNTS 936
Cdd:TIGR04523 676 DDIIELMKDWLKELSLHYKKYITRMIRIKDLPK---------------LEEKYKEIEKE---LKKLDEFSKELENIIKNF 737
|
....*...
gi 19924129 937 NKIAQDKL 944
Cdd:TIGR04523 738 NKKFDDAF 745
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-619 |
6.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 170 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIR---DQITSKEAQLTSSKEIVKSYEN 246
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAKKKAEE 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 247 --ELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQlndlyhnhQRTVREKERKLVD 324
Cdd:PTZ00121 1430 kkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--------KKKAEEAKKKADE 1501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 325 CHRELEKLNKESRLLNQEKS----ELLVEQGRLQLQADRHQEHIRARDSL--IQSLATQLELDGFERGPFSERQIKNFHK 398
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 399 LVRERQEGEAKTANQLMNDFAEKETLKQKQI---DEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRIL 475
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 476 ELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKI 555
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19924129 556 KSRHSDELTSLLGyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKE 619
Cdd:PTZ00121 1742 DKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-53 |
6.03e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 6.03e-03
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
713-911 |
8.59e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 713 KSTESELKKKEKRRDemlglvpmrqSIIDLKEKEIPEL-RNKLQNVNRDIQRLKNDIEEQetllgtimpeeesakvcltd 791
Cdd:PRK12704 27 KIAEAKIKEAEEEAK----------RILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKE-------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 792 vtIMERFQmELKDVERKIAQQAAKL--QGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNE 869
Cdd:PRK12704 77 --LRERRN-ELQKLEKRLLQKEENLdrKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19924129 870 lkseklqistnlQRRQQLEEQTV-ELSTEVQSLYREI-KDAKEQ 911
Cdd:PRK12704 154 ------------EAKEILLEKVEeEARHEAAVLIKEIeEEAKEE 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
34-65 |
8.61e-03 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 39.68 E-value: 8.61e-03
10 20 30
....*....|....*....|....*....|..
gi 19924129 34 LVGPNGAGKTTIIEclkyICTGDFPPgTKGNT 65
Cdd:COG1119 34 ILGPNGAGKSTLLS----LITGDLPP-TYGND 60
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
34-82 |
8.83e-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: 8.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 19924129 34 LVGPNGAGKTTIIECLkyicTGDFPPgTKGNTFV--HDPKvAQETDVRAQI 82
Cdd:cd03230 31 LLGPNGAGKTTLIKII----LGLLKP-DSGEIKVlgKDIK-KEPEEVKRRI 75
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
31-63 |
8.87e-03 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 39.34 E-value: 8.87e-03
10 20 30
....*....|....*....|....*....|...
gi 19924129 31 LTILVGPNGAGKTTIIECLkyicTGDFPPgTKG 63
Cdd:cd03219 28 IHGLIGPNGAGKTTLFNLI----SGFLRP-TSG 55
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
31-61 |
9.00e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 39.37 E-value: 9.00e-03
10 20 30
....*....|....*....|....*....|.
gi 19924129 31 LTILVGPNGAGKTTIIECLkyicTGDFPPGT 61
Cdd:PRK13548 30 VVAILGPNGAGKSTLLRAL----SGELSPDS 56
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1192-1269 |
9.02e-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: 9.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19924129 1192 DTALDMRG-RCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1269
Cdd:COG1132 467 DTVVGERGvNLSGGQRQ------RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT------TIVIAH 533
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
34-97 |
9.07e-03 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 39.28 E-value: 9.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19924129 34 LVGPNGAGKTTIIECLkyiCTGDFPPGTKGNTFVHDpKVAQETDVRAQIRLQFRD--VNGELIAVQ 97
Cdd:cd03265 31 LLGPNGAGKTTTIKML---TTLLKPTSGRATVAGHD-VVREPREVRRRIGIVFQDlsVDDELTGWE 92
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1200-1277 |
9.52e-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: 9.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1200 RCSAGQKvlasliIRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSqQRNFQLLVITHDEDFVELL 1277
Cdd:cd03230 95 KLSGGMK------QRLALAQALLHDPELLILDEPTSGLDPES----RREFWELLRELK-KEGKTILLSSHILEEAERL 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1214-1271 |
9.70e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 39.38 E-value: 9.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19924129 1214 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVeiikSRSQQRNFQLLVITHDE 1271
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF----SLNREHGTTLILVTHDL 207
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
662-890 |
9.71e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 662 ATAVYSQFITQLTDENQsccpvcQRVFQTEAELQEVISDLQSKLRLAPDKLksteSELKKKEKrrdemlglvpmrqsIID 741
Cdd:COG3206 154 ANALAEAYLEQNLELRR------EEARKALEFLEEQLPELRKELEEAEAAL----EEFRQKNG--------------LVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 742 LKEkEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTI---MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 818
Cdd:COG3206 210 LSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALraqLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924129 819 -----IDLDRTVQQVNQE-KQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQIS-------------- 878
Cdd:COG3206 289 nhpdvIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlerevevarelye 368
|
250
....*....|..
gi 19924129 879 TNLQRRQQLEEQ 890
Cdd:COG3206 369 SLLQRLEEARLA 380
|
|
| |
