|
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: 1843.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 2 SRIEKMSILGVRSFGIEDKDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 81
Cdd:TIGR00606 1 AKFLKMSILGVRSFGIEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 82 IRLQFRDVNGEMVAVHRSMLCSQKNKKTEFKTLEGVITRMKHGEKVSLSSKCAEIDREMISCLGVSKSVLNNVIFCHQED 161
Cdd:TIGR00606 81 IRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 162 SNWPLSEGKALKQKFDEIFSATRYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIV 241
Cdd:TIGR00606 161 SNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 242 RSYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVFQGTDEQLNDLYHNHQRTVREKERR 321
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 322 LVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLELDGFERGPFSERQIKNFHELVK 401
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 402 ERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQEL 481
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 482 TKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKSRHSD 561
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 562 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDLESD 641
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 642 LGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKK 721
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 722 KERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME 801
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 802 LKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNL 881
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 882 QRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKVKNIHGYMKDI 961
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 962 ENYIQDGKDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNLTLRKRRDELKEVEEERKQH 1041
Cdd:TIGR00606 961 ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQH 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1042 LKEMGQMQVLQMKNEHQKLEENIDTIKRNHSLALGRQKGYEDEILHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1121
Cdd:TIGR00606 1041 LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1122 DIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRC 1201
Cdd:TIGR00606 1121 DIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRC 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1202 SAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSE 1281
Cdd:TIGR00606 1201 SAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSE 1280
|
1290 1300 1310
....*....|....*....|....*....|.
gi 153945822 1282 YVEKFYRVKKNMDQCSEIVKCSISSLGSYVH 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 |
9.14e-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: 9.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1195 LDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIEslaHALVEIIKSRSQQRNFQLLVITHDEDFV 1274
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIE---ESLAEIIEERKSQKNFQLIVITHDEELV 186
|
90 100
....*....|....*....|...
gi 153945822 1275 ELLGrseyveKFYRVKKNMDQCS 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 |
2.37e-36 |
|
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: 136.58 E-value: 2.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 4 IEKMSILGVRSFgiedKDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNtfVHDPKVAQETDVRAQIR 83
Cdd:cd03240 1 IDKLSIRNIRSF----HERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGG--AHDPKLIREGEVRAQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 84 LQFRDVNGEMVAVHRSMlcsqknkktefktlegvitrmkhgekvslsskcaeidremisclgvskSVLNNVIFCHQEDSN 163
Cdd:cd03240 75 LAFENANGKKYTITRSL------------------------------------------------AILENVIFCHQGESN 106
|
...
gi 153945822 164 WPL 166
Cdd:cd03240 107 WPL 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-1155 |
3.87e-21 |
|
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: 100.52 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 316 REKERRLVDCQRELEKLNKEARllnqekaELLVEQGRLQLQADRHQEHIRARDSLiqslaTHLELDgfergpfseRQIKN 395
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILN-------ELERQLKSLERQAEKAERYKELKAEL-----RELELA---------LLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 396 FHELVKERQE--REAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEIL-------TKKQSELRHVRSELQQ 466
Cdd:TIGR02168 234 LEELREELEElqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneiSRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 467 LEGS----SDRILELDQELTKAERELSKAEKNSS-----IETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHH------ 531
Cdd:TIGR02168 314 LERQleelEAQLEELESKLDELAEELAELEEKLEelkeeLESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlel 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 532 --TTTRTQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKN 609
Cdd:TIGR02168 394 qiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 610 HINNELKKKEEQLSSYEDKLFDVCGSQDLESDLGRLKEEIEKSSKQramLAGATAVYSQFITqlTDENqsccpvcqrvFQ 689
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG---LSGILGVLSELIS--VDEG----------YE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 690 TEAE------LQEVISDLQSKLRLAPDKLKSTESEL-----------KKKERRRDEMLGLVPVRQSIIDLKEKEIPELRN 752
Cdd:TIGR02168 537 AAIEaalggrLQAVVVENLNAAKKAIAFLKQNELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 753 RLQS------VNRDIQ---RLKNDIEEQETLL----------GTIMPEEESakvclTDVTIMERfQMELKDVERKIAQQA 813
Cdd:TIGR02168 617 ALSYllggvlVVDDLDnalELAKKLRPGYRIVtldgdlvrpgGVITGGSAK-----TNSSILER-RREIEELEEKIEELE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 814 AKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTN-----------ELKSEKLQIATNLQ 882
Cdd:TIGR02168 691 EKIA--ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeriaqlskELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 883 RRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEEL---IHRKHTSNKMAQDKINDIKEKVKNIHGYMK 959
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 960 DIENYI------QDGKDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTqkiqerWLQDNLTLRKRRDELKE 1033
Cdd:TIGR02168 849 ELSEDIeslaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE------LESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1034 VEEERKQHLK--EMGQMQVLQMKNEHQKLEEniDTIKRNHSLALGRQKGYEDEILHFKKELRE---------PQFRDAEE 1102
Cdd:TIGR02168 923 KLAQLELRLEglEVRIDNLQERLSEEYSLTL--EEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaiEEYEELKE 1000
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 153945822 1103 KYREMmivmrTTELvnKDLDIYYKTLDQAImkfhsmkmEEINKIIRDLWRSTY 1155
Cdd:TIGR02168 1001 RYDFL-----TAQK--EDLTEAKETLEEAI--------EEIDREARERFKDTF 1038
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-215 |
2.57e-19 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 87.17 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 7 MSILGVRSFgiedkDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGDFP---PGTKGNTFVHDPKVAQETDVRAQIR 83
Cdd:pfam13476 1 LTIENFRSF-----RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSrlkRKSGGGFVKGDIRIGLEGKGKAYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 84 LQFRDVNGE-MVAVHRSMLCSQKNKKTEFKTLEGVITRmkhgekvslsskcaEIDREMISCLGVSKSVLNNVIFCHQEDS 162
Cdd:pfam13476 76 ITFENNDGRyTYAIERSRELSKKKGKTKKKEILEILEI--------------DELQQFISELLKSDKIILPLLVFLGQER 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153945822 163 NWPLSEgkalKQKFDEIFSATRYIKALDTLRQVRQTQgQKVKECQTELKYLKQ 215
Cdd:pfam13476 142 EEEFER----KEKKERLEELEKALEEKEDEKKLLEKL-LQLKEKKKELEELKE 189
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-1137 |
3.95e-19 |
|
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: 93.98 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 4 IEKMSILGVRSFGiedkDKQIISFFSPLTILVGPNGAGKTTIIECLKyictgdFPPGTKGNT---------FVHDPKVAQ 74
Cdd:TIGR02169 2 IERIELENFKSFG----KKKVIPFSKGFTVISGPNGSGKSNIGDAIL------FALGLSSSKamraerlsdLISNGKNGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 75 ---ETDVRAQIRLQFRDVNGEMVaVHRSMLCSQKNKKTEFKTlegvitrmkHGEKVSLSskcaEIDrEMISCLGVSKSVL 151
Cdd:TIGR02169 72 sgnEAYVTVTFKNDDGKFPDELE-VVRRLKVTDDGKYSYYYL---------NGQRVRLS----EIH-DFLAAAGIYPEGY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 152 NNVIfchQEDSNWPLS-EGKALKQKFDEIFSATRY----IKALDTLRQVRQTQGQ---KVKECQTELKYLKQNKEKAceI 223
Cdd:TIGR02169 137 NVVL---QGDVTDFISmSPVERRKIIDEIAGVAEFdrkkEKALEELEEVEENIERldlIIDEKRQQLERLRREREKA--E 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 224 RDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVfqGTDEQ 303
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL--GEEEQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 304 LndlyhNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQadrhqehirardslIQSLATHLELDGF 383
Cdd:TIGR02169 290 L-----RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE--------------IEELEREIEEERK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 384 ERGPFSERQIKNFHELVKERQEREAKTASqlLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSE 463
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKE--FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 464 LQQLEgssDRILELDQELTKAERELSKAEKNssietlkaeVMSLQNEKADLDRSLRKLDQEMEQLNhhtttrtqmemltK 543
Cdd:TIGR02169 429 IAGIE---AKINELEEEKEDKALEIKKQEWK---------LEQLAADLSKYEQELYDLKEEYDRVE-------------K 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 544 DKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLhsksKEINQTRDRLAKLNKELASAEQNK--NHINNELKKKEEQ 621
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI----QGVHGTVAQLGSVGERYATAIEVAagNRLNNVVVEDDAV 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 622 LSSYEDKLFDVCGSQDLESDLGRLKeeieksSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAelqeVISDL 701
Cdd:TIGR02169 560 AKEAIELLKRRKAGRATFLPLNKMR------DERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTL----VVEDI 629
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 702 QSKLRLAPD-KLKSTESELKKKE------RRRDEMLGLVPVRQsiidlkEKEIPELRNRLQSVNRDIQRLKNDIEEQETL 774
Cdd:TIGR02169 630 EAARRLMGKyRMVTLEGELFEKSgamtggSRAPRGGILFSRSE------PAELQRLRERLEGLKRELSSLQSELRRIENR 703
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 775 LgtimpeeESAKVCLTDVTIM-ERFQMELKDVERKIAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIElnrkli 853
Cdd:TIGR02169 704 L-------DELSQELSDASRKiGEIEKEIEQLEQEEEKLKERLE--ELEEDLSSLEQEIENVKSELKELEARIE------ 768
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 854 qDQQEQIQHLKSKTNELKSEKLQiatnlQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRk 933
Cdd:TIGR02169 769 -ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ- 841
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 934 htsNKMAQDKINDIKEKVKNIHGYMKDIENYIqdgkddykKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKI 1013
Cdd:TIGR02169 842 ---RIDLKEQIKSIEKEIENLNGKKEELEEEL--------EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1014 QERWLQDNLTLRKRR-----DELKEVEEERKQHLKEMGQMQVL-QMKNEHQKLEENIDTIKRNHSLALgrqKGYEDEILH 1087
Cdd:TIGR02169 911 QIEKKRKRLSELKAKlealeEELSEIEDPKGEDEEIPEEELSLeDVQAELQRVEEEIRALEPVNMLAI---QEYEEVLKR 987
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 153945822 1088 FkKELREPQFRDAEEKYRemmIVMRTTELVNKDLDIYYKTLDQAIMKFHS 1137
Cdd:TIGR02169 988 L-DELKEKRAKLEEERKA---ILERIEEYEKKKREVFMEAFEAINENFNE 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-931 |
8.50e-18 |
|
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: 89.73 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 181 SATRYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEI-- 258
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILre 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 259 --EHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEkVFQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEA 336
Cdd:TIGR02168 310 rlANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 337 RLLNQEKA-------ELLVEQGRLQLQADRHQEHIRARDSLIQSLA---THLELDGFERGPFSERQIKNFHELVKERQER 406
Cdd:TIGR02168 389 AQLELQIAslnneieRLEARLERLEDRRERLQQEIEELLKKLEEAElkeLQAELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 407 EAKTASQLLSDLTDKEALKQRQLDELRD---RKSGLGRTIelKTEILTKKQ--------SELRHVRSELQQ-----LEGS 470
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERlqeNLEGFSEGV--KALLKNQSGlsgilgvlSELISVDEGYEAaieaaLGGR 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 471 SDRILELDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQMEML--------- 541
Cdd:TIGR02168 547 LQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvl 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 542 -TKDKTDKDEQIRKIKSRHSdeLTSLLGYFPNKkqleDWLHSKSKE-----INQTRDRLAKLNKELASAEQNKNHINNEL 615
Cdd:TIGR02168 627 vVDDLDNALELAKKLRPGYR--IVTLDGDLVRP----GGVITGGSAktnssILERRREIEELEEKIEELEEKIAELEKAL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 616 KKKEEQLSSYEDKLFDV-CGSQDLESDLGRLKEEIEKSSKQRAMLAgatavysQFITQLTDENqsccpvcqrvfqteAEL 694
Cdd:TIGR02168 701 AELRKELEELEEELEQLrKELEELSRQISALRKDLARLEAEVEQLE-------ERIAQLSKEL--------------TEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 695 QEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETL 774
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 775 LGTIMPEEESAKVcltdvtIMERFQMELKDVERKIAQQAAKLQGVDLDRTVQQV-----NQEKQEKQHRLDTVTSKIELN 849
Cdd:TIGR02168 840 LEDLEEQIEELSE------DIESLAAEIEELEELIEELESELEALLNERASLEEalallRSELEELSEELRELESKRSEL 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 850 RKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQSVE-----LSTEVQSLNREIKDAKEQISPL----ETALE 920
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEalenkIEDDEEEARRRLKRLENKIKELgpvnLAAIE 993
|
810
....*....|.
gi 153945822 921 KLQQEKEELIH 931
Cdd:TIGR02168 994 EYEELKERYDF 1004
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-772 |
9.63e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 3 RIEKMSILGVRSfgiedKDKQIISFFSPLTILVGPNGAGKTTIIECLK---YICTGDFPPGTKGNTFVHDPKVaqetdvR 79
Cdd:PRK03918 2 KIEELKIKNFRS-----HKSSVVEFDDGINLIIGQNGSGKSSILEAILvglYWGHGSKPKGLKKDDFTRIGGS------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 80 AQIRLQFrDVNGEMVAVHRSmlcSQKNKKTeFKTLEGVITRMKHGEKVSlsskcAEIDREmisclgVSKSVLNNVIFCHQ 159
Cdd:PRK03918 71 TEIELKF-EKNGRKYRIVRS---FNRGESY-LKYLDGSEVLEEGDSSVR-----EWVERL------IPYHVFLNAIYIRQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 160 EDSNWPLSEGKALKQKFDEIFSATRYIKALDTLRQVRqtqgqkvKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQE 239
Cdd:PRK03918 135 GEIDAILESDESREKVVRQILGLDDYENAYKNLGEVI-------KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 240 IVRSYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMekvfQGTDEQLNDLyHNHQRTVREKE 319
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI----RELEERIEEL-KKEIEELEEKV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 320 RRLvdcqRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLELDGFERGPFSERQIKnfhel 399
Cdd:PRK03918 283 KEL----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR----- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 400 vKERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILEldq 479
Cdd:PRK03918 354 -LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE--- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 480 ELTKAE-------RELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNhhtTTRTQMEMLTKDKTDKDeQI 552
Cdd:PRK03918 430 ELKKAKgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE---KVLKKESELIKLKELAE-QL 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 553 RKIKSRhsdeltsLLGYfpNKKQLEdwlhSKSKEINQTRDRLAKLNKELASAEQN----------KNHINNELKKKEEQL 622
Cdd:PRK03918 506 KELEEK-------LKKY--NLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKElekleelkkkLAELEKKLDELEEEL 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 623 SSYEDKLFDVcGSQDLESDLGRLKeEIEKSSKQRAMLAGATavysqfiTQLTDENQSCCPVCQRVFQTEAELQEVISDLQ 702
Cdd:PRK03918 573 AELLKELEEL-GFESVEELEERLK-ELEPFYNEYLELKDAE-------KELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 703 sKLRLAPDKLKSTESElKKKERRRDEMLGLvpvrQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQE 772
Cdd:PRK03918 644 -ELRKELEELEKKYSE-EEYEELREEYLEL----SRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1197-1298 |
5.21e-15 |
|
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: 73.93 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1197 MRGRCSAGQKVLASLIIRLALAEtfCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNfQLLVITHDEDFVEL 1276
Cdd:cd03227 74 TRLQLSGGEKELSALALILALAS--LKPRPLYILDEIDRGLDPRD----GQALAEAILEHLVKGA-QVIVITHLPELAEL 146
|
90 100
....*....|....*....|..
gi 153945822 1277 LgrseyvEKFYRVKKNMDQCSE 1298
Cdd:cd03227 147 A------DKLIHIKKVITGVYK 162
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
313-929 |
8.08e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 313 RTVREKERRlvdcqRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLELDGFErgpfSERQ 392
Cdd:COG1196 216 RELKEELKE-----LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE----LEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 393 IKNFHELVKE--RQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEgs 470
Cdd:COG1196 287 QAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 471 sDRILELDQELTKAERELskAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLnhhtttRTQMEMLTKDKTDKDE 550
Cdd:COG1196 365 -EALLEAEAELAEAEEEL--EELAEELLEALRAAAELAAQLEELEEAEEALLERLERL------EEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 551 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLf 630
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 631 dvcGSQDLESDLGRLKEEIEKSSKQRAMLAGATAVYSQfitqltdenqsccpvcQRVFQTEAELQEVISDLQSKL----- 705
Cdd:COG1196 515 ---LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ----------------NIVVEDDEVAAAAIEYLKAAKagrat 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 706 RLAPDKLKstESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLlgtimpeEESA 785
Cdd:COG1196 576 FLPLDKIR--ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL-------AGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 786 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKS 865
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945822 866 KTNELKSEKLQIATNLQRRQQMEEQSVELSTE---VQSLNREIKDAKEQISPLET----ALEKLQQEKEEL 929
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEppdLEELERELERLEREIEALGPvnllAIEEYEELEERY 797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
448-1102 |
6.40e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 448 EILTKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSkaEKNSSIETLKAEVMSLQNEKADLDrslrKLDQEMEQ 527
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN--EISSELPELREELEKLEKEVKELE----ELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 528 LnhhtttRTQMEMLTKDKTDKDEQIRKIKSR------HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKEL 601
Cdd:PRK03918 243 L------EKELESLEGSKRKLEEKIRELEERieelkkEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 602 ASAEQNKNHINNELKKKEEqlssyedklfdvcgsqdLESDLGRLKEEIEKSSKQRAMLAGATAVYsqfitqltdenqscc 681
Cdd:PRK03918 317 SRLEEEINGIEERIKELEE-----------------KEERLEELKKKLKELEKRLEELEERHELY--------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 682 pvcQRVFQTEAELQEVisdlqsKLRLAPDKLKSTESELKKKERRRDEMlglvpvrqsiidlkEKEIPELRNRLQSVNRDI 761
Cdd:PRK03918 365 ---EEAKAKKEELERL------KKRLTGLTPEKLEKELEELEKAKEEI--------------EEEISKITARIGELKKEI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 762 QRLKNDIEEQET------LLGTIMPEEESAKvcltdvtIMERFQMELKDVERKIAQQAAKLQgvdldrtvqqvnqekqEK 835
Cdd:PRK03918 422 KELKKAIEELKKakgkcpVCGRELTEEHRKE-------LLEEYTAELKRIEKELKEIEEKER----------------KL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 836 QHRLDTVTSKIELNRKLIQDQQ--EQIQHLKSKTNELKSEKLQIATNLQRRqqMEEQSVELSTEVQSLNREIKDAKEQIS 913
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEK--LKEKLIKLKGEIKSLKKELEKLEELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 914 PLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKVKNIHGY------MKDIENYIQDGKDDYKKQkETELNGVAVQL 987
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneyleLKDAEKELEREEKELKKL-EEELDKAFEEL 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 988 NECEKHREKINKDMGTMRQDIDTQ---KIQERWLQDNLTLRKRRDELKEVEEERKQHLKEMGQMQvlQMKNEHQKLEENI 1064
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEeyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK--EELEEREKAKKEL 713
|
650 660 670
....*....|....*....|....*....|....*...
gi 153945822 1065 DTIKRnhslALGRQKGYEDEILHFKKELREPQFRDAEE 1102
Cdd:PRK03918 714 EKLEK----ALERVEELREKVKKYKALLKERALSKVGE 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-1171 |
5.79e-13 |
|
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: 73.94 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 390 ERQIKNFhelvkERQEREAKTASQLLSDLTDKE-ALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLE 468
Cdd:TIGR02168 199 ERQLKSL-----ERQAEKAERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 469 gssDRILELDQELTKAERELSkaEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLnhhtttRTQMEMLTKDKTDK 548
Cdd:TIGR02168 274 ---LEVSELEEEIEELQKELY--ALANEISRLEQQKQILRERLANLERQLEELEAQLEEL------ESKLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 549 DEQIRKIKSrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLaklNKELASAEQNKNHINNELKKKEEQLSSYE-- 626
Cdd:TIGR02168 343 EEKLEELKE----ELESLEAELEELEAELEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLEARLERLEdr 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 627 -DKLFDVCGSQDLESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKL 705
Cdd:TIGR02168 416 rERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 706 RLAPDKLKSTESeLKKKERRRDEMLGLVPVRQSIIDLKEK-----EIpELRNRLQSV--------NRDIQRLK-NDIEEQ 771
Cdd:TIGR02168 496 RLQENLEGFSEG-VKALLKNQSGLSGILGVLSELISVDEGyeaaiEA-ALGGRLQAVvvenlnaaKKAIAFLKqNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 772 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVErKIAQQAAK-----LQGVDLDRTVQQVNQEKQEKQHRLDTVTSKI 846
Cdd:TIGR02168 574 TFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV-KFDPKLRKalsylLGGVLVVDDLDNALELAKKLRPGYRIVTLDG 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 847 ELnrkliqdqqeqiqhLKSKTNELKSEKLQIATNLQRRQQMEEqsvelstevqsLNREIKDAKEQISPLETALEKLQQEK 926
Cdd:TIGR02168 653 DL--------------VRPGGVITGGSAKTNSSILERRREIEE-----------LEEKIEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 927 EELIHRKHTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQD---------GKDDYKKQKETELNGVAVQLNECEKHREKI 997
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskeltELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 998 NKDMGTMRQDIDTQKIQERWLQDNLTLRKRRDELKEVEEERKQHLKEMGQMQVLQMKNEHQKLEENIDTIKRNHSLALGR 1077
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1078 QKGYEDEILHFKKELR--EPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFH------SMKMEEINKIIRD 1149
Cdd:TIGR02168 868 IEELESELEALLNERAslEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSE 947
|
810 820
....*....|....*....|..
gi 153945822 1150 LWRSTYRGQDIEYIEIRSDADE 1171
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEE 969
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
190-949 |
1.78e-12 |
|
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: 72.46 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 190 DTLRQVRQTQGQKVKECQTELKYLKQNKEKA-CEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKL 268
Cdd:pfam15921 127 DAMADIRRRESQSQEDLRNQLQNTVHELEAAkCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 269 DNEIKALESRKkqmekdnseLEQKMEKVFQGTDEQLNDLyhnhqrtvrekERRLVDCQRELEKLNKEArllnQEKAELLV 348
Cdd:pfam15921 207 HDSMSTMHFRS---------LGSAISKILRELDTEISYL-----------KGRIFPVEDQLEALKSES----QNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 349 EQgrlqlqadrHQEHIRardsliQSLATH-LELDGF-ERGPFSERQIKNFHELVKERQEREAKTASQLLSDLTDKEALKQ 426
Cdd:pfam15921 263 QQ---------HQDRIE------QLISEHeVEITGLtEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 427 RQLDELRDRKsglgRTIELKTEILTKK----QSELRHVRSELQQLEGSS----DRILELDQELTKAERELS-KAEKNS-- 495
Cdd:pfam15921 328 QLRSELREAK----RMYEDKIEELEKQlvlaNSELTEARTERDQFSQESgnldDQLQKLLADLHKREKELSlEKEQNKrl 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 496 ---------SIETLKAEVMSLQNEKADLDRSLR--------KLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKSR 558
Cdd:pfam15921 404 wdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKamksecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 559 HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDL 638
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 639 ESDLGRLKEEIEKSSKQRAMLAGATAV-YSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLqSKLRLAPDKLKSTES 717
Cdd:pfam15921 564 IEILRQQIENMTQLVGQHGRTAGAMQVeKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV-SDLELEKVKLVNAGS 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 718 E----LKKKERRRDEMLglvpvrqsiidlkeKEIPELRNRLQSVNRDIQRLK----NDIEEQETllgtimpeeesakvcl 789
Cdd:pfam15921 643 ErlraVKDIKQERDQLL--------------NEVKTSRNELNSLSEDYEVLKrnfrNKSEEMET---------------- 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 790 tdvtIMERFQMELKDVERKIAQQAAKL---QGVDLDRTVQQVNQEKQ--EKQHRLDTVTSKIELNRKLIQDQQEQIQHLK 864
Cdd:pfam15921 693 ----TTNKLKMQLKSAQSELEQTRNTLksmEGSDGHAMKVAMGMQKQitAKRGQIDALQSKIQFLEEAMTNANKEKHFLK 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 865 SKTNELKSEKLQIATnlqrrqqmeeQSVELSTEVQSLNREIKDAKEQISPLETALEK--LQ-QEKEELIHRK-HTSNKMA 940
Cdd:pfam15921 769 EEKNKLSQELSTVAT----------EKNKMAGELEVLRSQERRLKEKVANMEVALDKasLQfAECQDIIQRQeQESVRLK 838
|
....*....
gi 153945822 941 QDKINDIKE 949
Cdd:pfam15921 839 LQHTLDVKE 847
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-932 |
2.97e-12 |
|
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: 71.63 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 3 RIEKMSILGVRSFGiedkDKQIISFFSPLTILVGPNGAGKTTIIECLKYIC--------------------TGDFPPGTk 62
Cdd:TIGR02168 1 RLKKLELAGFKSFA----DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLgeqsakalrggkmedvifngSETRKPLS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 63 gntfvhdpkvaqetdvRAQIRLQFRDVNGEMVAVHRSmlcsqknkktefktlEGVITRMKH--GEKVSL--SSKCAEID- 137
Cdd:TIGR02168 76 ----------------LAEVELVFDNSDGLLPGADYS---------------EISITRRLYrdGESEYFinGQPCRLKDi 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 138 REMISCLGVSKSVLNNVifchqedsnwplSEGkalkqKFDEIFSAT----RYI------------KALDTLRQVRQTQG- 200
Cdd:TIGR02168 125 QDLFLDTGLGKRSYSII------------EQG-----KISEIIEAKpeerRAIfeeaagiskykeRRKETERKLERTREn 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 201 -QKV----KECQTELKYLKQNKEKA---CEIRDQItsKEAQLASSQEIVRSYEDELEPLKNRLKEIEHnlsKIMKLDNEI 272
Cdd:TIGR02168 188 lDRLedilNELERQLKSLERQAEKAeryKELKAEL--RELELALLVLRLEELREELEELQEELKEAEE---ELEELTAEL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 273 KALESRKKQMEKDNSELEQKME---KVFQGTDEQLNDLYHNHQRTVREKER----------RLVDCQRELEKLNKEARLL 339
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEelqKELYALANEISRLEQQKQILRERLANlerqleeleaQLEELESKLDELAEELAEL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 340 NQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLeldgfergpfsERQIKNFHELvKERQEREAKTASQLLSDLT 419
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-----------ETLRSKVAQL-ELQIASLNNEIERLEARLE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 420 DKEALKQRQLDELRD--------RKSGLGRTIELKTEILTKKQSELRHVRselQQLEGSSDRILELDQELTKAERELskA 491
Cdd:TIGR02168 411 RLEDRRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELERLE---EALEELREELEEAEQALDAAEREL--A 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 492 EKNSSIETLKaevmSLQNEKADLDRSLRKLDQEMEQLNHHTTT-----------RTQME---------MLTKDKTDKDEQ 551
Cdd:TIGR02168 486 QLQARLDSLE----RLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyEAAIEaalggrlqaVVVENLNAAKKA 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 552 IRKIKS-----RHSDELTSLLGYFPNKKQLEdwlhsKSKEINQTRDRLAKLNKELASAE----------------QNKNH 610
Cdd:TIGR02168 562 IAFLKQnelgrVTFLPLDSIKGTEIQGNDRE-----ILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALE 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 611 INNELkKKEEQLSSYEDKLFDVCGS---QDLESDLGRL--KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcq 685
Cdd:TIGR02168 637 LAKKL-RPGYRIVTLDGDLVRPGGVitgGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELE------- 708
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 686 rvfqteaELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLK 765
Cdd:TIGR02168 709 -------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 766 NDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKLQG-----VDLDRTVQQVNQEKQEKQHRLD 840
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALR------EALDELRAELTLLNEEAANLRERLESlerriAATERRLEDLEEQIEELSEDIE 855
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 841 TVTSKIELNRKLIQDQQEQIQHLkskTNELKSEKLQIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALE 920
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
1050
....*....|..
gi 153945822 921 KLQQEKEELIHR 932
Cdd:TIGR02168 933 GLEVRIDNLQER 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-527 |
7.14e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 218 EKACEIRDQITSKEAQLASSQeiVRSYEDELEPLKNRLKEIEhnlskimkldNEIKALESRKKQMEKDNSELEQKMekvf 297
Cdd:COG1196 213 ERYRELKEELKELEAELLLLK--LRELEAELEELEAELEELE----------AELEELEAELAELEAELEELRLEL---- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 298 qgtdEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATH 377
Cdd:COG1196 277 ----EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 378 LELDGFERGpFSERQIKNFHELVKERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSEL 457
Cdd:COG1196 353 LEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 458 RHVRSELQQLEGSSDRILELDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQ 527
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-537 |
4.35e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 187 KALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQItskEAQLASSQEIVRSYEDELEPLKNRLKEIEhnlSKIM 266
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL---SKELTELEAEIEELEERLEEAEEELAEAE---AEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 267 KLDNEIKALESRKKQMEKDNSELEQKMEkvfqgtdeQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAEL 346
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 347 LVEQGRLQLQADRHQEHIRARDSLIQSLATHLELDGFERGPFSERQIKNFHELVKERQEREAKTASqlLSDL-TDKEALK 425
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK--LAQLeLRLEGLE 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 426 QR---QLDELRDRKSGLGRTIELKTEILTKKQSELRHvrsELQQLEGSSDRILELDQEltkAERELskaeknssiETLKA 502
Cdd:TIGR02168 936 VRidnLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGPVNLA---AIEEY---------EELKE 1000
|
330 340 350
....*....|....*....|....*....|....*
gi 153945822 503 EVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQ 537
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
170-604 |
5.13e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 170 KALKQKFDEIFSAT-----RYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSY 244
Cdd:COG4717 49 ERLEKEADELFKPQgrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 245 ED--ELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVFQGTDEQLNDLYHNHQRTVREKERRL 322
Cdd:COG4717 129 PLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 323 VDCQRELEKLNKEARLLNQEKAELlveqgRLQLQADRHQEHIRARDSLIQSLATHLELDGFERGPFSER----------- 391
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 392 QIKNFHELVKERQEREAKTASQLLSDLTDKEALKQRQLDELRDRksgLGRTIELKTEILTKKQSELRHVRSELQQLEGSS 471
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA---LGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 472 DRILEldQELTKAERELSKAEKNSSIETL------KAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQMEMLTKDK 545
Cdd:COG4717 361 EELQL--EELEQEIAALLAEAGVEDEEELraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945822 546 TDKDEQIRKIKSRHSD--ELTSLLGYFPNKKQLEDWLHskskEINQTRDRLAKLNKELASA 604
Cdd:COG4717 439 EELEELEEELEELREElaELEAELEQLEEDGELAELLQ----ELEELKAELRELAEEWAAL 495
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-85 |
5.38e-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: 62.38 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 6 KMSILGVRSFGIEdkdkQIISFFSP-LTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRL 84
Cdd:cd03227 1 KIVLGRFPSYFVP----NDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRL 76
|
.
gi 153945822 85 Q 85
Cdd:cd03227 77 Q 77
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
20-902 |
5.98e-11 |
|
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: 67.30 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 20 KDKQIISF--FSPLTILVGPNGAGKTTIIECLKYICTGDFPpgTKGNTFVHDPKVAQETDVRAQIRLQFrDVNGEMVAVH 97
Cdd:TIGR00618 15 KGTHTIDFtaLGPIFLICGKTGAGKTTLLDAITYALYGKLP--RRSEVIRSLNSLYAAPSEAAFAELEF-SLGTKIYRVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 98 RSMLCSQKNKKTEfkTLEGVITRMKHGEKVSLSSKCAEIDREMISCLGVSKSVLNNVIFchqedsnwpLSEGKalkqkfd 177
Cdd:TIGR00618 92 RTLRCTRSHRKTE--QPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVL---------LPQGE------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 178 eifsATRYIKALDTLRqvrqtqgqkvKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKE 257
Cdd:TIGR00618 154 ----FAQFLKAKSKEK----------KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 258 IEHNLSKimkldnEIKALESRKKQMEKDNSELEQKMEKVFQGTD-EQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEA 336
Cdd:TIGR00618 220 RKQVLEK------ELKHLREALQQTQQSHAYLTQKREAQEEQLKkQQLLKQLRARIEELRAQEAVLEETQERINRARKAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 337 RLLNQEKAELLVEQGRLQLQAdRHQEHIRARDSLIQSLATHLELD-GFERGPFSERQIKNFHELVKERQEREAKTASQLL 415
Cdd:TIGR00618 294 PLAAHIKAVTQIEQQAQRIHT-ELQSKMRSRAKLLMKRAAHVKQQsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 416 SDLTDKEALKQRQLDElrdrksglgRTIELKTEILTKKQSELRHVRSElQQLEGSSDRILELDQELTKAERELSKAEKNS 495
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQK---------TTLTQKLQSLCKELDILQREQAT-IDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 496 SIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNhhtttrtQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLG---YFPN 572
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-------TKEQIHLQETRKKAVVLARLLELQEEPCPLCGsciHPNP 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 573 KKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDV--------CGSQDLESDLGR 644
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrskEDIPNLQNITVR 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 645 LKEEIEKSSKQRAMLAGAtavySQFITQLTDENQSCCPVCQRVFQTEAELQEVISDL-QSKLRLAPDK-----LKSTESE 718
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACE----QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhALQLTLTQERvrehaLSIRVLP 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 719 LKKKERRRDEMLGLVPVRQSIIDLKEkEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERF 798
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 799 QMELKDVERKIAQQAAKLQGV----------DLDRTVQQVNQEKQEKQHRLDTVTSKIE---------LNRKLIQDQQE- 858
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTaalqtgaelsHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipsdediLNLQCETLVQEe 830
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 153945822 859 -----QIQHLKSKTNELKSEKLQIATNLQRRQQMEEQSVELSTEVQSLN 902
Cdd:TIGR00618 831 eqflsRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-929 |
7.06e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 396 FHELVKERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTI--------ELKTEI------LTKKQSELRHVR 461
Cdd:COG1196 215 YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleaeleELRLELeeleleLEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 462 SELQQLEGSSDRILELDQEL--TKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNH--------H 531
Cdd:COG1196 295 AELARLEQDIARLEERRRELeeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEalleaeaeL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 532 TTTRTQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHI 611
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 612 NNELKKKEEQLSSYEDKLfdvcgsQDLESDLGRLKEEIEKSSKQRAMLAGATAVYSQFI-----TQLTDENQSCCPVCQR 686
Cdd:COG1196 455 EEEEEALLELLAELLEEA------ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegvkaALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 687 VFQTEAELQEVISD-----LQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQ-SIIDLKEKEIPELRNRLQSVNRD 760
Cdd:COG1196 529 LIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRArAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 761 IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVE------RKIAQQAAKLQGVDLDRTVQQVNQEKQE 834
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 835 KQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEqisp 914
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE---- 764
|
570
....*....|....*
gi 153945822 915 LETALEKLQQEKEEL 929
Cdd:COG1196 765 LERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-622 |
7.93e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 263 SKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVfQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQE 342
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 343 KAELLVEQGRLQLQadrhqehIRARDSLIQSLATHLELDgfergpfsERQIKNFHELVkERQEREAKTASQLLSDLTDKE 422
Cdd:TIGR02168 749 IAQLSKELTELEAE-------IEELEERLEEAEEELAEA--------EAEIEELEAQI-EQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 423 ALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSsdrILELDQELTKAEREL-----SKAEKNSSI 497
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE---IEELEELIEELESELeallnERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 498 ETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHtttRTQMEM-LTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQL 576
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 153945822 577 EDWLHSKSKEINQTRDRLAKLN----KELASAEQNKNHINNE---LKKKEEQL 622
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELGPVNlaaiEEYEELKERYDFLTAQkedLTEAKETL 1019
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
497-1272 |
2.74e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 497 IETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNhhtttrtQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQL 576
Cdd:PRK01156 175 IDMLRAEISNIDYLEEKLKSSNLELENIKKQIA-------DDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 577 EDWLHSKSKEINQTRDRLA----KLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVcgsQDLESDLGRLKEEIEKS 652
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSmeleKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDI---ENKKQILSNIDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 653 SKQRAMLAGATAVYSQFITQLTDENQsccpvcqrVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGL 732
Cdd:PRK01156 325 HAIIKKLSVLQKDYNDYIKKKSRYDD--------LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 733 VPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDI------EEQETLLGTIMPEEESAKVCLTDV------TIMERFQM 800
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIralrenLDELSRNMEMLNGQSVCPVCGTTLgeeksnHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 801 ELKDVERKIAQqaaklqgvdLDRTVQQVNQEKQEKQHRLDTVTSKiELNRKLIQDQQeqiqhLKSKTNELKSEKLQIATN 880
Cdd:PRK01156 477 KKSRLEEKIRE---------IEIEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNK-----IESARADLEDIKIKINEL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 881 LQRRQQMEEqsveLSTEVQSLNREIKDAK--------EQISPLEtaLEKLQQEKEELihrkhtsnkmaQDKINDIKEKVK 952
Cdd:PRK01156 542 KDKHDKYEE----IKNRYKSLKLEDLDSKrtswlnalAVISLID--IETNRSRSNEI-----------KKQLNDLESRLQ 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 953 NIHGYMKDIENYIqdgkDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQdidtqkiqerwlqdnltLRKRRDELK 1032
Cdd:PRK01156 605 EIEIGFPDDKSYI----DKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN-----------------YKKQIAEID 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1033 EVEEERKQHlkemgQMQVLQMKNEHQKLEENIDTIKRNHslalgrqkgYEDEILHFKKELREPQFRDAEEKYREMMIVMR 1112
Cdd:PRK01156 664 SIIPDLKEI-----TSRINDIEDNLKKSRKALDDAKANR---------ARLESTIEILRTRINELSDRINDINETLESMK 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1113 TTELVNKDLDIYYKTLDQAIMKfhSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSAsdkrrnynYRVVMLKGD 1192
Cdd:PRK01156 730 KIKKAIGDLKRLREAFDKSGVP--AMIRKSASQAMTSLTRKYLFEFNLDFDDIDVDQDFNITV--------SRGGMVEGI 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1193 TALdmrgrcSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSQQRnfQLLVITHDED 1272
Cdd:PRK01156 800 DSL------SGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIP--QVIMISHHRE 871
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1202-1283 |
6.27e-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: 59.18 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVELLGRSE 1281
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-----AEEGRTVIIVTHDPELAELAADRV 150
|
..
gi 153945822 1282 YV 1283
Cdd:cd00267 151 IV 152
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
183-771 |
8.88e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 183 TRYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNL 262
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 263 SKIMKLDNEIKALESRKKQMEKDNSELeQKMEKVFQGTDEQLNDLyhnhqrtvrekERRLvdcqRELEKLNKEARLLNQE 342
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGI-----------EERI----KELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 343 KAELLVEQGRLQlqaDRHQEHIRARdsliqSLATHLELDGFERGPFSERQIKNFHELVKERQ---EREAKTASQLLSDLT 419
Cdd:PRK03918 347 LKELEKRLEELE---ERHELYEEAK-----AKKEELERLKKRLTGLTPEKLEKELEELEKAKeeiEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 420 DKEALKQRQLDELRDRKS-----GLGRTIELKTEILTKKQSELRHVRSELQQLEgssDRILELDQELTKAERELSKAEKN 494
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIE---EKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 495 SSIETLKAEVMSLQNEKADLDrsLRKLDQEMEQLNhhtttrtqmemLTKDKTDKdeqIRKIKSRHSDELTSLLGYFPNKK 574
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYN--LEELEKKAEEYE-----------KLKEKLIK---LKGEIKSLKKELEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 575 QLEDWLHSKSKEinqtrdrLAKLNKELasaEQNKNHINNELKKKEEQLSSYEDKLFDVCGS-QDLESDLGRLKEEIEKSS 653
Cdd:PRK03918 560 ELEKKLDELEEE-------LAELLKEL---EELGFESVEELEERLKELEPFYNEYLELKDAeKELEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 654 KQRAMLAGATAVYSQFITQLTDENQSCCP-VCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEmlgl 732
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE---- 705
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 153945822 733 vpvrqsiIDLKEKEIPEL---RNRLQSVNRDIQRLKNDIEEQ 771
Cdd:PRK03918 706 -------REKAKKELEKLekaLERVEELREKVKKYKALLKER 740
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1202-1275 |
1.07e-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: 58.23 E-value: 1.07e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1275
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYFLD 131
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
719-1070 |
1.22e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 719 LKKKERRRDEMLGLVPVRQSIIDLkEKEIPELRNRLQSVNR------DIQRLKNDIEEQETLLGTIMPEEESAKvcltdv 792
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRL-EDILNELERQLKSLERqaekaeRYKELKAELRELELALLVLRLEELREE------ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 793 tiMERFQMELKDVERKIAQQAAKLQGVDLDrtVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKS 872
Cdd:TIGR02168 241 --LEELQEELKEAEEELEELTAELQELEEK--LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 873 EKLQIATnlqRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKVK 952
Cdd:TIGR02168 317 QLEELEA---QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 953 NIHGYMKDIENYIQDGKDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNL-TLRKRRDEL 1031
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALeELREELEEA 473
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 153945822 1032 KEVEEERKQHLKEMGQMQVL--QMKNEHQKLEENIDTIKRN 1070
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSleRLQENLEGFSEGVKALLKN 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
326-1298 |
1.82e-09 |
|
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: 62.30 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 326 QRELEKLNKEARLLNQEKAELLVEQGRLQL-QADRHQEHIRARDSLIQSLATHLELDGFERGPFSERQIKNFHELVKERQ 404
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLdYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 405 EREAKTASQLLsdLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDrILELDQELTKA 484
Cdd:pfam02463 280 EKKLQEEELKL--LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 485 ERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQM----EMLTKDKTDKDEQIRKIKSRHS 560
Cdd:pfam02463 357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLlelaRQLEDLLKEEKKEELEILEEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 561 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDLES 640
Cdd:pfam02463 437 ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 641 DLGRLKEEIEKSSKQRAMlagatavysqfitQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELK 720
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDL-------------GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 721 KKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRdiqRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQM 800
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA---KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 801 ELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLDTvTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATN 880
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI-KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELK 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 881 LQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKVKNIHGYMKD 960
Cdd:pfam02463 740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 961 IENYIQDGKDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNLTLRKRRDELKEVEEERKQ 1040
Cdd:pfam02463 820 EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1041 HLKEMGQmQVLQMKNEHQKLEENIDTIKRNHSLALGRQKgYEDEILHFKKELREPQFRDAEEKYREMMIVMRT--TELVN 1118
Cdd:pfam02463 900 KELEEES-QKLNLLEEKENEIEERIKEEAEILLKYEEEP-EELLLEEADEKEKEENNKEEEEERNKRLLLAKEelGKVNL 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1119 KDLDIYYKTL---DQAIMKFHSMKMEEINKIIRDLWRSTYR---------------GQDIEYIEIRSDADENVSASDKRR 1180
Cdd:pfam02463 978 MAIEEFEEKEeryNKDELEKERLEEEKKKLIRAIIEETCQRlkeflelfvsinkgwNKVFFYLELGGSAELRLEDPDDPF 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1181 NYNYRV-VMLKGDTALDMRgRCSAGQKVLASLIIRLALAE----TFCLncgilaLDEPTTNLDRENIESLAHALveiiks 1255
Cdd:pfam02463 1058 SGGIEIsARPPGKGVKNLD-LLSGGEKTLVALALIFAIQKykpaPFYL------LDEIDAALDDQNVSRVANLL------ 1124
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 153945822 1256 RSQQRNFQLLVITHDEDFVELlgrseyVEKFYRVKKNMDQCSE 1298
Cdd:pfam02463 1125 KELSKNAQFIVISLREEMLEK------ADKLVGVTMVENGVST 1161
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
491-1084 |
2.01e-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: 62.05 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 491 AEKNSSIETLKAEVMSLQnekADLDRSLRKLDQEMEQLNHHTTTrTQMEMLTKDKTDKdEQIRKIKSRHSDELTSllgyf 570
Cdd:pfam05483 168 AEKTKKYEYEREETRQVY---MDLNNNIEKMILAFEELRVQAEN-ARLEMHFKLKEDH-EKIQHLEEEYKKEIND----- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 571 pNKKQLEDWLHSKSKEINQTRDrlakLNKELASAEQNKNHINNELKKKEEQLSSYEDKlfdvcgSQDLESDLGRLKEEIE 650
Cdd:pfam05483 238 -KEKQVSLLLIQITEKENKMKD----LTFLLEESRDKANQLEEKTKLQDENLKELIEK------KDHLTKELEDIKMSLQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 651 KSSKQRAMLAGATAVYSQFITQLTDENQSCCP-----------VCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESEL 719
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnkakaahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 720 KKKERRRDEMLGLVPVRQsiIDLKE-KEIPELRNRLQSVNRDIQRLKNDIEEQET----LLGTIMPEEESAKVCLTDVTI 794
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKE--VELEElKKILAEDEKLLDEKKQFEKIAEELKGKEQelifLLQAREKEIHDLEIQLTAIKT 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 795 MERFQM-ELKDVERKIAQQaaKLQGVDLDRTVQQVNQEkqekqhrldtvtskielNRKLIQDQQEQIQHLKSKTNELKSE 873
Cdd:pfam05483 465 SEEHYLkEVEDLKTELEKE--KLKNIELTAHCDKLLLE-----------------NKELTQEASDMTLELKKHQEDIINC 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 874 KLQIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKVKN 953
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 954 IHgymKDIENYIQDGKDDYKK--QKETELNGVAVQLN----ECEKHREKINKDMGTMRQDIDTQKI-QERWLQDNLTLRK 1026
Cdd:pfam05483 606 KN---KNIEELHQENKALKKKgsAENKQLNAYEIKVNklelELASAKQKFEEIIDNYQKEIEDKKIsEEKLLEEVEKAKA 682
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945822 1027 RRDELKEVEEE---RKQHlkEMGQMQVLQMKNEHQkleenIDTIKRNHSLALGRQKGYEDE 1084
Cdd:pfam05483 683 IADEAVKLQKEidkRCQH--KIAEMVALMEKHKHQ-----YDKIIEERDSELGLYKNKEQE 736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
424-914 |
2.10e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 424 LKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSKA-------EKNSS 496
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeleklEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 497 IETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHhttTRTQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGYFpnKKQL 576
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRE---LEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 577 EDWlhskSKEINQTRDRLAKLNKELASAEQNKNHINNEL--KKKEEQLSSYEDKLFDVCGSQDLESDLGRLKEEIEKSSK 654
Cdd:COG4717 202 EEL----QQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 655 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKERrrdemlglvp 734
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE---------- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 735 vrqsiidlkekEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAA 814
Cdd:COG4717 348 -----------ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 815 KLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKtNELKSEKLQIATNLQRRQQMEEQSVEL 894
Cdd:COG4717 417 ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAAL 495
|
490 500
....*....|....*....|
gi 153945822 895 STEVQSLNREIKDAKEQISP 914
Cdd:COG4717 496 KLALELLEEAREEYREERLP 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
741-1061 |
2.21e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 741 DLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLgtimpeeesakvcltdvtimERFQMELKDVERKIAQQAAKLQgvd 820
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAEL--------------------EELEAELAELEAELEELRLELE--- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 821 ldrtvqQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIAtnlQRRQQMEEQSVELSTEVQS 900
Cdd:COG1196 278 ------ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE---EELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 901 LNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQDgKDDYKKQKETEL 980
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 981 NGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNLTLRKRRDELKEVEEERKQHLKEMGQMQVLQMKNEHQKL 1060
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
.
gi 153945822 1061 E 1061
Cdd:COG1196 508 E 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
244-810 |
2.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 244 YEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKdnsELEQKMEKVfqgtdeqlndlyhnhqRTVREKERRLV 323
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK---ELEEVLREI----------------NEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 324 DCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLEL--DGFERGPFSERQIKNFHELVK 401
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEleEKVKELKELKEKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 402 ERQEREAKTA--SQLLSDLTDKEALKQRQLDELRDRKSGLGRtielkteiLTKKQSELRHVRSELQQLEGSSDRILELDQ 479
Cdd:PRK03918 301 FYEEYLDELReiEKRLSRLEEEINGIEERIKELEEKEERLEE--------LKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 480 ELtkaeRELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTR-TQMEMLTKDKTD--------KDE 550
Cdd:PRK03918 373 EL----ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELkKAIEELKKAKGKcpvcgrelTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 551 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKN-------HINNELKKKEEQLS 623
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEleeklkkYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 624 SYEDKLFDVCGSQD-LESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcqrvFQTEAELQEVISDLQ 702
Cdd:PRK03918 529 KLKEKLIKLKGEIKsLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG----------FESVEELEERLKELE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 703 S------KLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPEL------------RNRLQSVNRDIQRL 764
Cdd:PRK03918 599 PfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyeelREEYLELSRELAGL 678
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 153945822 765 KNDIEEQETLLGTIMPEEESAKvclTDVTIMERFQMELKDVERKIA 810
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLK---EELEEREKAKKELEKLEKALE 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
689-928 |
2.81e-09 |
|
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: 60.55 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 689 QTEAELQEV---ISDLQSKLRLAPDKLKSTESELKKKERRRDEmlglvpvRQSIIDLKEKEIPELRNRLQSVNRDIQRLK 765
Cdd:COG4942 24 EAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 766 NDIEEQETLLGTIMPeeesakvcltdvtimERFQMELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEkqhRLDTVTSK 845
Cdd:COG4942 97 AELEAQKEELAELLR---------------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE---QAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 846 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQsveLSTEVQSLNREIKDAKEQISPLETALEKLQQE 925
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
|
...
gi 153945822 926 KEE 928
Cdd:COG4942 236 AAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-660 |
3.48e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 182 ATRYIKALDTLRQVRQTQGQKVKECQtELKYLK------QNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRL 255
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLA-ELEYLRaalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 256 KEIEHNLS-----KIMKLDNEIKALESRKKQMEKDNSELEQKMEKV---FQGTDEQLNDLYHNHQRTVREKERRLVDCQR 327
Cdd:COG4913 326 DELEAQIRgnggdRLEQLEREIERLERELEERERRRARLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 328 ELEKLNKEARLLNQEKAELLVEQGRLQLQADR-HQEHIRARDSLIQSL---ATHL----EL-----------DGFER--G 386
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNiPARLLALRDALAEALgldEAELpfvgELievrpeeerwrGAIERvlG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 387 PFSerqiknFHELVKERQEREAKTAsqllsdlTDKEALKQR-QLDELRDRKSGLGRTIELKTEILTK---KQSELRH-VR 461
Cdd:COG4913 486 GFA------LTLLVPPEHYAAALRW-------VNRLHLRGRlVYERVRTGLPDPERPRLDPDSLAGKldfKPHPFRAwLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 462 SELQQlegSSDRIL-ELDQELTKAERELSKA----------EKN----------------SSIETLKAEVMSLQNEKADL 514
Cdd:COG4913 553 AELGR---RFDYVCvDSPEELRRHPRAITRAgqvkgngtrhEKDdrrrirsryvlgfdnrAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 515 DRSLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIkSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRL 594
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI-AELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945822 595 AKLNKELASAEQNKNHINNELKKKEEQLSSYEDKlfdvcGSQDLESDLGRLKEEIEKSSKQRAMLA 660
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDL-----ARLELRALLEERFAAALGDAVERELRE 769
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
312-1064 |
3.62e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 312 QRTVREKERRLVDCQRELEKLNKEarllnQEKAELLVEQGRLQLQAdRHQEHIRARDSLIqslathlelDGFERGPFSER 391
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNEL-----HEKQKFYLRQSVIDLQT-KLQEMQMERDAMA---------DIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 392 QIKNfhelvkerqereaktasQLLSDLTDKEALKQRQLDELRDRKSglgrTIELKTEILTKKQSELRHVRSELQQLE-GS 470
Cdd:pfam15921 142 DLRN-----------------QLQNTVHELEAAKCLKEDMLEDSNT----QIEQLRKMMLSHEGVLQEIRSILVDFEeAS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 471 SDRILELDQELTKAERELSKAeKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEmeqlnhhttTRTQMEMLTKDKTDKDE 550
Cdd:pfam15921 201 GKKIYEHDSMSTMHFRSLGSA-ISKILRELDTEISYLKGRIFPVEDQLEALKSE---------SQNKIELLLQQHQDRIE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 551 QIrkiKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEIN-QTRDRLAKLNKELASAEQNKNHINNELKkkeEQLSSYEDKL 629
Cdd:pfam15921 271 QL---ISEHEVEITGLTEKASSARSQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELR---EAKRMYEDKI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 630 fdvcgsQDLESDLGRLKEEIEKSSKQRAMlagatavYSQFITQLTDEnqsccpvcqrvfqteaeLQEVISDLQSKlrlap 709
Cdd:pfam15921 345 ------EELEKQLVLANSELTEARTERDQ-------FSQESGNLDDQ-----------------LQKLLADLHKR----- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 710 DKLKSTESELKKKERRRDEMLGLVpvrqsiIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQ-ETLLGTIMPEEESakvc 788
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSIT------IDHLRRELDDRNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNES---- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 789 LTDVTIMERFQMELKDVERKIAQQ--AAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSK 866
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEEltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 867 TNELKSE-------KLQIATNLQ----RRQQMEE-----------------QSVELSTEVQSLNREIKDAK-------EQ 911
Cdd:pfam15921 540 GDHLRNVqtecealKLQMAEKDKvieiLRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKilkdkkdAK 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 912 ISPLETALEKLQQEKEELIHrkhtSNKMAQDKINDIKEKVKNIHGYMKDIENYIQDGKDDYK----------KQKETELN 981
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVN----AGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnksEEMETTTN 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 982 GVAVQLNECEKHREKINKDMGTM---------------------RQDIDTQKIQERWLQDNLT-LRKRRDELKEVEEERK 1039
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSMegsdghamkvamgmqkqitakRGQIDALQSKIQFLEEAMTnANKEKHFLKEEKNKLS 775
|
810 820 830
....*....|....*....|....*....|...
gi 153945822 1040 QHL--------KEMGQMQVLqmKNEHQKLEENI 1064
Cdd:pfam15921 776 QELstvateknKMAGELEVL--RSQERRLKEKV 806
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
215-748 |
7.37e-09 |
|
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: 60.52 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 215 QNKEKACEIRDqITSKEAQLASS-QEIVRSYEDELEPLKNRLkeiehnlskiMKLDNEIKALESRKKQMEKDNSELEQKM 293
Cdd:pfam15921 311 QNSMYMRQLSD-LESTVSQLRSElREAKRMYEDKIEELEKQL----------VLANSELTEARTERDQFSQESGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 294 EKVfqgtdeqLNDLYHNHQRTVREKE--RRLVD-----------CQRELEKLNKEARLLnqeKAELLVEQGRLQLQADRH 360
Cdd:pfam15921 380 QKL-------LADLHKREKELSLEKEqnKRLWDrdtgnsitidhLRRELDDRNMEVQRL---EALLKAMKSECQGQMERQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 361 QEHIRARDSLIQ---SLATHLEldgfergPFSERQIKNFHELVKERQEREakTASQLLSDLTDKEALKQRQLDELRDRKS 437
Cdd:pfam15921 450 MAAIQGKNESLEkvsSLTAQLE-------STKEMLRKVVEELTAKKMTLE--SSERTVSDLTASLQEKERAIEATNAEIT 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 438 GLGRTIELKTEILTKKQSE---LRHVRSELQQLE---GSSDRILEL---------------------------------- 477
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKlqmAEKDKVIEIlrqqienmtqlvgqhgrtagamqvekaqlekein 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 478 DQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLD-------RSLRKLDQEMEQ-LNHHTTTRTQMEMLTKDKtdkd 549
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQlLNEVKTSRNELNSLSEDY---- 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 550 EQIRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSyedkl 629
Cdd:pfam15921 677 EVLKRNFRNKSEEMET------TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDA----- 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 630 fdvcgsqdLESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAP 709
Cdd:pfam15921 746 --------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
570 580 590
....*....|....*....|....*....|....*....
gi 153945822 710 DKLKSTESELKKKERRRDEMlglvpVRQSIIDLKEKEIP 748
Cdd:pfam15921 818 LQFAECQDIIQRQEQESVRL-----KLQHTLDVKELQGP 851
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
201-779 |
7.54e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 201 QKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEhnlSKIMKLDNEIKALESRKK 280
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETE---REREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 281 QMEKDNSELEQKMEkVFQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRh 360
Cdd:PRK02224 290 ELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 361 qehirardsliqsLATHLELDGFERGPFSERQiknfhelvkERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGL- 439
Cdd:PRK02224 368 -------------LESELEEAREAVEDRREEI---------EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELr 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 440 GRTIELKTEIltkkqSELRHVRSELQQL--EGssdRILELDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRS 517
Cdd:PRK02224 426 EREAELEATL-----RTARERVEEAEALleAG---KCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 518 LRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIrkikSRHSDELTSLLgyfPNKKQLEDWLHSKSKEINQTRDRLAKL 597
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDLEELIAERRETI----EEKRERAEELR---ERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 598 NKELASAEQNKNHINNELkkkeEQLSSYEDKLFDVcgsQDLESDLGRLKEeieksskQRAMLAgatAVYSQFITQLTDEN 677
Cdd:PRK02224 571 REEVAELNSKLAELKERI----ESLERIRTLLAAI---ADAEDEIERLRE-------KREALA---ELNDERRERLAEKR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 678 QsccpvcqRVFQTEAELQEV-ISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLV-PVRQSIidlkeKEIPELRNRLQ 755
Cdd:PRK02224 634 E-------RKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgAVENEL-----EELEELRERRE 701
|
570 580
....*....|....*....|....
gi 153945822 756 SVNRDIQRLKNDIEEQETLLGTIM 779
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESMYG 725
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1201-1273 |
1.04e-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: 56.88 E-value: 1.04e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945822 1201 CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAhalvEIIKSRSQQRNfQLLVITHDEDF 1273
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG----ELIRELAAQGK-AVIVITHDYEF 188
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
693-932 |
1.10e-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: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 693 ELQEVISDLQSKLRLApdKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKND----I 768
Cdd:COG1196 217 ELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyelL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 769 EEQETLLGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKLQGVDLDRTVQQ------VNQEKQEKQHRLDTV 842
Cdd:COG1196 295 AELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEELEEELEEAEeeleeaEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 843 TSKIELNRKLIQDQQEQIQHLKSKTNELKSEK---LQIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETAL 919
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEeleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250
....*....|...
gi 153945822 920 EKLQQEKEELIHR 932
Cdd:COG1196 452 AELEEEEEALLEL 464
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
446-1102 |
1.68e-08 |
|
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: 59.21 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 446 KTEILTKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEM 525
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 526 EQLNH--------HTTTRTQMEMLTKDKTdKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKL 597
Cdd:TIGR00618 300 KAVTQieqqaqriHTELQSKMRSRAKLLM-KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-HEVATSIREISCQQHTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 598 NKELASAEQNKNHinneLKKKEEQLSSYEDKLFDVCGSQD--------LESDLGRLKEEIEKSSKQRAMLAGATAVYSQF 669
Cdd:TIGR00618 378 TQHIHTLQQQKTT----LTQKLQSLCKELDILQREQATIDtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 670 IT----------QLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSI 739
Cdd:TIGR00618 454 EKlekihlqesaQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 740 ID---LKEKEIPELRNRLQSVNRDIQRLKNDIEE--QETLLGTIMPEEESAkvcltdvtIMERFQMELKDVERKIAQQAA 814
Cdd:TIGR00618 534 EQtyaQLETSEEDVYHQLTSERKQRASLKEQMQEiqQSFSILTQCDNRSKE--------DIPNLQNITVRLQDLTEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 815 KLQGVDLDRTVQQVnqEKQEKQHRLDtvtsKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQME--EQSV 892
Cdd:TIGR00618 606 AEDMLACEQHALLR--KLQPEQDLQD----VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllASRQ 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 893 ELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKvknihgymkdiENYIQDGKDDY 972
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR-----------EDALNQSLKEL 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 973 KKQKETELngvavQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNLtLRKRRDELKEVEEERKQHLKEMGQMQVLQ 1052
Cdd:TIGR00618 749 MHQARTVL-----KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL-REEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 153945822 1053 MKNEHQKLEENIDTIKRNHSL--ALGRQKGYEDEILHFKKELREPQFRDAEE 1102
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
801-1104 |
2.14e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 801 ELKDVERKIAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIATN 880
Cdd:COG1196 233 KLRELEAELEELEAELE--ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---DIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 881 LQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKvknihgymkd 960
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---------- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 961 ienyiQDGKDDYKKQKETELNGVAVQLNECEKHREKInkdmgtmrqdidtQKIQERWLQDNLTLRKRRDELKEVEEERKQ 1040
Cdd:COG1196 378 -----EEELEELAEELLEALRAAAELAAQLEELEEAE-------------EALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945822 1041 HLKEMGQMQVLQMKNEHQKLEENIDTIKRNHSLALGRQKGYEDEILHFKKELREPQFRDAEEKY 1104
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
25-744 |
2.66e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 25 ISFFSPLTILVGPNGAGKTTIIECLKYICTGDfppgtKGNTFVHDpkVAQETDVRAQIRLQFRdVNGEMVAVHRSMLCSQ 104
Cdd:PRK01156 19 IEFDTGINIITGKNGAGKSSIVDAIRFALFTD-----KRTEKIED--MIKKGKNNLEVELEFR-IGGHVYQIRRSIERRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 105 KNKKTEFKTlegvitrMKHGEKVSLSSKCAEIDREMiSCLGVSKSVLNNVIFCHQEDSNWPLSEGKALKQK-FDEIFSAT 183
Cdd:PRK01156 91 KGSRREAYI-------KKDGSIIAEGFDDTTKYIEK-NILGISKDVFLNSIFVGQGEMDSLISGDPAQRKKiLDEILEIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 184 RYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLS 263
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 264 KIMKLDNEIKALESRKKQMEKDNSELEQKMEKvFQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEK 343
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 344 AELLVEQGRLQ-LQADRHQEHIRAR--DSLIQSLathLELDGFERGPFSerQIKNFHELVKERQErEAKTASQLLSDLTD 420
Cdd:PRK01156 322 NKYHAIIKKLSvLQKDYNDYIKKKSryDDLNNQI---LELEGYEMDYNS--YLKSIESLKKKIEE-YSKNIERMSAFISE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 421 KEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQL----------------------EGSSDRILELD 478
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELsrnmemlngqsvcpvcgttlgeEKSNHIINHYN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 479 QELTKAERELSKAEKN-SSIETLKAEVMSLQN--EKADLDRSLRKlDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIR-K 554
Cdd:PRK01156 476 EKKSRLEEKIREIEIEvKDIDEKIVDLKKRKEylESEEINKSINE-YNKIESARADLEDIKIKINELKDKHDKYEEIKnR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 555 IKSRHSDEL----TSLLGYFPNKKQLE-DWLHSKSKEIN-QTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDK 628
Cdd:PRK01156 555 YKSLKLEDLdskrTSWLNALAVISLIDiETNRSRSNEIKkQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 629 LFDVcgsQDLESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEVISDlQSKLRLA 708
Cdd:PRK01156 635 YNEI---QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIE-------DNLKKSRKALDDAKAN-RARLEST 703
|
730 740 750
....*....|....*....|....*....|....*..
gi 153945822 709 PDKLKSTESELKKKERRRDEML-GLVPVRQSIIDLKE 744
Cdd:PRK01156 704 IEILRTRINELSDRINDINETLeSMKKIKKAIGDLKR 740
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
574-1094 |
3.18e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 574 KQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQD-LESDLGRLKEEIEKS 652
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINkLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 653 SKQRAMLAGAtavYSQFITQLTDENQSCCPVCQRVFQTEAELQEV----------ISDLQSKLRLAPDKLKSTESEL--- 719
Cdd:TIGR04523 116 KEQKNKLEVE---LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyndlkkqKEELENELNLLEKEKLNIQKNIdki 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 720 KKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV-TIMERF 798
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 799 QMELKDVERKIAQQAAKLQGV-----DLDRTVQQ-----VNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKS--- 865
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLkseisDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKelt 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 866 ---------------KTNELKSEKLQIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELI 930
Cdd:TIGR04523 353 nsesensekqreleeKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 931 HRKHTSNKMAQD---KINDIKEKVKNIHGYMKDIENYIQDGKDDYKK------QKETELNGVAVQLNECEKHREKINKDM 1001
Cdd:TIGR04523 433 ETIIKNNSEIKDltnQDSVKELIIKNLDNTRESLETQLKVLSRSINKikqnleQKQKELKSKEKELKKLNEEKKELEEKV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1002 GTMRQDIDTQKIQERWL-----QDNLTLRKRRDELKEVEEERKqhlKEMGQMQVLQMKNEHQKLEENIDTIKRNHSLALG 1076
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLesekkEKESKISDLEDELNKDDFELK---KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQE 589
|
570
....*....|....*...
gi 153945822 1077 RQKGYEDEILHFKKELRE 1094
Cdd:TIGR04523 590 LIDQKEKEKKDLIKEIEE 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-925 |
3.51e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 391 RQIKNFHELVkERQEREAKTASQLLSDLTDKEALKQRqLDELRDRKSGLGR-TIELKTEILTKKQSELRHVRSELQ-QLE 468
Cdd:COG4913 235 DDLERAHEAL-EDAREQIELLEPIRELAERYAAARER-LAELEYLRAALRLwFAQRRLELLEAELEELRAELARLEaELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 469 GSSDRILELDQELTKAERELSKAeKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTrtqmemltkDKTDK 548
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGN-GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA---------SAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 549 DEQIRKIKsRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKK----EEQLSS 624
Cdd:COG4913 383 AALRAEAA-ALLEALEEEL------EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalAEALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 625 YEDKLFDVCgsqdlesdlgrlkEEIEKSSKQRA-------MLAGA-------TAVYSQFITQLTDENQSCCPVCQRVFQT 690
Cdd:COG4913 456 DEAELPFVG-------------ELIEVRPEEERwrgaierVLGGFaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 691 EAELQEVISDLQS---KLRLAPDKLKS----------------TESELKKKER-----------------------RRDE 728
Cdd:COG4913 523 LPDPERPRLDPDSlagKLDFKPHPFRAwleaelgrrfdyvcvdSPEELRRHPRaitragqvkgngtrhekddrrriRSRY 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 729 MLGLVPVRQsiIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTImpeeesakvcltdvTIMERFQMELKDV--- 805
Cdd:COG4913 603 VLGFDNRAK--LAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------------QRLAEYSWDEIDVasa 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 806 ERKIAQQAAKLQGVD--------LDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNEL-KSEKLQ 876
Cdd:COG4913 667 EREIAELEAELERLDassddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLE 746
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 153945822 877 IATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQE 925
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-1125 |
3.68e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 219 KACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEkvfq 298
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE---- 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 299 gtdEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELlVEQGRLQLQADRHQEHIRARDSLIQSLATHL 378
Cdd:PTZ00121 1259 ---EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 379 ELDGFERgpfserqiKNFHELVKERQEREAKTAsqllsdltdKEALKQRQLDELRDRKSglgrtiELKTEILTKKQSELR 458
Cdd:PTZ00121 1335 KKKAEEA--------KKAAEAAKAEAEAAADEA---------EAAEEKAEAAEKKKEEA------KKKADAAKKKAEEKK 1391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 459 hvrsELQQLEGSSDRILELDQELTKAERELSKAE--KNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQlnhhtttrt 536
Cdd:PTZ00121 1392 ----KADEAKKKAEEDKKKADELKKAAAAKKKADeaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK--------- 1458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 537 qmemlTKDKTDKDEQIRKiksrhSDELTSLlgyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNhinNELK 616
Cdd:PTZ00121 1459 -----AEEAKKKAEEAKK-----ADEAKKK----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK---AEEA 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 617 KKEEQLSSYEDKLfdvcgsqdlESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT----EA 692
Cdd:PTZ00121 1522 KKADEAKKAEEAK---------KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEA 1592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 693 ELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMlglvPVRQSIIDLKEKEIPELRNrlqsvnrdIQRLKNDIEEQE 772
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE----EEKKKVEQLKKKEAEEKKK--------AEELKKAEEENK 1660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 773 tllgtiMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKL 852
Cdd:PTZ00121 1661 ------IKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 853 IQDQQEQIQHLKSKTNELKSEKlqiatnlqrrqqmeeqsvELSTEVQSLNREIKDAKEQISPletalEKLQQEKEELIHR 932
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDE------------------EEKKKIAHLKKEEEKKAEEIRK-----EKEAVIEEELDEE 1788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 933 KHTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNGVAVQLNEC---EKHREKINKDMGtmrqdid 1009
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAdafEKHKFNKNNENG------- 1861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1010 tqkiqerwlqdnltlrkrRDELKEVEEERKQHLKEMGQMQVLQMKNEHQKLEENIDTIKRNHSLalgrqKGYEDEILHFK 1089
Cdd:PTZ00121 1862 ------------------EDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNM-----AGKNNDIIDDK 1918
|
890 900 910
....*....|....*....|....*....|....*.
gi 153945822 1090 KELREPQFRDAEEKyREMMIVMRTTELVNKDLDIYY 1125
Cdd:PTZ00121 1919 LDKDEYIKRDAEET-REEIIKISKKDMCINDFSSKF 1953
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1202-1291 |
3.73e-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: 55.17 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIEslahALVEIIKsRSQQRNFQLLVITHDEDFVEllgrsE 1281
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDPAGRR----ELLELLK-KLKAEGKTIIIVTHDLDLLL-----E 199
|
90
....*....|
gi 153945822 1282 YVEKFYRVKK 1291
Cdd:cd03225 200 LADRVIVLED 209
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
211-655 |
7.84e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 211 KYLKQNKEKACEIRDQITSKEAQLASSQEIVR-------SYEDELEPLKNRLKEIEHN--------------LSKIMKLD 269
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNdlkkqkeELENELNLLEKEKLNIQKNidkiknkllklellLSNLKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 270 NEIKALESRKKQMEKDNSELE----------QKMEKVFQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLL 339
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKdniekkqqeiNEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 340 NQEKAELLV-EQGRLQLQADRHQEHIRARDSLIQSLATHLE-----LDGFERGPFSERQIKNFHELVKERQEREAKTASQ 413
Cdd:TIGR04523 291 NQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 414 LLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSK--A 491
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdS 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 492 EKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQM-EMLTKDKTDKDEQIRKIKSRHSDELTSLLGYF 570
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 571 PNKKQLEDWLHSKSKEINQTRDRLAK---------LNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDL-ES 640
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEkEK 610
|
490
....*....|....*
gi 153945822 641 DLGRLKEEIEKSSKQ 655
Cdd:TIGR04523 611 KISSLEKELEKAKKE 625
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
164-928 |
1.22e-07 |
|
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: 56.27 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 164 WPLSEGKALKQKFDEIFSATRYIKALDTLRQVRQTQGQKVK-ECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVR 242
Cdd:pfam05483 93 WKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSlKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 243 SYEDELEPLKNRLKEIEHNLSKImkldneIKALESRKKQMEKDNSELEQKMEKVFqgtdEQLNDLYHNHQRTVREKERR- 321
Cdd:pfam05483 173 KYEYEREETRQVYMDLNNNIEKM------ILAFEELRVQAENARLEMHFKLKEDH----EKIQHLEEEYKKEINDKEKQv 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 322 ---LVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLathleldgfERGPFSERQIKNFHE 398
Cdd:pfam05483 243 sllLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL---------EDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 399 LVKERQEREAKTASQLLSDltdkealKQRQLDELRDRKSGLGRTIelkTEILTKKQSELRHVRSELQQLEGSSDRILELD 478
Cdd:pfam05483 314 ALEEDLQIATKTICQLTEE-------KEAQMEELNKAKAAHSFVV---TEFEATTCSLEELLRTEQQRLEKNEDQLKIIT 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 479 QELTKAERELSkaeknssietlkaEVMSLQNEKADLDRSLRKLDQEMEQLnhhtttrtqmemltkdkTDKDEQIRKIKSR 558
Cdd:pfam05483 384 MELQKKSSELE-------------EMTKFKNNKEVELEELKKILAEDEKL-----------------LDEKKQFEKIAEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 559 HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLfdVCGSQDL 638
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL--TQEASDM 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 639 ESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEVISDLQSKLRLAPDKLKSTESE 718
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES----------VREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 719 LKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERF 798
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 799 QMELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRkliqdqqeqiqHLKSKTNELKSEKLQIA 878
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHK-----------HQYDKIIEERDSELGLY 730
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 153945822 879 TNlqRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEE 928
Cdd:pfam05483 731 KN--KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
218-617 |
2.00e-07 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 55.51 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 218 EKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDNE-IKALESRKKQMEKdnseLEQKMEKV 296
Cdd:COG4694 99 EENIELEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKkLFASSGRNYRKAN----LEKKLSAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 297 FQGTDEQLNDLYhnhqRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQAdrHQEHIRARDSLIQSLAT 376
Cdd:COG4694 175 KSSSEDELKEKL----KLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAVSSAIEELAA--LIQNPGNSDWVEQGLAY 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 377 HLELDG----FERGPFSERQIKNFHELVKERQEREAKTASQLLSDLTD-KEALKQRQLDELRDRKSGLGRTIELKTEILT 451
Cdd:COG4694 249 HKEEEDdtcpFCQQELAAERIEALEAYFDDEYEKLLAALKDLLEELESaINALSALLLEILRTLLPSAKEDLKAALEALN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 452 KKQSELrhvrseLQQLEGSSDRIL---ELDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDqemeqL 528
Cdd:COG4694 329 ALLETL------LAALEEKIANPStsiDLDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAHE-----L 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 529 NHhtttrtqmemLTKDKTDKDEQIRKIKSRHsdeltsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLNKELASAEQNK 608
Cdd:COG4694 398 AE----------LKEDLSRYKAEVEELIEEL------------------KTIKALKKALEDLKTEISELEAELSSVDEAA 449
|
....*....
gi 153945822 609 NHINNELKK 617
Cdd:COG4694 450 DEINEELKA 458
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
190-649 |
2.23e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 190 DTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEplknrlkeiehnlskimKLD 269
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE-----------------ELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 270 NEIKALESRkkqmekdnseleqkmekvFQGTDEQLNDLyHNHQRTVREKERRLVDCQRELEKLNKEARlLNQEKAELLVE 349
Cdd:PRK02224 391 EEIEELRER------------------FGDAPVDLGNA-EDFLEELREERDELREREAELEATLRTAR-ERVEEAEALLE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 350 QGRL-----QLQADRHQEHIRARDSLIQSLATHLEldgfergpfserQIKNFHELVKERQEReaktasqlLSDLTDKEal 424
Cdd:PRK02224 451 AGKCpecgqPVEGSPHVETIEEDRERVEELEAELE------------DLEEEVEEVEERLER--------AEDLVEAE-- 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 425 kqRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQEL-TKAERELSK-AEKNSSIETLKA 502
Cdd:PRK02224 509 --DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAeEEAEEAREEvAELNSKLAELKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 503 EVMSLQNEKADLDRsLRKLDQEMEQLNHHTTTRTQMEMLTKDK-TDKDEQIRKIKSRHSDELTSLLGyfPNKKQLEDWLH 581
Cdd:PRK02224 587 RIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERlAEKRERKRELEAEFDEARIEEAR--EDKERAEEYLE 663
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 582 SKSKEINQTRDRLAKLNKELASAEqNKNHINNELKKKEEQLSSYEDKLFDVCG-SQDLESDLGRLKEEI 649
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGAVE-NELEELEELRERREALENRVEALEALYDeAEELESMYGDLRAEL 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
695-952 |
2.88e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 695 QEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETl 774
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 775 lgtimpeeesakvcltdvtimerfqmELKDVERKIAQQAAKLQgvdldRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQ 854
Cdd:COG4942 98 --------------------------ELEAQKEELAELLRALY-----RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 855 DQQEQIQHLKSKTNELKSEKLQIAtnlQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKH 934
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELE---AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*...
gi 153945822 935 TSNKMAQDKINDIKEKVK 952
Cdd:COG4942 224 ELEALIARLEAEAAAAAE 241
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-98 |
3.29e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 52.32 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 3 RIEKMSILGVRSFgiedKDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTK-GNTFVHDPkvaqetDVRAQ 81
Cdd:COG0419 1 KLLRLRLENFRSY----RDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKlRSDLINVG------SEEAS 70
|
90
....*....|....*..
gi 153945822 82 IRLQFrDVNGEMVAVHR 98
Cdd:COG0419 71 VELEF-EHGGKRYRIER 86
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-923 |
3.86e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 302 EQLNDLYHNHQRTVREKER--------RLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRArdsLIQS 373
Cdd:COG4913 255 EPIRELAERYAAARERLAEleylraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE---LEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 374 LATHleldGFERGPFSERQIKNfHELVKERQEREAKTASQLLSDL-----TDKEALK--QRQLDELRDR-KSGLGRTIEL 445
Cdd:COG4913 332 IRGN----GGDRLEQLEREIER-LERELEERERRRARLEALLAALglplpASAEEFAalRAEAAALLEAlEEELEALEEA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 446 KTEI---LTKKQSELRHVRSELQQLEGSSDRIlelDQELTKAERELSKAEKNSSIEtLK--AEVMSLQNE---------- 510
Cdd:COG4913 407 LAEAeaaLRDLRRELRELEAEIASLERRKSNI---PARLLALRDALAEALGLDEAE-LPfvGELIEVRPEeerwrgaier 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 511 ------------KADLDRSLRKLDQemeqlnHHTTTRtqmemLTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKkqLED 578
Cdd:COG4913 483 vlggfaltllvpPEHYAAALRWVNR------LHLRGR-----LVYERVRTGLPDPERPRLDPDSLAGKLDFKPHP--FRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 579 WLHSkskEINQ--------------------TRDRLAKLNKELasAEQNKNHINNEL----KKKEEQLSSYEDKLfdvcg 634
Cdd:COG4913 550 WLEA---ELGRrfdyvcvdspeelrrhpraiTRAGQVKGNGTR--HEKDDRRRIRSRyvlgFDNRAKLAALEAEL----- 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 635 sQDLESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcQRVFQTEAELQEVISDLQSkLRLAPDKLKS 714
Cdd:COG4913 620 -AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE--------IDVASAEREIAELEAELER-LDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 715 TESELKKKERRRDEmlglvpVRQSIIDLKEKEIpELRNRLQSVNRDIQRLK---NDIEEQETLLGTIMPEEESAKVCLTD 791
Cdd:COG4913 690 LEEQLEELEAELEE------LEEELDELKGEIG-RLEKELEQAEEELDELQdrlEAAEDLARLELRALLEERFAAALGDA 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 792 V--TIMERFQMELKDVERKIAQQAAKLQgvdldRTVQQVNQEKQEKQHRLDTVtskielnrklIQDQQEQIQHLksktNE 869
Cdd:COG4913 763 VerELRENLEERIDALRARLNRAEEELE-----RAMRAFNREWPAETADLDAD----------LESLPEYLALL----DR 823
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 870 LKSEKLqiatnLQRRQQMEEQSVELSTE-----VQSLNREIKDAKEQISPLETALEKLQ 923
Cdd:COG4913 824 LEEDGL-----PEYEERFKELLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1192-1275 |
4.82e-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: 53.99 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1192 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITHD 1270
Cdd:COG4988 464 DTPLGEGGRGlSGGQAQ------RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT------VILITHR 531
|
....*
gi 153945822 1271 EDFVE 1275
Cdd:COG4988 532 LALLA 536
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
825-1044 |
5.04e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.25 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 825 VQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQ----IQHLKSKTNELKSEKLQIatnlqrrqqmEEQSVELSTEVQS 900
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKngenIARKQNKYDELVEEAKTI----------KAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 901 LNREIKDAKEQISPLETALEKLQQE-----KEELIHRKH------TSN-KMAQDKINDIKEKVKNIHGYMKDIENYIQdg 968
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKieqfqKVIKMYEKGgvcptcTQQiSEGPDRITKIKDKLKELQHSLEKLDTAID-- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 969 kddykkqketELNGVAVQLNECEKHREKINKDMGTMRQDIDT------------QKIQERWLQDNLTLRKRRDELKEVEE 1036
Cdd:PHA02562 324 ----------ELEEIMDEFNEQSKKLLELKNKISTNKQSLITlvdkakkvkaaiEELQAEFVDNAEELAKLQDELDKIVK 393
|
....*...
gi 153945822 1037 ERKQHLKE 1044
Cdd:PHA02562 394 TKSELVKE 401
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
326-1122 |
6.61e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 326 QRELEKLNKEARLlNQEKAELLVEQGRLQLQADRHQEH-IRARDSLIQSLATHLELDGFERGPFSERQIKNFHELVKERQ 404
Cdd:pfam02463 169 RKKKEALKKLIEE-TENLAELIIDLEELKLQELKLKEQaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 405 EREAKTASQllSDLTDKEALKQRQLDELRDRKSglgRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQELTKA 484
Cdd:pfam02463 248 DEQEEIESS--KQEIEKEEEKLAQVLKENKEEE---KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 485 ERELSKAEKNSsietlKAEVMSLQNEKADLDRSLRKLDQEMEQLnhhtttrtqMEMLTKDKTDKDEQIRKiKSRHSDELT 564
Cdd:pfam02463 323 KKKAEKELKKE-----KEEIEELEKELKELEIKREAEEEEEEEL---------EKLQEKLEQLEEELLAK-KKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 565 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNK----NHINNELKKKEEQLSSYEDKLFDVCGSQDLES 640
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIleeeEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 641 DLG-RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVF-QTEAELQEVISDLQSKLRLAPDKLKSTES- 717
Cdd:pfam02463 468 KKSeDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIkDGVGGRIISAHGRLGDLGVAVENYKVAISt 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 718 ------------ELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQET-------LLGTI 778
Cdd:pfam02463 548 avivevsatadeVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAdeddkraKVVEG 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 779 MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLdtvtSKIELNRKLIQDQQE 858
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE----LAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 859 QIQHLKSKTNELKSEKLQIATNLQRRQQmEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNK 938
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQ-DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 939 MAQDKINDIKEKVKNIhgyMKDIENYIQDGKDDYKKQKETELNGVAVQLNECEKHREKINKdmgtmrqDIDTQKIQERWL 1018
Cdd:pfam02463 783 TEKLKVEEEKEEKLKA---QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL-------ELKEEQKLEKLA 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1019 QDNLTLRKRRDELKEVEEERKQHLKEMGQMQVLQMKNEHQKLEENIDTIKRNHSlalgrQKGYEDEILHFKKELREPQFR 1098
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES-----QKLNLLEEKENEIEERIKEEA 927
|
810 820
....*....|....*....|....
gi 153945822 1099 DAEEKYREMMIVMRTTELVNKDLD 1122
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKE 951
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
224-554 |
6.98e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 224 RDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDN-------------EIKALESRKKQMEKDNSELe 290
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASSDDL- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 291 qkmekvfqgtdEQLndlyhnhQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEhirardsl 370
Cdd:COG4913 688 -----------AAL-------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED-------- 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 371 IQSLATHLELDgfERgpFSERQIKNFHELVKERQEREAKTASQLLSDLTDK-EALKQRQLDELRDRKSGLGRTIElktei 449
Cdd:COG4913 742 LARLELRALLE--ER--FAAALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLE----- 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 450 ltkkqsELRHVRSELQQLEgssdrilelDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLN 529
Cdd:COG4913 813 ------SLPEYLALLDRLE---------EDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIP 877
|
330 340
....*....|....*....|....*
gi 153945822 530 HHTTTRTQMEMltkdKTDKDEQIRK 554
Cdd:COG4913 878 FGPGRYLRLEA----RPRPDPEVRE 898
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
194-1107 |
9.42e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.64 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 194 QVRQTQGQKVKECQT----ELKYLKQNKEKACEIRDQITSK---EAQLASSQEIVRSyedELEPLKNRLKEIEHNL-SKI 265
Cdd:pfam01576 8 QAKEEELQKVKERQQkaesELKELEKKHQQLCEEKNALQEQlqaETELCAEAEEMRA---RLAARKQELEEILHELeSRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 266 MKLDNEIKALESRKKQMEKDNSELEQKMEKVfQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAE 345
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEE-EAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 346 LLVEQGRLQLQADRHQEHIRARDSLIQSLATHLEldgfergpfseRQIKNFHELVKERQEREAKTasqllSDLTDKEALK 425
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK-----------KEEKGRQELEKAKRKLEGES-----TDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 426 QRQLDELRDRksgLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSKAEK-----NSSIETL 500
Cdd:pfam01576 228 QAQIAELRAQ---LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKqrrdlGEELEAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 501 KAEVMSLQNEKADLDRSLRKLDQEMEQLNhhtttrtqmEMLTKDKTDKDEQIRKIKSRHS---DELTSLLGYFP-NKKQL 576
Cdd:pfam01576 305 KTELEDTLDTTAAQQELRSKREQEVTELK---------KALEEETRSHEAQLQEMRQKHTqalEELTEQLEQAKrNKANL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 577 EDWLHSKSKEINQtrdrlakLNKELASAEQNKNHINNELKKKEEQLSSYEDKLfdvcgsqdleSDLGRLKEEI-EKSSKQ 655
Cdd:pfam01576 376 EKAKQALESENAE-------LQAELRTLQQAKQDSEHKRKKLEGQLQELQARL----------SESERQRAELaEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 656 RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEvisDLQSKLRLApDKLKSTESELKKKERRRDEmlglvpv 735
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE---ETRQKLNLS-TRLRQLEDERNSLQEQLEE------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 736 rqsiidlKEKEIPELRNRLQSVNRDIQRLKNDIEEQetlLGTIMPEEESAKvcltdvtimeRFQMELKDVERKIAQQAAK 815
Cdd:pfam01576 508 -------EEEAKRNVERQLSTLQAQLSDMKKKLEED---AGTLEALEEGKK----------RLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 816 LQgvDLDRTVQQVNQEkqekqhrLDTVTSKIELNRKLIQDQQEQiqhLKSKTNELKSEKLQIATNLQRRQQMEEQSVELS 895
Cdd:pfam01576 568 YD--KLEKTKNRLQQE-------LDDLLVDLDHQRQLVSNLEKK---QKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 896 TEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQD---KINDIKEKVKNIHGYMKDIENYIQDGKDD- 971
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHElerSKRALEQQVEEMKTQLEELEDELQATEDAk 715
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 972 ---------YKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNLTLrkrrdELKEVEEE----- 1037
Cdd:pfam01576 716 lrlevnmqaLKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLEL-----DLKELEAQidaan 790
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 1038 --RKQHLKEMGQMQVlQMKNEHQKLEENidTIKRNHSLALGRQ-----KGYEDEILHFKKEL--REPQFRDAEEKYREM 1107
Cdd:pfam01576 791 kgREEAVKQLKKLQA-QMKDLQRELEEA--RASRDEILAQSKEsekklKNLEAELLQLQEDLaaSERARRQAQQERDEL 866
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
204-964 |
9.81e-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: 53.49 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 204 KECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEiehNLSKIMKLDNEIKALES----RK 279
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK---NKDKINKLNSDLSKINSeiknDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 280 KQMEKDNSELeQKMEKVFQGTDEQLNDLyhnhqrtvrekERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADR 359
Cdd:TIGR04523 117 EQKNKLEVEL-NKLEKQKKENKKNIDKF-----------LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 360 HQEHIrardsliqslathleldgfergpfseRQIKNfhelvkerQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGL 439
Cdd:TIGR04523 185 IQKNI--------------------------DKIKN--------KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 440 GRTIELKTEILTKKQSELRHVRSELQQLEGSSDRIL----ELDQELTKAERELSKAEKNssIETLKAEVMSLQNEK-ADL 514
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsEKQKELEQNNKKIKELEKQ--LNQLKSEISDLNNQKeQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 515 DRSLRklDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKSrhsdeltsllgyfpNKKQLEDWLHSKSKEINQTRDRL 594
Cdd:TIGR04523 309 NKELK--SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK--------------ELTNSESENSEKQRELEEKQNEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 595 AKLNKELASAEQNKNHINNELKKKEEQLSSYEDKlfdvcgSQDLESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLT 674
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKL------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 675 DENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKErrrDEMLGLVPVRQSIidlkEKEIPELRNRL 754
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE---KELKKLNEEKKEL----EEKVKDLTKKI 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 755 QSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTdvtimerfQMELKDVERKIAQQAAKLQ--GVDLDRTVQQVNQEK 832
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--------KENLEKEIDEKNKEIEELKqtQKSLKKKQEEKQELI 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 833 QEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNL----QRRQQMEEQSVELSTEVQSLNREIKDA 908
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKnklkQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945822 909 KEQISPLETALEKLQQEKeELIHRKHTSNKMAQDKINDIKEKVKNIHGYMKDIENY 964
Cdd:TIGR04523 672 KTKIDDIIELMKDWLKEL-SLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEF 726
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1192-1279 |
1.11e-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: 53.06 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1192 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDREniesLAHALVEIIKSRSQQRNfqLLVITHD 1270
Cdd:TIGR02857 449 DTPIGEGGAgLSGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAE----TEAEVLEALRALAQGRT--VLLVTHR 516
|
....*....
gi 153945822 1271 EDFVELLGR 1279
Cdd:TIGR02857 517 LALAALADR 525
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1199-1275 |
1.49e-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: 50.56 E-value: 1.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 1199 GRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIEslahALVEIIKSRSQQRnfQLLVI-THDEDFVE 1275
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGVA----LLAELIAAHLARG--GAVLLtTHQPLELA 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-417 |
2.31e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 188 ALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEiehnlskimk 267
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 268 LDNEIKALESRKKQMEKDNSELEQKMEK---------VFQGTD-EQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEAR 337
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRlgrqpplalLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 338 LLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLELDGfERGPFSERQIKNFHELVKERQEREAKTASQLLSD 417
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
431-1036 |
2.57e-06 |
|
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: 52.15 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 431 ELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLegssdrILELDQELTKAERELSKAEknSSIETLKAEvmSLQNE 510
Cdd:pfam12128 266 GYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADAAVAKDR--SELEALEDQ--HGAFL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 511 KADLDRslRKLDQEMEQLnhhttTRTQMEMLTKDKTDKDEQIRKIkSRHSDELTSLLGYfPNKKQLEDwLHSKSKEINQT 590
Cdd:pfam12128 336 DADIET--AAADQEQLPS-----WQSELENLEERLKALTGKHQDV-TAKYNRRRSKIKE-QNNRDIAG-IKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 591 RDRLA--------KLNKELASA-EQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDL-------ESDLGRLKEEIEKSSK 654
Cdd:pfam12128 406 RDRQLavaeddlqALESELREQlEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllqlenfDERIERAREEQEAANA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 655 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVIS----DLQSKLR-------------LAPDKLKSTES 717
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpqagTLLHFLRkeapdweqsigkvISPELLHRTDL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 718 ELKKKERRRDEMLGLVPVRqsiIDLKEKEIPE-------LRNRLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 790
Cdd:pfam12128 566 DPEVWDGSVGGELNLYGVK---LDLKRIDVPEwaaseeeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 791 DVtimerfqmelkdverkiaqqAAKLQGVDLDrtVQQVNQEKQEKQHRldtvtskieLNRKLIQDQQEQIQHLKSKTNEL 870
Cdd:pfam12128 643 FA--------------------RTALKNARLD--LRRLFDEKQSEKDK---------KNKALAERKDSANERLNSLEAQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 871 KSEKLQIAtnlQRRQQMEEQSVELSTEVQSLNREIKDAKE-QISPLETALEKLQQEK-------EELIHRKHTSNKMAQD 942
Cdd:pfam12128 692 KQLDKKHQ---AWLEEQKEQKREARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAkaelkalETWYKRDLASLGVDPD 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 943 KINDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKET----------ELNGVAVQLNECEKHREKINKDMGTMRQDIDTQK 1012
Cdd:pfam12128 769 VIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETwlqrrprlatQLSNIERAISELQQQLARLIADTKLRRAKLEMER 848
|
650 660
....*....|....*....|....*.
gi 153945822 1013 IQERWLQDNLT--LRKRRDELKEVEE 1036
Cdd:pfam12128 849 KASEKQQVRLSenLRGLRCEMSKLAT 874
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-676 |
2.78e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 426 QRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEgssDRILELDQELTKAERELSKAEKNssIETLKAEVM 505
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEAE--LAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 506 SLQNEKADLDRSLRKLDQEMEQLNHHTTtrtqMEMLtkdktdkdeqirkIKSRHSDELTSLLGYFpnkKQLEDWLHSKSK 585
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPP----LALL-------------LSPEDFLDAVRRLQYL---KYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 586 EINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEdklfdvcgsQDLESDLGRLKEEIEKSSKQRAMLAGATAV 665
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALK---------AERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|.
gi 153945822 666 YSQFITQLTDE 676
Cdd:COG4942 225 LEALIARLEAE 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
187-628 |
3.17e-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: 51.56 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 187 KALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASS----QEIVRSYEDELEPLKNRLKEIEHNL 262
Cdd:TIGR04523 304 KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesenSEKQRELEEKQNEIEKLKKENQSYK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 263 SKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVfqgtdeqlndlyhnhQRTVREKERRLVDCQRELEKLNKEARLLNQE 342
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL---------------QQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 343 KAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLeldgfergpfserqiknfhelvkERQEREAKTASQLLSDLTDKE 422
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL-----------------------EQKQKELKSKEKELKKLNEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 423 ALKQRQLDELRDRKSGLGRTIE-LKTEILTKKqselrhvrSELQQLEgssDRILELDQELTKAERELSKAEKNSSIETLK 501
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEkLESEKKEKE--------SKISDLE---DELNKDDFELKKENLEKEIDEKNKEIEELK 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 502 AEVMSLQNEKADLDRSLRKLDQEMEQLnhhtttRTQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 581
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDL------IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 153945822 582 SKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDK 628
Cdd:TIGR04523 649 QIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK 695
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
587-1044 |
3.58e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 587 INQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVcgsQDLESDLGRLKEEIEKSSKQRAMLAGATAvy 666
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL---ETLEAEIEDLRETIAETEREREELAEEVR-- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 667 sqfitqltdenqsccpvcqrvfqteaELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMlglvpvrqsiidlkEKE 746
Cdd:PRK02224 283 --------------------------DLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL--------------EDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 747 IPELRNRLQSVNRDIQRLKNDIEeqeTLLGTIMPEEESAKVCLTDVTIMERfqmELKDVERKIAQQAAKLQgvDLDRTVQ 826
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAE---SLREDADDLEERAEELREEAAELES---ELEEAREAVEDRREEIE--ELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 827 QVNQEKQEKQHRLDTVTSKIELnrkLIQDQQEQIQHLKSKTNELKSEKLQIATNlqrRQQMEE-------QSVELSTEVQ 899
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEE---LREERDELREREAELEATLRTARERVEEA---EALLEAgkcpecgQPVEGSPHVE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 900 SlnreIKDAKEQISPLETALEKLQQEKEELIHR--KHTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQ----------- 966
Cdd:PRK02224 469 T----IEEDRERVEELEAELEDLEEEVEEVEERleRAEDLVEAEDRIERLEERREDLEELIAERRETIEekreraeelre 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 967 ---------DGKDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNLTLRKRRDELKEVEEE 1037
Cdd:PRK02224 545 raaeleaeaEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
....*..
gi 153945822 1038 RKQHLKE 1044
Cdd:PRK02224 625 RRERLAE 631
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-58 |
5.63e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.61 E-value: 5.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 3 RIEKMSILGVRsfGIEDKDkqiISF--FSPLTILVGPNGAGKTTIIECLKYICTGDFP 58
Cdd:COG3950 2 RIKSLTIENFR--GFEDLE---IDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLS 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
729-929 |
5.93e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 729 MLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTImpEEESAKVcltdvtimerfQMELKDVERK 808
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAAL-----------ARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 809 IAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIELN-------------------------RKLIQDQQEQIQHL 863
Cdd:COG4942 78 LAALEAELA--ELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqylKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 864 KSKTNELKSEKLQIATNLQR----RQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEEL 929
Cdd:COG4942 156 RADLAELAALRAELEAERAElealLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-1044 |
6.06e-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: 50.74 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 4 IEKMSILGVRSFgiedKDKQIISFFSPLTILVGPNGAGKTTIIECLKY---ICTGDFPPGTKGNTFVHdpKVAQETDVRA 80
Cdd:pfam02463 2 LKRIEIEGFKSY----AKTVILPFSPGFTAIVGPNGSGKSNILDAILFvlgERSAKSLRSERLSDLIH--SKSGAFVNSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 81 QIRLQFRD------VNGEMVAVHRSMLcsqKNKKTEFKTlegvitrmkHGEKVSLSskcaEIDREMIScLGVSKSVLNNV 154
Cdd:pfam02463 76 EVEITFDNedhelpIDKEEVSIRRRVY---RGGDSEYYI---------NGKNVTKK----EVAELLES-QGISPEAYNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 155 IFCHQEDsNWPLSEGKALKQKFDEIFSATRYIKALDTLRQVRQTQGQKVKE----CQTELKYLKQNKEKACEIRDQITSK 230
Cdd:pfam02463 139 VQGGKIE-IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELiidlEELKLQELKLKEQAKKALEYYQLKE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 231 EAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVFQGTDEQLNDLYHN 310
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 311 HQRTVREKERRLVDCQRELEKLNKEARL----LNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLE-----LD 381
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLKESEKEKKKaekeLKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQleeelLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 382 GFERGPFSERQIKNFHELVKERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVR 461
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 462 SELQQLEGSSDRILELDQELTKAERELSKAEKNSSIetLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQmeml 541
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ--KLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL---- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 542 TKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQ 621
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 622 LSSYEDKLFDVCGSQDLESDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEVISDL 701
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLS---ELTKELLEIQELQEKAESE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 702 QSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTIMPE 781
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 782 EESakvcltdvtimerfQMELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKL----IQDQQ 857
Cdd:pfam02463 769 LSL--------------KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEqeekIKEEE 834
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 858 EQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSN 937
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 938 KMAQDKINDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERW 1017
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
1050 1060
....*....|....*....|....*..
gi 153945822 1018 LQDNLTLRKRRDELKEVEEERKQHLKE 1044
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1177-1251 |
6.35e-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: 45.69 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1177 DKRRNYNYRVVMLKGDTA----LDMRGRCSAGQK-VLASLIIRLALAETFCLN------CGILALDEPTTNLDRENIESL 1245
Cdd:pfam13558 5 DYRNWLSFEVEVRDEDGSevetYRRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTA 84
|
....*.
gi 153945822 1246 AHALVE 1251
Cdd:pfam13558 85 LELLRA 90
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
361-655 |
6.67e-06 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 50.57 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 361 QEHIRARDSLIQSLATHLEldgFERGPFSERQIKNFHELVKERQEREAKTASQLLSDLTDKEALKqRQLDELRDRKSGLG 440
Cdd:COG5391 221 EERRQSLQNFLRRVSTHPL---LSNYKNSKSWESHSTLLSSFIENRKSVPTPLSLDLTSTTQELD-MERKELNESTSKAI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 441 RTIELKTEILTKKQSELRHVRSELQQLEgsSDRILELDQELTKAERELSKAEK--NSSIETLKAEVMSLQNEKADLDRSL 518
Cdd:COG5391 297 HNILSIFSLFEKILIQLESEEESLTRLL--ESLNNLLLLVLNFSGVFAKRLEQnqNSILNEGVVQAETLRSSLKELLTQL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 519 RKLDQEMEQLNHhtttrtQMEMLTKDKTDKDEQIRKI------KSRHSDELTS--LLGYFPNKKQ--LEDWLH--SKSKE 586
Cdd:COG5391 375 QDEIKSRESLIL------TDSNLEKLTDQNLEDVEELsrslrkNSSQRAVVSQqpEGLTSFSKLSykLRDFVQekSRSKS 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 587 INQTRDRLAKLNKELASAEQNKNHINNELKkkeeqlssYEDKLFDVCGSQDLESDLGRLKEEIEKSSKQ 655
Cdd:COG5391 449 IESLQQDKEKLEEQLAIAEKDAQEINEELK--------NELKFFFSVRNSDLEKILKSVADSHIEWAEE 509
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-56 |
6.89e-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: 50.00 E-value: 6.89e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 153945822 3 RIEKMSILGVRSFGiedkdKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGD 56
Cdd:COG3593 2 KLEKIKIKNFRSIK-----DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
317-662 |
8.23e-06 |
|
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: 49.68 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 317 EKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHL-----ELDGFERGPFSE- 390
Cdd:pfam19220 52 ELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELrdktaQAEALERQLAAEt 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 391 RQIKNFHELVKERQErEAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIE---LKTEILTKKQSELRhvrselQQL 467
Cdd:pfam19220 132 EQNRALEEENKALRE-EAQAAEKALQRAEGELATARERLALLEQENRRLQALSEeqaAELAELTRRLAELE------TQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 468 EGSSDRILELDQEL--TKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQmEMLTKDK 545
Cdd:pfam19220 205 DATRARLRALEGQLaaEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDE-AIRAAER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 546 TDKDEQI-RKIKSRHSDELtsllgyfpnKKQLEDwLHSKSKEINQTR----DRLAKLNKELASAEQNKNHINNELKKKEE 620
Cdd:pfam19220 284 RLKEASIeRDTLERRLAGL---------EADLER-RTQQFQEMQRARaeleERAEMLTKALAAKDAALERAEERIASLSD 353
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 153945822 621 QLSSYEDKLFDVcgSQDLESDLGRLKEEIEKSSKQRAMLAGA 662
Cdd:pfam19220 354 RIAELTKRFEVE--RAALEQANRRLKEELQRERAERALAQGA 393
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
182-835 |
9.26e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 182 ATRYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNR--LKEIE 259
Cdd:pfam10174 190 AEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNglLHTED 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 260 HNlskimkldNEIKALE---SRKKQMEKDNSELEQKMEKvfqgtdeqlndlyhnhqrtvreKERRLVDCQRELEKLNKEA 336
Cdd:pfam10174 270 RE--------EEIKQMEvykSHSKFMKNKIDQLKQELSK----------------------KESELLALQTKLETLTNQN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 337 RLLNQEkAELLVEQGRLQLQadrhqehiraRDSLIQSLATHLELDGFERGPFSERQIKNFHELVKERqereaKTASQLLS 416
Cdd:pfam10174 320 SDCKQH-IEVLKESLTAKEQ----------RAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEK-----STLAGEIR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 417 DLTDKEALKQRQLDelrdrksGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRIlelDQELTKAERELSkaEKNSS 496
Cdd:pfam10174 384 DLKDMLDVKERKIN-------VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNT---DTALTTLEEALS--EKERI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 497 IETLKAEVMSLQNEKADLDRSLRKLDQEMEQlnhhtttrtQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQL 576
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKE---------KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 577 EDWLHSKSKEINQTRDRLAKLnKELASAEQNKNHINNELKKKEEQLSSYEDklfDVCGSQ-DLESDLGRLKE-EIEKSSK 654
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKKA-HNAEEAVRTNPEINDRIRLLEQEVARYKE---ESGKAQaEVERLLGILREvENEKNDK 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 655 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPD-KLKSTESELKKKERRRDEMLGLV 733
Cdd:pfam10174 599 DKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQlQLEELMGALEKTRQELDATKARL 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 734 PVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKndieeQETLLGTImpEEESAKVCLtdvtimerfqMELKDVERKIAQQA 813
Cdd:pfam10174 679 SSTQQSLAEKDGHLTNLRAERRKQLEEILEMK-----QEALLAAI--SEKDANIAL----------LELSSSKKKKTQEE 741
|
650 660
....*....|....*....|..
gi 153945822 814 AKLQGVDLDRTVQQVNQEKQEK 835
Cdd:pfam10174 742 VMALKREKDRLVHQLKQQTQNR 763
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1069 |
9.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 843 TSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIatnLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKL 922
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 923 QQE----KEELIHRKHTSNKMAQD-------KINDIKEKVKNIHgYMKDIENYIQDgkddykkqketELNGVAVQLNECE 991
Cdd:COG4942 96 RAEleaqKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQ-YLKYLAPARRE-----------QAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 992 KHREKINKDMGTMRQDIDTQKIQERWLQDNLTlrKRRDELKEVEEERKQHLKEMGQMQvlqmkNEHQKLEENIDTIKR 1069
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKA--ERQKLLARLEKELAELAAELAELQ-----QEAEELEALIARLEA 234
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
692-925 |
1.21e-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: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 692 AELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEmlglvpvrqsiidlKEKEIPELRNRLQSVNRDIQRLKNDIEEQ 771
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 772 ETLLGTIMpeeESAKVCLTDVTIMERFqmelkdverkiaqqaakLQGVDLDRTVQqvnqekqekqhRLDTVTSKIELNRK 851
Cdd:COG3883 85 REELGERA---RALYRSGGSVSYLDVL-----------------LGSESFSDFLD-----------RLSALSKIADADAD 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 852 LIQDQQEQIQHLKSKTNELKSEKLQIATNL----QRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQE 925
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKaeleAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
34-106 |
1.31e-05 |
|
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: 47.88 E-value: 1.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945822 34 LVGPNGAGKTTIIECLkyicTGDFPPgTKGNTFVHDpkvaqetdvraqirlqfRDVNGEMVAVHRSM-LCSQKN 106
Cdd:cd03263 33 LLGHNGAGKTTTLKML----TGELRP-TSGTAYING-----------------YSIRTDRKAARQSLgYCPQFD 84
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
222-520 |
1.33e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 222 EIRDQITSKEAQLASSQEIVRSYEDELEPLK-----NRLKEIEHnLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKV 296
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSPH-VETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 297 --FQGTDEQLNDLYHNHQRTVR---EKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLI 371
Cdd:PRK02224 502 edLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 372 QSLAThlELDGFERGPFSERQIKNFHELVKERQEReaktasqlLSDLTDKEALKQRQLDELRDRKSGLGRTI-------- 443
Cdd:PRK02224 582 AELKE--RIESLERIRTLLAAIADAEDEIERLREK--------REALAELNDERRERLAEKRERKRELEAEFdearieea 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 444 -------ELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQELTkaERELSKAEKNSSIETLKAEVMSLQNEKADLDR 516
Cdd:PRK02224 652 redkeraEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELR--ERREALENRVEALEALYDEAEELESMYGDLRA 729
|
....
gi 153945822 517 SLRK 520
Cdd:PRK02224 730 ELRQ 733
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1227-1280 |
1.50e-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: 47.48 E-value: 1.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 153945822 1227 ILAlDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRS 1280
Cdd:cd03255 162 ILA-DEPTGNLDSET----GKEVMELLRELNKEAGTTIVVVTHDPELAEYADRI 210
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
737-930 |
1.88e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 737 QSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTImpEEESAKVcltdvtimerfQMELKDVERKIAQQAAKL 816
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL--QAEIAEA-----------EAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 817 Q--GVDLDRTVQQVNQEKqekqhrLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIAtnlQRRQQMEEQSVEL 894
Cdd:COG3883 96 YrsGGSVSYLDVLLGSES------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE---AKLAELEALKAEL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 153945822 895 STEVQSLNREIKDAKEQISPLETALEKLQQEKEELI 930
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-929 |
2.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 736 RQSIIDLKE-KEIPELRNRLQSVNRDIQRLKNDIEEQETLLgtimpeeesakvcltdvtimERFQMELKDVERKIAQQAA 814
Cdd:COG4717 64 RKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEEL--------------------EELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 815 KLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI-ATNLQRRQQMEEQSVE 893
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 153945822 894 LSTEVQSLNREIKDAKEQISPLETALEKLQQEKEEL 929
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1202-1278 |
2.24e-05 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 46.41 E-value: 2.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDREniesLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLG 1278
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALDPI----TRREVRALLKSLQAQLGITVVLVTHDLDEAARLA 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1202-1269 |
2.93e-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: 45.84 E-value: 2.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNfqLLVITH 1269
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPET----EALILEALRALAKGKT--VIVIAH 153
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-557 |
3.30e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 167 SEGKALKQKFDEIFSATRYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYED 246
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 247 ELEPLKNRLKEIEHNLSK---------------IMKLDNEIKALESRKKQMEKDNSELEQK---MEKVFQGTDEQLNDLY 308
Cdd:PRK03918 353 RLEELEERHELYEEAKAKkeelerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 309 H--------NHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLEL 380
Cdd:PRK03918 433 KakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 381 DGFERGPFSERQIKnfHELVKERQEREAKTASQLLSDLTDKEALKQR------QLDELRDRKSGLGRTIELK----TEIL 450
Cdd:PRK03918 513 KKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaelekKLDELEEELAELLKELEELgfesVEEL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 451 TKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSKAEK-----NSSIETLKAEVMSLQ------------NEKAD 513
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEelaetEKRLEELRKELEELEkkyseeeyeelrEEYLE 670
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 153945822 514 LDRSLRKLDQEMEQLNHH-TTTRTQMEMLTKDKTDKDEQIRKIKS 557
Cdd:PRK03918 671 LSRELAGLRAELEELEKRrEEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
534-772 |
3.50e-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: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 534 TRTQMEMLTKDKTDKDEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINN 613
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 614 ELKKKEEQLSSYEDKLFdvcgsqdlesDLGRLKEEIEKSSKQRAMLAGATAVYSQFITQltdenqsccpvcQRVFQTEaE 693
Cdd:COG4942 98 ELEAQKEELAELLRALY----------RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP------------ARREQAE-E 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 694 LQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQE 772
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
401-628 |
3.60e-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: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 401 KERQEREAKTASQLLSDLTDKEALKQRQLDELRDRksglgrtIELKTEILTKKQSELRHVRSELQQLEgssDRILELDQE 480
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELE---KEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 481 LTKAERELSK----AEKNSSIETLKaeVMSLQNEKADLDRSLRKLDQEMEQLnhhtttRTQMEMLTKDKTDKDEQIRKIK 556
Cdd:COG4942 99 LEAQKEELAEllraLYRLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945822 557 SRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDK 628
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
744-927 |
4.80e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 744 EKEIPELRNRLQSVNRDIQRLKN-----DIEEQETLLGTIMPEEESAkvcLTDVtimerfQMELKDVERKIAQQAAKLQG 818
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQ---LAEA------RAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 819 VDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIATNLQR-RQQMEEQSVELSTE 897
Cdd:COG3206 252 GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA---QLQQEAQRiLASLEAELEALQAR 328
|
170 180 190
....*....|....*....|....*....|...
gi 153945822 898 VQSLNREIKDAKEQIS---PLETALEKLQQEKE 927
Cdd:COG3206 329 EASLQAQLAQLEARLAelpELEAELRRLEREVE 361
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
300-491 |
5.37e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 300 TDEQLN--DLYHNHQ---RTVREKERRLVDCQRELEKLNKEARLLNQEkAELLVEQ----GRLQLQADR----HQEHIRA 366
Cdd:COG0497 140 PDAQREllDAFAGLEellEEYREAYRAWRALKKELEELRADEAERARE-LDLLRFQleelEAAALQPGEeeelEEERRRL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 367 R--DSLIQSLAT-HLELDGFERGPFSE--------RQIKNFHELVKERQER------EAKTASQLLSDLTDK-------- 421
Cdd:COG0497 219 SnaEKLREALQEaLEALSGGEGGALDLlgqalralERLAEYDPSLAELAERlesaliELEEAASELRRYLDSlefdperl 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945822 422 EALKQRqLDELRD--RKsgLGRTIElktEILTKKQSelrhVRSELQQLEGSSDRILELDQELTKAERELSKA 491
Cdd:COG0497 299 EEVEER-LALLRRlaRK--YGVTVE---ELLAYAEE----LRAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
187-350 |
5.94e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 187 KALDTLRQVRQTQGqKVKECQTELKY------LKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDE---LEPLKN---- 253
Cdd:PRK05771 57 EALDKLRSYLPKLN-PLREEKKKVSVksleelIKDVEEELEKIEKEIKELEEEISELENEIKELEQEierLEPWGNfdld 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 254 ------------RLKEIEHNLSKIMKLDNEIKALESRKKQMEKDN------SELEQKMEKVFQGTDEQLNDLYHNH--QR 313
Cdd:PRK05771 136 lslllgfkyvsvFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlKELSDEVEEELKKLGFERLELEEEGtpSE 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 153945822 314 TVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQ 350
Cdd:PRK05771 216 LIREIKEELEEIEKERESLLEELKELAKKYLEELLAL 252
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
659-712 |
5.99e-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: 5.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 153945822 659 LAGATAVYSQFITQLTDENQsCCPVCQRVFQTEaELQEVISDLQSKLRLAPDKL 712
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEG-CCPLCGRPLDEE-HRSELIKELQSKLERLPEEL 52
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
294-620 |
5.99e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 294 EKVFQGTDEQLNDLYHNHQRTVR----EKERRLVDCQRE--LEKLNKEARLLNQEKAELLVEQGRLQlqadrhqehiRAR 367
Cdd:COG3096 746 DSVFDAEELEDAVVVKLSDRQWRysrfPEVPLFGRAAREkrLEELRAERDELAEQYAKASFDVQKLQ----------RLH 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 368 DSLIQSLATHLELdGFERGPFSERQiknfhELVKERQEREAKtasqlLSDLTDKEALKQRQLDELRDRKSGLGRTIE--- 444
Cdd:COG3096 816 QAFSQFVGGHLAV-AFAPDPEAELA-----ALRQRRSELERE-----LAQHRAQEQQLRQQLDQLKEQLQLLNKLLPqan 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 445 -LKTEILTKKqseLRHVRSELQQLEGSSDRILELDQELTKAERELSKAEKN-SSIETLKAEVMSLQNEKADLDRSLRKLD 522
Cdd:COG3096 885 lLADETLADR---LEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDpEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 523 QEMEQLNH----------------HTTTRTQMEMLTKDKTDKDEQIRKIKSRHSD---ELTSLLGYFPNKKQL------- 576
Cdd:COG3096 962 EVVQRRPHfsyedavgllgensdlNEKLRARLEQAEEARREAREQLRQAQAQYSQynqVLASLKSSRDAKQQTlqeleqe 1041
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 577 ------------EDWLHSKSKEINQ----TRDRLAKLNKELASAEQNKNHINNELKKKEE 620
Cdd:COG3096 1042 leelgvqadaeaEERARIRRDELHEelsqNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
25-70 |
7.54e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 45.91 E-value: 7.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 153945822 25 ISFFSPLTILVGPNGAGKTTIIECLKYICtgDFPP--GTKGNTFVHDP 70
Cdd:COG3910 33 LEFHPPVTFFVGENGSGKSTLLEAIAVAA--GFNPegGSKNFRFSTRE 78
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
421-659 |
9.57e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 421 KEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRhvRSELQQLEGSSDRILELDQELTKAERELSkaEKNSSIETL 500
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLRE--EKKKVSVKSLEELIKDVEEELEKIEKEIK--ELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 501 KAEVMSLQNEKADLDRsLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKI-------------------KSRHSD 561
Cdd:PRK05771 113 ENEIKELEQEIERLEP-WGNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVenveyistdkgyvyvvvvvLKELSD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 562 ELTSLL---GY----FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAeqnKNHINNELKKKEEQLSSYEDKlFDVCg 634
Cdd:PRK05771 192 EVEEELkklGFerleLEEEGTPSELIREIKEELEEIEKERESLLEELKEL---AKKYLEELLALYEYLEIELER-AEAL- 266
|
250 260 270
....*....|....*....|....*....|....*...
gi 153945822 635 SQDLESD-------------LGRLKEEIEKSSKQRAML 659
Cdd:PRK05771 267 SKFLKTDktfaiegwvpedrVKKLKELIDKATGGSAYV 304
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
571-772 |
1.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 571 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLfdvcgsQDLESDLGRLKEEIE 650
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI------AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 651 K--SSKQR--------AMLAGATAVySQFITQLTdenqsccpVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELK 720
Cdd:COG3883 90 EraRALYRsggsvsylDVLLGSESF-SDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153945822 721 KKERRRDEMLGLVpvrQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQE 772
Cdd:COG3883 161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
691-924 |
1.06e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 691 EAELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMlglvpvrQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEE 770
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-------QAEIAEAEAEIEERREELGERARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 771 QETLLGTIMPEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIElnr 850
Cdd:COG3883 105 LDVLLGSESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKA--ELEAKLAELEALKAELEAAKAELEAQQA--- 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945822 851 kliqDQQEQIQHLKSKTNELKSEKLQiatnLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQ 924
Cdd:COG3883 179 ----EQEALLAQLSAEEAAAEAQLAE----LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1199-1275 |
1.18e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.21 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 1199 GRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFVE 1275
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL----------DDFPgtVLLVSHDRYFLD 493
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
210-1023 |
1.21e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 210 LKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIE--HNLSKIMKLDNEI-KALESRKKQMEKDN 286
Cdd:TIGR01612 1485 INELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAikNKFAKTKKDSEIIiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 287 SELEQKMEKVFQGTDEQLNDLYHNHQrtvreKERRLVDCQRELEKL-NKEARLLNQEKaellveqgrlqlqadrhqehiR 365
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKNDK-----SNKAAIDIQLSLENFeNKFLKISDIKK---------------------K 1618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 366 ARDSLIQSLAThleldgfergpfsERQIKNFHelvKERQEREAKTASQLLSDLtdkealkQRQLDELRDRKsglgRTIEL 445
Cdd:TIGR01612 1619 INDCLKETESI-------------EKKISSFS---IDSQDTELKENGDNLNSL-------QEFLESLKDQK----KNIED 1671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 446 KTEILTKKQSELRHVRSELQQLEGSSD-RILELDQELTKAERELSKAEKNSSIETLKAEVMSLQN---EKADLDRSLRKL 521
Cdd:TIGR01612 1672 KKKELDELDSEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTndlEGIDPNEKLEEY 1751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 522 DQEM-----EQLNHHTTTRTQMEMLTKDKTDKDEqirkIKSRHSDELTSLLGYFPNKKQLEDWLHS-KSKE----INQTR 591
Cdd:TIGR01612 1752 NTEIgdiyeEFIELYNIIAGCLETVSKEPITYDE----IKNTRINAQNEFLKIIEIEKKSKSYLDDiEAKEfdriINHFK 1827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 592 DRLAKLNKELASAEQNKNHINNELKKKEEQL--SSYEDKLFDVCgSQDLESDLGRL-------KEEIEKSSKQRAMLAGA 662
Cdd:TIGR01612 1828 KKLDHVNDKFTKEYSKINEGFDDISKSIENVknSTDENLLFDIL-NKTKDAYAGIIgkkyysyKDEAEKIFINISKLANS 1906
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 663 TAVYSQfitqltdeNQSCCPVCQRVfqTEAELQEVISDLQSKLRLAPDKLKSTESELKKkerrRDEMLGLVPVRQSIIDL 742
Cdd:TIGR01612 1907 INIQIQ--------NNSGIDLFDNI--NIAILSSLDSEKEDTLKFIPSPEKEPEIYTKI----RDSYDTLLDIFKKSQDL 1972
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 743 KEKEipelRNRLQSVNRDiQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGVDLD 822
Cdd:TIGR01612 1973 HKKE----QDTLNIIFEN-QQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKLSCDSQNYDTILELSKQD 2047
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 823 RTVQQVNQEKQEKQH-----RLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKlqiATNLQRRQQMEEQSVELSTE 897
Cdd:TIGR01612 2048 KIKEKIDNYEKEKEKfgidfDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEK---DNIIQSKKKLKELTEAFNTE 2124
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 898 VQSLNREIKDAKEQISPLetalekLQQEKEELIHRKHTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKE 977
Cdd:TIGR01612 2125 IKIIEDKIIEKNDLIDKL------IEMRKECLLFSYATLVETLKSKVINHSEFITSAAKFSKDFFEFIEDISDSLNDDID 2198
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 153945822 978 TElnGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNLT 1023
Cdd:TIGR01612 2199 AL--QIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINNLT 2242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
172-608 |
1.56e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 172 LKQKFDEIFSATRYIKALDTLRQVRQTQGQKVKECQT-ELKYLKQNKEKACEIRDQITSKEAQLASS------QEIVRSY 244
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAvVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 245 EDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVFQGTDEQLNDLYHNHQRTVREKERRLVD 324
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 325 CQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIrardSLIQSLATHleldgfergpfSERQIKNFHELVKERQ 404
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL----TLTQERVRE-----------HALSIRVLPKELLASR 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 405 EREAKTASQLLSDLT-DKEALKQRQ--LDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRI------- 474
Cdd:TIGR00618 679 QLALQKMQSEKEQLTyWKEMLAQCQtlLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQartvlka 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 475 LELDQElTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQ-LNHHTTTRT-QMEMLTKDKTDKDEQI 552
Cdd:TIGR00618 759 RTEAHF-NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeIPSDEDILNlQCETLVQEEEQFLSRL 837
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945822 553 RKiKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNK 608
Cdd:TIGR00618 838 EE-KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDA 892
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1227-1279 |
1.56e-04 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 44.65 E-value: 1.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 153945822 1227 ILAlDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGR 1279
Cdd:COG1136 166 ILA-DEPTGNLDSKT----GEEVLELLRELNRELGTTIVMVTHDPELAARADR 213
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
327-620 |
1.58e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 327 RE--LEKLNKEARLLNQEKAELLVEQGRLQlqadrhqehiRARDSLIQSLATHLELdGFERGPfsERQIKnfhELVKERQ 404
Cdd:PRK04863 784 REkrIEQLRAEREELAERYATLSFDVQKLQ----------RLHQAFSRFIGSHLAV-AFEADP--EAELR---QLNRRRV 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 405 EREAKtasqlLSDLTDKEALKQRQLDELRDRKSGLGRTIE----LKTEILTKKQSELRHVRSELQQLEGSSDRileLDQE 480
Cdd:PRK04863 848 ELERA-----LADHESQEQQQRSQLEQAKEGLSALNRLLPrlnlLADETLADRVEEIREQLDEAEEAKRFVQQ---HGNA 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 481 LTKAERELSK-AEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTT----------------RTQMEMLTK 543
Cdd:PRK04863 920 LAQLEPIVSVlQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEdaaemlaknsdlneklRQRLEQAEQ 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 544 DKTDKDEQIRKIKSRHSDE---LTSLLGYFPNKKQ-------------------LEDWLHSKSKEINQ----TRDRLAKL 597
Cdd:PRK04863 1000 ERTRAREQLRQAQAQLAQYnqvLASLKSSYDAKRQmlqelkqelqdlgvpadsgAEERARARRDELHArlsaNRSRRNQL 1079
|
330 340
....*....|....*....|...
gi 153945822 598 NKELASAEQNKNHINNELKKKEE 620
Cdd:PRK04863 1080 EKQLTFCEAEMDNLTKKLRKLER 1102
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
463-660 |
1.59e-04 |
|
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: 44.92 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 463 ELQQLEgssDRILELDQELTKAERELSKAEKNssIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNhhtttrtqmEMLT 542
Cdd:COG1579 11 DLQELD---SELDRLEHRLKELPAELAELEDE--LAALEARLEAAKTELEDLEKEIKRLELEIEEVE---------ARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 543 KDKtdkdEQIRKIKSrhSDELTSLLgyfpnkKQLEdwlhSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQL 622
Cdd:COG1579 77 KYE----EQLGNVRN--NKEYEALQ------KEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 153945822 623 SSYEdklfdvcgsQDLESDLGRLKEEIEKSSKQRAMLA 660
Cdd:COG1579 141 EEKK---------AELDEELAELEAELEELEAEREELA 169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
186-651 |
1.66e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 186 IKALDTLRQVRQTQGQKVKECQTELKYLKQNKEkacEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNL--- 262
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALlea 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 263 -SKIMKLDNEIKALESRKKQMEKDNSELEQKMEKV------FQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKE 335
Cdd:COG1196 371 eAELAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 336 ARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLEL--------DGFERGPFSERQIKNFHEL-------- 399
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLlleaeadyEGFLEGVKAALLLAGLRGLagavavli 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 400 ---VKERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGlgrtielKTEILTKKQSELRHVRSELQQLEGSSDRILE 476
Cdd:COG1196 531 gveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-------RATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 477 LDQELTKAERELSKAEKNSSIETLKAEVM-SLQNEKADLDRSLRKLDQEMEQLNhhtTTRTQMEMLTKDKTDKDEQIRKI 555
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGS---AGGSLTGGSRRELLAALLEAEAE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 556 KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCG- 634
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPp 760
|
490
....*....|....*...
gi 153945822 635 -SQDLESDLGRLKEEIEK 651
Cdd:COG1196 761 dLEELERELERLEREIEA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
829-1022 |
1.69e-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: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 829 NQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIATNLQRRQQMEEQSVELSTEVQSLNREIKDA 908
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---QLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 909 KEQISPLETALEKL--------QQEKEELIHRKHTSNKMA-------------QDKINDIKEKVKNIHGYMKDIENYIQD 967
Cdd:COG4942 96 RAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVrrlqylkylaparREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153945822 968 gKDDYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKIQERWLQDNL 1022
Cdd:COG4942 176 -LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-50 |
2.18e-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: 2.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 153945822 4 IEKMSILGVRSFGiedkDKQIISFFSPLTILVGPNGAGKTTIIECLK 50
Cdd:cd03278 1 LKKLELKGFKSFA----DKTTIPFPPGLTAIVGPNGSGKSNIIDAIR 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-546 |
2.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 3 RIEKMSILGVRSFgiedkDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGDFppgtkgntfvhdpkvaqetdvraqi 82
Cdd:COG4717 2 KIKELEIYGFGKF-----RDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 83 rlqfrdvngemvavhrsmlcsQKNKKTEFKtlegvitrmKHGEKVSLSSKCAEIDREMIsclgvsksvlnnvifchqeds 162
Cdd:COG4717 52 ---------------------EKEADELFK---------PQGRKPELNLKELKELEEEL--------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 163 nwplsegKALKQKFDEIFSAtryIKALDTLRQVRQTQGQKVKECQTELKYLKQnKEKACEIRDQITSKEAQLASSQEIVR 242
Cdd:COG4717 81 -------KEAEEKEEEYAEL---QEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERLE 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 243 SYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDnsELEQKMEKVfqgtdEQLNDLYHNHQRTVREKERRL 322
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEEL-----EELQQRLAELEEELEEAQEEL 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 323 VDCQRELEKLNKEARLLNQEK---------------AELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLELDGFERG- 386
Cdd:COG4717 223 EELEEELEQLENELEAAALEErlkearlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGk 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 387 PFSERQIKNFHELVKERQEREAKTASQLLSDLTDKEAL----KQRQLDELRDRKSGLGRTIELKtEILTKKQSELRHV-- 460
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLelldRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAgv 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 461 --RSELQQLEGSSDRILELDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHH-TTTRTQ 537
Cdd:COG4717 382 edEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREElAELEAE 461
|
....*....
gi 153945822 538 MEMLTKDKT 546
Cdd:COG4717 462 LEQLEEDGE 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
692-1278 |
2.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 692 AELQEVISDLQSKLRLAPDKLKSTESELKKKERrrdeMLGLVPVRQSIIDLKEkEIPELRNRLQSVNRDIQRLKNDIEEQ 771
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 772 ETLLGTIMPEEESAKVCLTDVTIMERfqMELKDVERKIAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRK 851
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLA--ELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 852 LIQDQQEQ--------IQHLKSKTNELKSEKLQIATNLQRRQQMeeqsveLSTEVQSLNREIKDAKEQISPLE--TALEK 921
Cdd:COG4717 242 EERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQalPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 922 LQQEK-EELIHRKHTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQDGK------------DDYKKQKETELNGVAVQLN 988
Cdd:COG4717 316 LEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqeiaallAEAGVEDEEELRAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 989 ECEKHREKINkdmgTMRQDIDTQKIQERWLQDNLTLRKRRDELKEVEEERKQHLKEMGQMQvlqmkNEHQKLEENIDTIK 1068
Cdd:COG4717 396 EYQELKEELE----ELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR-----EELAELEAELEQLE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1069 RNHSLAlgrqkgyedEILHFKKELREpQFRDAEEKYREMMIVmrttelvnkdldiyYKTLDQAIMKFHSMKMEEINKIIR 1148
Cdd:COG4717 467 EDGELA---------ELLQELEELKA-ELRELAEEWAALKLA--------------LELLEEAREEYREERLPPVLERAS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1149 DLWRSTYRGqdiEYIEIRSDADENVSASDKRRNYnYRVVMLkgdtaldmrgrcSAGQKVLASLIIRLALAETFCLNCGIL 1228
Cdd:COG4717 523 EYFSRLTDG---RYRLIRIDEDLSLKVDTEDGRT-RPVEEL------------SRGTREQLYLALRLALAELLAGEPLPL 586
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 153945822 1229 ALDEPTTNLDRENIESLAHALVEIIKSRsqqrnfQLLVITHDEDFVELLG 1278
Cdd:COG4717 587 ILDDAFVNFDDERLRAALELLAELAKGR------QVIYFTCHEELVELFQ 630
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
168-642 |
3.07e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 168 EGKALKQKFDEIFSATRYIKALDTLRQVRQTQgQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLAS-SQEIVRSYED 246
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSA-QRVELAERQLQELKIDVKSISSLKLVNLELESEIIElKKSLSSDLIE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 247 ELEPLKNRLKEIEHNLSKIMKLDNEIKALESrKKQMEKDNSElEQKMEKvfqgTDEQLNDLYHNHQRTVREkerrlvdcq 326
Cdd:COG5022 922 NLEFKTELIARLKKLLNNIDLEEGPSIEYVK-LPELNKLHEV-ESKLKE----TSEEYEDLLKKSTILVRE--------- 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 327 reLEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEhiraRDSLIQSLATHLELDGFErgPFSERQIKNFHELVKERQER 406
Cdd:COG5022 987 --GNKANSELKNFKKELAELSKQYGALQESTKQLKE----LPVEVAELQSASKIISSE--STELSILKPLQKLKGLLLLE 1058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 407 EAKTASQLLSDLTDKEALKQRQLDELRDRK-SGLGRTIELKTEILTKKQSELRhvRSELQQLEGSSDRILELDQeltkae 485
Cdd:COG5022 1059 NNQLQARYKALKLRRENSLLDDKQLYQLEStENLLKTINVKDLEVTNRNLVKP--ANVLQFIVAQMIKLNLLQE------ 1130
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 486 relskaeknsSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKSRHS----- 560
Cdd:COG5022 1131 ----------ISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSssevn 1200
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 561 ---DELTSLLGYFPnkkqlEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHIN-NELKKKEEQLSSYEDKLFDVCGSQ 636
Cdd:COG5022 1201 dlkNELIALFSKIF-----SGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFdTPASMSNEKLLSLLNSIDNLLSSY 1275
|
....*.
gi 153945822 637 DLESDL 642
Cdd:COG5022 1276 KLEEEV 1281
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
402-896 |
3.10e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 402 ERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELdqel 481
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL---- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 482 tKAERELSKAEknssIETLKAEVMSLQNEKADLDRSLRkldqemEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKSRHSD 561
Cdd:PRK02224 299 -LAEAGLDDAD----AEAVEARREELEDRDEELRDRLE------ECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 562 eltsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQ-DLES 640
Cdd:PRK02224 368 --------------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREaELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 641 DLGRLKEEIEKSSkqramlagatavysqfitQLTDENQscCPVC-----------------QRVFQTEAELQEV---ISD 700
Cdd:PRK02224 434 TLRTARERVEEAE------------------ALLEAGK--CPECgqpvegsphvetieedrERVEELEAELEDLeeeVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 701 LQSKLRLAPDkLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPELRNR--------------------------- 753
Cdd:PRK02224 494 VEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERaaeleaeaeekreaaaeaeeeaeeare 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 754 --------LQSVNRDIQRLkNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME-LKDVERKIAQQAAKLQGvdlDRt 824
Cdd:PRK02224 573 evaelnskLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRErLAEKRERKRELEAEFDE---AR- 647
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945822 825 VQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKT---NELKSEKLQIATNLQRRQQMEEQSVELST 896
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELeelEELRERREALENRVEALEALYDEAEELES 722
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1192-1270 |
3.10e-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: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1192 DTALDMRGRC-SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHD 1270
Cdd:COG4618 458 DTRIGEGGARlSGGQRQ------RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-----KARGATVVVITHR 526
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
800-951 |
3.23e-04 |
|
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: 43.76 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 800 MELKDVERKIAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEK----- 874
Cdd:COG1579 17 SELDRLEHRLKELPAELA--ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyeal 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 875 -LQIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEKV 951
Cdd:COG1579 95 qKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1195-1279 |
3.38e-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: 43.73 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1195 LDM----RGR-CSAGQKVLasliirLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1269
Cdd:cd03245 130 LDLqigeRGRgLSGGQRQA------VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT------LIIITH 197
|
90
....*....|
gi 153945822 1270 DEDFVELLGR 1279
Cdd:cd03245 198 RPSLLDLVDR 207
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-50 |
3.56e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.54 E-value: 3.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 153945822 3 RIEKMSILGVRSFGIEDKDkqiisfFSPLTILVGPNGAGKTTIIECLK 50
Cdd:COG4637 1 MITRIRIKNFKSLRDLELP------LGPLTVLIGANGSGKSNLLDALR 42
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-55 |
4.22e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 43.99 E-value: 4.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 153945822 3 RIEKMSILGVRSFgiedkDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTG 55
Cdd:COG1195 1 RLKRLSLTNFRNY-----ESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATG 48
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
662-929 |
4.86e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 662 ATAVYSQFITQLTDENQsccpvcQRVFQTEAELQEVISDLQSKLRlapdklkstESELKKKERRRdemlglvpvRQSIID 741
Cdd:COG3206 154 ANALAEAYLEQNLELRR------EEARKALEFLEEQLPELRKELE---------EAEAALEEFRQ---------KNGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 742 LKEkEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTI---MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQg 818
Cdd:COG3206 210 LSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALraqLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYT- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 819 vDLDRTVQQVNQEKQEKQHRLDtvtskiELNRKLIQDQQEQIQHLKSKTNELKSeklQIATNLQRRQQMEEQSVELstev 898
Cdd:COG3206 288 -PNHPDVIALRAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQA---QLAQLEARLAELPELEAEL---- 353
|
250 260 270
....*....|....*....|....*....|.
gi 153945822 899 QSLNREIKDAKEQispletaLEKLQQEKEEL 929
Cdd:COG3206 354 RRLEREVEVAREL-------YESLLQRLEEA 377
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1202-1275 |
4.92e-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: 43.03 E-value: 4.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 1202 SAGQKVLASLIIRLALAETFCLNCGI----LALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITHDEDFVE 1275
Cdd:cd03279 125 SGGETFLASLSLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALELI-----RTENRMVGVISHVEELKE 197
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1214-1270 |
5.19e-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: 42.88 E-value: 5.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 153945822 1214 RLALAETFCLNCGILALDEPTTNLDRenieSLAHALVEIIKSRSQQRNFQLLVITHD 1270
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDV----SVQAQILDLLKKLQEELGLTLLFITHD 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1202-1273 |
5.75e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.29 E-value: 5.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDF 1273
Cdd:COG0488 154 SGGWRR------RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----------KNYPgtVLVVSHDRYF 211
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
795-1064 |
5.92e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 795 MERFQM-ELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIelnrkliqdqqeqIQHLKSKTNELKSE 873
Cdd:PRK05771 6 MKKVLIvTLKSYKDEVLEALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEA-------------LDKLRSYLPKLNPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 874 KLQIATnlQRRQQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIH--------RKHTSNKMAQDKIN 945
Cdd:PRK05771 73 REEKKK--VSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdldlSLLLGFKYVSVFVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 946 DIKEKVKNIHGYMKDIENYIqdgkddYKKQKETELNGVAVQLNECEKHREKINKDMGTMRQDIDTQKI-QERwlqdnltL 1024
Cdd:PRK05771 151 TVPEDKLEELKLESDVENVE------YISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLELEEEGTpSEL-------I 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 153945822 1025 RKRRDELKEVEEERKQHLKEmgqmqvlqMKNEHQKLEENI 1064
Cdd:PRK05771 218 REIKEELEEIEKERESLLEE--------LKELAKKYLEEL 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1214-1281 |
6.34e-04 |
|
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: 42.81 E-value: 6.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 1214 RLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEdfvELLGRSE 1281
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAAT----GEQIIDLLFELNRERGTTLVLVTHDP---ALAARCD 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1202-1269 |
6.37e-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: 42.20 E-value: 6.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEiIKSRSQQRnfqlLVITH 1269
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGATR----IVIAH 154
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
853-1050 |
6.79e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 853 IQDQQEQIQHLKSKTNELKSEKLQIATNLQrrqQMEEQSVELSTEVQSLNREIKDAKEQISPLETALEKLQQEKEELIHR 932
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 933 KHTS------------NKMAQDKINDIkEKVKNIHGYMKDIENYIQDGKDDYKKQKETelngVAVQLNECEKHRekinKD 1000
Cdd:COG3883 95 LYRSggsvsyldvllgSESFSDFLDRL-SALSKIADADADLLEELKADKAELEAKKAE----LEAKLAELEALK----AE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153945822 1001 MGTMRQDIDTQKIQERWLQDNLT--LRKRRDELKEVEEERKQHLKEMGQMQV 1050
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSaeEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
586-1067 |
7.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 586 EINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDLES-DLGRLKEEIEKSSKQRAMLAGATA 664
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 665 VYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKL---RLAPDKLKSTESELKKKERRRDEMLGLVPVR----Q 737
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeeaREAVEDRREEIEELEEEIEELRERFGDAPVDlgnaE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 738 SIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGT------IMPEEESAKVCltdvTIMERFQmELKDVERKIAQ 811
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGSPHVE----TIEEDRE-RVEELEAELED 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 812 QAAKLQGVD--LDRTVQQVNQEKQ--EKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKlqiatnlqrrQQM 887
Cdd:PRK02224 487 LEEEVEEVEerLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA----------EEK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 888 EEQSVELSTEVQSLNREIKDAKEQISPLETALEKLqqekeelihrkhtsnkmaqDKINDIKEkvknihgymkDIENYIQD 967
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESL-------------------ERIRTLLA----------AIADAEDE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 968 gkddykkqketelngvAVQLNECEKHREKINkdmgtmrqdidtqkiqerwlqdnltlRKRRDELKEVEEERKQHLKEMGQ 1047
Cdd:PRK02224 608 ----------------IERLREKREALAELN--------------------------DERRERLAEKRERKRELEAEFDE 645
|
490 500
....*....|....*....|
gi 153945822 1048 MQVLQMKNEHQKLEENIDTI 1067
Cdd:PRK02224 646 ARIEEAREDKERAEEYLEQV 665
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1192-1269 |
8.04e-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: 43.49 E-value: 8.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 1192 DTALDMRGR-CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsQQRNFQLLVITH 1269
Cdd:TIGR01842 445 DTVIGPGGAtLSGGQRQ------RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-----KARGITVVVITH 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
225-376 |
9.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 225 DQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEhnlSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVFQGTDEQL 304
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 305 NDLYHNHQ------------------------RTVREKERRLVDCQREL-EKLNKEARLLNQEKAELLVEQGRLQLQADR 359
Cdd:COG3883 93 RALYRSGGsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADkAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170
....*....|....*..
gi 153945822 360 HQEHIRARDSLIQSLAT 376
Cdd:COG3883 173 LEAQQAEQEALLAQLSA 189
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
205-295 |
9.84e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 205 ECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEK 284
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERE 486
|
90
....*....|.
gi 153945822 285 DNSELEQKMEK 295
Cdd:COG2433 487 RIEELKRKLER 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-528 |
1.17e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 311 HQRTVREKERRLVDCQRELEklnkEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATHLELDGFERGPFSE 390
Cdd:COG1196 592 LARGAIGAAVDLVASDLREA----DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 391 RQIKNFHELVKERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGS 470
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 471 SDRIL-----------ELDQELTKAERELSK------------AEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQ 527
Cdd:COG1196 748 LEEEAleelpeppdleELERELERLEREIEAlgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
.
gi 153945822 528 L 528
Cdd:COG1196 828 R 828
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
298-529 |
1.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 298 QGTDEQLNDLyhnhQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQGRLQLQADRHQEHIRARDSLIQSLATH 377
Cdd:COG3883 19 QAKQKELSEL----QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 378 LELDGFERGPFSErqiknfheLVkerqerEAKTASQLLSDLTDKEALKQRQLDELRDRKSglgrtielKTEILTKKQSEL 457
Cdd:COG3883 95 LYRSGGSVSYLDV--------LL------GSESFSDFLDRLSALSKIADADADLLEELKA--------DKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945822 458 RHVRSELQQLEGssdrilelDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLN 529
Cdd:COG3883 153 EAKLAELEALKA--------ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
264-548 |
1.41e-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: 43.19 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 264 KIMKLDNEIKALESRKKQMEKDNSELEQKMEKVFQGTDEQLNDLYHNHQRTVREKER-----RLVDCQRELEKLNKEARL 338
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREReleriRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 339 LNQEKaelLVEQGRLQLQADRHQEHIRA--------------RDSLIQSLATHLELDGFERGPFSERQIKNFHELVKERQ 404
Cdd:pfam17380 372 MEISR---MRELERLQMERQQKNERVRQeleaarkvkileeeRQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 405 ER---EAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQ--------QLEGSSDR 473
Cdd:pfam17380 449 ERvrlEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEErkrkllekEMEERQKA 528
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945822 474 ILElDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDrSLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDK 548
Cdd:pfam17380 529 IYE-EERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE-AMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
688-935 |
1.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 688 FQTEAELQEVISDLqsklrlapDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEK--EIPELRNRLQSVN--RDIQR 763
Cdd:COG4913 221 PDTFEAADALVEHF--------DDLERAHEALEDAREQIELLEPIRELAERYAAARERlaELEYLRAALRLWFaqRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 764 LKNDIEEQETLLGTIMPEEESAKVcltdvtimerfqmELKDVERKIAQQAAKLQGVDLDRtVQQVNQEKQEKQHRLDTVt 843
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEA-------------RLDALREELDELEAQIRGNGGDR-LEQLEREIERLERELEER- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 844 skielnRKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQmeeqsvELSTEVQSLNREIKDAKEQISPLETALEKLQ 923
Cdd:COG4913 358 ------ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE------ALEEELEALEEALAEAEAALRDLRRELRELE 425
|
250
....*....|..
gi 153945822 924 QEKEELIHRKHT 935
Cdd:COG4913 426 AEIASLERRKSN 437
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
166-765 |
1.59e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 166 LSEGKALKQKFDEIFSATRYIKALDTLRQVRQTQGQKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYE 245
Cdd:pfam05557 31 ELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 246 DELEPLKnrlkeiehnlSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVfqgtdEQLNDLYHNHQRTVREKERRLVDC 325
Cdd:pfam05557 111 NELSELR----------RQIQRAELELQSTNSELEELQERLDLLKAKASEA-----EQLRQNLEKQQSSLAEAEQRIKEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 326 QRELEKLNKEARLLNQEKAELLvEQGRLQLQADRHQEHIRARDSLIQS-LATHLELDGFERGpfSERQIKNFHELVKERQ 404
Cdd:pfam05557 176 EFEIQSQEQDSEIVKNSKSELA-RIPELEKELERLREHNKHLNENIENkLLLKEEVEDLKRK--LEREEKYREEAATLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 405 EREaktasQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQ------SELRHVRSELQQLEGssdrilELD 478
Cdd:pfam05557 253 EKE-----KLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEenssltSSARQLEKARRELEQ------ELA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 479 QELTKAERELSKAEKNSS-IETLKAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKS 557
Cdd:pfam05557 322 QYLKKIEDLNKKLKRHKAlVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 558 RHSDELTSLLGYfpnkkqledwlhskskeinqtRDRLAKLNKELASAEQNKNHinNELKKKEEQLSSYEDKLfdvcgsQD 637
Cdd:pfam05557 402 QLSVAEEELGGY---------------------KQQAQTLERELQALRQQESL--ADPSYSKEEVDSLRRKL------ET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 638 LESDLGRLKEEIE--KSSKQRAMLAGatavysqfitqltDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKst 715
Cdd:pfam05557 453 LELERQRLREQKNelEMELERRCLQG-------------DYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLK-- 517
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 153945822 716 esELKKKERRRDEMLGLVPvrQSIIDLKEKEIPELRNRLQSVNRDIQRLK 765
Cdd:pfam05557 518 --RLLKKLEDDLEQVLRLP--ETTSTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1190-1270 |
1.71e-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: 41.36 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1190 KGDTALDMRG------RC----SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIEslahALVEIIKsRSQQ 1259
Cdd:cd03235 112 KVDEALERVGlseladRQigelSGGQQQ------RVLLARALVQDPDLLLLDEPFAGVDPKTQE----DIYELLR-ELRR 180
|
90
....*....|.
gi 153945822 1260 RNFQLLVITHD 1270
Cdd:cd03235 181 EGMTILVVTHD 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1214-1270 |
1.82e-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: 1.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 1214 RLALAETFCLNCGILALDEPTTNLDreniesLAH--ALVEIIKSRSQQRNFQLLVITHD 1270
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLD------IAHqiELLELLRRLARERGKTVVMVLHD 157
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
794-943 |
1.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 794 IMERFQMELKDVERKI---AQQAAKLQGVDLDRTVQQVNQEKQEKQHRL----DTVTSKIELNRKLIQDQQEQIQHLKSK 866
Cdd:PRK12704 43 ILEEAKKEAEAIKKEAlleAKEEIHKLRNEFEKELRERRNELQKLEKRLlqkeENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945822 867 TNELKSEKLQIATNLQRRQQMEEQSVELSTEvqslnreikDAKEQIspLETALEKLQQEKEELIHRKHTSNKMAQDK 943
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEIL--LEKVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
821-954 |
1.93e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 821 LDRTVQQVNQEKQEKQHRLDTVTSKIELNRKLIQDQQEQIQH-LKSKTNELKSEKLQIATNLQRRQQMEEQSVELSTEVQ 899
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIE 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 153945822 900 SLNREIKDAKEQISPLETALEKlqqekeelihrkhtSNKMAQDKINDIKEKVKNI 954
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQ--------------CRGFTFKEIEKLKEQLKLL 283
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
204-660 |
2.01e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 204 KECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDNEIKALESRKKQME 283
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 284 KDNSELEQ--KMEKVFQGTDEQLNdlyhnhqrtvREKERRLVDcqrELEKLNKEARllNQEKAELLVEQGRLQLQADRHQ 361
Cdd:PTZ00121 1402 EDKKKADElkKAAAAKKKADEAKK----------KAEEKKKAD---EAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKA 1466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 362 EHIRARDSLIQSLATHLELDGFERGpfSERQIKNFHELVKERQER----EAKTASQLLSDLTDKEALKQRQLDELRdrks 437
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKK--AEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEAKKADEAK---- 1540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 438 glgRTIELKTEILTKKQSELRHVRsELQQLEGSSDRILELDQELTKAErELSKAEKnSSIETLKAEVMSLQNEKADLDRS 517
Cdd:PTZ00121 1541 ---KAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAE-EAKKAEE-ARIEEVMKLYEEEKKMKAEEAKK 1614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 518 LRKLDQEMEQLNHHTTTRTQMEMLTKDKTD---KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRL 594
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945822 595 AKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDLESDLGRLKEEIEKSSKQRAMLA 660
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
573-1107 |
2.17e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 573 KKQLEDWLHSKSKEINQTRDRLaklNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCgSQDLE------SDLGRLK 646
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDEL---NGELSAADAAVAKDRSELEALEDQHGAFLDADIETA-AADQEqlpswqSELENLE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 647 EEIE-----KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRlapDKLKSTESELKK 721
Cdd:pfam12128 361 ERLKaltgkHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR---EQLEAGKLEFNE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 722 KERRRDEMLGLVPVRQSIIDLKEKEIPELRNRLQSVNRdiqrlkndieEQETLlgtimpEEESAKVcltdvtimERFQME 801
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPELLLQLENFDERIER----------AREEQ------EAANAEV--------ERLQSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 802 LKDVERKIAQQAAKLQgvDLDRTVQQVNQEKQEKQHRLDTVT-SKIELNRKLIQDQQEQIQHLKSK-------------- 866
Cdd:pfam12128 494 LRQARKRRDQASEALR--QASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVISPellhrtdldpevwd 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 867 ---------------------------TNELKSEKLQIATNLQ----RRQQMEEQSVELSTEVQSLNREIKDAKEQISPL 915
Cdd:pfam12128 572 gsvggelnlygvkldlkridvpewaasEEELRERLDKAEEALQsareKQAAAEEQLVQANGELEKASREETFARTALKNA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 916 ETALEKLQQEKEELIHRKHTSNKMAQDKINdikEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNGVAVQLNECEkhrE 995
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNKALAERKDSAN---ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE---G 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 996 KINKDMGTMRQDIDTQKIQerwlqdnltlrkRRDELKEVEEERKQHLKEMG--QMQVLQMKNEHQKLEENIDTIKRNHSL 1073
Cdd:pfam12128 726 ALDAQLALLKAAIAARRSG------------AKAELKALETWYKRDLASLGvdPDVIAKLKREIRTLERKIERIAVRRQE 793
|
570 580 590
....*....|....*....|....*....|....
gi 153945822 1074 ALGRQKGYEDEILHFKKELREpQFRDAEEKYREM 1107
Cdd:pfam12128 794 VLRYFDWYQETWLQRRPRLAT-QLSNIERAISEL 826
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1192-1269 |
2.34e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.07 E-value: 2.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 1192 DTALDMRG-RCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSqqrnfqLLVITH 1269
Cdd:COG1132 467 DTVVGERGvNLSGGQRQ------RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT------TIVIAH 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1202-1274 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945822 1202 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDreniESLAHALVEIIKSRSQQRNFQLLVITHDEDFV 1274
Cdd:COG1123 144 SGGQRQ------RVAIAMALALDPDLLIADEPTTALD----VTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
34-98 |
2.72e-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: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945822 34 LVGPNGAGKTTIIECLkyicTGDFPPgTKGntfvhdpkvaqetdvraQIRLQFRDVNGemVAVHR 98
Cdd:COG0411 35 LIGPNGAGKTTLFNLI----TGFYRP-TSG-----------------RILFDGRDITG--LPPHR 75
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-98 |
2.73e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.13 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 9 ILGVRSFGIEDKDKQIISffspltiLVGPNGAGKTTIIECLkyicTGDFPP--GT---KGNTFVHDP--KVAQETDVRA- 80
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVS-------LIGPNGAGKTTVFNCL----TGFYKPtgGTillRGQHIEGLPghQIARMGVVRTf 86
|
90 100
....*....|....*....|..
gi 153945822 81 -QIRLqFRD---VNGEMVAVHR 98
Cdd:PRK11300 87 qHVRL-FREmtvIENLLVAQHQ 107
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
661-928 |
2.95e-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: 42.03 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 661 GATAVYSQFITQLTDENQSCCPVCQRVFQTEAElqevisdlqsklRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSII 740
Cdd:pfam17380 262 GQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE------------KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 741 DLKEKEIPELRNRLQSVNRDIQRLKndIEEQETLLGTIMPEEESAKVclTDVTIMERFQMELKDVERKIAQQ-------- 812
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIR--QEERKRELERIRQEEIAMEI--SRMRELERLQMERQQKNERVRQEleaarkvk 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 813 --------AAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSK-IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQR 883
Cdd:pfam17380 406 ileeerqrKIQQQKVEMEQIRAEQEEARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 153945822 884 RQQMEEQSVELstevqsLNREIKDAKEQISPLETALEKLQQEKEE 928
Cdd:pfam17380 486 RKRAEEQRRKI------LEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| 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 153945822 31 LTILVGPNGAGKTTIIECLkyicTGDFPPGT 61
Cdd:COG4559 29 LTAIIGPNGAGKSTLLKLL----TGELTPSS 55
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
478-630 |
3.74e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 478 DQELTKAERELSKaeKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLnhhtttrtqmemltkdktdKDEQIRKIKs 557
Cdd:COG2433 405 ERELTEEEEEIRR--LEEQVERLEAEVEELEAELEEKDERIERLERELSEA-------------------RSEERREIR- 462
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945822 558 rhsdeltsllgyfpnkkqledwlhsKSKEINQTRDRLAKLNKELASAEQNknhiNNELKKKEEQLSSYEDKLF 630
Cdd:COG2433 463 -------------------------KDREISRLDREIERLERELEEERER----IEELKRKLERLKELWKLEH 506
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1202-1285 |
4.10e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 41.24 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1202 SAGQKVLasliirLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIiksrsqQRNFQLLVITH------DEDFVE 1275
Cdd:PRK10790 478 SVGQKQL------LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV------REHTTLVVIAHrlstivEADTIL 545
|
90
....*....|
gi 153945822 1276 LLGRSEYVEK 1285
Cdd:PRK10790 546 VLHRGQAVEQ 555
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1192-1276 |
4.31e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 41.36 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 1192 DTALDMRGRC-SAGQKvlasliIRLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSQQRNfqLLVITHD 1270
Cdd:COG2274 602 DTVVGEGGSNlSGGQR------QRLAIARALLRNPRILILDEATSALDAET----EAIILENLRRLLKGRT--VIIIAHR 669
|
....*.
gi 153945822 1271 EDFVEL 1276
Cdd:COG2274 670 LSTIRL 675
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1214-1271 |
4.34e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.15 E-value: 4.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 1214 RLALAETFCLNCGILALDEPTTNLDRENIESLAHALVeiikSRSQQRNFQLLVITHDE 1271
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF----SLNREHGTTLILVTHDL 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1200-1277 |
4.34e-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: 39.69 E-value: 4.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 1200 RCSAGQKvlasliIRLALAETFCLNCGILALDEPTTNLDRENieslAHALVEIIKSRSqQRNFQLLVITHDEDFVELL 1277
Cdd:cd03230 95 KLSGGMK------QRLALAQALLHDPELLILDEPTSGLDPES----RREFWELLRELK-KEGKTILLSSHILEEAERL 161
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-53 |
4.84e-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: 4.84e-03
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
848-1003 |
5.35e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 848 LNRKLIQDQQEQIQHLKSKTNELkseklqIATNLQRRQQMEEQSVELSTEVQSLNREIKDAKEQIspletalEKLQQEKE 927
Cdd:PRK00409 499 LPENIIEEAKKLIGEDKEKLNEL------IASLEELERELEQKAEEAEALLKEAEKLKEELEEKK-------EKLQEEED 565
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945822 928 ELIHRKHtsnKMAQDKINDIKEKVKNIhgymkdIENYIQDGKDDYKKQKETELNGVAVQLNECEKHREKINKDMGT 1003
Cdd:PRK00409 566 KLLEEAE---KEAQQAIKEAKKEADEI------IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
197-817 |
5.36e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 197 QTQGQKVKE-CQTELKYLKQNKEKACEIRDQitSKEAQLASSQEIVRSYEDELEPLKNRLKE----IEHNLSKIMKLDNE 271
Cdd:pfam12128 378 NRRRSKIKEqNNRDIAGIKDKLAKIREARDR--QLAVAEDDLQALESELREQLEAGKLEFNEeeyrLKSRLGELKLRLNQ 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 272 IKALESRKKQMEKDNSELEQKMEKVFQGTDEQLNdlyhnhqrtvREKERRLVDCQRE--LEKLNKEARLLNQEKAELLVE 349
Cdd:pfam12128 456 ATATPELLLQLENFDERIERAREEQEAANAEVER----------LQSELRQARKRRDqaSEALRQASRRLEERQSALDEL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 350 QGRLQLQADRHQEHIRA-----RDSLIQSLATHL----ELDGFERGPfSERQIKNFHELVKERQEREAKTASQLLSDLTD 420
Cdd:pfam12128 526 ELQLFPQAGTLLHFLRKeapdwEQSIGKVISPELlhrtDLDPEVWDG-SVGGELNLYGVKLDLKRIDVPEWAASEEELRE 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 421 KEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSKAEKNSSIEtl 500
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE-- 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 501 kaEVMSLQNEKADLDRSLRK-LDQEMEQLNHHTTTRTQ----MEMLTKDKTDK-DEQIRKIKSRHSDELtsllgyfpnkK 574
Cdd:pfam12128 683 --RLNSLEAQLKQLDKKHQAwLEEQKEQKREARTEKQAywqvVEGALDAQLALlKAAIAARRSGAKAEL----------K 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 575 QLEDWLHSKSKEINQTRDRLAKLNKE-------LASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGS-----QDLESDL 642
Cdd:pfam12128 751 ALETWYKRDLASLGVDPDVIAKLKREirtlerkIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNieraiSELQQQL 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 643 GRLKEEIE----KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqRVFQTEAELQEVISDLQSKLRLAPDKLKSTESE 718
Cdd:pfam12128 831 ARLIADTKlrraKLEMERKASEKQQVRLSENLRGLRCEMSKLATL--KEDANSEQAQGSIGERLAQLEDLKLKRDYLSES 908
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 719 LKKKERRRDEML------GLVPVRQSIIDlKEKEIPELRNRLQSVNRDIQRLkndieeqETLLGTIMPEEESA---KVCL 789
Cdd:pfam12128 909 VKKYVEHFKNVIadhsgsGLAETWESLRE-EDHYQNDKGIRLLDYRKLVPYL-------EQWFDVRVPQSIMVlreQVSI 980
|
650 660
....*....|....*....|....*...
gi 153945822 790 TDVTIMErFQMELKDVERKIAQQAAKLQ 817
Cdd:pfam12128 981 LGVDLTE-FYDVLADFDRRIASFSRELQ 1007
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-52 |
6.05e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.21 E-value: 6.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 153945822 4 IEKMSILGVRSFGiedkDKQIISFFSPLTILVGPNGAGKTTIIECLKYI 52
Cdd:cd03239 1 IKQITLKNFKSYR----DETVVGGSNSFNAIVGPNGSGKSNIVDAICFV 45
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
402-522 |
6.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 402 ERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEILTKKQSELRHVRSELQQLEGSSDRILELDQEL 481
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 153945822 482 TKAERELSKAEKNssIETLKAEVMSLqnekadldRSLRKLD 522
Cdd:COG2433 475 ERLERELEEERER--IEELKRKLERL--------KELWKLE 505
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
450-673 |
6.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 450 LTKKQSELRHVRSELQQlegssdRILELDQELTKAERELSKAEKNSSIETLKAEVMSLQNEKADLDRSLRKLDQEMEQLN 529
Cdd:COG3206 166 LELRREEARKALEFLEE------QLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 530 H-HTTTRTQMEMLTKDKTD--KDEQIRKIKSRHSD---ELTSLLGYF----PNKKQLEdwlhsksKEINQTRDRLAK-LN 598
Cdd:COG3206 240 ArLAALRAQLGSGPDALPEllQSPVIQQLRAQLAEleaELAELSARYtpnhPDVIALR-------AQIAALRAQLQQeAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945822 599 KELASAEQNKNHINNELKKKEEQLSSYEDKLFDVcgsQDLESDLGRLKEEIEKsskqramlagATAVYSQFITQL 673
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAEL---PELEAELRRLEREVEV----------ARELYESLLQRL 374
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
222-1075 |
6.68e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 222 EIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNLSKIMKLDN----EIKALESRKKQMEKDNSELEQKMEKVF 297
Cdd:TIGR01612 755 KILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNikdeDAKQNYDKSKEYIKTISIKEDEIFKII 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 298 QGT----DEQLN--DLYHNHQRTVREKerrlVDCQREleklnKEARLLNQEKAELLVEqgrlqlQADRHQEHIRARDSLI 371
Cdd:TIGR01612 835 NEMkfmkDDFLNkvDKFINFENNCKEK----IDSEHE-----QFAELTNKIKAEISDD------KLNDYEKKFNDSKSLI 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 372 -----------QSLATHLELDGFERGPFSERQ-IKNFH--------------ELVKERQEREAKTASQLLSDLTDK---- 421
Cdd:TIGR01612 900 neinksieeeyQNINTLKKVDEYIKICENTKEsIEKFHnkqnilkeilnkniDTIKESNLIEKSYKDKFDNTLIDKinel 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 422 ------------EALKQRQLDELRDRKSGLGR------------------TIELKTEILTKKQSELR--------HVRSE 463
Cdd:TIGR01612 980 dkafkdaslndyEAKNNELIKYFNDLKANLGKnkenmlyhqfdekekatnDIEQKIEDANKNIPNIEiaihtsiyNIIDE 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 464 LQQLEGSSdrILELDQELTKaERELSKAEKNSSIETLKA----------------EVMSLQNEKADLDRSLRKLDQEMEQ 527
Cdd:TIGR01612 1060 IEKEIGKN--IELLNKEILE-EAEINITNFNEIKEKLKHynfddfgkeenikyadEINKIKDDIKNLDQKIDHHIKALEE 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 528 L-----NHHTTTRTQMEMLTK--DKTDKDEQIRKIKSRHSDELTSLlgyfPNKKQLEDwlhskskEINQTRDRLAKLNKE 600
Cdd:TIGR01612 1137 IkkkseNYIDEIKAQINDLEDvaDKAISNDDPEEIEKKIENIVTKI----DKKKNIYD-------EIKKLLNEIAEIEKD 1205
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 601 LASAEQNKN---------------HINNELKKKEEQLSSYEDKLFDVcgsqdlesdlgrlkEEIEKSSKQRAMLAGATAV 665
Cdd:TIGR01612 1206 KTSLEEVKGinlsygknlgklfleKIDEEKKKSEHMIKAMEAYIEDL--------------DEIKEKSPEIENEMGIEMD 1271
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 666 YSQFITQLTDENQSccpvCQRVFQTEAELQEVISDLQSK-LRLAPDklKSTESELKKKERRRDEMLGLVPVRQSIIDLKE 744
Cdd:TIGR01612 1272 IKAEMETFNISHDD----DKDHHIISKKHDENISDIREKsLKIIED--FSEESDINDIKKELQKNLLDAQKHNSDINLYL 1345
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 745 KEIPELRN--RLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimeRFQMELKDVERKIaqqAAKLQGVDLD 822
Cdd:TIGR01612 1346 NEIANIYNilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKI----KDDINLEECKSKI---ESTLDDKDID 1418
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 823 RTVQQVNQEKQ---EKQHRLDTVTSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIAT-----NLQRRQQMEEQSVEL 894
Cdd:TIGR01612 1419 ECIKKIKELKNhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATndhdfNINELKEHIDKSKGC 1498
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 895 STEVQSLNREIKDAKEqispletALEKLQQEKEELIHRKHT---SNKMAQDK------INDIKEKVKNI-------HGYM 958
Cdd:TIGR01612 1499 KDEADKNAKAIEKNKE-------LFEQYKKDVTELLNKYSAlaiKNKFAKTKkdseiiIKEIKDAHKKFileaeksEQKI 1571
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 959 KDIENYIQDGKDDYKKQKETELNGVAVQL-------------------NECEKHREKINKDMGTMrqDIDTQKIQERWLQ 1019
Cdd:TIGR01612 1572 KEIKKEKFRIEDDAAKNDKSNKAAIDIQLslenfenkflkisdikkkiNDCLKETESIEKKISSF--SIDSQDTELKENG 1649
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945822 1020 DNLT-----LRKRRDELKEVEEERKqhlkemgqmQVLQMKNEHQKLEENIDTIKRNHSLAL 1075
Cdd:TIGR01612 1650 DNLNslqefLESLKDQKKNIEDKKK---------ELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
34-82 |
6.93e-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: 38.92 E-value: 6.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 153945822 34 LVGPNGAGKTTIIECLkyicTGDFPPgTKGNTFV--HDPKvAQETDVRAQI 82
Cdd:cd03230 31 LLGPNGAGKTTLIKII----LGLLKP-DSGEIKVlgKDIK-KEPEEVKRRI 75
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
222-362 |
7.46e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 222 EIRDQITSKEAQLASSQEIVRSYEDELEPLKNRLKEIEHNlSKIMKLDNEIKALESRKKQMEK---DNS----ELEQKME 294
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSArytPNHpdviALRAQIA 301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945822 295 KVFQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLveqgRLQLQADRHQE 362
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARE 365
|
|
| 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 153945822 31 LTILVGPNGAGKTTIIECLkyicTGDFPPGT 61
Cdd:PRK13548 30 VVAILGPNGAGKSTLLRAL----SGELSPDS 56
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1227-1274 |
9.66e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 9.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 153945822 1227 ILALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITHDEDFV 1274
Cdd:PRK15064 459 VLVMDEPTNHMDMESIESLNMAL----------EKYEgtLIFVSHDREFV 498
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
740-953 |
9.96e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 740 IDLKEKEIPELRnrlQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimerfqMELKDVE---RKIAQQAAKL 816
Cdd:PHA02562 197 IKTYNKNIEEQR---KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLV------MDIEDPSaalNKLNTAAAKI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945822 817 QGvdldrTVQQVNQEKQ--EKQHRLDTVTSKIElnrkliqDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQSVEL 894
Cdd:PHA02562 268 KS-----KIEQFQKVIKmyEKGGVCPTCTQQIS-------EGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQ 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945822 895 STEVQSLNREIKDAKEQISPLETALEKLQQEKEELiHRKHTSNKMAQDKINDIKEKVKN 953
Cdd:PHA02562 336 SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL-QAEFVDNAEELAKLQDELDKIVK 393
|
|
| |
