|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
7-1270 |
3.78e-133 |
|
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: 441.02 E-value: 3.78e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 7 AKIDKLSILGVRSF--DNTRSETIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDLPPNSKGGAFIHDPKLCGEKEVFAQ 84
Cdd:TIGR00606 1 AKFLKMSILGVRSFgiEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 85 VKLAFKATSAAKMVVTRSLQLTVKKLTRQQKTLEGQLLMIKEGERTAISSRVAELDQIMPQYLGVSKAVLDSVIFCHQDE 164
Cdd:TIGR00606 81 IRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 165 SLWPMSEPSVLKKKFDEIFEALKYTKAIDNIKALRKKQNEELAKYKIMENHARDDKDKADRAEKRSLKLQEEIEAlraeS 244
Cdd:TIGR00606 161 SNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLES----S 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 245 HELSKEMRRVAELADKAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEEsdEWLQSTLEQ----FESRQAEY 320
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKME--KVFQGTDEQlndlYHNHQRTV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 321 RSQEdtlkEKYMDLKELIEQNRHKLGLKQTECGKNENDKAQFDRQVER-------RVRLIKDIARQNNFRGYDGDLD-EM 392
Cdd:TIGR00606 315 REKE----RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehiraRDSLIQSLATRLELDGFERGPFsER 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 393 EINDFMDRIQKLTKERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISvndKESDTIQRSINEMDVDE 472
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE---KKQEELKFVIKELQQLE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 473 GKRAAIESRMEETEKILEKEKEKAKNASWETDIQQNDS---ELRSLEDKSSKLNAELIQGTKKAGDLARLDHLKKELKDR 549
Cdd:TIGR00606 468 GSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSlqnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 550 DDVL---------------------KEASTLVTTAERERDGTGKELELIDFKLKNARKSLHQHGADVENA-------AKK 601
Cdd:TIGR00606 548 DEQIrkiksrhsdeltsllgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKeeqlssyEDK 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 602 INDVIGDEPEEYphTVKQKQTELDMARKDADQYAGLGKYLNMCLDAVNDKK--VCRTCARPFKTESELQIFKNKLKALIK 679
Cdd:TIGR00606 628 LFDVCGSQDEES--DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsCCPVCQRVFQTEAELQEFISDLQSKLR 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 680 KATDEDAVAEIEAREAELENVREVGTFYETWN--RLTNTDIPALKKEQSDLETEREVVLTKLEDHDKIVAQRVESKRDIE 757
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSiiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 758 SLSKNIATIVRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELK 837
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 838 LRDLRRDLDNVNFQLEKKATLVSRVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVSG 917
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 918 LNDSLHQLDLASEDITNYIERGGPAQLERSKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQ 997
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 998 ESKALISVNQEIADLESQNAEVDRSRFKEESERNTREHNALAAKQASKMGEMKSKDDQLMQLLADWNT-DYKDAGAKFKE 1076
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREpQFRDAEEKYRE 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1077 AHIKVETTKAAVDDLGRYGGALDKAIMKYHGLKMEEINRIIGELWQKTYRGTDVDTILIRSDNE----SARGNRSYNYRV 1152
Cdd:TIGR00606 1106 MMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADenvsASDKRRNYNYRV 1185
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1153 CMVKQDAEMDMRGRCSAGQKVLASIIIRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHEIIRTRQQQANFQLIV 1232
Cdd:TIGR00606 1186 VMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLV 1265
|
1290 1300 1310
....*....|....*....|....*....|....*...
gi 315056489 1233 ITHDEEFLRSMQCGDFCDYYYRVSRNERQKSIIERQSI 1270
Cdd:TIGR00606 1266 ITHDEDFVELLGRSEYVEKFYRLKKNEDQCSEIVKCSP 1303
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1161-1264 |
3.98e-46 |
|
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: 164.70 E-value: 3.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1161 MDMRGRCSAGQKVLASIIIRLALAECFGVNCGLIALDEPTTNLDRDNIRslaESLHEIIRTRQQQANFQLIVITHDEEFL 1240
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIE---ESLAEIIEERKSQKNFQLIVITHDEELV 186
|
90 100
....*....|....*....|....
gi 315056489 1241 RSMqcgdfcDYYYRVSRNERQKSI 1264
Cdd:cd03240 187 DAA------DHIYRVEKDGRQKSR 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
9-172 |
2.56e-38 |
|
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: 142.36 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 9 IDKLSILGVRSFDNtrSETIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDLPPNSKGGAfiHDPKLCGEKEVFAQVKLA 88
Cdd:cd03240 1 IDKLSIRNIRSFHE--RSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGA--HDPKLIREGEVRAQVKLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 89 FKATSAAKMVVTRSLqltvkkltrqqktlegqllmikegertaissrvaeldqimpqylgvskAVLDSVIFCHQDESLWP 168
Cdd:cd03240 77 FENANGKKYTITRSL------------------------------------------------AILENVIFCHQGESNWP 108
|
....
gi 315056489 169 MSEP 172
Cdd:cd03240 109 LLDM 112
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
12-214 |
2.79e-23 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 98.72 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 12 LSILGVRSFDNtrsETIQFHTPLTLIVGYNGSGKTTIIECLKYATTGD---LPPNSKGGAFIHDPKLCGEKEVFAQVKLA 88
Cdd:pfam13476 1 LTIENFRSFRD---QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKtsrLKRKSGGGFVKGDIRIGLEGKGKAYVEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 89 FKATSAAKMVVTRSLQLTVKKLTRQQKTLEGQLLMIKegertaissrvaELDQIMPQYLGVSKAVLDsVIFCHQDESLWP 168
Cdd:pfam13476 78 FENNDGRYTYAIERSRELSKKKGKTKKKEILEILEID------------ELQQFISELLKSDKIILP-LLVFLGQEREEE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 315056489 169 MSEPSvLKKKFDEIFEALKYTKAIDNIKALRKKQNEELAKYKIMEN 214
Cdd:pfam13476 145 FERKE-KKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-975 |
1.72e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.58 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 195 IKALRKKQNEELAKYKIMENHARDDKDKADRAEKRSLKLQEEIEALRAESHELSKEmrrVAELADKAWKESESYAEILGA 274
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK---LEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 275 LEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRSQEDTLKEKYMDLKELIEQNRHKL----GLKQT 350
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeeleAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 351 ECGKNENDKAQFDRQVERRVRLIKDIARQNNFRGYdgdlDEMEINDFMDRIQKLTKERSQALEK----AKQEAQSQLKDA 426
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKleeaELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 427 QSLLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEMDvdeGKRAAIESRMEETEKILEKEKEKAKNASWETDIQ 506
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ---ARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 507 QNDSELRSLEDK---------SSKLNAELIQGTKKAGDLarLDHLKKELKDR----------DDVLKEASTLVTTAERER 567
Cdd:TIGR02168 523 GVLSELISVDEGyeaaieaalGGRLQAVVVENLNAAKKA--IAFLKQNELGRvtflpldsikGTEIQGNDREILKNIEGF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 568 DGTGKELELIDFKLKNARKSLHQHGADVENAAKKIND----------------------VIGDEPEEYPHTVKQKQTELD 625
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELakklrpgyrivtldgdlvrpggVITGGSAKTNSSILERRREIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 626 MARKDADQYAGLGKYLNMCLDAVndkkvcrtcarpfktESELQIFKNKLKALIKKAtdEDAVAEIEAREAELENVR-EVG 704
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAEL---------------RKELEELEEELEQLRKEL--EELSRQISALRKDLARLEaEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 705 TFYETWNRLTNTDIPALKKEQSDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIATIVRYNNEISTLQTQIQELS 784
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 785 AKQEetGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQL----EKKATLVS 860
Cdd:TIGR02168 824 ERLE--SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallrSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 861 RVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDI----STRGEQRERELQQEVSGLNDSLHQLDLASEDITNYI 936
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
810 820 830
....*....|....*....|....*....|....*....
gi 315056489 937 ERGGPAQLErSKRELQNISDEIKRLEAEQTDLTRELNSI 975
Cdd:TIGR02168 982 KELGPVNLA-AIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-1125 |
9.16e-14 |
|
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: 76.63 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 226 AEKRSLKLQEEIEALRAESHELSKEMRRVAELADKAwkesESYAEILGALEgkRIEAKSIQTSINNLRQHLVEVEESDEW 305
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELR--ELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 306 LQSTLEQFESRQAEYRSQEDTLKEKYMDLKELIEQNRHKLGLKQTECGKNENDKAqfdRQVERRVRLIKDIARqnnfrgY 385
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ---ILRERLANLERQLEE------L 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 386 DGDLDEMEindfmdRIQKLTKERSQALEKAKQEAQsqlKDAQSLLNQLSQRKSALQEAKNAAKKQisvnDKESDTIQRSI 465
Cdd:TIGR02168 322 EAQLEELE------SKLDELAEELAELEEKLEELK---EELESLEAELEELEAELEELESRLEEL----EEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 466 NEMdvdEGKRAAIESRMEETEKILEKEKEKaknaswetdIQQNDSELRSLEDKSSKLNAELIQGTKKAGDlARLDHLKKE 545
Cdd:TIGR02168 389 AQL---ELQIASLNNEIERLEARLERLEDR---------RERLQQEIEELLKKLEEAELKELQAELEELE-EELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 546 LKDRDDVLKEASTLVTTAERERDGTGKELELIDFKLK------NARKSLHQHGADVENAAKKINDVIGDEPEEYphTVKQ 619
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDslerlqENLEGFSEGVKALLKNQSGLSGILGVLSELI--SVDE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 620 K-QTELDMARKDADQYAgLGKYLNMCLDAVN---DKKVCRTCARPFKTESELQIFKNKLKALIKKATDEDAVAEIEAREA 695
Cdd:TIGR02168 534 GyEAAIEAALGGRLQAV-VVENLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 696 ELENVrevgtfYETW-NRLTNTDIPALKKEQSDLETEREVVLTKleDHDKIVAQRVESKRDieslSKNIATIVRYNNEIS 774
Cdd:TIGR02168 613 KLRKA------LSYLlGGVLVVDDLDNALELAKKLRPGYRIVTL--DGDLVRPGGVITGGS----AKTNSSILERRREIE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 775 TLQTQIQELSAKQEETgtSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEK 854
Cdd:TIGR02168 681 ELEEKIEELEEKIAEL--EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 855 KATLVSRVEDYRNQNlkqREAIEKADNDIESLVPEVSKAQARHDDISTRGeqreRELQQEVSGLNDSLHQLDLASEDITN 934
Cdd:TIGR02168 759 LEAEIEELEERLEEA---EEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEAANLRERLESLER 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 935 yierggpaQLERSKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKALISVNQEIADLES 1014
Cdd:TIGR02168 832 --------RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1015 QNAEVDRSRFKEESERNTREHNALAAKQAskmgEMKSKDDQLM-QLLADWNTDYKDAGAK-------FKEAHIKVETTKA 1086
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE----GLEVRIDNLQeRLSEEYSLTLEEAEALenkieddEEEARRRLKRLEN 979
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1087 AVDDLG---------------RYG------GALDKAIMKYHGLkMEEINRIIGELWQKTY 1125
Cdd:TIGR02168 980 KIKELGpvnlaaieeyeelkeRYDfltaqkEDLTEAKETLEEA-IEEIDREARERFKDTF 1038
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
538-1258 |
4.00e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 538 RLDHLKKELKDRDDVLKEASTLVTTAERERDGTGKELELIDfKLKNARKSLHQHGADVENAAKKINDVIGD------EPE 611
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIREleerieELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 612 EYPHTVKQKQTELDMARKDADQYAGLGKYLNMCLDAVND------------KKVCRTCARPFKTESELQIFKNKLKALIK 679
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREiekrlsrleeeiNGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 680 KatdedaVAEIEAREAELENVREVGTFYETWN-RLTNTDIPALKKEQSDLETEREVVLTKLEdhdKIVAQRVESKRDIES 758
Cdd:PRK03918 353 R------LEELEERHELYEEAKAKKEELERLKkRLTGLTPEKLEKELEELEKAKEEIEEEIS---KITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 759 LSKNIATIVRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLEL-- 836
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELae 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 837 KLRDLRRDLDNVNFQ-LEKKAtlvsrvEDYRnqnlKQREAIEKADNDIESLVPEVSKAQARHDDISTRgEQRERELQQEV 915
Cdd:PRK03918 504 QLKELEEKLKKYNLEeLEKKA------EEYE----KLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL-EKKLDELEEEL 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 916 SGLNDSLHQLDLASEDitnyierggpaQLERSKRELQNISDEIKRLEAEQTDLTRELNsistRLKDSESTKRQYSDNLRy 995
Cdd:PRK03918 573 AELLKELEELGFESVE-----------ELEERLKELEPFYNEYLELKDAEKELEREEK----ELKKLEEELDKAFEELA- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 996 rQESKALISVNQEIADLESQNAEVDRSRFKEESERNTREHNALAAKqaskMGEMKSKDDQLMQLLadwnTDYKDAGAKFK 1075
Cdd:PRK03918 637 -ETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAE----LEELEKRREEIKKTL----EKLKEELEERE 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1076 EAHIKVETTKAAVDDLGRYGGALD--KAIMKYHGLKmeEINRIIGELWQKTYRGTDVDTILIRSDNEsargnrsynYRVC 1153
Cdd:PRK03918 708 KAKKELEKLEKALERVEELREKVKkyKALLKERALS--KVGEIASEIFEELTEGKYSGVRVKAEENK---------VKLF 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1154 MVKQDAEMDMrGRCSAGQKVLASIIIRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAEslheiIRTRQQQANFQLIVI 1233
Cdd:PRK03918 777 VVYQGKERPL-TFLSGGERIALGLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVD-----IMERYLRKIPQVIIV 850
|
730 740
....*....|....*....|....*
gi 315056489 1234 THDEEFlrsmqcGDFCDYYYRVSRN 1258
Cdd:PRK03918 851 SHDEEL------KDAADYVIRVSLE 869
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1163-1240 |
1.27e-12 |
|
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: 67.00 E-value: 1.27e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315056489 1163 MRGRCSAGQKVLASIIIRLALAECfgVNCGLIALDEPTTNLDRDNIRSLAESlheIIRTRQQQAnfQLIVITHDEEFL 1240
Cdd:cd03227 74 TRLQLSGGEKELSALALILALASL--KPRPLYILDEIDRGLDPRDGQALAEA---ILEHLVKGA--QVIVITHLPELA 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-802 |
6.19e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 8 KIDKLSILGVRSFDNTRsetIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDLPPNSKGGAfIHDPKLCGEKEVFAQVKL 87
Cdd:PRK03918 2 KIEELKIKNFRSHKSSV---VEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLK-KDDFTRIGGSGTEIELKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 88 AFKATsaaKMVVTRSLQLTVKKLTRQQktlegqllmIKEGERTAISSRVAELDQIMPQYlgvskaVLDSVIFCHQDESLW 167
Cdd:PRK03918 78 EKNGR---KYRIVRSFNRGESYLKYLD---------GSEVLEEGDSSVREWVERLIPYH------VFLNAIYIRQGEIDA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 168 PMSEPSVLKKKFDEIFEALKYTKAIDNIKALRKKQNEELAKYKIMENHARDDKDKADRAEKRSLKLQEEIEalraeshEL 247
Cdd:PRK03918 140 ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-------EI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 248 SKEMRRVAELADKAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRSQEDtL 327
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE-K 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 328 KEKYMDLKELIEQNRHKLGLKQTECGKNENDKAQFDRQVERRVRLIKDIAR-QNNFRGYDGDLDEME--------INDFM 398
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElKKKLKELEKRLEELEerhelyeeAKAKK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 399 DRIQKLTKERS-----------QALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISV---------NDKES 458
Cdd:PRK03918 372 EELERLKKRLTgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 459 DTIQRSINEMDVDEGKRAAIESRMEETEKILEKEKEKAKNASWETDIQQNDSELRSLEDKSSKLNAE-LIQGTKKAGDL- 536
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLk 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 537 ARLDHLKKELKDRDDVLKEASTLVttaererdgtgKELELIDFKLKNARKSLhqhgadvenaaKKINDVIGDEPEEYPHT 616
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELK-----------KKLAELEKKLDELEEEL-----------AELLKELEELGFESVEE 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 617 VKQKQTELDMARKdadqyaglgKYLNMcLDAVNDKKvcrtcarpfKTESELQIFKNKLKALIKKATDEDAVAE-IEAREA 695
Cdd:PRK03918 590 LEERLKELEPFYN---------EYLEL-KDAEKELE---------REEKELKKLEEELDKAFEELAETEKRLEeLRKELE 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 696 ELENVREVGTFYETWNRLT--NTDIPALKKEQSDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIATIVRYNNEI 773
Cdd:PRK03918 651 ELEKKYSEEEYEELREEYLelSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKV 730
|
810 820
....*....|....*....|....*....
gi 315056489 774 STLQTQIQELSAKQEETGTSRTLEDIQDE 802
Cdd:PRK03918 731 KKYKALLKERALSKVGEIASEIFEELTEG 759
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
708-1036 |
3.01e-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: 61.61 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 708 ETWNRLTNTDIpALKKEQsDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIAT--IVRYNNEISTLQTQIQELSA 785
Cdd:TIGR02168 176 ETERKLERTRE-NLDRLE-DILNELERQLKSLERQAEKAERYKELKAELRELELALLVlrLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 786 KQEETgtSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKATlvsRVEDY 865
Cdd:TIGR02168 254 ELEEL--TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA---QLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 866 RNQNLKQREAIEKADNDIESLVPEVSKAQARHD---DISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGGpA 942
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEeleAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE-A 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 943 QLERSKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKALISVNQEIADLESQNAEVDRS 1022
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330
....*....|....
gi 315056489 1023 RFKEESERNTREHN 1036
Cdd:TIGR02168 488 QARLDSLERLQENL 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
716-992 |
3.19e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 716 TDIPALKKEQSDLETEREVVLTKLEDHDKIVAQRVeskRDIESLSKNIATIVryNNEISTLQTQIQELSAKQEETGTS-- 793
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIE---QLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLERSia 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 794 ---RTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKATlvsRVEDYRNQNL 870
Cdd:TIGR02169 312 ekeRELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK---EFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 871 KQREAIEKADNDIESLVPEVSKAQarhdDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGG------PAQL 944
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQ----EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlAADL 464
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 315056489 945 ERSKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDN 992
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1167-1249 |
5.32e-09 |
|
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: 57.65 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1167 CSAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHEIirTRQQQANfqlIVITHDEEFLrsMQCG 1246
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL--AAQGKAV---IVITHDYEFL--AKVC 193
|
...
gi 315056489 1247 DFC 1249
Cdd:cd03226 194 DRV 196
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
359-1076 |
8.07e-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: 60.13 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 359 KAQFDRQVERRVRLIKDIARQNNfrgYDGDLDEME-------INDFMDRIQKLTKERSQALEKAKQEAQSQlkdaQSLLN 431
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLN---ESNELHEKQkfylrqsVIDLQTKLQEMQMERDAMADIRRRESQSQ----EDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 432 QLSQRKSALQEAKNAAKKQISVNDKESDTIQR----------SINEMDVD----EGKRAAIESRMEETEKILEKEKEKAK 497
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKmmlshegvlqEIRSILVDfeeaSGKKIYEHDSMSTMHFRSLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 498 NASWETDIQQNDSELRSLEDKSSKLNAEliqgtkkagDLARLDHLKKELKDR-DDVLKEASTLVT-------TAERERDG 569
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSE---------SQNKIELLLQQHQDRiEQLISEHEVEITgltekasSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 570 TGKELELIDFKLKNARKSLHQHGADVENAAKKINDVIGDEPEEYPHTVK--QKQ-----TELDMARKDADQYAGLGKYLn 642
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEelEKQlvlanSELTEARTERDQFSQESGNL- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 643 mcldavnDKKVCRTCARPFKTESELQIFKNKLKALIKKATDEDAVAEIEAREAELENVrEVgtfyetwNRLTNTdIPALK 722
Cdd:pfam15921 376 -------DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM-EV-------QRLEAL-LKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 723 KE-QSDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIATIVRYNNEISTLQTQIQELSAKQEEtgTSRTLEDIQD 801
Cdd:pfam15921 440 SEcQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE--KERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 802 EIATLGE----KSRQLKRASSKLTHELN-QSRVDVGKLELKLRD-----LRRDLDNVN------------FQLEkKATLV 859
Cdd:pfam15921 518 EITKLRSrvdlKLQELQHLKNEGDHLRNvQTECEALKLQMAEKDkvieiLRQQIENMTqlvgqhgrtagaMQVE-KAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 860 SRVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIErg 939
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE-- 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 940 gpaQLERSKRELQNISDEIK--------RLEAEQTDLTRELNSI-STRLKDSESTKRQYSDNLRYRQESKALISVNQEIA 1010
Cdd:pfam15921 675 ---DYEVLKRNFRNKSEEMEtttnklkmQLKSAQSELEQTRNTLkSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQ 751
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315056489 1011 DLES--QNAEVDRSRFKEESERNTREHNALAAKQASKMGE---MKSKDDQLMQLLADWNTDYKDAGAKFKE 1076
Cdd:pfam15921 752 FLEEamTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGElevLRSQERRLKEKVANMEVALDKASLQFAE 822
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
360-1091 |
8.22e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 360 AQFDRQVERRVRLIkDIARQNNFRGydgDLDEMEINDFMDRIQ--KLTKERSQALEKAKQEAqsqlkdaqsllnqlsqRK 437
Cdd:TIGR02169 166 AEFDRKKEKALEEL-EEVEENIERL---DLIIDEKRQQLERLRreREKAERYQALLKEKREY----------------EG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 438 SALQEAKNAAKKQISVNDKESDTIQRSINEMDVdegkraaiesrmeetekilekekekaknaswetDIQQNDSELRSLED 517
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTE---------------------------------EISELEKRLEEIEQ 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 518 KSSKLNA--------ELIQGTKKAGDL-ARLDHLKKELKDRDDVLKEASTLVTTAERERDGTGKELELIDFKLKNARKSL 588
Cdd:TIGR02169 273 LLEELNKkikdlgeeEQLRVKEKIGELeAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 589 HQHGADVENAAKKINDV---IGDEPEEYPHT---VKQKQTELDMARKDADQyaglgkyLNMCLDAVNDKKVcrtcarpfK 662
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLraeLEEVDKEFAETrdeLKDYREKLEKLKREINE-------LKRELDRLQEELQ--------R 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 663 TESELQIFKNKLKALIKK-----ATDEDAVAEIEAREAELENVREVGTFYETWNRLTNTDIPALKKEQSDLETErevvLT 737
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKineleEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE----LA 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 738 KLEDHDKIVAQRVESKRDIES-LSKNIATIVrynNEISTLQTQIQELSAKQEETGTSR-------TLEDIQDEIATLgeK 809
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEvLKASIQGVH---GTVAQLGSVGERYATAIEVAAGNRlnnvvveDDAVAKEAIELL--K 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 810 SRQLKRASSKLTHELNQSRVDVGKLELK-----------------------LRDL---------RRDLDNVNF------- 850
Cdd:TIGR02169 569 RRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvFGDTlvvedieaaRRLMGKYRMvtlegel 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 851 -----------------------QLEKKATLVSRVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQR 907
Cdd:TIGR02169 649 feksgamtggsraprggilfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 908 ERELQQEVSGLNDSLHQLDLASEDITNYierggpaqlersKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDS--EST 985
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENV------------KSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 986 KRQYSDNLRYRQE-SKALISVNQEIADL---------ESQNAEVDRSRFKEESERNTREHNALAAKQASKMGEMKSKDDQ 1055
Cdd:TIGR02169 797 QAELSKLEEEVSRiEARLREIEQKLNRLtlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
810 820 830
....*....|....*....|....*....|....*....
gi 315056489 1056 LMQL---LADWNTDYKDAGAKFKEAHIKVETTKAAVDDL 1091
Cdd:TIGR02169 877 LRDLesrLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1132-1241 |
1.64e-08 |
|
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: 54.94 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1132 TILIRSDNESARGNRSYNYRVCMVKQdaemdmrgrCSAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSL 1211
Cdd:cd00267 55 EILIDGKDIAKLPLEELRRRIGYVPQ---------LSGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
90 100 110
....*....|....*....|....*....|
gi 315056489 1212 AESLHEIirtrqQQANFQLIVITHDEEFLR 1241
Cdd:cd00267 120 LELLREL-----AEEGRTVIIVTHDPELAE 144
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
293-1057 |
2.23e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 293 RQHLVEVEESDEWLQSTLEqfESRQAEYRSQEDTLK-EKYMDLKELIEQNRHKLGLKQTEcgKNENDKAQFDRQVERRVR 371
Cdd:TIGR02169 176 LEELEEVEENIERLDLIID--EKRQQLERLRREREKaERYQALLKEKREYEGYELLKEKE--ALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 372 LIKDIARQNNFRGYDGDLDEMEINDFMDRIQKLTKERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQI 451
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 452 SVNDKESDTIQRSINEMDVdegKRAAIESRMEETEKILEKEkekaknaswETDIQQNDSELRSLEDKSSKLNAELIQGTK 531
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERK---RRDKLTEEYAELKEELEDL---------RAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 532 KAGDLAR-LDHLKKELKDRDDVLKEASTLVTTAERERDGTGKELELIDFKLKNARKSLHQHGADVENAAKKINDvIGDEP 610
Cdd:TIGR02169 400 EINELKReLDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD-LKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 611 EEYPHTVKQKQTELDMARKDAD---QYAGLGKYLNMCLDAvNDKKVCRTCARPFKTESELQI-----FKNKLKALIKKaT 682
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARaseERVRGGRAVEEVLKA-SIQGVHGTVAQLGSVGERYATaievaAGNRLNNVVVE-D 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 683 DEDAVAEIE-------------------AREAELENVREVGT------------------FYETWNRLTNTDIPALKKEQ 725
Cdd:TIGR02169 557 DAVAKEAIEllkrrkagratflplnkmrDERRDLSILSEDGVigfavdlvefdpkyepafKYVFGDTLVVEDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 726 ----------------------SDLETEREVVLTKLEDHDKIVAQRVES-KRDIESLSKNIATIVRYNNE---------- 772
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDElsqelsdasr 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 773 -ISTLQTQIQELsaKQEETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVnfQ 851
Cdd:TIGR02169 717 kIGEIEKEIEQL--EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--R 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 852 LEKKATLVSRVEDYRNQNLKQREAIEKADNDI----ESLVPEVSKAQARHDDIstrgEQRERELQQEVSGLNDSLHQLDL 927
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlekEYLEKEIQELQEQRIDL----KEQIKSIEKEIENLNGKKEELEE 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 928 ASEDITNYIERGGpAQLERSKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLR-YRQESKALISVN 1006
Cdd:TIGR02169 869 ELEELEAALRDLE-SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDEEIP 947
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 315056489 1007 QEIADLESQNAEVDRsrfKEESERNTREHNALAAKQ----ASKMGEMKSKDDQLM 1057
Cdd:TIGR02169 948 EEELSLEDVQAELQR---VEEEIRALEPVNMLAIQEyeevLKRLDELKEKRAKLE 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-567 |
2.35e-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: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 196 KALR-KKQNEELAKYKIMENHARDD--KDKADRAEKRSLKLQEEIEALRAESHELSKEMRRVAEladkawkesesyaeil 272
Cdd:COG1196 211 KAERyRELKEELKELEAELLLLKLRelEAELEELEAELEELEAELEELEAELAELEAELEELRL---------------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 273 gALEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRSQEDTLKEKYMDLKELIEQNRHKLGLKQTEC 352
Cdd:COG1196 275 -ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 353 GKNENDKAQFDRQVERRVRLIKDIARQnnfrgydgdldemeindfmdriQKLTKERSQALEKAKQEAQSQLKDAQSLLNQ 432
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEE----------------------LEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 433 LSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEMDVDEGKRAAIESRMEETEKILEKEKEKAKNASWETDIQQNDSEL 512
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 315056489 513 RSLEDKSSKLNAE-LIQGTKKAGDLARLDHLKKELKDRDDVLKEASTLVTTAERER 567
Cdd:COG1196 492 RLLLLLEAEADYEgFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
775-1115 |
2.98e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 775 TLQTQIQELSAKQeetgTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNvnfQLEK 854
Cdd:COG1196 217 ELKEELKELEAEL----LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE---AQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 855 KATLVSRVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITN 934
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 935 YIERGGPAQLERS--KRELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKALISVNQEIADL 1012
Cdd:COG1196 370 AEAELAEAEEELEelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1013 ESQNAEVDRSRFKEESERNTREHNALAAKQASKMGEMKSKDDQL-MQLLADWNTDYKDAGAKFKEAHIKVETTKAAVDDL 1091
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
330 340
....*....|....*....|....
gi 315056489 1092 GRYGGALDKAIMKYHGLKMEEINR 1115
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVV 553
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
249-1240 |
3.03e-08 |
|
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: 58.44 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 249 KEMRRVAELADKAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRSQEDTLK 328
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 329 EK----YMDLKELIEQNRHKLGlkqtecgKNENDKAQFDRQVERRVRLIKDIARQNNfrgydgdldemEINDFMDRIQKL 404
Cdd:pfam02463 222 EEeyllYLDYLKLNEERIDLLQ-------ELLRDEQEEIESSKQEIEKEEEKLAQVL-----------KENKEEEKEKKL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 405 TKERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEMDVDEGKRAAIESRMEE 484
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 485 TEKILEKEKEKAKnASWETDIQQNDSELRSLEDKSSKLNAELIQGTKKAGDLARLDHLKKELKDRDDVLKEASTLVTTAE 564
Cdd:pfam02463 364 LQEKLEQLEEELL-AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 565 RERDGTGKELELIDFKLKNARKSlhqhgadvenaAKKINDVIGDEPEEYPHTVKQKQTELDMARKDADQYAGLGKYLNMC 644
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDEL-----------ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 645 LDAVNDKKVCRTCARPFKTESELQIFKNKLKALIKKATDEDAVAEIEAREAELENVREVGTFYETWNRLTNTDIPALKKE 724
Cdd:pfam02463 512 LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 725 QSDLETEREVVLTKLEDHDKIVAQRVESKR-----DIESLSKNIATIVRYNNEISTLQTQIQELSAKQEETGTSRTLEDI 799
Cdd:pfam02463 592 KSIAVLEIDPILNLAQLDKATLEADEDDKRakvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 800 QDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKATLVSRV-EDYRNQNLKQREAIEK 878
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKInEELKLLKQKIDEEEEE 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 879 ADNDIESLVPEVSKAQARHDDIStrgEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGGPAQLERSKRELQNISDEI 958
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEK---ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 959 KRLEAEQ---------TDLTRELNSISTRLKDSESTKRQYSD--NLRYRQESKALISVNQEIADLESQNAEVDRSRFKEE 1027
Cdd:pfam02463 829 KIKEEELeelalelkeEQKLEKLAEEELERLEEEITKEELLQelLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1028 SERNTREHNALAAKQASKMGEMKSKDDQLMQLLADWNTDYKDAGAKFKEAHIKVETTKAAVDDLGRyGGALDKAIMKYhg 1107
Cdd:pfam02463 909 LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK-VNLMAIEEFEE-- 985
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1108 lKMEEINRIIGELWQKTYRGTDVDTILIRSDNE----------SARGNRSYNYRVCMVKQDAEM---------------D 1162
Cdd:pfam02463 986 -KEERYNKDELEKERLEEEKKKLIRAIIEETCQrlkeflelfvSINKGWNKVFFYLELGGSAELrledpddpfsggieiS 1064
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1163 MRGR---------CSAGQKVLASIIIRLALAECFGVNcgLIALDEPTTNLDRDNIRSLAESLHEiirtrqQQANFQLIVI 1233
Cdd:pfam02463 1065 ARPPgkgvknldlLSGGEKTLVALALIFAIQKYKPAP--FYLLDEIDAALDDQNVSRVANLLKE------LSKNAQFIVI 1136
|
....*..
gi 315056489 1234 THDEEFL 1240
Cdd:pfam02463 1137 SLREEML 1143
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
535-1242 |
3.20e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 535 DLARLDHLKKELKDRDDVLKEASTLVTTAERERDGTGKELELIDFKLKNARKSLhqhgaDVENAAKKINDVIGDEPEEYP 614
Cdd:PRK01156 181 EISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY-----NNLKSALNELSSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 615 HTVKQKQTELDMARKDADQYAGLGKYL------------NMCLDAVNDKKVCRTCARPFKT-ESELQIFKNKLKALIKKA 681
Cdd:PRK01156 256 SEIKTAESDLSMELEKNNYYKELEERHmkiindpvyknrNYINDYFKYKNDIENKKQILSNiDAEINKYHAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 682 TDEDAVAEIEAREAELENVR-EVGTFYETWNRLTNT------DIPALKKEQSDLETEREVVLTKLE-DHDKIVAQRVESK 753
Cdd:PRK01156 336 KDYNDYIKKKSRYDDLNNQIlELEGYEMDYNSYLKSieslkkKIEEYSKNIERMSAFISEILKIQEiDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 754 RDIEslskniativRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLG-----EKSRQLKR----ASSKLTHEL 824
Cdd:PRK01156 416 VKLQ----------DISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGttlgeEKSNHIINhyneKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 825 NQSRVDVGKLELKLRDLRRDLDnvnfQLEKKAtlVSRVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTrg 904
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKE----YLESEE--INKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS-- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 905 eQRERELQQEVSGLNDSLHQLDLAseDITNYIERggpaqLERSKRELQNISDEIKRLEAEQTDLTrelNSISTRLKDSES 984
Cdd:PRK01156 558 -LKLEDLDSKRTSWLNALAVISLI--DIETNRSR-----SNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 985 TKRQYSDNLRYRQESKALISVNQE-IADLESQNAEVDrSRFKEESERNTREHNA-----LAAKQASKMGEMKSKDDQLMQ 1058
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGkIDNYKKQIAEID-SIIPDLKEITSRINDIednlkKSRKALDDAKANRARLESTIE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1059 LLADWNTDYKDAGAKFKEAHIKVETTKAAVDDLGRYGGALDKAIMKyhGLKMEEINRIIGELWQKTYRGTDVDTILIRSD 1138
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVP--AMIRKSASQAMTSLTRKYLFEFNLDFDDIDVD 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1139 NEsargnrsYNYRVCMVKQDAEMDmrgRCSAGQKVLASIIIRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHEI 1218
Cdd:PRK01156 784 QD-------FNITVSRGGMVEGID---SLSGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYS 853
|
730 740
....*....|....*....|....
gi 315056489 1219 IrtRQQQANFQLIVITHDEEFLRS 1242
Cdd:PRK01156 854 L--KDSSDIPQVIMISHHRELLSV 875
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
318-918 |
3.90e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 318 AEYRSQEDTLK------EKYMDLKELIEQNRHKLGLKQTEcgKNENDKAQFDRQVERRVRLIKDIARQnnfrgydgdLDE 391
Cdd:COG1196 196 GELERQLEPLErqaekaERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAE---------LAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 392 MEindfmDRIQKLtKERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEM--- 468
Cdd:COG1196 265 LE-----AELEEL-RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeee 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 469 ------DVDEGKRAAIESRMEETEKILEKEKEKAKNASWETDIQQ-NDSELRSLEDKSSKLNAELIQGTKKAGDLARLDH 541
Cdd:COG1196 339 leeleeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 542 LKKELKDRDDVLKEASTLVTTAERERDGTGKELELIDFKLKNARKSLHQHGADVENAAKKINDVIGDEpeeyphtvKQKQ 621
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--------AEAA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 622 TELDMARKDADQYAGLGKYLNMCLDAVNDKKVCRTCARPFKTESELQI-FKNKLKALIKKATDEDAVAEIEAREAELENV 700
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaLEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 701 REVGTFyetwnrLTNTDIPALKKEQSDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIATIVRYNNEISTLQTQI 780
Cdd:COG1196 571 AGRATF------LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 781 QELSAKQEETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNvnfQLEKKATLVS 860
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE---AEEERLEEEL 721
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 861 RVEDYRNQNLKQREAIEKADNDIESLVPEVskAQARHDDISTRGEQRER--ELQQEVSGL 918
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEE--ALEELPEPPDLEELEREleRLEREIEAL 779
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1168-1242 |
5.18e-08 |
|
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: 53.22 E-value: 5.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLheiirtrqqqANFQ--LIVITHDEEFLRS 1242
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYFLDQ 132
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
184-1027 |
6.18e-08 |
|
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: 57.29 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 184 EALKYTKAIDNIKALRKKQNEELAKYKIMENHARDDKDKADRAEKRSLKLQEEI-----EALRAESHELSKEMRRVAELA 258
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyldylKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 259 DKAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEESdewLQSTLEQFESRQAEYRSQEDTLKEKYMDLKELI 338
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 339 EQNRHKLGLKQTECGKNENDKAQFDRQVER-RVRLIKDIARQNNFRGYDGDLDEMEINDFMDRIQKLTK--ERSQALEKA 415
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEElEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELksEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 416 KQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISvNDKESDTIQRSINEMDVDEGKRAAIEsrmeetEKILEKEKEK 495
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT-EEKEELEKQELKLLKDELELKKSEDL------LKETQLVKLQ 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 496 AKNASWETDIQQNDSELRSLEDKSSKLNAELIQGTKKAGDLARLDHLKKELKDRDDVLKEASTLVTTAERERDG----TG 571
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAdeveER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 572 KELELIDFKLKNARKSLHQHGADVENAAKKINDVIGDePEEYPHTVKQKQTELDMARKDADQYAGLGKYLNMCLDAVNDK 651
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEID-PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 652 KVCRTCARpFKTESELQIFKNKLKALIKKATDEDAVAEIEAREAELENVREVGTFYETWNRLTNTDIPALKKEQSDLETE 731
Cdd:pfam02463 643 AKESGLRK-GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 732 REVVLTKLEDHD---KIVAQRVESKRDIESLSKNIATIVRYNNEISTLQTQIQELSAKQEETGTsRTLEDIQDEIATLGE 808
Cdd:pfam02463 722 LLADRVQEAQDKineELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK-LKVEEEKEEKLKAQE 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 809 KSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKATLVSRVEDYRN---QNLKQREAIEKADNDIES 885
Cdd:pfam02463 801 EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLeeeITKEELLQELLLKEEELE 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 886 LVPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGGPAQLERSKRELQNISDEIKRLEAEQ 965
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315056489 966 TDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKALISVNQEIADLESQNAEVDRSRFKEE 1027
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1168-1257 |
7.42e-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: 54.40 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHEIirtrqQQANFQLIVITHDEEFLRsmqcgD 1247
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-----KAEGKTIIIVTHDLDLLL-----E 199
|
90
....*....|
gi 315056489 1248 FCDYYYRVSR 1257
Cdd:cd03225 200 LADRVIVLED 209
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-1000 |
1.34e-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: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 198 LRKKQNEELAKYKIMENHARDDKDKADRAEKRSLKLQEEIEalraESHELSKEMRRVAELADKAWKESESYAEILGALEG 277
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQ----ENKDLIKENNATRHLCNLLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 278 KRIEAKSIQTSINNLRQHLVEVEEsdewlqstleqfesrqaEYRSQ-EDTLKEKYMDLKELIEQNRHklglKQTECGKNE 356
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFE-----------------ELRVQaENARLEMHFKLKEDHEKIQH----LEEEYKKEI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 357 NDKaqfDRQVErrVRLIKDIARQNNFRGYDGDLDEMEinDFMDRIQKLTKERSQALEKA---KQEAQSQLKDAQSLLNQL 433
Cdd:pfam05483 236 NDK---EKQVS--LLLIQITEKENKMKDLTFLLEESR--DKANQLEEKTKLQDENLKELiekKDHLTKELEDIKMSLQRS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 434 SQRKSALQEAKNAAKKQISVNDKESDTiqrsinemDVDEGKRAAIESRMEETEKILEKEKEKAKNASWETDIQQNDSELR 513
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEA--------QMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 514 SLEDKSSKLNAELIQGTK-KAGDLARLDHLKKELKDRDDVLKEASTLVTTAERERdgtGKELELIdFKLKNARKSLHQHG 592
Cdd:pfam05483 381 IITMELQKKSSELEEMTKfKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK---GKEQELI-FLLQAREKEIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 593 ADVEnaakkindVIGDEPEEYPHTVKQKQTELDMARkdadqyaglgkylnmcldavndkkvcrtcarpfKTESELQIFKN 672
Cdd:pfam05483 457 IQLT--------AIKTSEEHYLKEVEDLKTELEKEK---------------------------------LKNIELTAHCD 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 673 KLKALIKKATDE--DAVAEIEAREAELENVRevgtfyETWNRLTNtDIPALKKEQSDLETEREVVltkledHDKIVAQRV 750
Cdd:pfam05483 496 KLLLENKELTQEasDMTLELKKHQEDIINCK------KQEERMLK-QIENLEEKEMNLRDELESV------REEFIQKGD 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 751 ESKRDIESLSKNIATIvrynnEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVD 830
Cdd:pfam05483 563 EVKCKLDKSEENARSI-----EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 831 VGKLELKLRDLRRDLDNVNFQLEKKatlvsrVEDYRNQNLKQREAIEKAdndiESLVPEVSKAQarhDDISTRGEQRERE 910
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKE------IEDKKISEEKLLEEVEKA----KAIADEAVKLQ---KEIDKRCQHKIAE 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 911 LqqeVSGLNDSLHQLDLASEditnyiERGGPAQLERSKRELQniSDEIKRLEAEQTDLTRELNSISTRL----KDSESTK 986
Cdd:pfam05483 705 M---VALMEKHKHQYDKIIE------ERDSELGLYKNKEQEQ--SSAKAALEIELSNIKAELLSLKKQLeiekEEKEKLK 773
|
810
....*....|....
gi 315056489 987 RQYSDNLRYRQESK 1000
Cdd:pfam05483 774 MEAKENTAILKDKK 787
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
8-89 |
2.98e-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: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 8 KIDKLSILGVRSFDNTrsETIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDLppnSKGGAFIHDpkLCGEKEVFAQVKL 87
Cdd:COG0419 1 KLLRLRLENFRSYRDT--ETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKA---RSRSKLRSD--LINVGSEEASVEL 73
|
..
gi 315056489 88 AF 89
Cdd:COG0419 74 EF 75
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
306-481 |
4.47e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 306 LQSTLEQFESRQAEYRSQEDTLKEKYMDLKELIEQNRHKLGLKQTECGKNENDKAQFDRQVERRVRLIKDIARQNNFRGY 385
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 386 DGDLDEM-----EINDFMDRIQKLT-------------KERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAA 447
Cdd:COG3883 101 SVSYLDVllgseSFSDFLDRLSALSkiadadadlleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190
....*....|....*....|....*....|....
gi 315056489 448 KKQISVNDKESDTIQRSINEMDVDEGKRAAIESR 481
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
8-83 |
9.73e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 51.92 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 8 KIDKLSILGVRSFDNTrseTIQFHTP--LTLIVGYNGSGKTTIIECLKYATTGDLP--PNSKGGAF-IHDPKLCGEKEVF 82
Cdd:COG3950 2 RIKSLTIENFRGFEDL---EIDFDNPprLTVLVGENGSGKTTLLEAIALALSGLLSrlDDVKFRKLlIRNGEFGDSAKLI 78
|
.
gi 315056489 83 A 83
Cdd:COG3950 79 L 79
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
15-886 |
1.06e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 15 LGVRSFDNTRSETIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDlppnsKGGAFIHDPKLCGEKEVfaQVKLAFKATSA 94
Cdd:PRK01156 6 IRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTD-----KRTEKIEDMIKKGKNNL--EVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 95 AKMVvtrslqltVKKLTRQQKTLEGQLLMIKEGERTAISSRVAElDQIMPQYLGVSKAVLDSVIFCHQDESLWPMS-EPS 173
Cdd:PRK01156 79 VYQI--------RRSIERRGKGSRREAYIKKDGSIIAEGFDDTT-KYIEKNILGISKDVFLNSIFVGQGEMDSLISgDPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 174 VLKKKFDEIFEALKYTKAIDNIKALRKKQNEELAKYKIMENHARDDKDKADRAEKrSLKLQEEIEALraeshelskemrr 253
Cdd:PRK01156 150 QRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKK-QIADDEKSHSI------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 254 vaeladkAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRSQEdtlkEKYMD 333
Cdd:PRK01156 216 -------TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELE----ERHMK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 334 LkelieqnrhklglkqtecgknENDKAQFDR-QVERRVRLIKDIARQNN-FRGYDGDLDEMEinDFMDRIQKLTKERSQA 411
Cdd:PRK01156 285 I---------------------INDPVYKNRnYINDYFKYKNDIENKKQiLSNIDAEINKYH--AIIKKLSVLQKDYNDY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 412 LEKAKQ---------EAQSQLKDAQSLLNQLSQRKSALQEAKnaaKKQISVNDKESDTIQRSINEMDVDEGKRAAIESRM 482
Cdd:PRK01156 342 IKKKSRyddlnnqilELEGYEMDYNSYLKSIESLKKKIEEYS---KNIERMSAFISEILKIQEIDPDAIKKELNEINVKL 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 483 EEtekilekekekaknasWETDIQQNDSELRSLEDKSSKL--NAELIQGTKKAGDLArlDHLKKElkdrddvlkeastlv 560
Cdd:PRK01156 419 QD----------------ISSKVSSLNQRIRALRENLDELsrNMEMLNGQSVCPVCG--TTLGEE--------------- 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 561 tTAERERDGTGKELELIDFKLKnarkslhqhgaDVENAAKKINDVIgdepeeyphtVKQKQTELDMARKDADQYAglgKY 640
Cdd:PRK01156 466 -KSNHIINHYNEKKSRLEEKIR-----------EIEIEVKDIDEKI----------VDLKKRKEYLESEEINKSI---NE 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 641 LNMCLDAvndkkvcrtcarpfktESELQIFKNKLKALIKKATDEDAVAEiEAREAELENVREVgtfYETWNRL----TNT 716
Cdd:PRK01156 521 YNKIESA----------------RADLEDIKIKINELKDKHDKYEEIKN-RYKSLKLEDLDSK---RTSWLNAlaviSLI 580
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 717 DIPALKKeqsdletEREVVLTKLEDHDKIVAQRVESKRDIESLSKNiaTIVRYNNEISTLQTQIQELSAKQEETGTSR-T 795
Cdd:PRK01156 581 DIETNRS-------RSNEIKKQLNDLESRLQEIEIGFPDDKSYIDK--SIREIENEANNLNNKYNEIQENKILIEKLRgK 651
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 796 LEDIQDEIATLGEKSRQLKRASSKltheLNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKATLVSRVEDY---RNQNLKQ 872
Cdd:PRK01156 652 IDNYKKQIAEIDSIIPDLKEITSR----INDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRindINETLES 727
|
890
....*....|....
gi 315056489 873 REAIEKADNDIESL 886
Cdd:PRK01156 728 MKKIKKAIGDLKRL 741
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1165-1245 |
1.48e-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: 50.17 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1165 GRCSAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIrslaESLHEIIRTRQQQAnfQLIVI-THDEEFLRSM 1243
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGV----ALLAELIAAHLARG--GAVLLtTHQPLELAAA 197
|
..
gi 315056489 1244 QC 1245
Cdd:COG4133 198 RV 199
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
796-1043 |
1.57e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 796 LEDIQDEIA----TLGEKSRQLKRASsKLTHELNQSRVDVgkLELKLRDLRRDLDNVNFQLEKKATlvsRVEDYRNQNLK 871
Cdd:COG1196 191 LEDILGELErqlePLERQAEKAERYR-ELKEELKELEAEL--LLLKLRELEAELEELEAELEELEA---ELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 872 QREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGG--PAQLERSKR 949
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEelEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 950 ELQNISDEIKRLEAEQTDLTRELNSISTRLKDSEstKRQYSDNLRYRQESKALISVNQEIADLESQNAEVDRSRFKEESE 1029
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAE--EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250
....*....|....
gi 315056489 1030 RNTREHNALAAKQA 1043
Cdd:COG1196 423 LEELEEALAELEEE 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-803 |
3.10e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 176 KKKFDEIFEALKYTKAIDNIKALRKKQNEELAKYKIMENHARDDKDKADRAEKRSlklqeeiEALRAESHELSKEMRRVA 255
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA-------DAAKKKAEEAKKAAEAAK 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 256 ELADKAWKESESYAEILGALEGKRIEAKSiqtSINNLRQHLVEVEESDEwLQSTLEQFESRQAEYRSQEDTlKEKYMDLK 335
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKK---KADAAKKKAEEKKKADE-AKKKAEEDKKKADELKKAAAA-KKKADEAK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 336 ELIEQNRHKLGLKQTECGKNENDKAQFDRQVERRVRLIKDIARQNNfrgydgdldemeindFMDRIQKLTKERSQAlEKA 415
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------------KADEAKKKAEEAKKA-DEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 416 KQEAQSQLKDAQSLLNQLSQRKSAlQEAKNAAKKQISVNDKESDTiQRSINEMDVDEGKRAAIESRMEETEKILEkekek 495
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKA-DEAKKAEEAKKADEAKKAEE-AKKADEAKKAEEKKKADELKKAEELKKAE----- 1561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 496 aknaswetDIQQNDSELRSLEDKSSKL-NAELIQGTKKAGDLARLDHLKKELKDRDDVLKEASTLVTTAERERDGTGKEL 574
Cdd:PTZ00121 1562 --------EKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 575 ELIDFKLKNA---RKSLHQHGADVENAAKKINDVIGDEPEeyphtvKQKQTELDMARKDADQYAGLGKYLNMCLDAVND- 650
Cdd:PTZ00121 1634 KVEQLKKKEAeekKKAEELKKAEEENKIKAAEEAKKAEED------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEl 1707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 651 -KKVCRTCARPFKTESELQIFKNKLKALIKKATDEDAVAEiEAREAELENvrevgtfyetwNRLTNTDIPALKKEQSDLE 729
Cdd:PTZ00121 1708 kKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEK-----------KKIAHLKKEEEKKAEEIRK 1775
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315056489 730 TEREVVLTKLEDHDKivAQRVESKRDIESLSKNIATIVRYNNEISTLQTQIQEL--SAKQEETGTSRTLEDIQDEI 803
Cdd:PTZ00121 1776 EKEAVIEEELDEEDE--KRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMedSAIKEVADSKNMQLEEADAF 1849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
8-557 |
4.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 8 KIDKLSILGVRSFDNTrseTIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDLppnSKGGAFIHDPKLCGEKEVFAQVKL 87
Cdd:COG4717 2 KIKELEIYGFGKFRDR---TIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL---EKEADELFKPQGRKPELNLKELKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 88 AFKATSAAKMVVT--RSLQLTVKKLTRQQKTLEGQLLMIKEGERtaissRVAELDQIMPQYLGVSKAvldsvifchQDES 165
Cdd:COG4717 76 LEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQELEAL---------EAEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 166 LWPMSEPSVLKKKFDEIFEAL-KYTKAIDNIKALRKKQNEELAKYKI-MENHARDDKDKADRAEKRSLKLQEEIEALRAE 243
Cdd:COG4717 142 AELPERLEELEERLEELRELEeELEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 244 SHELSKEMRRV-AELADKAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRS 322
Cdd:COG4717 222 LEELEEELEQLeNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 323 QEDTLKEKYMDLKELIEQNRHKLglkQTECGKNENDKAQFDRQVERRVRLIKDIARQnnfrgYDGDLDEMEINDFMDRIQ 402
Cdd:COG4717 302 KEAEELQALPALEELEEEELEEL---LAALGLPPDLSPEELLELLDRIEELQELLRE-----AEELEEELQLEELEQEIA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 403 KLTKERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKES--DTIQRSINEMDVDEGKRAAIES 480
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELRE 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 481 RMEETEKILEKEKEKAKNASWETDIQQNDSELRSLEDKSSKLNAeliqgtkkAGDLarLDHLKKELKDR--DDVLKEAS 557
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL--------ALEL--LEEAREEYREErlPPVLERAS 522
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
8-63 |
5.08e-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: 50.39 E-value: 5.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 315056489 8 KIDKLSILGVRSFDNTrseTIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDLPPN 63
Cdd:COG3593 2 KLEKIKIKNFRSIKDL---SIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRK 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-976 |
7.38e-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: 49.76 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 719 PALKKEQSDLETEREVVLTKLEDHDKIVAQRvesKRDIESLSKNIATIvryNNEISTLQTQIQELSAKQEEtgTSRTLED 798
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAAL---KKEEKALLKQLAAL---ERRIAALARRIRALEQELAA--LEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 799 IQDEIATLGEKSRQLKRASSKLTHEL-NQSRVDVGKLELKLRDLrrdldnvnFQLEKKATLVSRVEDYRNQnlkQREAIE 877
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDF--------LDAVRRLQYLKYLAPARRE---QAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 878 KADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLdlaSEDITNYierggPAQLERSKRELQNISDE 957
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAEL-----AAELAELQQEAEELEAL 228
|
250
....*....|....*....
gi 315056489 958 IKRLEAEQTDLTRELNSIS 976
Cdd:COG4942 229 IARLEAEAAAAAERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
711-994 |
9.13e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 711 NRLTNTDIPALKKEQSDLETEREV---------VLTKLEDHDKIVAQRVESKRDIESLSKNIaTIVRYNN----EIS--- 774
Cdd:COG3206 66 SDVLLSGLSSLSASDSPLETQIEIlksrpvlerVVDKLNLDEDPLGEEASREAAIERLRKNL-TVEPVKGsnviEISyts 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 775 -----------TLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSRQLKRASS--KLTHELNQSRVDVGKLELKLRDL 841
Cdd:COG3206 145 pdpelaaavanALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 842 RRDLDNVNFQLEKKATLVSRVEDYRNQNLKQREAIeKADNDIESLVPEVSKAQARHDDISTR-GEQ--RERELQQEVSGL 918
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARyTPNhpDVIALRAQIAAL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 919 NDSLHQ-LDLASEDITNYIE--RGGPAQLERSKRELQNISDEIKRLEAEQTDLTREL-------NSISTRLKDSESTKRQ 988
Cdd:COG3206 304 RAQLQQeAQRILASLEAELEalQAREASLQAQLAQLEARLAELPELEAELRRLEREVevarelyESLLQRLEEARLAEAL 383
|
....*.
gi 315056489 989 YSDNLR 994
Cdd:COG3206 384 TVGNVR 389
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-468 |
1.12e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 49.73 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 8 KIDKLSilGVRSFDNTRseTIQFHTPLTLIVGYNGSGKTTIIECLKYATTGDLPPNSKGGAFIHDPKLCGEKEV------ 81
Cdd:COG4694 4 KIKKLK--NVGAFKDFG--WLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNPSVrvfnrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 82 FAQVKLAFKATSAAKMVVTRSLQLTVKKLTRQQKTLEgQLLMIKEGERTAISSRVAELDQIMPQYLGVSKAVLDSVIFC- 160
Cdd:COG4694 80 FVEENLRSGEEIKGIFTLGEENIELEEEIEELEKEIE-DLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLFASs 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 161 HQDESlwpmsepsvlKKKFDEIFEALKYTKAIDNIKALRKKQNEELAKYKIMENharDDKDKADRAEKRSLkLQEEIEAL 240
Cdd:COG4694 159 GRNYR----------KANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITP---LPDLKALLSEAETL-LEKSAVSS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 241 RAEshELSKEmrrVAELADKAW-KESESYAEI---------LGALEGKRIEA------KSIQTSINNLRQHLVEVEESDE 304
Cdd:COG4694 225 AIE--ELAAL---IQNPGNSDWvEQGLAYHKEeeddtcpfcQQELAAERIEAleayfdDEYEKLLAALKDLLEELESAIN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 305 WLQSTLeqFESRQAEYRSQEDTLKEKYMDLKELIEQNRHKLGLKQtecgKNENDKAQFDrQVERRVRLIKDIARQNNfrg 384
Cdd:COG4694 300 ALSALL--LEILRTLLPSAKEDLKAALEALNALLETLLAALEEKI----ANPSTSIDLD-DQELLDELNDLIAALNA--- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 385 ydgdldemEINDFMDRIQKLTKERSQALEKAKQ-------EAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKE 457
Cdd:COG4694 370 --------LIEEHNAKIANLKAEKEEARKKLEAhelaelkEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEAE 441
|
490
....*....|.
gi 315056489 458 SDTIQRSINEM 468
Cdd:COG4694 442 LSSVDEAADEI 452
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1161-1217 |
1.18e-05 |
|
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: 44.92 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315056489 1161 MDMRGRCSAGQK-VLASIIIRLALAECFGVN------CGLIALDEPTTNLDRDNIRSLAESLHE 1217
Cdd:pfam13558 27 YRRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
727-983 |
1.23e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 727 DLETEREVVLTKLEdhdKIVAQRVESKRDIESLSKNIATIVRYNNEISTLQTQIQELSAKQEETGTSRtlEDIQDEIATL 806
Cdd:PRK02224 210 GLESELAELDEEIE---RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER--EELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 807 GEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKkatlvsrvedyrnqnlkQREAIEKADNDIESL 886
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE-----------------CRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 887 VPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIER--GGPAQLERSKRELQNISDEIKRLEAE 964
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNAEDFLEELREERDELRER 427
|
250
....*....|....*....
gi 315056489 965 QTDLTRELNSISTRLKDSE 983
Cdd:PRK02224 428 EAELEATLRTARERVEEAE 446
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-69 |
2.76e-05 |
|
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: 45.81 E-value: 2.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 11 KLSILGVRSFDNTRSETIqFHTPLTLIVGYNGSGKTTIIECLKYATTGDLPPNSKGGAF 69
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTF-GEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGV 58
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
175-465 |
3.15e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 175 LKKKFDEIFEALKYtkaidniKALRKKQnEELAKYKIMENHARDDKDKAdRAEKRSLKLQEEIEALRAESHELSKEMRRV 254
Cdd:TIGR02169 200 LERLRREREKAERY-------QALLKEK-REYEGYELLKEKEALERQKE-AIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 255 AELADKAWKE-----SESYAEILGALEGKRIEAKSIQTSINNLRQHL-------VEVEESDEWLQSTLEQFESRQAEYRS 322
Cdd:TIGR02169 271 EQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELedaeerlAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 323 QEDTLKEKYMDLKELIEQNRHKLGLKQTEcgknenDKAQFDRQVERRVRLIKDIARQNnfrgydgdldemEINDFMDRIQ 402
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKE------FAETRDELKDYREKLEKLKREIN------------ELKRELDRLQ 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315056489 403 KLTKERSQALEKAKQEaqsqLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSI 465
Cdd:TIGR02169 413 EELQRLSEELADLNAA----IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
407-1239 |
4.45e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 407 ERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKnaaKKQisvndKESDTIQRSINEMDVDEGKRAAIESRMEETE 486
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL---KKQ-----QLLKQLRARIEELRAQEAVLEETQERINRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 487 KILEKEKEKAKNASWETDIQQNDSELRSLEDKSSKLNAELIQGTKKAGDLARLDHLKKELKDRDDVLKEASTLVTTAERE 566
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 567 RDGTGKELELIdfklkNARKSLHQHGADVENAAKKINDVIGDEPEEY-PHTVKQKQTELDMARKDADQYAGLgKYLNMCL 645
Cdd:TIGR00618 371 SCQQHTLTQHI-----HTLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 646 DAVNDKKVCRTCARPfktesELQIFKNKLKALIKKATDEDAVAEIEAREAELENVREVGTFYETWNRLTNTDIPALKKEQ 725
Cdd:TIGR00618 445 AAITCTAQCEKLEKI-----HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 726 SDLETEREVVLTKLEDHDKIVAQRVESKRDI-ESLSKNIAtivRYNNEISTLQTQIQEL-----SAKQEETGTSRTLEDI 799
Cdd:TIGR00618 520 IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQlTSERKQRA---SLKEQMQEIQQSFSILtqcdnRSKEDIPNLQNITVRL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 800 QDEIATLGEKSRQLKRASS----KLTHELNQSRVDV------GKLELKLRDLRRDLDNVNFQLEKKATLVSRVEDYRNQN 869
Cdd:TIGR00618 597 QDLTEKLSEAEDMLACEQHallrKLQPEQDLQDVRLhlqqcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLA 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 870 LKQREaIEKADNDIESLVPEV-------SKAQARHDDISTRGEQRErELQQEVSGLNDSLHQLDLASEDITNYIERGGPA 942
Cdd:TIGR00618 677 SRQLA-LQKMQSEKEQLTYWKemlaqcqTLLRELETHIEEYDREFN-EIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 943 QLERSKRELQNIS----------DEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSD------NLRYRQESKALISVN 1006
Cdd:TIGR00618 755 VLKARTEAHFNNNeevtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPsdedilNLQCETLVQEEEQFL 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1007 QEIADLESQNAEVDRSrfKEESERNTREHNALAAKQAskmgemkskddQLMQLLADWNTDYKDAGAKFKEAHIKV--ETT 1084
Cdd:TIGR00618 835 SRLEEKSATLGEITHQ--LLKYEECSKQLAQLTQEQA-----------KIIQLSDKLNGINQIKIQFDGDALIKFlhEIT 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1085 KAAVDDLGryggalDKAIMKYHGlkmeeinRIIGELWQKTyRGTDVDTILIRSDNESARGNRSYnyrvcmvkqdaemdmr 1164
Cdd:TIGR00618 902 LYANVRLA------NQSEGRFHG-------RYADSHVNAR-KYQGLALLVADAYTGSVRPSATL---------------- 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 1165 grcSAGQKVLASIIIRLALAECF----GVNCGLIALDEPTTNLDRDNIRSLAESLHEIirtrqQQANFQLIVITHDEEF 1239
Cdd:TIGR00618 952 ---SGGETFLASLSLALALADLLstsgGTVLDSLFIDEGFGSLDEDSLDRAIGILDAI-----REGSKMIGIISHVPEF 1022
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
234-472 |
4.80e-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: 47.07 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 234 QEEIEALRAESHELSKEMRRVAELADKAWKESESYAEilgalegkriEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQF 313
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----------QLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 314 ESRQAEYRSQEDTLKEKYMD-LKELIEQNRH---KLGLKQTECGknendkaqfdrQVERRVRLIKDIARQNNfrgydgdl 389
Cdd:COG4942 89 EKEIAELRAELEAQKEELAElLRALYRLGRQpplALLLSPEDFL-----------DAVRRLQYLKYLAPARR-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 390 demeindfmDRIQKLTKERsQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEMD 469
Cdd:COG4942 150 ---------EQAEELRADL-AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
...
gi 315056489 470 VDE 472
Cdd:COG4942 220 QEA 222
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
221-330 |
5.04e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 221 DKADRAEKRSLKLQEeieaLRAESHELSKEMRRVAELADKAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVE 300
Cdd:PRK02224 527 ERRETIEEKRERAEE----LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA 602
|
90 100 110
....*....|....*....|....*....|
gi 315056489 301 ESDEWLQSTLEQFESRQAEYRSQEDTLKEK 330
Cdd:PRK02224 603 DAEDEIERLREKREALAELNDERRERLAEK 632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
720-981 |
5.54e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 720 ALKKEQSDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIATIVrynnEISTLQTQIQELSAKQEEtgtsrtLEDI 799
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI----DVASAEREIAELEAELER------LDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 800 QDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKATLVSRVEDYRNQNLKQREAIEKA 879
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 880 DNDIeslvpeVSKAQARHDDISTRGEQRERELQQEVSGLN----DSLHQLDLASEDITNYIER-------GGPAQLERSK 948
Cdd:COG4913 764 EREL------RENLEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLALldrleedGLPEYEERFK 837
|
250 260 270
....*....|....*....|....*....|....
gi 315056489 949 REL-QNISDEIKRLeaeQTDLTRELNSISTRLKD 981
Cdd:COG4913 838 ELLnENSIEFVADL---LSKLRRAIREIKERIDP 868
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-447 |
5.62e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 195 IKALRKKQNEELAKYKIMENHARDDKDKADRAEKRSLKLQEEIEALRAESHELSKEMRRVAELADKAwkeSESYAEILGA 274
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL---EEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 275 LEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRSQEDTLKEKYMDLKELIEQNRHKLGLKQTECGK 354
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 355 NENDKAQFDRQVERRVRLIKDIARqnnfrgydgdldemEINDFMDRIQKLTKERSQALEKAKQEAQsQLKDAQSLLNQLS 434
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAE--------------EEAELEEEEEALLELLAELLEEAALLEA-ALAELLEELAEAA 490
|
250
....*....|...
gi 315056489 435 QRKSALQEAKNAA 447
Cdd:COG1196 491 ARLLLLLEAEADY 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
189-950 |
6.08e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 189 TKAIDNIKALRKKQNEEL-AKYKIMENHARDDKDKAD----RAEKRSLKLQEEIEALRAESHELSKEMRRVAELADKAWK 263
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLeEIEQLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 264 ESESYAEilgalegkriEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAEYRSQEDTLKEKYMDLKELIEQNRH 343
Cdd:TIGR02169 330 EIDKLLA----------EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 344 KLGLKQTECGKNENDKAQFDRQVERRVRLIKDI-ARQNNFrgydgdldEMEINDFMDRIQKLTKERSQA---LEKAKQE- 418
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIeAKINEL--------EEEKEDKALEIKKQEWKLEQLaadLSKYEQEl 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 419 ---------AQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEM-DVDEGKRAAIES----RMEE 484
Cdd:TIGR02169 472 ydlkeeydrVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgSVGERYATAIEVaagnRLNN 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 485 TEKILEKEKEK------AKNASWETDIQQNdsELRSLEDKSSKLN-------------------------------AELI 527
Cdd:TIGR02169 552 VVVEDDAVAKEaiellkRRKAGRATFLPLN--KMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdtlvVEDI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 528 QGTKKAGDLARLDHLKKELKDRDDVLKEAS-TLVTTAERERDGTGKELELID--FKLKNARKSLHQHGADVENAAKKIND 604
Cdd:TIGR02169 630 EAARRLMGKYRMVTLEGELFEKSGAMTGGSrAPRGGILFSRSEPAELQRLRErlEGLKRELSSLQSELRRIENRLDELSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 605 VIGDEPEEyphtVKQKQTELDMARKDADQYAGLGKYLnmcldavndkkvcrtcarpfktESELQIFKNKLKALIKKATDE 684
Cdd:TIGR02169 710 ELSDASRK----IGEIEKEIEQLEQEEEKLKERLEEL----------------------EEDLSSLEQEIENVKSELKEL 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 685 DavAEIEAREAELENVREvgTFYETWNRLTNTDIPALKKEQSDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIA 764
Cdd:TIGR02169 764 E--ARIEELEEDLHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 765 TIVRY-NNEISTLQTQIQELSAKQEEtgTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRr 843
Cdd:TIGR02169 840 EQRIDlKEQIKSIEKEIENLNGKKEE--LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR- 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 844 dlDNVNFQLEKKATLVSRVEDYrNQNLKQREAIEKADNDIESLVPEVSKAQAR---HDDISTRGEQRERELQQEVSGLND 920
Cdd:TIGR02169 917 --KRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEiraLEPVNMLAIQEYEEVLKRLDELKE 993
|
810 820 830
....*....|....*....|....*....|
gi 315056489 921 SLHQLDLASEDITNYIErggpaQLERSKRE 950
Cdd:TIGR02169 994 KRAKLEEERKAILERIE-----EYEKKKRE 1018
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1168-1243 |
6.52e-05 |
|
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: 47.28 E-value: 6.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHEIIRTRqqqanfQLIVITHDEEFLRSM 1243
Cdd:TIGR02857 460 SGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR------TVLLVTHRLALAALA 523
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-455 |
7.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 174 VLKKKFDEIFEAL-KYTKAIDNIKALRKKQNEELAKYKIMENHARDDKDKADraekrslkLQEEIEALRAESHELSKEMR 252
Cdd:COG4913 614 ALEAELAELEEELaEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--------AEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 253 RVAEL---ADKAWKESESYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFEsrqAEYRSQEDTLKE 329
Cdd:COG4913 686 DLAALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 330 KYMDLKELIEQNRHKLglkqtecgknendKAQFDRQVERRVRLIKDIARQNNFRGYDGDLDEMEINDFMDRIQKLTKERs 409
Cdd:COG4913 763 VERELRENLEERIDAL-------------RARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG- 828
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 315056489 410 qaLEKAKQEAQSQLKDAQSllNQLSQRKSALQEAKNAAKKQIS-VND 455
Cdd:COG4913 829 --LPEYEERFKELLNENSI--EFVADLLSKLRRAIREIKERIDpLND 871
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1168-1243 |
9.68e-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: 44.49 E-value: 9.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLD---RDNIRSLAESLHeiirtrqQQANFQLIVITHDEEFLRSM 1243
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQ-------AQLGITVVLVTHDLDEAARL 167
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
761-1266 |
9.92e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 46.65 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 761 KNIATIVRYNNEIstlQTQIQELSAKqeetgtsrtLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRD 840
Cdd:COG4694 92 KGIFTLGEENIEL---EEEIEELEKE---------IEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLFASSG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 841 LRRDLDNVNFQLEKkatLVSRVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDI---STRGEQRErELQQEVSG 917
Cdd:COG4694 160 RNYRKANLEKKLSA---LKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLlekSAVSSAIE-ELAALIQN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 918 LNDS--------LHQL-----------DLASE---DITNYIERGGPAQLERSKRELQNISDEIKRLEA-EQTDLTRELNS 974
Cdd:COG4694 236 PGNSdwveqglaYHKEeeddtcpfcqqELAAErieALEAYFDDEYEKLLAALKDLLEELESAINALSAlLLEILRTLLPS 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 975 ISTRLKDSESTKRQYSDNLRYRQESKalISVNQEIADLESQNAEVDRSRFKEESERNTREHNALAAKQASKMGEMKSK-- 1052
Cdd:COG4694 316 AKEDLKAALEALNALLETLLAALEEK--IANPSTSIDLDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKle 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1053 DDQLMQLLADWnTDYKDAGAKFKEAHIKVETTKAAVDDLGRYGGALDKAIMKYHGLKmEEINRIIGELWQKTYR-----G 1127
Cdd:COG4694 394 AHELAELKEDL-SRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVDEAA-DEINEELKALGFDEFSleaveD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1128 TDVDTILIRSDNESARGNRSYnyrvcmvkqdaemdmrgrcSAGQKVlasiIIRLA--LAECFGVN----CGLIALDEPTT 1201
Cdd:COG4694 472 GRSSYRLKRNGENDAKPAKTL-------------------SEGEKT----AIALAyfLAELEGDEndlkKKIVVIDDPVS 528
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315056489 1202 NLDRDNIrslaESLHEIIRTRQQQANfQLIVITHDEEFLRSMQcgDFCDY--------YYRVSRNERQKSIIE 1266
Cdd:COG4694 529 SLDSNHR----FAVASLLKELSKKAK-QVIVLTHNLYFLKELR--DLADEdnkkkncaFYEIRKDNRGSKIIK 594
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
8-58 |
1.09e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 45.92 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 315056489 8 KIDKLSILGVRSFdntRSETIQFHTPLTLIVGYNGSGKTTIIECLKYATTG 58
Cdd:COG1195 1 RLKRLSLTNFRNY---ESLELEFSPGINVLVGPNGQGKTNLLEAIYLLATG 48
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
195-813 |
1.29e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 195 IKALRKKQNEELAKYKIME-NHARDDKDKADRAEKRSLKLQEEIEALRAES----HELSKEMRRVAELADKAWKESE-SY 268
Cdd:pfam12128 363 LKALTGKHQDVTAKYNRRRsKIKEQNNRDIAGIKDKLAKIREARDRQLAVAeddlQALESELREQLEAGKLEFNEEEyRL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 269 AEILGALEGKRIEAKSIQTSINNLRQHLVEVEESDEWLQSTLEQFESRQAE---YRSQEDTLKEKYMDLKELIEQNRHKL 345
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSElrqARKRRDQASEALRQASRRLEERQSAL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 346 G----------------LKQTECGKNENDKAQFDRQVERRVRLIKDI-----ARQNNFRGYDGDLDEMEINDFMDRIQKL 404
Cdd:pfam12128 523 DelelqlfpqagtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVwdgsvGGELNLYGVKLDLKRIDVPEWAASEEEL 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 405 tKERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDkesDTIQRSINEMDVDEGK-RAAIESRMe 483
Cdd:pfam12128 603 -RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNAR---LDLRRLFDEKQSEKDKkNKALAERK- 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 484 etekilekekekaknASWETDIQQNDSELRSLeDKSSKLNAELIQGTKKAGDLARLDHLKKELKDRDDVLkeaSTLVTTA 563
Cdd:pfam12128 678 ---------------DSANERLNSLEAQLKQL-DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL---ALLKAAI 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 564 ERERDGTGKELELIDFKLKNARKSLHQHG-------ADVENAAKKINDVIGDEPEE------YPHT-------------- 616
Cdd:pfam12128 739 AARRSGAKAELKALETWYKRDLASLGVDPdviaklkREIRTLERKIERIAVRRQEVlryfdwYQETwlqrrprlatqlsn 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 617 VKQKQTEL--DMARKDADQYAGLGKyLNMCLDAVNDKKVcrtcaRPFKTESELQIFKNKLKALIKKATDEDAVAEIEARE 694
Cdd:pfam12128 819 IERAISELqqQLARLIADTKLRRAK-LEMERKASEKQQV-----RLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERL 892
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 695 AELENVR------------EVGTF------------YETWNRLTNTDiPALKKEQSDLETEREVVLTKLEDHDKIVAQRV 750
Cdd:pfam12128 893 AQLEDLKlkrdylsesvkkYVEHFknviadhsgsglAETWESLREED-HYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSI 971
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315056489 751 ESKRDIESLSKNiaTIVRYNNEISTLQTQIQELSAK-QEETGTSRTLEDIQDEIATLGEKSRQL 813
Cdd:pfam12128 972 MVLREQVSILGV--DLTEFYDVLADFDRRIASFSRElQREVGEEAFFEGVSESAVRIRSKVSEL 1033
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
755-972 |
1.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 755 DIESLSKNIATIVRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSR--QLKRASSKLTHELNQSRVDVG 832
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 833 KLELKLRDLRRDLDnvnfqlEKKATLVSRVEDYRNQNLKQREAIEKadnDIESLVPEVSKAQARHDDISTRGEQRERELQ 912
Cdd:COG4913 306 RLEAELERLEARLD------ALREELDELEAQIRGNGGDRLEQLER---EIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315056489 913 QEVSGLNDSLHQLDLASEDITNYIERGGPA------QLERSKRELQNISDEIKRLEAEQTDLTREL 972
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEAlaeaeaALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1178-1242 |
1.62e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315056489 1178 IIRLALAECFGVNCG--LIALDEPTTNLDRDNIRSLAESLHEIIrtrqQQANfQLIVITHDEEFLRS 1242
Cdd:cd03238 93 LQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLI----DLGN-TVILIEHNLDVLSS 154
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-1056 |
1.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 219 DKDKADRAEKRSLKLQEE---IEALRAESHELSKEMRRVAELADKAwkesesyAEILGALEGKRIEAksiqtsinnlrqh 295
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEakkTETGKAEEARKAEEAKKKAEDARKA-------EEARKAEDARKAEE------------- 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 296 lVEVEESDEWLQSTLEQFESRQAEY-RSQEDTLKekymdlkelIEQNRHKLGLKQTEcgknENDKAQFDRQVERrVRLIK 374
Cdd:PTZ00121 1145 -ARKAEDAKRVEIARKAEDARKAEEaRKAEDAKK---------AEAARKAEEVRKAE----ELRKAEDARKAEA-ARKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 375 DIARQNNFRGYDgDLDEMEINDFMDRIQKLTKERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVN 454
Cdd:PTZ00121 1210 EERKAEEARKAE-DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 455 DKESDTIQRSINEMDVDEGKRAAIESRMEETEKILEKEKEKAKNAS-WETDIQQNDSELRSLEDKSSKLNAELIQGTKKA 533
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAkKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 534 GDLARLDHLKK--ELKDRDDVLKEASTLVTTAERERdgtgKELELIDFKLKNARKSlhqhgadvENAAKKINDVIGDEPE 611
Cdd:PTZ00121 1369 AEKKKEEAKKKadAAKKKAEEKKKADEAKKKAEEDK----KKADELKKAAAAKKKA--------DEAKKKAEEKKKADEA 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 612 EYPHTVKQKQTELDMARKDADQYAGLGKYLNMCLDAVNDKKVCRTCARPFKTESELQIFKNKL-----KALIKKATDEDA 686
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeakkAAEAKKKADEAK 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 687 VAEIEAREAELENVREVGTFYETWNRLTNTDIPALKK--EQSDLETEREVVLTKLEDHDKIVA-QRVESKRDIESlSKNI 763
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMAlRKAEEAKKAEE-ARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 764 ATIVRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRR 843
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 844 DLDNVNFQLE---KKATLVSRVEDYRN--QNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVSGL 918
Cdd:PTZ00121 1676 KAEEAKKAEEdekKAAEALKKEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 919 NDSLHQLDLASEDITNYIERGGPAQLERSKRElqniSDEIKRLEAEQTdltrelnsISTRLKDSESTKRQYSDNLRYRQE 998
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE----EDEKRRMEVDKK--------IKDIFDNFANIIEGGKEGNLVIND 1823
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 999 SKAL-ISVNQEIADleSQNAEVDRSrfkEESERNTREHNALAAKQASKMGEMKSKDDQL 1056
Cdd:PTZ00121 1824 SKEMeDSAIKEVAD--SKNMQLEEA---DAFEKHKFNKNNENGEDGNKEADFNKEKDLK 1877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
234-428 |
1.72e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 234 QEEIEALRAESHELSKEMRRVAELADKAWKESESYAEILGALEG------KRIEAKSIQTSINNLRQHLVEVEESDEWLQ 307
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 308 stleqfesrqaeyrsqedTLKEKYMDLKELIEQNRHKLGLKQTECGKNENDKAQFDRQVER---RVRLIKDIARQNNFRG 384
Cdd:COG4913 689 ------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRAL 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 315056489 385 YDGDLDEMEINDFMDRIQKLTKERSQALEKAKQEAQSQLKDAQS 428
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
803-1005 |
1.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 803 IATLGEKSRQLKRASSKlTHELNQSRVDvgKLELKLRDLRRDLDNVNFQLEKKATLVSRVEDYRNQNLKQREAIEKADND 882
Cdd:COG4717 48 LERLEKEADELFKPQGR-KPELNLKELK--ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 883 IE--SLVPEVSKAQARHDDISTRGE------QRERELQQEVSGLNDSLHQLDLASEDITNYIERGGPAQLERSKRELQNI 954
Cdd:COG4717 125 LQllPLYQELEALEAELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 315056489 955 SDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKALISV 1005
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1168-1244 |
3.29e-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: 42.97 E-value: 3.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESlheIIRTRQQQANfqLIVITHDEEFLRSMQ 1244
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQA---IAALKAAGAT--RIVIAHRPETLASAD 163
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
593-1001 |
3.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 593 ADVENAAKKINDVIGDEPEEYPHTVKQKQTELDMARKDADQYAGLGKYLNMCLDAVNDKKVCRTCARpfkteSELQIFKN 672
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR-----EELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 673 KLKALIKKATDEDAVAEIEAREAELENVREVgtfYETWNRLTNtDIPALKKEQSDLETEREvvlTKLEDHDKIVAQRVES 752
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEER---LEELRELEE-ELEELEAELAELQEELE---ELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 753 -KRDIESLSKNIAtivRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSR-------------------- 811
Cdd:COG4717 197 lAEELEELQQRLA---ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 812 ------------------QLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKAT----LVSRVEDYRNQN 869
Cdd:COG4717 274 tiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEelleLLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 870 LKQREAIEKADND--IESLVPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGGPAQLERs 947
Cdd:COG4717 354 REAEELEEELQLEelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE- 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 315056489 948 krELQNISDEIKRLEAEQTDLTRELNSISTRLKDSEsTKRQYSDNLRYRQESKA 1001
Cdd:COG4717 433 --ELEELEEELEELEEELEELREELAELEAELEQLE-EDGELAELLQELEELKA 483
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
378-972 |
3.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 378 RQNNFRGYDGDLDEMEINDFMDRIQKLTKERSQA------LEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKK-- 449
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEEKDLHERLNGLESELAELdeeierYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlr 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 450 -QISVNDKESDTIQRSINEM-DVDEGKRAAIESRMEETEKILEKEKEKAKNASwetDIQQNDSELR-SLEDKSSKLNAEL 526
Cdd:PRK02224 265 eTIAETEREREELAEEVRDLrERLEELEEERDDLLAEAGLDDADAEAVEARRE---ELEDRDEELRdRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 527 IQGTKKAGDLARLDHLKKELKDRDDVLKEAstlVTTAERERDGTGKELELIDFKLKNARKSLHQHGADVENAAKKINDVI 606
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESE---LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 607 GDEPEeyphtVKQKQTELDMARKDADQYAGLGKYLnmcLDAVNdkkvCRTCARPFKTESELQIFknklkalikkATDEDA 686
Cdd:PRK02224 419 EERDE-----LREREAELEATLRTARERVEEAEAL---LEAGK----CPECGQPVEGSPHVETI----------EEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 687 VAEIEAREAELENvrEVGTFYETWNRLTntDIPALKKEQSDLETEREVVLTKLEDHdkivAQRVESKRD-IESLSKNIAt 765
Cdd:PRK02224 477 VEELEAELEDLEE--EVEEVEERLERAE--DLVEAEDRIERLEERREDLEELIAER----RETIEEKRErAEELRERAA- 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 766 ivrynnEISTLQTQIQELSAKQEETGtsrtlEDIQDEIATLGEKSRQLKRASSKLTH--ELNQSRVDVGKLELKLRDLRR 843
Cdd:PRK02224 548 ------ELEAEAEEKREAAAEAEEEA-----EEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 844 DLDNVNFQL--------EKKATLVSRVEDYRNQNLKQR-----EAIEKADNDIESLvpevskaqarhddistrgEQRERE 910
Cdd:PRK02224 617 ALAELNDERrerlaekrERKRELEAEFDEARIEEAREDkeraeEYLEQVEEKLDEL------------------REERDD 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315056489 911 LQQEVSGLNDSLHQLDLASEDITnyierggpaQLERSKRELQNISDEIKRLEAEQTDLTREL 972
Cdd:PRK02224 679 LQAEIGAVENELEELEELRERRE---------ALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
667-1238 |
4.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 667 LQIFKNKLKALIKKA--TDEDAVAEIEAREAELENVRE-VGTFYETWNRL--TNTDIPALKKEQSDLETEREVvLTKLED 741
Cdd:COG4717 48 LERLEKEADELFKPQgrKPELNLKELKELEEELKEAEEkEEEYAELQEELeeLEEELEELEAELEELREELEK-LEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 742 HDKIVAQRVESKRDIESLSKNIATIVRYNNEISTLQTQIQELSAKQEET-------------GTSRTLEDIQDEIATLGE 808
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELqeeleelleqlslATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 809 KSRQLKRASSKLTHELNQSRVDVGKLELKLRDLR--------------------------RDLDNVNFQLEKKATLVSRV 862
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallallglggSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 863 EDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGGPA 942
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 943 QLERSKREL---QNISDE---IKRLEA--EQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKALISVNQEIADLEs 1014
Cdd:COG4717 367 ELEQEIAALlaeAGVEDEeelRAALEQaeEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1015 qnaevdrsrfkeeserntREHNALAAKQASKMGEMK--SKDDQLMQLLAdwntDYKDAGAKFKEAHIKVETTKAAVDdlg 1092
Cdd:COG4717 446 ------------------EELEELREELAELEAELEqlEEDGELAELLQ----ELEELKAELRELAEEWAALKLALE--- 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1093 ryggALDKAIMKYHGLK----MEEINRIIGELWQKTYRGTDVDtilirsDNESARGNRSYNYRVCMvkqdAEMdmrgrcS 1168
Cdd:COG4717 501 ----LLEEAREEYREERlppvLERASEYFSRLTDGRYRLIRID------EDLSLKVDTEDGRTRPV----EEL------S 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315056489 1169 AGQKVLASIIIRLALAECF-GVNCGLIaLDEPTTNLDRDNIRSLAESLHEIIRTRqqqanfQLIVITHDEE 1238
Cdd:COG4717 561 RGTREQLYLALRLALAELLaGEPLPLI-LDDAFVNFDDERLRAALELLAELAKGR------QVIYFTCHEE 624
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
400-824 |
4.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 400 RIQKLTKERSQALEKAKQEAQSQLKDaqslLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEMDVDEGKRAAIE 479
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 480 SRMEETEKILEKEKEKAKNASWETDIQQNDSELRSLEDKSSKLNAELIQGTKKA--GDLARLDHLKKELKDRDDVLKEAS 557
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 558 TLVTTAERERDGTGKELELIDFKLKNARKSL---------------HQHGADVENAAKKINDVIGDEPEEYPHTVKQKQT 622
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLllliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 623 eldmARKDADQYAGLGKylnmcLDAVNDKKVCRTCAR-PFKTESELQIFKNKLKALIKKatdEDAVAEIEAREAELENVR 701
Cdd:COG4717 300 ----LGKEAEELQALPA-----LEELEEEELEELLAAlGLPPDLSPEELLELLDRIEEL---QELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 702 EVGTFYETWNRLTNTDIPAL------KKEQSDLETEREVVLTKLEDHDKIVAQRVES------KRDIESLSKNIAtivRY 769
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELraaleqAEEYQELKEELEELEEQLEELLGELEELLEAldeeelEEELEELEEELE---EL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 315056489 770 NNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSRQL--KRASSKLTHEL 824
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELaeEWAALKLALEL 501
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
848-1088 |
5.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 848 VNFQLEKKATLVSRVEDYRNQNLKQ-REAIEKADNDIESLvpevskaQARHDDISTrgEQRERELQQEVSGLNDSLHQLD 926
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPElRKELEEAEAALEEF-------RQKNGLVDL--SEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 927 LASEDITNYIERGGpAQLERSKRELQNI--SDEIKRLEAEQTDLTRELNSISTRLKDsestkrqysdnlryrqESKALIS 1004
Cdd:COG3206 233 AELAEAEARLAALR-AQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTP----------------NHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1005 VNQEIADLESQ-NAEVDRSRFKEESERNT-----REHNALAAKQASKMGEMKSKDDQLMQLLADWNTD---YKDAGAKFK 1075
Cdd:COG3206 296 LRAQIAALRAQlQQEAQRILASLEAELEAlqareASLQAQLAQLEARLAELPELEAELRRLEREVEVArelYESLLQRLE 375
|
250
....*....|...
gi 315056489 1076 EAHIKVETTKAAV 1088
Cdd:COG3206 376 EARLAEALTVGNV 388
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1165-1242 |
5.95e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.90 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1165 GRCSAGQKVlasiiiRLALAECF--GVNCgLIaLDEPTTNLDRDNIRSLAESLheiirtrqqqANFQ--LIVITHDEEFL 1240
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLlsPPNV-LL-LDEPTNHLDIETLEALEEAL----------DDFPgtVLLVSHDRYFL 492
|
..
gi 315056489 1241 RS 1242
Cdd:COG0488 493 DR 494
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
9-55 |
6.12e-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: 42.45 E-value: 6.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 315056489 9 IDKLSILGVRSF-DNTrseTIQFHTPLTLIVGYNGSGKTTIIECLKYA 55
Cdd:cd03278 1 LKKLELKGFKSFaDKT---TIPFPPGLTAIVGPNGSGKSNIIDAIRWV 45
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1168-1238 |
6.63e-04 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain] Cd Length: 213 Bit Score: 42.51 E-value: 6.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDnirsLAESLHEIIRTRQQQANFQLIVITHDEE 1238
Cdd:cd03259 132 SGGQQQ------RVALARALAREPSLLLLDEPLSALDAK----LREELREELKELQRELGITTIYVTHDQE 192
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1193-1241 |
7.42e-04 |
|
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: 42.48 E-value: 7.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 315056489 1193 LIALDEPTTNLDRDNirslAESLHEIIRTRQQQANFQLIVITHDEEFLR 1241
Cdd:cd03255 161 IILADEPTGNLDSET----GKEVMELLRELNKEAGTTIVVVTHDPELAE 205
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
715-1059 |
7.70e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 715 NTDIPALKKEQSDLETEREVVLTKLEDHDKIVAQrveSKRDIESLSKNIATIVRYNNEISTLQTQIQELSAKQEETGTSR 794
Cdd:TIGR04523 158 NNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK---IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 795 TLE--DIQDEIATLGEKSRQLKRASSKLTHELNQ---SRVDVGKLELKLRDLRRDLDNVNFQLEKkatLVSRVEDYRNQN 869
Cdd:TIGR04523 235 EKKqqEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQNNKKIKELEKQLNQLKSEISD---LNNQKEQDWNKE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 870 LKqrEAIEKADNDIESLVPEVSKAqarhddistrgEQRERELQQEVSGLNDSLHQLDLASEDITNyierggpaQLERSKR 949
Cdd:TIGR04523 312 LK--SELKNQEKKLEEIQNQISQN-----------NKIISQLNEQISQLKKELTNSESENSEKQR--------ELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 950 ELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKALIS------------VNQEIADLESQNA 1017
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEkeierlketiikNNSEIKDLTNQDS 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 315056489 1018 EVD---------RSRFKEESERNTREHNALAAKQASKMGEMKSKDDQLMQL 1059
Cdd:TIGR04523 451 VKEliiknldntRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1193-1238 |
9.07e-04 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 42.34 E-value: 9.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 315056489 1193 LIAlDEPTTNLDRDNirslAESLHEIIRTRQQQANFQLIVITHDEE 1238
Cdd:COG1136 166 ILA-DEPTGNLDSKT----GEEVLELLRELNRELGTTIVMVTHDPE 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
714-1090 |
9.44e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 714 TNTDIPALKKEQSDLETEREVVLTKleDHDKIVAQRVESKRDIES-LSKNIATIVRYNNEISTLQTQIQEL-----SAKQ 787
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNqISQNNKIISQLNEQISQLKKELTNSesensEKQR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 788 EETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQ----LEKKATLVSRVE 863
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEierlKETIIKNNSEIK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 864 DYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQ---QEVSGLNDSLHQLDLASEDITNyiergg 940
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKskeKELKKLNEEKKELEEKVKDLTK------ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 941 paQLERSKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDS--ESTKRQYSDNLRYRQESKALISVNQEIADLESQNAE 1018
Cdd:TIGR04523 518 --KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1019 VDRSRFKEESERNTREHNAL------AAKQASKMGEMK----SKDDQLMQLLADWNTDYKDAGAKFKEAHIKVETTKAAV 1088
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLekelekAKKENEKLSSIIknikSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
..
gi 315056489 1089 DD 1090
Cdd:TIGR04523 676 DD 677
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
37-72 |
1.08e-03 |
|
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: 42.11 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|....*.
gi 315056489 37 IVGYNGSGKTTIIECLkyatTGDLPPNSkGGAFIHD 72
Cdd:cd03263 33 LLGHNGAGKTTTLKML----TGELRPTS-GTAYING 63
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
168-1012 |
1.26e-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: 43.50 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 168 PMSEPSVLKKKFDEIFEalKYTKAIDNIKALRKKQNEElAKYKIMENHARDDKDKADRAEkrsLKLQEEIEALRAESHEL 247
Cdd:TIGR01612 457 PKSKLKALEKRFFEIFE--EEWGSYDIKKDIDENSKQD-NTVKLILMRMKDFKDIIDFME---LYKPDEVPSKNIIGFDI 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 248 SKEMRRVaeladkawkeseSYAEILGALegkrieaKSIQTSINNLRQHLVEVeesdewlQSTLEQFESRQAEYRSQEDTL 327
Cdd:TIGR01612 531 DQNIKAK------------LYKEIEAGL-------KESYELAKNWKKLIHEI-------KKELEEENEDSIHLEKEIKDL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 328 KEKYMDL-KELIEQNRHKLGLKqtECGKNENDKAQFdrqVERRVRLIKDIARQNNFRGYDGDLDEMEINDFMDRIQKLTK 406
Cdd:TIGR01612 585 FDKYLEIdDEIIYINKLKLELK--EKIKNISDKNEY---IKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYS 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 407 ERSQALEKAKQEaqsqlkDAQSLLNQLS-----------QRKSALQEAKNAAKKQIS-VNDKESDTIQRSINEMdvdEGK 474
Cdd:TIGR01612 660 TIKSELSKIYED------DIDALYNELSsivkenaidntEDKAKLDDLKSKIDKEYDkIQNMETATVELHLSNI---ENK 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 475 RAAIESRMEETEKILEKEKEKAKNASWEtDIQQNDSELRSLEDKSSKLNAELIQGTKKAG-------DLARLDHLKKE-L 546
Cdd:TIGR01612 731 KNELLDIIVEIKKHIHGEINKDLNKILE-DFKNKEKELSNKINDYAKEKDELNKYKSKISeiknhynDQINIDNIKDEdA 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 547 KDRDDVLKEASTLVTTAERERDGTGKELE------------LIDFKLKNARKSLHQHGADVENAAKKINDVIGDEPEEYP 614
Cdd:TIGR01612 810 KQNYDKSKEYIKTISIKEDEIFKIINEMKfmkddflnkvdkFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDYE 889
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 615 HTVKQKQTELDMARKDADQyaglgKYLNM-CLDAVNDK-KVCRTCARPFKTESELQ-IFKNKLKALIKKATDEDAVAE-- 689
Cdd:TIGR01612 890 KKFNDSKSLINEINKSIEE-----EYQNInTLKKVDEYiKICENTKESIEKFHNKQnILKEILNKNIDTIKESNLIEKsy 964
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 690 -------IEAREAELENVREVGTF--YETWNrltNTDIPALKKEQSDLETEREVVLTKLEDHDKIVAQRVESKrdIESLS 760
Cdd:TIGR01612 965 kdkfdntLIDKINELDKAFKDASLndYEAKN---NELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQK--IEDAN 1039
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 761 KNIATI-VRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQDEIATLGEKSRQL---------KRASSKLTHELNQSRVD 830
Cdd:TIGR01612 1040 KNIPNIeIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLkhynfddfgKEENIKYADEINKIKDD 1119
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 831 VGKLELKLRDLRRDLDNV-----NFQLEKKATlVSRVEDYRNQNLKQrEAIEKADNDIESLVPEVSKAQARHDDIS---- 901
Cdd:TIGR01612 1120 IKNLDQKIDHHIKALEEIkkkseNYIDEIKAQ-INDLEDVADKAISN-DDPEEIEKKIENIVTKIDKKKNIYDEIKklln 1197
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 902 --TRGEQRERELqQEVSGLNDS---------LHQLDLASEDITNYIErggpaQLERSKRELQNI---SDEIKRLEAEQTD 967
Cdd:TIGR01612 1198 eiAEIEKDKTSL-EEVKGINLSygknlgklfLEKIDEEKKKSEHMIK-----AMEAYIEDLDEIkekSPEIENEMGIEMD 1271
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 315056489 968 LTRELNSIS---TRLKDSESTKRQYSDNLR-YRQESKALISVNQEIADL 1012
Cdd:TIGR01612 1272 IKAEMETFNishDDDKDHHIISKKHDENISdIREKSLKIIEDFSEESDI 1320
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-373 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 180 DEIFEALKytKAIDNIKALR--KKQNEELAKYKIMENHARDDKDKAD--RAEKRSLKLQEEIEALRAESHELSKEMRRVA 255
Cdd:COG4913 238 ERAHEALE--DAREQIELLEpiRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 256 ELADKAWKESESYAEILGALEGKRIEakSIQTSINNLRQHLVEVEES----DEWLQS-------TLEQFESRQAEYRSQE 324
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLE--QLEREIERLERELEERERRrarlEALLAAlglplpaSAEEFAALRAEAAALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 315056489 325 DTLKEkymdLKELIEQNRHKLGLKQTECGKNENDKAQFDRQVERRVRLI 373
Cdd:COG4913 394 EALEE----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
664-1061 |
1.53e-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: 42.90 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 664 ESELQIFKNKLKALIKK-ATDEDAVAEIEAR--------EAELENVR-EVGTFYETWNRLTNTDIPALKKEQSDLETERe 733
Cdd:pfam12128 275 ASRQEERQETSAELNQLlRTLDDQWKEKRDElngelsaaDAAVAKDRsELEALEDQHGAFLDADIETAAADQEQLPSWQ- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 734 vvlTKLEDHDKIVAQRVESKRDIESlskniativRYNNEISTLQTQ-IQELSAKQEETGTSRTLEDIQDEIAtlgekSRQ 812
Cdd:pfam12128 354 ---SELENLEERLKALTGKHQDVTA---------KYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVA-----EDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 813 LKRASSKLTHELNQS--RVDVGKLELKLRdlrrdLDNVNFQLEKKATLVSRVEDYRNQNL---KQREAIEKADNDIESLV 887
Cdd:pfam12128 417 LQALESELREQLEAGklEFNEEEYRLKSR-----LGELKLRLNQATATPELLLQLENFDErieRAREEQEAANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 888 PEVSKAQARHDDISTRGEQRERELQQEVSGLNDSLHQLDLASEDITNYIERGGPAQLER----SKRELQNISDEIKRLEA 963
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSigkvISPELLHRTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 964 EQTDLTRELNSISTRLKDSESTK-RQYSDNLRYR--QESKALISVNQEIADLESQ----NAEVDRSRFKEESERNTREHN 1036
Cdd:pfam12128 572 GSVGGELNLYGVKLDLKRIDVPEwAASEEELRERldKAEEALQSAREKQAAAEEQlvqaNGELEKASREETFARTALKNA 651
|
410 420
....*....|....*....|....*
gi 315056489 1037 ALAAKQASkmGEMKSKDDQLMQLLA 1061
Cdd:pfam12128 652 RLDLRRLF--DEKQSEKDKKNKALA 674
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
783-1049 |
1.57e-03 |
|
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: 42.44 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 783 LSAKQEETGTSRTLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLekkatlvsrv 862
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 863 edyrNQNLKQREAIEKADNDIESLVPEVSKAQARHddistrGEQREREL---QQEVSGLNDSLHQLDLASEDITNYIErg 939
Cdd:COG4942 86 ----AELEKEIAELRAELEAQKEELAELLRALYRL------GRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAE-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 940 gpaQLERSKRELQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQESKAlisvnQEIADLESQNAEV 1019
Cdd:COG4942 154 ---ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-----AELAELQQEAEEL 225
|
250 260 270
....*....|....*....|....*....|
gi 315056489 1020 DRSRFKEESERNTREHNALAAKQASKMGEM 1049
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
26-50 |
1.60e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 41.67 E-value: 1.60e-03
10 20
....*....|....*....|....*
gi 315056489 26 ETIQFHTPLTLIVGYNGSGKTTIIE 50
Cdd:COG3910 31 EGLEFHPPVTFFVGENGSGKSTLLE 55
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1180-1248 |
1.64e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.52 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1180 RLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHEIIrtrQQQAnfqLIVITHDEEFLRSM------------QCGD 1247
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS---RRQT---TLMVTHQLEDLAQWdqiwvmqdgqivQQGD 566
|
.
gi 315056489 1248 F 1248
Cdd:PRK11174 567 Y 567
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
716-1034 |
2.12e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 716 TDIPALKKeQSDLETEREVVLTKLEDHDKIVAQRVESKRDIESLSKNIA----TIVRYNNEISTLQTQIQELSAKQEETG 791
Cdd:PRK11281 43 AQLDALNK-QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAqapaKLRQAQAELEALKDDNDEETRETLSTL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 792 TSRTLEdiqdeiatlgeksrqlkrasSKLTHELNQsrvdvgklelkLRDLRRDLDNVNFQLEKKATLVSRVEDYRNQNLK 871
Cdd:PRK11281 122 SLRQLE--------------------SRLAQTLDQ-----------LQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 872 QREAIEKADNDI----ESLVPE-VSKAQARHDDISTRGEQRERELQQevsglNDSLHQLDLASEDITNyierggpAQLER 946
Cdd:PRK11281 171 RLQQIRNLLKGGkvggKALRPSqRVLLQAEQALLNAQNDLQRKSLEG-----NTQLQDLLQKQRDYLT-------ARIQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 947 SKRELQNISDEI--KRLEAEQTDLTRELNS-ISTRLKDSESTKRQYSDNlryRQESKALISVNQEIADLESQNAEV---- 1019
Cdd:PRK11281 239 LEHQLQLLQEAInsKRLTLSEKTVQEAQSQdEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVknwl 315
|
330
....*....|....*
gi 315056489 1020 DRSrfkEESERNTRE 1034
Cdd:PRK11281 316 DRL---TQSERNIKE 327
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
12-58 |
2.33e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 41.51 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 315056489 12 LSILGVRSFDNTRSETIQFHTPLTLIVGYNGSGKTTIIECLKYATTG 58
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATG 47
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
808-1040 |
2.35e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 808 EKSRQLKRASSkLTHELNQSRVDVGKLELKLRDLRRDLDNVNFQLEKKATLVSRVEDYRN--QN-LKQREAIEKADNDIE 884
Cdd:PRK04863 280 ERRVHLEEALE-LRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvQTaLRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 885 SLVP---EVSKAQARHDDISTRGEQRERELQQEV----SGLNDSLHQLDLASEDITNYieRGGPAQLERSKR-------E 950
Cdd:PRK04863 359 ELEErleEQNEVVEEADEQQEENEARAEAAEEEVdelkSQLADYQQALDVQQTRAIQY--QQAVQALERAKQlcglpdlT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 951 LQNISDEIKRLEAEQTDLTRELNSISTRLKDSESTKRQYsdnlryrqeSKALISVnQEIADlesqnaEVDRSRFKE---E 1027
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF---------EQAYQLV-RKIAG------EVSRSEAWDvarE 500
|
250
....*....|...
gi 315056489 1028 SERNTREHNALAA 1040
Cdd:PRK04863 501 LLRRLREQRHLAE 513
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1179-1242 |
2.61e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315056489 1179 IRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHeiirtrqqQANFQLIVITHDEEFLRS 1242
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN--------ERNSTMIIISHDRHFLNS 217
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
732-997 |
2.82e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 732 REVVLTKLE-----DHDKIVAQRV-ESKRDIESLSKNIATIvryNNEISTLQTQIQELSAKQEETgtsrtLEDIQDEIAT 805
Cdd:PHA02562 153 RKLVEDLLDisvlsEMDKLNKDKIrELNQQIQTLDMKIDHI---QQQIKTYNKNIEEQRKKNGEN-----IARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 806 LGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLdnvnFQLEKKATLVSRVEDYRNQN-----LKQreAIEKAD 880
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA----AKIKSKIEQFQKVIKMYEKGgvcptCTQ--QISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 881 NDIESLVPEVSKAQARHDDISTRgeqrerelQQEVSGLNDSLHQLDLASEDITNYIERGGpAQLERSKRELQNISDEIKR 960
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTA--------IDELEEIMDEFNEQSKKLLELKNKISTNK-QSLITLVDKAKKVKAAIEE 369
|
250 260 270
....*....|....*....|....*....|....*..
gi 315056489 961 LEAEQTDLTRELNSISTRLKDSESTKRQYSDNLRYRQ 997
Cdd:PHA02562 370 LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1180-1253 |
2.84e-03 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain] Cd Length: 235 Bit Score: 40.95 E-value: 2.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315056489 1180 RLALAECFGVNCGLIALDEPTTNLDrdNIRSLAesLHEIIRTRQQQANFQLIVITHDEEFLRSMqcgdfCDYYY 1253
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLD--PIASGV--IDDLIRSLKKELGLTSIMVTHDLDTAFAI-----ADRIA 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
662-815 |
2.95e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 662 KTESELQIFKNK---------LKALIKKATD-EDAVAEIEAREAELENVRE------VGTFYETWNRLTNTDIPALKKEQ 725
Cdd:COG3206 193 EAEAALEEFRQKnglvdlseeAKLLLQQLSElESQLAEARAELAEAEARLAalraqlGSGPDALPELLQSPVIQQLRAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 726 SDLETEREVVLTKL-EDHDKIVAQRveskRDIESLSKNIATIVRynNEISTLQTQIQELSAKQEEtgTSRTLEDIQDEIA 804
Cdd:COG3206 273 AELEAELAELSARYtPNHPDVIALR----AQIAALRAQLQQEAQ--RILASLEAELEALQAREAS--LQAQLAQLEARLA 344
|
170
....*....|.
gi 315056489 805 TLGEKSRQLKR 815
Cdd:COG3206 345 ELPELEAELRR 355
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1168-1244 |
3.14e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.71 E-value: 3.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315056489 1168 SAGQKVLAsiiiRLALAECFGVNcgLIALDEPTTNLDRDNIRSLAESLHEIIRtrqqQANFQLIVITHDEEFLRSMQ 1244
Cdd:COG2401 138 STGQKFRF----RLALLLAERPK--LLVIDEFCSHLDRQTAKRVARNLQKLAR----RAGITLVVATHHYDVIDDLQ 204
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
837-1053 |
3.14e-03 |
|
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: 41.29 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 837 KLRDLRRDLDNVNFQLEKKATLVSRVEDYRNQNLKQREAIEKADNDIESLVPEVSKAQARHDDISTRGEQRERELQQEVS 916
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 917 GLNDSLHQLDLASEDITNY------IERGGPAQLERS-----------KRELQNISDEIKRLEAEQTDLTRELNSISTRL 979
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRlqylkylaparREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315056489 980 KDSESTKRQYSDNLRYRQesKALISVNQEIADLESQNAEvdrsrFKEESERNTREHNALAAKQASKMGEMKSKD 1053
Cdd:COG4942 181 AELEEERAALEALKAERQ--KLLARLEKELAELAAELAE-----LQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1168-1243 |
3.50e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.59 E-value: 3.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLheiirtrqqqANFQ--LIVITHDEEFLRSM 1243
Cdd:COG0488 154 SGGWRR------RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----------KNYPgtVLVVSHDRYFLDRV 215
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
8-53 |
3.52e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 3.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 315056489 8 KIDKLSILGVRSFdntRSETIQFHtPLTLIVGYNGSGKTTIIECLK 53
Cdd:COG4637 1 MITRIRIKNFKSL---RDLELPLG-PLTVLIGANGSGKSNLLDALR 42
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1192-1269 |
3.68e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 3.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315056489 1192 GLIALDEPTTNLDRDNIRSLAESLHEIIRTRQqqanfqLIVITHDEEFLRSMQCGDFcdyyYRVSRNERQKSIIERQS 1269
Cdd:COG4637 280 PLLCIEEPENGLHPDLLPALAELLREASERTQ------VIVTTHSPALLDALEPEEV----LVLEREDDGETRIRRLS 347
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
721-889 |
4.50e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 721 LKKEQSDLETEREVVLTKLEdhdkivaqrvESKRDIESLSKNIAtivRYNNEISTLQTQIQELSAKQEETGTSRTLEDIQ 800
Cdd:COG1579 29 LPAELAELEDELAALEARLE----------AAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 801 DEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLELKLRDLRRDLDnvnfqlEKKATLVSRVEDYRnqnlKQREAIEKAD 880
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE------EKKAELDEELAELE----AELEELEAER 165
|
....*....
gi 315056489 881 NDIESLVPE 889
Cdd:COG1579 166 EELAAKIPP 174
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1193-1244 |
5.18e-03 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 40.04 E-value: 5.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 315056489 1193 LIAlDEPTTNLDRDNIRSLAESLHEIIR---TrqqqanfqLIVITHDEEFLRSMQ 1244
Cdd:COG2884 159 LLA-DEPTGNLDPETSWEIMELLEEINRrgtT--------VLIATHDLELVDRMP 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1168-1235 |
5.86e-03 |
|
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: 38.90 E-value: 5.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAESLHEIIRTRqqqanfQLIVITH 1235
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK------TVIVIAH 153
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1168-1235 |
6.16e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 39.47 E-value: 6.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAeslhEIIRTRQQQANfqlIVI--TH 1235
Cdd:PRK13539 129 SAGQKR------RVALARLLVSNRPIWILDEPTAALDAAAVALFA----ELIRAHLAQGG---IVIaaTH 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1168-1236 |
7.27e-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: 40.66 E-value: 7.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 1168 SAGQKVLASIIIRLALaecfgvNCGLIALDEPTTNLDrdnIRSLAESLhEIIRTRQQQANFQLIVITHD 1236
Cdd:COG1123 144 SGGQRQRVAIAMALAL------DPDLLIADEPTTALD---VTTQAEIL-DLLRELQRERGTTVLLITHD 202
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
8-112 |
7.45e-03 |
|
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: 39.17 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 8 KIDKLSILGVRSFDNTrsETIQF----HTPLTLIVGYNGSGKTTIIECLKYATTGDLPPNSKGGAfIHDPKLCGEKEvfA 83
Cdd:cd03279 2 KPLKLELKNFGPFREE--QVIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQEN-LRSVFAPGEDT--A 76
|
90 100
....*....|....*....|....*....
gi 315056489 84 QVKLAFKAtSAAKMVVTRSLQLTVKKLTR 112
Cdd:cd03279 77 EVSFTFQL-GGKKYRVERSRGLDYDQFTR 104
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1180-1238 |
7.51e-03 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 39.34 E-value: 7.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 1180 RLALAECFGVNCGLIALDEPTTNLDRDNirslAESLHEIIRTRQQQANFQLIVITHDEE 1238
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAAT----GEQIIDLLFELNRERGTTLVLVTHDPA 208
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
757-865 |
7.90e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 40.13 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 757 ESLSKNIATIVRYNNEISTLQTQIQELSAKqeetgtsrtLEDIQDEIATLGEKSRQLKRASSKLTHELNQSRVDVGKLEL 836
Cdd:pfam10186 36 DSLKKKVEEALEGKEEGEQLEDNIGNKKLK---------LRLLKSEVAISNERLNEIKDKLDQLRREIAEKKKKIEKLRS 106
|
90 100 110
....*....|....*....|....*....|
gi 315056489 837 KLRDLRRDLDNVNFQLEKK-ATLVSRVEDY 865
Cdd:pfam10186 107 SLKQRRSDLESASYQLEERrASQLAKLQNS 136
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
407-606 |
7.93e-03 |
|
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: 40.13 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 407 ERSQALEKAKQEAQSQLKDAQSLLNQLSQRKSALQEAKNAAKKQISVNDKESDTIQRSINEMDVDEGKRAAIESRMEETE 486
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 487 KILEKEKEKAKNASWETDIQQNDSELRSLED-----KSSKLNAELIQGTKK-----AGDLARLDHLKKELKDRDDVLKEA 556
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDfldavRRLQYLKYLAPARREqaeelRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 315056489 557 STLVTTAERERDGTGKELELIDFKLKNARKSLHQHGADVENAAKKINDVI 606
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1168-1236 |
7.95e-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: 39.44 E-value: 7.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315056489 1168 SAGQKVlasiiiRLALAECFGVNCGLIALDEPTTNLDRDNIRSLAeslhEIIRtRQQQANFQLIVITHD 1236
Cdd:cd03235 134 SGGQQQ------RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIY----ELLR-ELRREGMTILVVTHD 191
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-564 |
8.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 175 LKKKFDEIF--EALKYTKAIDNIKALRKKQNEelakykimenhARDDKDKADRAEKRSLKLQEEIEALRAESHELSKEMR 252
Cdd:COG4717 51 LEKEADELFkpQGRKPELNLKELKELEEELKE-----------AEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 253 RVAELAD--KAWKESE-------SYAEILGALEGKRIEAKSIQTSINNLRQHLVEVEES-DEWLQSTLEQFESRQAEYRS 322
Cdd:COG4717 120 KLEKLLQllPLYQELEaleaelaELPERLEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 323 QEDTLKEKYMDLKELIEQNRHKLGLKQTECGKNENDK--AQFDRQVERRVRLIKDIARQNNFRGYDG------------- 387
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 388 -----------------------------------DLDEMEINDFMDRI---QKLTKERSQALEKAKQEAQSQLKDAQSL 429
Cdd:COG4717 280 flvlgllallflllarekaslgkeaeelqalpaleELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 430 LNQLsQRKSALQEAKNAAKKQISVNDKESDTIQRSINEMDVDEGKRAAIESRMEETEKILEKEKEKAKNASWETDIQQND 509
Cdd:COG4717 360 EEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315056489 510 SELRSLEDKSSKLNAEL------IQGTKKAGDLARLDHLKKELKDR-DDVLKEASTLVTTAE 564
Cdd:COG4717 439 EELEELEEELEELREELaeleaeLEQLEEDGELAELLQELEELKAElRELAEEWAALKLALE 500
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
909-1030 |
9.82e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315056489 909 RELQQEVSGLNDSLHQL--DLASEDI--------TNYIERGGPAQLERSK-RElqnISDEIKRLEAEQTDLTRELNSIST 977
Cdd:PRK10929 82 AELRQQLNNERDEPRSVppNMSTDALeqeilqvsSQLLEKSRQAQQEQDRaRE---ISDSLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315056489 978 RLK--DSESTKRQYSDNLRYRQESKALIS-VNQ-EIADLESQN-AEVDRSR---FKEESER 1030
Cdd:PRK10929 159 RLQtlGTPNTPLAQAQLTALQAESAALKAlVDElELAQLSANNrQELARLRselAKKRSQQ 219
|
|
| |
