|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-1295 |
4.94e-144 |
|
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: 471.84 E-value: 4.94e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 2 SSIESLSIQGIRSFGTYADDLQSIKFSSPVTLILGENGCGKTTVVECLKYALTGECPPGSdRGKSFVHDPKIFGLNEVLA 81
Cdd:TIGR00606 1 AKFLKMSILGVRSFGIEDKDKQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGT-KGNTFVHDPKVAQETDVRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 82 QIKMQVRDRRGAQVSICRTMKVSKKRNKMSFETMDSTINfltgagQSKREKQDSLSGRSVDIDVAISDFMGVSKAIINNV 161
Cdd:TIGR00606 80 QIRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVIT------RYKHGEKVSLSSKCAEIDREMISHLGVSKAVLNNV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 162 LFCHQEDSSWPLDESKKLKEKFDAIFGITEYNKALDKIIKLRKEAMEELKIKEANIKHVAYLKQEMEVKTLNLQKAQRKC 241
Cdd:TIGR00606 154 IFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 242 DAIKAQCSECEEEMKPIEARLVEIRNVEFEIGKYQAQKVEMDTKHKNCKDQISTLTLKIKKPFRGTLDELDQEISNFDQR 321
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 322 MLEMRQKRTEVEGDLSQIKRSSvaeqeKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCR-ELHIPIDCDLVEQPEKM 400
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKER-----RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIqSLATRLELDGFERGPFS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 401 GEVLRDIEAMIITKHCEITEIVEQN----EKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIET 476
Cdd:TIGR00606 389 ERQIKNFHTLVIERQEDEAKTAAQLcadlQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 477 SMQDLKKLEKEINEVNELYESATKNIDQQAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAECSLKQKELDKKN 556
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 557 QEVHRVRSRHSDHFGKLFKEpitCNYRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSE 636
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLGY---FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 637 ELIYQKCRSTPYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEPS--CPLCHHNM-TSDEACDLTSELTDEIQ 713
Cdd:TIGR00606 626 DKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQscCPVCQRVFqTEAELQEFISDLQSKLR 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 714 KLPDNITRAEKALKAEQIKYENLLQLKPTI-----LKVKELKDsLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNM 788
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRqsiidLKEKEIPE-LRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 789 ELANSMMGDMSLLDEALKDSARLTKdldlQKGQLPASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALN 868
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIA----QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 869 RLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERL--KKSESEKLAQ 946
Cdd:TIGR00606 861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELisSKETSNKKAQ 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 947 -----LNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKLDEIIMASKDKLRKLATEISLKTDELETiktecsnQQTV 1021
Cdd:TIGR00606 941 dkvndIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT-------QKIQ 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1022 ERDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDFHSVSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDE 1101
Cdd:TIGR00606 1014 ERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1102 PRFKESLKNFRKANYEIEVTRLCIEDLGQYRLALEWALIQFHSEKMEMINRLIREYWRKIYRGNDIDYIQVKTDEVSSDA 1181
Cdd:TIGR00606 1094 PQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVS 1173
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1182 SADRRKTYNYRVVQSKNYSEIEMRGRCSAGQRVLASLIIRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVE 1261
Cdd:TIGR00606 1174 ASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIK 1253
|
1290 1300 1310
....*....|....*....|....*....|....
gi 386768435 1262 ERQSQSNFMLIIITHDENFVSSLGKITSYHRVFR 1295
Cdd:TIGR00606 1254 SRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYR 1287
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1203-1302 |
1.06e-35 |
|
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: 135.04 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1203 EMRGRCSAGQRVLASLIIRLALAETFSSNCGVLALDEPTTNLDRANI-NSLCEalncIVEERQSQSNFMLIIITHDENFV 1281
Cdd:cd03240 111 DMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIeESLAE----IIEERKSQKNFQLIVITHDEELV 186
|
90 100
....*....|....*....|.
gi 386768435 1282 SSLGKitsYHRVFRNEECKSV 1302
Cdd:cd03240 187 DAADH---IYRVEKDGRQKSR 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-173 |
5.32e-27 |
|
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: 110.00 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 4 IESLSIQGIRSFgtyaDDLQSIKFSSPVTLILGENGCGKTTVVECLKYALTGECPPGSDRGksfVHDPKIFGLNEVLAQI 83
Cdd:cd03240 1 IDKLSIRNIRSF----HERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGG---AHDPKLIREGEVRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 84 KMQVRDRRGAQVSICRTMkvskkrnkmsfetmdstinfltgagqskrekqdslsgrsvdidvaisdfmgvskAIINNVLF 163
Cdd:cd03240 74 KLAFENANGKKYTITRSL------------------------------------------------------AILENVIF 99
|
170
....*....|
gi 386768435 164 CHQEDSSWPL 173
Cdd:cd03240 100 CHQGESNWPL 109
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-226 |
2.07e-21 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 93.33 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 7 LSIQGIRSFGTyaddlQSIKFSSPVTLILGENGCGKTTVVECLKYALTGECPPGSDRGK--SFVHDPKIFGLNEVLAQIK 84
Cdd:pfam13476 1 LTIENFRSFRD-----QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGggFVKGDIRIGLEGKGKAYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 85 MQVRDRRGA-QVSICRTMKVSKKRNKMSfetmdstinfltgagqskreKQDSLSGRSVDIDVAISDFMGVSKAIINNVLF 163
Cdd:pfam13476 76 ITFENNDGRyTYAIERSRELSKKKGKTK--------------------KKEILEILEIDELQQFISELLKSDKIILPLLV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768435 164 CHQEDSSWPLDESKKLKEkfdaifgITEYNKALDKIIKLRKEAMEELKIKEaNIKHVAYLKQE 226
Cdd:pfam13476 136 FLGQEREEEFERKEKKER-------LEELEKALEEKEDEKKLLEKLLQLKE-KKKELEELKEE 190
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
418-1157 |
1.16e-13 |
|
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: 76.26 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 418 ITEIVEQNEKADRSRQVKI--DELRIELTKSEQ-----SVTAQEKQRESSKRESETLGVEIKKIETSMQDlkkLEKEINE 490
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAEryQALLKEKREYEGyellkEKEALERQKEAIERQLASLEEELEKLTEEISE---LEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 491 VNELYESATKNID------QQAIKD-------AIARKKASIAENQIQFKKLDEQLtflgsmAKLVAECSLKQKELDKKNQ 557
Cdd:TIGR02169 270 IEQLLEELNKKIKdlgeeeQLRVKEkigeleaEIASLERSIAEKERELEDAEERL------AKLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 558 EVHRVRSRhsdhfgklfKEPITCNYrRSMQVVYEKLRREIQELNEKANT------------QKLKEQSYEIKR------- 618
Cdd:TIGR02169 344 EIEEERKR---------RDKLTEEY-AELKEELEDLRAELEEVDKEFAEtrdelkdyreklEKLKREINELKReldrlqe 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 619 --KNLISDISRMEKELKDSEELIYQ-KCRSTPYDDLLERSKTTISKLQFD-------HGALKSSEALYKKYIQKMDEEPS 688
Cdd:TIGR02169 414 elQRLSEELADLNAAIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADlskyeqeLYDLKEEYDRVEKELSKLQRELA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 689 CPLCHHNMTSDEACD---LTSELTDEIQKL-------------------------PDNITRAEKALKAEQIKYENLLQLK 740
Cdd:TIGR02169 494 EAEAQARASEERVRGgraVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrLNNVVVEDDAVAKEAIELLKRRKAG 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 741 P-TILKVKELKDslPQKKEELKKVEELLGDSVS------EYETLIALIGEPT---HNMELANSMMGD---MSLLDEALKD 807
Cdd:TIGR02169 574 RaTFLPLNKMRD--ERRDLSILSEDGVIGFAVDlvefdpKYEPAFKYVFGDTlvvEDIEAARRLMGKyrmVTLEGELFEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 808 SARLTKDLDLQKGQLPASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQqmdALNRLREKKNSLKDRQIHLREG 887
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE---LSQELSDASRKIGEIEKEIEQL 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 888 LQSLPQLKERLEKLNSFLTTVASEISELKAKIQplklNLRAAIEEKERLKKSESEKLAQLNSKYNsykstDHDIQRLNKE 967
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEEALNDLEARLS-----HSRIPEIQAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 968 AEdyaklDLRNEIKKLDEIIMASKDKLRKLATEISLKTDELETIKTE--------CSNQQTVERDLKDNRELK-QLEDKE 1038
Cdd:TIGR02169 800 LS-----KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkeqiKSIEKEIENLNGKKEELEeELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1039 AKLREscqvLDKQLGNLdfhsvSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKL--QREIDEPRFKESLKNFRKANY 1116
Cdd:TIGR02169 875 AALRD----LESRLGDL-----KKERDELEAQLRELERKIEELEAQIEKKRKRLSELkaKLEALEEELSEIEDPKGEDEE 945
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 386768435 1117 EIEVTrLCIEDLGQYRLALEWALiqfhsEKMEMIN-RLIREY 1157
Cdd:TIGR02169 946 IPEEE-LSLEDVQAELQRVEEEI-----RALEPVNmLAIQEY 981
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
474-1121 |
3.94e-13 |
|
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: 74.38 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 474 IETSMQDLKKLEKEINEVNELYES------------ATKNIDQQAIKDAIARKKASiaENQIQfKKLDEQLTflGSMAKL 541
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKqkfylrqsvidlQTKLQEMQMERDAMADIRRR--ESQSQ-EDLRNQLQ--NTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 542 VAECSLKQKELDKKNQEVHRVRSRHSDHFGKLFKepitcnyRRSMQVVYeklrreiqelnEKANTQKLKEQS--YEIKRK 619
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQE-------IRSILVDF-----------EEASGKKIYEHDsmSTMHFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 620 NLISDISRMEKELkdSEELIYQKCRSTPYDDLLERSKTTisklqfdhgALKSSEALYKKYIQKMDEepscplchhnMTSD 699
Cdd:pfam15921 217 SLGSAISKILREL--DTEISYLKGRIFPVEDQLEALKSE---------SQNKIELLLQQHQDRIEQ----------LISE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 700 EACDLTSeLTDEIQ--KLPDNITRAEKALKAEQIKYENLLQLKptilKVKELKDSLPQKKEELKKVEELLGDSVSEYETL 777
Cdd:pfam15921 276 HEVEITG-LTEKASsaRSQANSIQSQLEIIQEQARNQNSMYMR----QLSDLESTVSQLRSELREAKRMYEDKIEELEKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 778 IALI-GEPTHNMELANSMMGDMSLLDEALK----DSARLTKDLDLQKGQLPASYD----SSVSMDDLQAEKSKVSKELET 848
Cdd:pfam15921 351 LVLAnSELTEARTERDQFSQESGNLDDQLQkllaDLHKREKELSLEKEQNKRLWDrdtgNSITIDHLRRELDDRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 849 ERKELESAQNAVQQQMDALNRLREKKNslkdrqihlrEGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKL---N 925
Cdd:pfam15921 431 LEALLKAMKSECQGQMERQMAAIQGKN----------ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsD 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 926 LRAAIEEKERLKKSESEKLAQLNSKYNSYKstdHDIQRLNKEAEDYAKLDLRNEIKKLDeiiMASKDKL-----RKLATE 1000
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLRSRVDLKL---QELQHLKNEGDHLRNVQTECEALKLQ---MAEKDKVieilrQQIENM 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1001 ISLKTDELETIKTECSNQQTVERDLKDNR----ELKQLED-KEAKLREscqvLDKQLGNLDFHSVskEKVNLTKQRDKAT 1075
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKEINDRRlelqEFKILKDkKDAKIRE----LEARVSDLELEKV--KLVNAGSERLRAV 648
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 386768435 1076 ----VRKGELLGQLGEIHSQVNKLQREIDEPRfkeslKNFRKANYEIEVT 1121
Cdd:pfam15921 649 kdikQERDQLLNEVKTSRNELNSLSEDYEVLK-----RNFRNKSEEMETT 693
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1101 |
1.71e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 846 LETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLRegLQSLPQLKERLEKLNSFLTTVASEISELKAKIQplklN 925
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAELQ----E 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 926 LRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRlNKEAEDYAKLDLRNEIKKLDEIIM---ASKDKLRKLATEIS 1002
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-QKQILRERLANLERQLEELEAQLEeleSKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1003 LKTDELETIKTECSNQQTVERDLKDNRELK---------QLEDKEAKLRESCQVLDKQLGNLDfhsvsKEKVNLTKQRDK 1073
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRleeleeqleTLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRER 418
|
250 260
....*....|....*....|....*...
gi 386768435 1074 ATVRKGELLGQLGEihSQVNKLQREIDE 1101
Cdd:TIGR02168 419 LQQEIEELLKKLEE--AELKELQAELEE 444
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
398-996 |
1.78e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 398 EKMGEVLRDIEAMI------ITKHCEITEIVEQNEKADRSRQVKIDELRIELTKSEQsvtaqekqresskresetlgvEI 471
Cdd:PRK03918 165 KNLGEVIKEIKRRIerlekfIKRTENIEELIKEKEKELEEVLREINEISSELPELRE---------------------EL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 472 KKIETSMQDLKKLEKEINEVNELYESATKNIdqQAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAECSLKQKE 551
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSK--RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 552 LDKKNQEVHRVRSRHSDHFGKLFKEPITCNYRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEiKRKNLISDISRMEKE 631
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 632 LKDSE-ELIYQKCrstpydDLLERSKTT----ISKLQFDHGALKSSEALYKKYIQKMDE-EPSCPLCHHNMTSDEACDLT 705
Cdd:PRK03918 381 LTGLTpEKLEKEL------EELEKAKEEieeeISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 706 SELTDEIQKLPDNITRAEKA---LKAEQIKYENLLQLKPTILKVKELKDSLPQKKEELKKVEELLGDSVS-EYETLiali 781
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKerkLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAeEYEKL---- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 782 gepthnMELANSMMGDMSLLDEALKDSARLTKDLDLQKGQL-PASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAV 860
Cdd:PRK03918 531 ------KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLdELEEELAELLKELEELGFESVEELEERLKELEPFYNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 861 QQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNsflttvaSEISELKAKIQPLKL-NLRAAIEEKERLKKS 939
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR-------KELEELEKKYSEEEYeELREEYLELSRELAG 677
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 386768435 940 ESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKldlrnEIKKLdEIIMASKDKLRK 996
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEEREKAKK-----ELEKL-EKALERVEELRE 728
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
801-1052 |
3.38e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 801 LDEALKDSARLTKDLDLQKGQLPASydsSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDR 880
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 881 QIHLREGLQslpQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHD 960
Cdd:COG1196 311 RRELEERLE---ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 961 IQRLNKEAEDYAKL---DLRNEIKKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDK 1037
Cdd:COG1196 388 LLEALRAAAELAAQleeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250
....*....|....*
gi 386768435 1038 EAKLRESCQVLDKQL 1052
Cdd:COG1196 468 LLEEAALLEAALAEL 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
424-1106 |
1.06e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 424 QNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQ----DLKKLEKEINEVNELYESAT 499
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQeleeKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 500 K-----NIDQQAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMA-KLVAECSLKQKELDKKNQEVHRVRSRHSDHFGKL 573
Cdd:TIGR02168 288 KelyalANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 574 FKEPitcNYRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIK-------RKNLISDISRMEKELKDSEeliyQKCRST 646
Cdd:TIGR02168 368 EELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerledrRERLQQEIEELLKKLEEAE----LKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 647 PYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEepscplchhnmTSDEACDLTSELT--DEIQKLPDNITRAEK 724
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDA-----------AERELAQLQARLDslERLQENLEGFSEGVK 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 725 ALKAEQIKYENLLQLKPTILKVKE-----------------LKDSLPQKKEELKKVEELLGDSVSEYE-TLIALIGEPTH 786
Cdd:TIGR02168 510 ALLKNQSGLSGILGVLSELISVDEgyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPlDSIKGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 787 NMELANSMMGDMSLLDEALKDSARLTKDLDL----------------QKGQLPASYD-----------------SSVSMD 833
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnaleLAKKLRPGYRivtldgdlvrpggvitgGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 834 DLQAEKSKVSKELETERKELESAQNAVQQQMDAL-NRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEI 912
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 913 SELKAKIQPL---KLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKStdhdiqrlNKEAEDYAKLDLRNEIKKLDEIIMA 989
Cdd:TIGR02168 750 AQLSKELTELeaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 990 SKDKLRKLATEISLKTDELETIKTECSNQQtvERDLKDNRELKQLEDKEAKLRESCQVLDKQLG--NLDFHSVSKEKVNL 1067
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELS--EDIESLAAEIEELEELIEELESELEALLNERAslEEALALLRSELEEL 899
|
730 740 750
....*....|....*....|....*....|....*....
gi 386768435 1068 TKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRFKE 1106
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1199-1287 |
1.27e-09 |
|
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: 58.53 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1199 YSEIE---MRGRCSAGQRVLASLIIRLALAETfsSNCGVLALDEPTTNLDRANINSLCEALnciveERQSQSNFMLIIIT 1275
Cdd:cd03227 66 AVSAElifTRLQLSGGEKELSALALILALASL--KPRPLYILDEIDRGLDPRDGQALAEAI-----LEHLVKGAQVIVIT 138
|
90
....*....|..
gi 386768435 1276 HDENFVSSLGKI 1287
Cdd:cd03227 139 HLPELAELADKL 150
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-72 |
1.32e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 59.25 E-value: 1.32e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768435 4 IESLSIQGIRSFGtyadDLQSIKFSSPVTLILGENGCGKTTVVECLKYALTGECPPGSDRGKSFVHDPK 72
Cdd:COG0419 2 LLRLRLENFRSYR----DTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGS 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
833-1119 |
1.38e-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: 59.70 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 833 DDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKN--------SLKDRQIHLREGLQSLPQLKERLEKLNSF 904
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqalLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 905 LTTVASEISELKAKIQPLKLNLRAAI----EEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKlDLRNEI 980
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEqlleELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE-DAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 981 KKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLkdnreLKQLEDKEAKLRESCQVLDKQLGNLDfhSV 1060
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL-----RAELEEVDKEFAETRDELKDYREKLE--KL 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 386768435 1061 SKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEprFKESLKNFRKANYEIE 1119
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--LEEEKEDKALEIKKQE 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-626 |
4.36e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 365 QSELACRAQLLKRVKEFCRELHIPIDC--DLVEQPEKMGEVLRDIEAMIITKHCEITEIVEQNEKADRSRQVKIDELRIE 442
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAElrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 443 LTKSEQSVTAQEKQRESSKRESETLGVEIKK----IETSMQDLKKLEKEINEVNELY-----ESATKNIDQQAIKDAIAR 513
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEEleaqIEQLKEELKALREALDELRAELtllneEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 514 KKASIAENQIQFKKLDEQLTFL-GSMAKLVAECSLKQKELDKKNQEVHRV---RSRHSDHFGKLFKEpitcnyRRSMQVV 589
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLaAEIEELEELIEELESELEALLNERASLeeaLALLRSELEELSEE------LRELESK 909
|
250 260 270
....*....|....*....|....*....|....*..
gi 386768435 590 YEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDIS 626
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1209-1284 |
5.69e-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: 5.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNciveerqsQSNFMLIIITHDENFVSSL 1284
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK--------EYPGTVILVSHDRYFLDQV 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
801-1113 |
7.37e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 801 LDEALKDSARLTKDLDLQKGQLPASYDSSVSMDDLQAEKSKVSKELETERKELESAqnaVQQQMDALNRLREKKNSLKDR 880
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 881 QIHLREGLQslpQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHD 960
Cdd:TIGR02168 812 LTLLNEEAA---NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 961 IQRLNKEAEDYAK--LDLRNEIKKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRELKqLEDKE 1038
Cdd:TIGR02168 889 LALLRSELEELSEelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK-IEDDE 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1039 AKLRESCQVLDKQLGNL---------DFHSVSKEKVNLTKQRDKATvrkgELLGQLGEIHSQVNKLQREidepRFKESLK 1109
Cdd:TIGR02168 968 EEARRRLKRLENKIKELgpvnlaaieEYEELKERYDFLTAQKEDLT----EAKETLEEAIEEIDREARE----RFKDTFD 1039
|
....
gi 386768435 1110 NFRK 1113
Cdd:TIGR02168 1040 QVNE 1043
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1206-1288 |
9.86e-08 |
|
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: 54.02 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1206 GRCSAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALnciveERQSQSNFMLIIITHDENFVSSLG 1285
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI-----AAHLARGGAVLLTTHQPLELAAAR 198
|
...
gi 386768435 1286 KIT 1288
Cdd:COG4133 199 VLD 201
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-1014 |
1.16e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 4 IESLSIQGIRSFGTYAddlqSIKFSSPVTLILGENGCGKTTVVECLKYALTGECPPG--SDRGKSFVHDPK-IFGLNEVL 80
Cdd:TIGR02169 2 IERIELENFKSFGKKK----VIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAmrAERLSDLISNGKnGQSGNEAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 81 AQIKMQVRDRRGA-QVSICRTMKVSKKRNKMSFetmdstinFLTGAGQSKREKQDSLS-------GRSVDIDVAISDFMG 152
Cdd:TIGR02169 78 VTVTFKNDDGKFPdELEVVRRLKVTDDGKYSYY--------YLNGQRVRLSEIHDFLAaagiypeGYNVVLQGDVTDFIS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 153 VS----KAIINNVLFCHQ-----EDSSWPLDESKKLKEKFDAIFGI---------TEYNKALD-KIIKLRK---EAMEEL 210
Cdd:TIGR02169 150 MSpverRKIIDEIAGVAEfdrkkEKALEELEEVEENIERLDLIIDEkrqqlerlrREREKAERyQALLKEKreyEGYELL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 211 KIKEANIKHVAYLKQEMEVKTLNLQKAQRKCDAIKAQCSECEEEMKPIEARLV-----EIRNVEFEIGKYQAQKVEMDTK 285
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 286 HKNCKDQISTLTLKIKKPF--------------------RGTLDELDQEISNFDQRMLEMRQKRTEVEGDLSQIKRSSVA 345
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEaeidkllaeieelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 346 EQEKLGTQDRKHclakQRHQSELACRAQLLKRVKEFCRELHIPIDcDLVEQPEKMGEVLRDIEAMIITKHCEITEIVEQN 425
Cdd:TIGR02169 390 YREKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 426 EKADRS---RQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESATKnI 502
Cdd:TIGR02169 465 SKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE-V 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 503 DQQAIKDAIARKKASIAENQIQFKKLDE--QLTFLgSMAKLVAECSLKQK--------------ELDKKNQEVHR----- 561
Cdd:TIGR02169 544 AAGNRLNNVVVEDDAVAKEAIELLKRRKagRATFL-PLNKMRDERRDLSIlsedgvigfavdlvEFDPKYEPAFKyvfgd 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 562 ---VRS-----RHSDHF------GKLFkEP---ITCNYR--RSMQVVYEKLRREIQELNEkantqklKEQSYEIKRKNLI 622
Cdd:TIGR02169 623 tlvVEDieaarRLMGKYrmvtleGELF-EKsgaMTGGSRapRGGILFSRSEPAELQRLRE-------RLEGLKRELSSLQ 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 623 SDISRMEKELKDseeliyqkcrstpYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEPScplchhnmtsdeac 702
Cdd:TIGR02169 695 SELRRIENRLDE-------------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-------------- 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 703 DLTSELTDEIQKLPDNITR-AEKALKAEQIKyenllqlkptiLKVKELKDSLPQkkeelkKVEELLGDSVSEYETLIALI 781
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARiEELEEDLHKLE-----------EALNDLEARLSH------SRIPEIQAELSKLEEEVSRI 810
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 782 GEPTHNMELA-NSMMGDMSLLDEALKDSARLTKDLDLQKgqlpasydssvsmDDLQAEKSKVSKELETERKELESAQNAV 860
Cdd:TIGR02169 811 EARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQI-------------KSIEKEIENLNGKKEELEEELEELEAAL 877
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 861 QQQMDALNRLREKKnslKDRQIHLREglqslpqLKERLEKLNSFLTTVASEISELKAKIQPLKLNLrAAIEEKERLKKSE 940
Cdd:TIGR02169 878 RDLESRLGDLKKER---DELEAQLRE-------LERKIEELEAQIEKKRKRLSELKAKLEALEEEL-SEIEDPKGEDEEI 946
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768435 941 SEKLAQLNSKYNSYKSTDHDIQRL----NKEAEDYAKldlrnEIKKLDEiIMASKDKLRKLATEISLKTDELETIKTE 1014
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEEEIRALepvnMLAIQEYEE-----VLKRLDE-LKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
425-1280 |
1.47e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 425 NEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESATKNIDQ 504
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 505 QAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAECSLKQKELDkknqevhrvRSRHSDHFGKLFKEPITCNYRR 584
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAPLAAHIKAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 585 S--MQVVYEKLRREIQELNEKANTQKlKEQSYEIKRKnLISDISRMEKELKDSEEliyqkcRSTPYDDLLERSKTT---I 659
Cdd:TIGR00618 310 QriHTELQSKMRSRAKLLMKRAAHVK-QQSSIEEQRR-LLQTLHSQEIHIRDAHE------VATSIREISCQQHTLtqhI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 660 SKLQFDHGALKSSEALYKKYIQKMDEEPSCPLCHHNMTSDE---------ACDLTSELTDEIQKLPDNITRAEKALKAEQ 730
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 731 IKY--------ENLLQLKPTILKVKELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELANSMMGDMSLLD 802
Cdd:TIGR00618 462 QESaqslkereQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 803 EALKDS----ARLTKDLDLQKGQLPASYDSSVSM----DDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKK 874
Cdd:TIGR00618 542 TSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILtqcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 875 NSLKDRQ---IHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSES-----EKLAQ 946
Cdd:TIGR00618 622 QPEQDLQdvrLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltywkEMLAQ 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 947 LNSKYNSYKSTDHDIQRLNKEAEDyAKLDLRNEIKKLDEIIMASKDKLRKLATEislKTDELETIKTECSNQQTVERDLK 1026
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQART---VLKARTEAHFNNNEEVTAALQTG 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1027 DN-RELKQLEDKEAKLRESCQVLDKQLGNLDFHSVSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEprFK 1105
Cdd:TIGR00618 778 AElSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK--YE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1106 ESLKNFRKANYEIEVTRLCIEDLGQYR----LALEWALIQFHSEKMEMINRLIREYWRKIYRGNDIDYIQVKT-----DE 1176
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDKLNGINqikiQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARkyqglAL 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1177 VSSDASADRRKTYNyrvvqsknyseiemrgRCSAGQRVLASLIIRLALAETFSSNCGV----LALDEPTTNLDRANINSL 1252
Cdd:TIGR00618 936 LVADAYTGSVRPSA----------------TLSGGETFLASLSLALALADLLSTSGGTvldsLFIDEGFGSLDEDSLDRA 999
|
890 900
....*....|....*....|....*...
gi 386768435 1253 CEALNCIVEerqsqSNFMLIIITHDENF 1280
Cdd:TIGR00618 1000 IGILDAIRE-----GSKMIGIISHVPEF 1022
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-55 |
1.63e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 54.23 E-value: 1.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 386768435 4 IESLSIQGIRSFgtyaDDLqSIKFSSP--VTLILGENGCGKTTVVECLKYALTG 55
Cdd:COG3950 3 IKSLTIENFRGF----EDL-EIDFDNPprLTVLVGENGSGKTTLLEAIALALSG 51
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
174-638 |
2.92e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 174 DESKKLKE--KFDAIFGITEYNKALDKIIKLRKEA---MEELKIKEANIKHVAYL-KQEMEVKTLNLQKAQRKCDAIKAQ 247
Cdd:PTZ00121 1293 DEAKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAkkkADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 248 CSECEEEMKPIEARLVEIRNVEFEIGKYQAQKVEMDTKHKNCKDQISTLTLKIKKPFRGTLDELDQEISnfDQRMLEMRQ 327
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE--EAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 328 KRTEVEGDLSQIKRSSvaeQEKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRElhipidcdlVEQPEKMGEVLRDI 407
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKA---EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK---------AAEAKKKADEAKKA 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 408 EAmiiTKHCEITEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQR-ESSKRESETLGVEIKKIEtsmqDLKKLEK 486
Cdd:PTZ00121 1519 EE---AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAE----EAKKAEE 1591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 487 E-INEVNELYESATKNIDQQAIKDAIARKKASIAENQIQFKKLDEQLTFLGS--------------MAKLVAECSLKQKE 551
Cdd:PTZ00121 1592 ArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkkaeelkkaeeENKIKAAEEAKKAE 1671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 552 LDKKNQEvhrvRSRHSDHFGKLFKEPITCNYRRSMQVvyEKLRREIQELNEKANTQKLKEQSYEIKRKNLisdISRMEKE 631
Cdd:PTZ00121 1672 EDKKKAE----EAKKAEEDEKKAAEALKKEAEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEA---KKEAEED 1742
|
....*..
gi 386768435 632 LKDSEEL 638
Cdd:PTZ00121 1743 KKKAEEA 1749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
246-483 |
3.03e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 246 AQCSECEEEMKPIEARLVEIRNVEFEIGKYQAQKVEMDTKHKNCKDQISTLTLKIKKpFRGTLDELDQEISNFDQRMLEM 325
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 326 RQKRTEVEGDLSQIkrssVAEQEKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRElhipidcdLVEQPEKMGEVLR 405
Cdd:COG4942 96 RAELEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE--------QAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768435 406 DIEAMIITKHCEITEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKK 483
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
822-1056 |
3.25e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 822 LPASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRqihlreglqsLPQLKERLEKL 901
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----------IRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 902 NSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAqLNSKynsykstdhDIQRLNKEAEDYAKldLRNEIK 981
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL-LSPE---------DFLDAVRRLQYLKY--LAPARR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768435 982 KLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRE--LKQLEDKEAKLRESCQVLDKQLGNLD 1056
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQklLARLEKELAELAAELAELQQEAEELE 226
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-969 |
3.50e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 203 RKEAMEELKIKEANIKHVAYLKQEMEvKTLNLQKAQRKCdAIKAQcsECEEEMKPIEARLV---------EIRNVEFEIG 273
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELE-RQLKSLERQAEK-AERYK--ELKAELRELELALLvlrleelreELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 274 KYQAQKVEMDTKHKNCKDQISTLTLKI------KKPFRGTLDELDQEISNFDQRMLEMRQKRTEVEGDLSQIKRSSVAEQ 347
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVseleeeIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 348 EKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRELhipidcdlveqpEKMGEVLRDIEAMIITKHCEITEIVEQnEK 427
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAEL------------EELESRLEELEEQLETLRSKVAQLELQ-IA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 428 ADRSRQVKIDElRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESATKNID--QQ 505
Cdd:TIGR02168 397 SLNNEIERLEA-RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEeaEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 506 AIKDA------IARKKASIAENQIQFKKLDEQLTFL---------------------------------GSMAKLVAE-- 544
Cdd:TIGR02168 476 ALDAAerelaqLQARLDSLERLQENLEGFSEGVKALlknqsglsgilgvlselisvdegyeaaieaalgGRLQAVVVEnl 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 545 -------CSLKQKEL------------DKKNQEVHRVRSRHSDHFGKLFKEPITC------------------------- 580
Cdd:TIGR02168 556 naakkaiAFLKQNELgrvtflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFdpklrkalsyllggvlvvddldnal 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 581 ----NYRRSMQVVYEK-----------------------LRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELK 633
Cdd:TIGR02168 636 elakKLRPGYRIVTLDgdlvrpggvitggsaktnssileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 634 DSEELIYQKCR-STPYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEpscplchhnmtSDEACDLTSELTDEI 712
Cdd:TIGR02168 716 QLRKELEELSRqISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER-----------LEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 713 QKLPDNITRAEKALKAEQIKYENLLQlkptilKVKELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELAN 792
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRA------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 793 SMMGDMS-LLDEALKDSARLTKDLDLQKGQLPASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQmdaLNRLR 871
Cdd:TIGR02168 859 AEIEELEeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR---LEGLE 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 872 EKKNSLKDRqihLREGLQSLPQLKERLEKLNSFLTTVA-SEISELKAKIQPL-KLNLrAAIEEKERLKKSESEKLAQLNS 949
Cdd:TIGR02168 936 VRIDNLQER---LSEEYSLTLEEAEALENKIEDDEEEArRRLKRLENKIKELgPVNL-AAIEEYEELKERYDFLTAQKED 1011
|
890 900
....*....|....*....|
gi 386768435 950 KYNSYKSTDHDIQRLNKEAE 969
Cdd:TIGR02168 1012 LTEAKETLEEAIEEIDREAR 1031
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1209-1281 |
4.76e-07 |
|
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: 50.71 E-value: 4.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALnciveERQSQSNFMLIIITHDENFV 1281
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELL-----RELAEEGRTVIIVTHDPELA 143
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1209-1279 |
5.48e-07 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 53.83 E-value: 5.48e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERqsqsnfMLIIITHDEN 1279
Cdd:TIGR02857 460 SGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR------TVLLVTHRLA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
183-532 |
7.90e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 183 FDAIFGITEYnkaldkiiKLRK-EAMEELKIKEANIKHVAYLKQEME--VKTLNLQKAQ-RKCDAIKAQCSECEeemkpI 258
Cdd:COG1196 161 IEEAAGISKY--------KERKeEAERKLEATEENLERLEDILGELErqLEPLERQAEKaERYRELKEELKELE-----A 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 259 EARLVEIRNVEFEIGKYQAQKVEMDTKHKNCKDQISTLTLKIKKpFRGTLDELDQEISNFDQRMLEMRQKRTEVEGDLSQ 338
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 339 IKRSSVAEQEKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRELHipidcDLVEQPEKMGEVLRDIEAMIITKHCEI 418
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----EAEAELAEAEEALLEAEAELAEAEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 419 TEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESA 498
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350
....*....|....*....|....*....|....
gi 386768435 499 TKNIDQQAIKDAIARKKASIAENQIQFKKLDEQL 532
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
404-1095 |
8.19e-07 |
|
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: 53.69 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 404 LRDIEAMIItkhceitEIVEQNEKADRSRQVKIDEL-----------RIELTKSEQSVTAQE-KQRESSKRESETLGVEI 471
Cdd:pfam12128 195 FRDVKSMIV-------AILEDDGVVPPKSRLNRQQVehwirdiqaiaGIMKIRPEFTKLQQEfNTLESAELRLSHLHFGY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 472 KKIETSMQDLKKLEKE-INEVNELYESATKNIDQQ--AIKDAIARKKASIAENQIQFKKLDEQL-TFLGSMAKLVAecsL 547
Cdd:pfam12128 268 KSDETLIASRQEERQEtSAELNQLLRTLDDQWKEKrdELNGELSAADAAVAKDRSELEALEDQHgAFLDADIETAA---A 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 548 KQKELDKKNQEVHRVRSRHSDHFGKLFKepITCNYRRSMQVVYEKLRREIQELNEK-ANTQKLKEQSYEIKRknliSDIS 626
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQD--VTAKYNRRRSKIKEQNNRDIAGIKDKlAKIREARDRQLAVAE----DDLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 627 RMEKELKDSEEliyqkCRSTPYDDLLERSKTTISKLQFDHGALKSSEALykkyiqKMDEEPSCPLCHHNMTSDEACDLTS 706
Cdd:pfam12128 419 ALESELREQLE-----AGKLEFNEEEYRLKSRLGELKLRLNQATATPEL------LLQLENFDERIERAREEQEAANAEV 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 707 E-LTDEIQKLPdniTRAEKALKAEQIKYENLLQLKPTILKVKELKDslPQKKEELKKVEELLGDSVSEYETLIAliGEPT 785
Cdd:pfam12128 488 ErLQSELRQAR---KRRDQASEALRQASRRLEERQSALDELELQLF--PQAGTLLHFLRKEAPDWEQSIGKVIS--PELL 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 786 HNMELansmmgDMSLLDEALKDSARLTK-DLDLQKGQLPASYDS--------SVSMDDLQAEKSK----------VSKEL 846
Cdd:pfam12128 561 HRTDL------DPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASeeelrerlDKAEEALQSAREKqaaaeeqlvqANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 847 ETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHlreglqslpQLKERLEKLNSFLTTVASEISELKAKIQPLKLNL 926
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK---------ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQ 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 927 R-----AAIEEKERLKKSESEKLAQLNSkynsyKSTDHDIQRLNKEAE-DYAKLDLRNEIKKLDeiimASKDKLRKLATE 1000
Cdd:pfam12128 706 KeqkreARTEKQAYWQVVEGALDAQLAL-----LKAAIAARRSGAKAElKALETWYKRDLASLG----VDPDVIAKLKRE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1001 ISLKTDELETIKtecSNQQTVER---------DLKDNRELKQLEDKEAKLREscqvLDKQLGNLDfHSVSKEKVNLTKQR 1071
Cdd:pfam12128 777 IRTLERKIERIA---VRRQEVLRyfdwyqetwLQRRPRLATQLSNIERAISE----LQQQLARLI-ADTKLRRAKLEMER 848
|
730 740
....*....|....*....|....*..
gi 386768435 1072 ---DKATVRKGELLGQLGEIHSQVNKL 1095
Cdd:pfam12128 849 kasEKQQVRLSENLRGLRCEMSKLATL 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1119 |
1.40e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 840 SKVSKELETERKELES-------AQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEI 912
Cdd:PRK03918 168 GEVIKEIKRRIERLEKfikrtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 913 SELKAKIQPLKLNLRaAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYakLDLRNEIKKLDEIIMASKD 992
Cdd:PRK03918 248 ESLEGSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY--LDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 993 KLRKLATEISLKTDELETIKTECSNQQ----TVERDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDFHSVSKEKVNLT 1068
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEkrleELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768435 1069 KQRDKATVRKGELLGQLGEIHSQVNKLQ----------REIDEPRFKESLKNFRKANYEIE 1119
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKELLEEYTAELKRIE 465
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
335-1043 |
1.55e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 335 DLSQIKRSSVAEQEKLGTQDRKhclAKQRHQSELACRAQLLKRVKEFCR--ELHIPIDCDLVEQPEKMGEVLRDIEAMII 412
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRK---AEDARKAEAARKAEEERKAEEARKaeDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 413 TKHCEITEIVEQNEKADRSRQVKIDELRI--ELTKSEQSVTAQEKQRESSKRESEtlgvEIKKIETSMQDLKKLEKEINE 490
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKadELKKAEEKKKADEAKKAEEKKKAD----EAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 491 VNELYESATKNIDQQAIKDAIARKKASIAENQIQ-FKKLDEQLTFLGSMAKLVAECSLKQKELDKKNQEVHRVRSRHSDH 569
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK 1406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 570 FGKLFKEpitcnyrrsmqvvyEKLRREIQELNEKA-NTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIYQKCRSTPY 648
Cdd:PTZ00121 1407 ADELKKA--------------AAAKKKADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 649 DDLL----ERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEPScplchhnmTSDEACDLTSELTDEIQKLPDNITRAEK 724
Cdd:PTZ00121 1473 DEAKkkaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--------KAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 725 ALKAEQIKYENLLQLKPTILKVKELK-------DSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELANSMMGD 797
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKkaeedknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 798 MSLLDEALKDSARLTKDLDLQKGQLPASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSL 877
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 878 KDRQIHLREGLQSLPQLK----------ERLEKLNSFLTTVASEI---SELKAKIQPLKLNLRAAIEE---------KER 935
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKkaeeenkikaEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKKAEEirkekeaviEEE 1784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 936 LKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKLDEIIMaSKDKLRKLATEISLKTDELETIKTEC 1015
Cdd:PTZ00121 1785 LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVAD-SKNMQLEEADAFEKHKFNKNNENGED 1863
|
730 740
....*....|....*....|....*...
gi 386768435 1016 SNQQTVERDLKDNRELKQLEDKEAKLRE 1043
Cdd:PTZ00121 1864 GNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-490 |
2.22e-06 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 52.05 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 8 SIQGIRSFGTYADDlQSIKFSSPVTLILGENGCGKTTVVECLKYALTGecppgsdRGKSFVHDPKIFGLNEVLAQIKMQV 87
Cdd:COG4694 4 KIKKLKNVGAFKDF-GWLAFFKKLNLIYGENGSGKSTLSRILRSLELG-------DTSSEVIAEFEIEAGGSAPNPSVRV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 88 RDRRGAQVSICrtmkvSKKRNKMSFetmdstinFLTGAGQSKREKQDSLSGRSVDIDVAISDFMGVSKAIINNVlfchqe 167
Cdd:COG4694 76 FNRDFVEENLR-----SGEEIKGIF--------TLGEENIELEEEIEELEKEIEDLKKELDKLEKELKEAKKAL------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 168 dSSWPLDESKKLKEKFDAIFGITEYN----KALDKIIKLRKEAMEELKIKEANIKHVAYLKQEMEVKTLNLQKAQRKCDA 243
Cdd:COG4694 137 -EKLLEDLAKSIKDDLKKLFASSGRNyrkaNLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAET 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 244 IkaqcseceeemkpIEARLVEIRNVEFE--IGKYQAQK--VEMDTKHKNCKDQISTLTL-KIKKPFRGTLDE-LDQEISN 317
Cdd:COG4694 216 L-------------LEKSAVSSAIEELAalIQNPGNSDwvEQGLAYHKEEEDDTCPFCQqELAAERIEALEAyFDDEYEK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 318 FDQRMLEMRQKRTEVEGDLSQIKRSSVAEQEKLGTQDRKHCLAKQRHQselacRAQLLKRVKEFCRELHIPIDCDLVEQP 397
Cdd:COG4694 283 LLAALKDLLEELESAINALSALLLEILRTLLPSAKEDLKAALEALNAL-----LETLLAALEEKIANPSTSIDLDDQELL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 398 EKMGEVLRDIEAMIITKHCEITEIVEQNEKA-DRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGV---EIKK 473
Cdd:COG4694 358 DELNDLIAALNALIEEHNAKIANLKAEKEEArKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDlktEISE 437
|
490
....*....|....*..
gi 386768435 474 IETSMQDLKKLEKEINE 490
Cdd:COG4694 438 LEAELSSVDEAADEINE 454
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1221-1281 |
2.39e-06 |
|
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: 49.77 E-value: 2.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768435 1221 RLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERQSqsnfmLIIITHDENFV 1281
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT-----IIIVTHDLDLL 197
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
831-1143 |
2.91e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 831 SMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKknsLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVAS 910
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE---LEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 911 EISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKL------D 984
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELlkeanrN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 985 EIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDFHSVSKEK 1064
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1065 VNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPR-FKESLKNFRKANYEIEVTRLCIEDLGQYRLALEWALIQFH 1143
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEdALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1014 |
4.80e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 844 KELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKE------RLEKLNSFLTTVASEISELKA 917
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 918 KIQPLKlNLRAAIEEKERLKKSESEKLAQLNSKYNsyKSTDHDIQRLNKEAEdyaklDLRNEIKKLDEIIMASKDKLRKL 997
Cdd:COG4717 154 RLEELR-ELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELE-----ELQQRLAELEEELEEAQEELEEL 225
|
170
....*....|....*..
gi 386768435 998 ATEISLKTDELETIKTE 1014
Cdd:COG4717 226 EEELEQLENELEAAALE 242
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
472-1283 |
5.61e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 472 KKIETSMQDLKKLEKEINEVNELYESATKNI-DQQAIKDAIARKKASIAENQIQFKKLDEQLT-FLGSMAKLVAECSLKQ 549
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEIsNIDYLEEKLKSSNLELENIKKQIADDEKSHSiTLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 550 KELDKKNQEVHRVRSRhSDHFGKLFKEPITCNYRRSMQVVYEKLRREIQE-LNEKANTQKLKEQSYEIKRKNLISDISRm 628
Cdd:PRK01156 232 DDYNNLKSALNELSSL-EDMKNRYESEIKTAESDLSMELEKNNYYKELEErHMKIINDPVYKNRNYINDYFKYKNDIEN- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 629 ekelkdseeliyqkcrstpYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEpscplchhnmtsDEACDLTSEL 708
Cdd:PRK01156 310 -------------------KKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY------------DDLNNQILEL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 709 T---DEIQKLPDNITRAEKALKAEQIKYENLLQLKPTILKVKE-----LKDSLPQKKEELKKVEELLGDSVSEYETLIAL 780
Cdd:PRK01156 359 EgyeMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEidpdaIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 781 IGEPTHNME----------------------LANSMMGDMSLLDEALKDSARLTKDLDLQKGQLpasydssVSMDDLQAe 838
Cdd:PRK01156 439 LDELSRNMEmlngqsvcpvcgttlgeeksnhIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDL-------KKRKEYLE- 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 839 kSKVSKELETERKELESAQNAVQQQMDALNRLREKKnsLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISElkak 918
Cdd:PRK01156 511 -SEEINKSINEYNKIESARADLEDIKIKINELKDKH--DKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIE---- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 919 iqplklNLRAAIEEKERLKKSESEKLAQLNSKYNSYKS-TDHDIQRLNKEAEDYakldlRNEIKKLDEIiMASKDKLRKl 997
Cdd:PRK01156 584 ------TNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyIDKSIREIENEANNL-----NNKYNEIQEN-KILIEKLRG- 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 998 ateislktdELETIKTECSNQQTVERDLKD-NRELKQLEDKEAKLRESCQvldkqlgnldfhsvsKEKVNLTKQRDKATV 1076
Cdd:PRK01156 651 ---------KIDNYKKQIAEIDSIIPDLKEiTSRINDIEDNLKKSRKALD---------------DAKANRARLESTIEI 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1077 rkgeLLGQLGEIHSQVNKLQREIdeprfkESLKNFRKAnyeievtrlcIEDLGQYRLALEWALIQ--FHSEKMEMINRLI 1154
Cdd:PRK01156 707 ----LRTRINELSDRINDINETL------ESMKKIKKA----------IGDLKRLREAFDKSGVPamIRKSASQAMTSLT 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1155 REYwrkIYRGN-DIDYIQVKTDevssdasadrrktYNYRVVQSKNYSEIEmrgRCSAGQRVLASLIIRLALAETFSSNCG 1233
Cdd:PRK01156 767 RKY---LFEFNlDFDDIDVDQD-------------FNITVSRGGMVEGID---SLSGGEKTAVAFALRVAVAQFLNNDKS 827
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 386768435 1234 VLALDEPTTNLDRANINSLCEALNCIVeeRQSQSNFMLIIITHDENFVSS 1283
Cdd:PRK01156 828 LLIMDEPTAFLDEDRRTNLKDIIEYSL--KDSSDIPQVIMISHHRELLSV 875
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-1035 |
8.91e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 163 FCHQ-EDSSWPLDESKKL--KEKFDAIFGITEYNKALDKIiKLRKEAMEELKIKEANIKHvaYLKQEMEVKTLNLQKAQ- 238
Cdd:pfam15921 83 YSHQvKDLQRRLNESNELheKQKFYLRQSVIDLQTKLQEM-QMERDAMADIRRRESQSQE--DLRNQLQNTVHELEAAKc 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 239 RKCDAIKAQCSECEEEMKPI---EARLVEIRNVEFEIGKYQAQKVEMdtkhkncKDQISTLTLK-IKKPFRGTLDELDQE 314
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEASGKKIYE-------HDSMSTMHFRsLGSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 315 ISNFDQRMLEmrqkrteVEGDLSQIKRSSVAEQEKL--GTQDRKHCLAKQrHQSELACRAQLLKRVKEFCRELHipidcd 392
Cdd:pfam15921 233 ISYLKGRIFP-------VEDQLEALKSESQNKIELLlqQHQDRIEQLISE-HEVEITGLTEKASSARSQANSIQ------ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 393 lvEQPEKMGEVLRDIEAMIITKHCEITEIVEQNE----KADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLG 468
Cdd:pfam15921 299 --SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRselrEAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 469 VEIKKIetsMQDLKKLEKEINEVNE----LYESATKNidqqaiKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKlvAE 544
Cdd:pfam15921 377 DQLQKL---LADLHKREKELSLEKEqnkrLWDRDTGN------SITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--GQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 545 CSLKQKELDKKNQEVHRVRSRHSdhfgklfkepitcnyrrSMQVVYEKLRREIQELNEKANTQKLKEQSyeikrknlisd 624
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTA-----------------QLESTKEMLRKVVEELTAKKMTLESSERT----------- 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 625 ISRMEKELKDSEELIyqkcRSTPYDDLLERSKTTISKLQFDHgaLKSSEalykKYIQKMDEEpsCPLCHHNMTS-DEACD 703
Cdd:pfam15921 498 VSDLTASLQEKERAI----EATNAEITKLRSRVDLKLQELQH--LKNEG----DHLRNVQTE--CEALKLQMAEkDKVIE 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 704 LTSELTDEIQKLPDNITRAEKALKAEQIKYENllQLKPTILKVKELKdslpqkkeelkKVEELLGDSVSEYETLIAlige 783
Cdd:pfam15921 566 ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK--EINDRRLELQEFK-----------ILKDKKDAKIRELEARVS---- 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 784 pthNMELansmmgDMSLLDEALKDSARLTKDLDLQKGQLPASYDSSVS-MDDLQAEKSKVSKELETERKELESAQNAVQQ 862
Cdd:pfam15921 629 ---DLEL------EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNeLNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 863 QM-DALNRLREKKNSLKDRQIHLREGLQSLPQLKERleklnsfLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKsES 941
Cdd:pfam15921 700 QLkSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ-------ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKE-EK 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 942 EKLAQLNSKYNSYKstdhdiqrlNKEAEDYAKldLRNEIKKLDEIIMASKDKLRKlateISLKTDELETIkTECSNQQTV 1021
Cdd:pfam15921 772 NKLSQELSTVATEK---------NKMAGELEV--LRSQERRLKEKVANMEVALDK----ASLQFAECQDI-IQRQEQESV 835
|
890
....*....|....
gi 386768435 1022 ERDLKDNRELKQLE 1035
Cdd:pfam15921 836 RLKLQHTLDVKELQ 849
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1043 |
9.59e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 845 ELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREgLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKL 924
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-IAELEAELERLDASSDDLAALEEQLEELEAELEELEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 925 NLRAAIEEKERLKKseseKLAQLNSKYNSYKSTDHDIQRLNKE------AEDYAKLDLRNEIKKLDEIImasKDKLRKLA 998
Cdd:COG4913 707 ELDELKGEIGRLEK----ELEQAEEELDELQDRLEAAEDLARLelrallEERFAAALGDAVERELRENL---EERIDALR 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 386768435 999 TEISLKTDELETIKTECSNQ-----QTVERDLKDNRE----LKQLED-----KEAKLRE 1043
Cdd:COG4913 780 ARLNRAEEELERAMRAFNREwpaetADLDADLESLPEylalLDRLEEdglpeYEERFKE 838
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
845-1283 |
1.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 845 ELETERKELESAQNAVQQQMDALNRLREkknsLKDRQIHLREGLQSLPQL----KERLEKLNSFLTTVASEISELKAKIQ 920
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDLVE----AEDRIERLEERREDLEELiaerRETIEEKRERAEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 921 plklNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTdhdIQRLNKEAEDYAKL-DLRNEIKKLDEiimaskdklrKLAT 999
Cdd:PRK02224 555 ----EKREAAAEAEEEAEEAREEVAELNSKLAELKER---IESLERIRTLLAAIaDAEDEIERLRE----------KREA 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1000 EISLKTDELETIKTECSNQQTVERDLKDNRelkqLEDKEAKLRESCQVLDKQLGNLDfhsvskekvNLTKQRDkatvrkg 1079
Cdd:PRK02224 618 LAELNDERRERLAEKRERKRELEAEFDEAR----IEEAREDKERAEEYLEQVEEKLD---------ELREERD------- 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1080 ellgqlgEIHSQVNKLQREIDEprfkesLKNFRKANYEIEVTRLCIEDLGQYRLALEWALIQFHSE----KMEMINRLIR 1155
Cdd:PRK02224 678 -------DLQAEIGAVENELEE------LEELRERREALENRVEALEALYDEAEELESMYGDLRAElrqrNVETLERMLN 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1156 EYWRKIYRGNDIDYIQVKTDevssdasadrrktYNYRVVQsKNYSEIEMRgRCSAGQRVLASLIIRLA----LAETFSSN 1231
Cdd:PRK02224 745 ETFDLVYQNDAYSHIELDGE-------------YELTVYQ-KDGEPLEPE-QLSGGERALFNLSLRCAiyrlLAEGIEGD 809
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 386768435 1232 CGV--LALDEPTTNLDRANINSLCEalncIVEERQSQSNFMLIIITHDENFVSS 1283
Cdd:PRK02224 810 APLppLILDEPTVFLDSGHVSQLVD----LVESMRRLGVEQIVVVSHDDELVGA 859
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
4-56 |
1.13e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 49.23 E-value: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 386768435 4 IESLSIQGIRSFGtyadDLqSIKFSSPVTLILGENGCGKTTVVECLKYALTGE 56
Cdd:COG3593 3 LEKIKIKNFRSIK----DL-SIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1205-1277 |
1.71e-05 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 48.99 E-value: 1.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768435 1205 RGRC-SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERqsqsnfMLIIITHD 1277
Cdd:COG4988 470 GGRGlSGGQAQ------RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR------TVILITHR 531
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
897-1123 |
2.44e-05 |
|
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: 48.90 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 897 RLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKErlkKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKL-- 974
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE---LKAELRELELALLVLRLEELREELEELQEELKEAEEEle 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 975 DLRNEIKKLDEIIMASKDKLRKLATEISLKTDELETIKTEcsnQQTVERDLKDNRE-LKQLEDKEAKLRESCQVLDKQLG 1053
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE---ISRLEQQKQILRErLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768435 1054 NL---------DFHSVSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRFKESLKNFRKANYEIEVTRL 1123
Cdd:TIGR02168 334 ELaeelaeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1220-1283 |
2.83e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 2.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768435 1220 IRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNciveERQSqsnfMLIIITHDENFVSS 1283
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN----ERNS----TMIIISHDRHFLNS 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
827-1136 |
3.14e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 827 DSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLT 906
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 907 TVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKLDEI 986
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 987 IMASKDKLRKLATEISLKT-------DELETIKTECSNQQTveRDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDfhs 1059
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNkiisqlnEQISQLKKELTNSES--ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE--- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1060 vsKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPR-----FKESLKNFRKANYEIEVTrlcIEDLGQYRLA 1134
Cdd:TIGR04523 391 --SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKetiikNNSEIKDLTNQDSVKELI---IKNLDNTRES 465
|
..
gi 386768435 1135 LE 1136
Cdd:TIGR04523 466 LE 467
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-56 |
3.50e-05 |
|
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: 46.30 E-value: 3.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 386768435 4 IESLSIQGIRSFGtyadDLQSIKFSSPVTLILGENGCGKTTVVECLKYALtGE 56
Cdd:cd03278 1 LKKLELKGFKSFA----DKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVL-GE 48
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
838-1278 |
3.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 838 EKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLK-------------ERLEKLNSF 904
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteeHRKELLEEY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 905 ---LTTVASEISELKAKIQPLKLNLRAAieEKERLKKSESEKLAQLNSKYNSYKS--TDHDIQRLNKEAEDYAKL----- 974
Cdd:PRK03918 458 taeLKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELAEQLKELEEklKKYNLEELEKKAEEYEKLkekli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 975 DLRNEIKKLD---EIIMASKDKLRKLATEISLKTDELETIKTECSNQ--QTVERDLKDNRELKQLEDKEAKLRESCQVLD 1049
Cdd:PRK03918 536 KLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELgfESVEELEERLKELEPFYNEYLELKDAEKELE 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1050 KQLGNLDfhsvsKEKVNLTKQRDKATVRKGELlgqlGEIHSQVNKLQREIDEPRFKESLKNFRKANYEIEVTRLCIEDLG 1129
Cdd:PRK03918 616 REEKELK-----KLEEELDKAFEELAETEKRL----EELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELE 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1130 QYR---------LALEWALIQFHSEKMEMINRL------IREYWRKiYRGNDIDYIQVKTDEVSSDASAD--RRKTYNYR 1192
Cdd:PRK03918 687 KRReeikktlekLKEELEEREKAKKELEKLEKAlerveeLREKVKK-YKALLKERALSKVGEIASEIFEEltEGKYSGVR 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1193 VVQSKNYSEI--------EMRGRCSAGQRVLASLIIRLALAETFSSNCGVLALDEPTTNLDRANINSLCEalnciVEERQ 1264
Cdd:PRK03918 766 VKAEENKVKLfvvyqgkeRPLTFLSGGERIALGLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVD-----IMERY 840
|
490
....*....|....
gi 386768435 1265 SQSNFMLIIITHDE 1278
Cdd:PRK03918 841 LRKIPQVIIVSHDE 854
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
392-1282 |
4.30e-05 |
|
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: 48.04 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 392 DLVEQPEKMGEVLRDIEAMIITKHCEITEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEI 471
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 472 KKIETSMQDLKKLEKEINEVNELYESATKNIDQQAIKdaiaRKKASIAENQIQFKKLDEQltflgsmAKLVAECSLKQKE 551
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL----QEKLEQLEEELLAKKKLES-------ERLSSAAKLKEEE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 552 LDKKNQEVHRVRSRHSDHFGKLFKEPITCNYRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKE 631
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 632 LKDSEELIYQKCRSTPYDDLLERSKTTisklqfdhgalKSSEALYKKYIQKMDEEPSCPLCHHNMTSDEACDLTSELTDE 711
Cdd:pfam02463 477 TQLVKLQEQLELLLSRQKLEERSQKES-----------KARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 712 IQKLPDNITRAEKALKAEQIKYENLLQLKPTILKVKELKDSLpqkkeelkkveELLGDSVSEYETLIALIGEPTHNMELA 791
Cdd:pfam02463 546 STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKL-----------KLPLKSIAVLEIDPILNLAQLDKATLE 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 792 NSMMGDMSLLDEALKDSARLTKDLDLQKGQLPASYDSSVSMDDLqAEKSKVSKELETERKELESAQNAVQQQMDALNRLR 871
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGL-AEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 872 EKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKY 951
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 952 NSYKSTDHDIQRLNKEAEDYAKL----DLRNEIKKLDEIIMASKDKL---------RKLATEISLKTDELETIKTECSNQ 1018
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLkaqeEELRALEEELKEEAELLEEEqllieqeekIKEEELEELALELKEEQKLEKLAE 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1019 QTVERDLKDNRELKQLEDKEAKLRESCQVLDKQlgnlDFHSVSKEKVNLTKQRDKATVRKGELLGQLGEI--HSQVNKLQ 1096
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKD----ELESKEEKEKEEKKELEEESQKLNLLEEKENEIeeRIKEEAEI 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1097 REIDEPRFKESLKNFRKANYEIEVTrlcIEDLGQYRLALEWALIqfhsEKMEMINRLIREYWRKIYRGNDIDYIQVKTDE 1176
Cdd:pfam02463 930 LLKYEEEPEELLLEEADEKEKEENN---KEEEEERNKRLLLAKE----ELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1177 VSSDASADRRKTYNYRVVQ------------SKNYSEIEMRGRC--------------------------------SAGQ 1212
Cdd:pfam02463 1003 EKKKLIRAIIEETCQRLKEflelfvsinkgwNKVFFYLELGGSAelrledpddpfsggieisarppgkgvknldllSGGE 1082
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1213 RVLASLIIRLALAEtFSSNCGVLaLDEPTTNLDRANINSLCEALnciveeRQSQSNFMLIIITHDENFVS 1282
Cdd:pfam02463 1083 KTLVALALIFAIQK-YKPAPFYL-LDEIDAALDDQNVSRVANLL------KELSKNAQFIVISLREEMLE 1144
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
449-686 |
4.61e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 449 SVTAQEKQRESSKRESETLGVEIKKIEtsmQDLKKLEKEINEVNELYESATKNIDQ-----QAIKDAIARKKASIAENQI 523
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAAlarriRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 524 QFKKLDEQLTflgsmaklvaecslKQKELDKKNQEVHRVRSRHSDHFGKLFKEPITCNYRRS--MQVVYEKLRREIQELN 601
Cdd:COG4942 91 EIAELRAELE--------------AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 602 EKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIYQKcrstpyDDLLERSKTTISKLQFDHGALKSSEALYKKYIQ 681
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAER------QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
....*
gi 386768435 682 KMDEE 686
Cdd:COG4942 231 RLEAE 235
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
842-1077 |
4.74e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 842 VSKELETER-KELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGlqslpQLKERLEKLNSFLTTVASEISELKAKIQ 920
Cdd:PRK05771 36 LKEELSNERlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVK-----SLEELIKDVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 921 PLKLNLRAAIEEKERLkksesEKLAQLN---SKYNSYKSTDHDIQRLNKEAEDYAKLDLRN----EIKKLDE----IIMA 989
Cdd:PRK05771 111 ELENEIKELEQEIERL-----EPWGNFDldlSLLLGFKYVSVFVGTVPEDKLEELKLESDVenveYISTDKGyvyvVVVV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 990 SKDKLRKLATEIslktDELETIKTECSNQQTVERDLKD-NRELKQLEDKEAKLRESCQVLDKQLGnlDFHSVSKEKVNLT 1068
Cdd:PRK05771 186 LKELSDEVEEEL----KKLGFERLELEEEGTPSELIREiKEELEEIEKERESLLEELKELAKKYL--EELLALYEYLEIE 259
|
....*....
gi 386768435 1069 KQRDKATVR 1077
Cdd:PRK05771 260 LERAEALSK 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1287 |
4.96e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 844 KELETERKELESAQNAVQQQMDALNRLREKKNSLKdRQIHLREGLQSLPQLKERLEKLNSFL--TTVASEISELKAKIQP 921
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELE-EELEQLENELEAAALEERLKEARLLLliAAALLALLGLGGSLLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 922 LKLNLRAAI-----------EEKERLKKSESEKLAQLNSKYNSYKSTDHDIQR------LNKEAEDYAKLDLRNEIKKLD 984
Cdd:COG4717 271 LILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEEllaalgLPPDLSPEELLELLDRIEELQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 985 EIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDK----EAKLRESCQVLDKQLGNLDFHSV 1060
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEleelEEQLEELLGELEELLEALDEEEL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1061 SKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKL--QREIDEPRFKESLKNFRKANYEIEVTRLcieDLGQYrlALEWA 1138
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAAL---KLALE--LLEEA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1139 LIQFHSEKMEMINRLIREYWRKIYRGNdidYIQVKTDEvSSDASADRRktynyrvvQSKNYSEIEMrgrcSAGQRVLASL 1218
Cdd:COG4717 506 REEYREERLPPVLERASEYFSRLTDGR---YRLIRIDE-DLSLKVDTE--------DGRTRPVEEL----SRGTREQLYL 569
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768435 1219 IIRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERQsqsnfmLIIITHDENFVSSLGKI 1287
Cdd:COG4717 570 ALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQ------VIYFTCHEELVELFQEE 632
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
836-1101 |
5.02e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 836 QAEKSKVSKELETERKELESAQnavqqqmdALNRLREKKNSLKDRQIHLREglqslpqLKERLEKLNSFLTTVASEISEL 915
Cdd:COG1196 208 QAEKAERYRELKEELKELEAEL--------LLLKLRELEAELEELEAELEE-------LEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 916 KAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAK--LDLRNEIKKLDEIIMASKDK 993
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 994 LRKLATEISLKTDELETIKTEcsNQQTVERDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDfhsvsKEKVNLTKQRDK 1073
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAE--LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-----ERLERLEEELEE 425
|
250 260
....*....|....*....|....*...
gi 386768435 1074 ATVRKGELLGQLGEIHSQVNKLQREIDE 1101
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
401-936 |
1.03e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 401 GEVLRDIEAMIITKHCEITEIVEQNEKAdrsrqvKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQD 480
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDLHE------RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 481 LKKLEKEINEVNELYESATKniDQQAIKDAIARKKASIAEnqiqfkkLDEQLTflgsmaKLVAEC----------SLKQK 550
Cdd:PRK02224 253 LETLEAEIEDLRETIAETER--EREELAEEVRDLRERLEE-------LEEERD------DLLAEAglddadaeavEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 551 ELDKKNQEVHRVRSRHSDHFGKlFKEPITcNYRRSMqvvyEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEK 630
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQA-HNEEAE-SLREDA----DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 631 ELKDSEELI------------YQKCRSTPYDDLLERSKTTISKLQFDHGALKSSEALYkkyiqkmdEEPSCPLC------ 692
Cdd:PRK02224 392 EIEELRERFgdapvdlgnaedFLEELREERDELREREAELEATLRTARERVEEAEALL--------EAGKCPECgqpveg 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 693 -HHNMTSDEA----CDLTSELTD---EIQKLPDNITRAEKALKAEQiKYENLLQLKPTILK-VKELKDSLPQKKEELKKV 763
Cdd:PRK02224 464 sPHVETIEEDrervEELEAELEDleeEVEEVEERLERAEDLVEAED-RIERLEERREDLEElIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 764 EELLGDSVSE----YETLIALIGEPTHNMELANSMMGDMSLLDEALKDSARLTKDLDL------QKGQLPASYDSSVSMD 833
Cdd:PRK02224 543 RERAAELEAEaeekREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiadaedEIERLREKREALAELN 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 834 DLQ----AEKSKVSKELETE---------RKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEK 900
Cdd:PRK02224 623 DERrerlAEKRERKRELEAEfdearieeaREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 386768435 901 LNS---FLTTVASEISELKAKIQPLKLNLRAA-IEEKERL 936
Cdd:PRK02224 703 LENrveALEALYDEAEELESMYGDLRAELRQRnVETLERM 742
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
669-719 |
1.43e-04 |
|
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. The Rad50 coiled-coil region contains a dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn ion. This alignment includes the zinc hook motif and a short stretch of coiled-coil on either side.
Pssm-ID: 427940 [Multi-domain] Cd Length: 52 Bit Score: 40.64 E-value: 1.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 386768435 669 LKSSEALYKKYIQKMDEEP-SCPLCHHNMTSDEACDLTSELTDEIQKLPDNI 719
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEgCCPLCGRPLDEEHRSELIKELQSKLERLPEEL 52
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
4-55 |
1.70e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 45.53 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 386768435 4 IESLSIQGIRSfgtYADdlQSIKFSSPVTLILGENGCGKTTVVECLKYALTG 55
Cdd:COG1195 2 LKRLSLTNFRN---YES--LELEFSPGINVLVGPNGQGKTNLLEAIYLLATG 48
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
831-1035 |
2.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 831 SMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVAs 910
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 911 EISELKAKIQPLKLNLRAAIEEKERLKksesEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKLDEIimas 990
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL---- 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 386768435 991 KDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRELKQLE 1035
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1212-1278 |
2.97e-04 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 43.96 E-value: 2.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1212 QRVlasliirlALAETFSSNCGVLALDEPTTNLDRAN---INSLCEALNcivEERQSQsnfmLIIITHDE 1278
Cdd:COG4181 153 QRV--------ALARAFATEPAILFADEPTGNLDAATgeqIIDLLFELN---RERGTT----LVLVTHDP 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1206-1284 |
3.01e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.06 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1206 GRCSAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNciveerqsqsNF--MLIIITHDENFVSS 1283
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD----------DFpgTVLLVSHDRYFLDR 494
|
.
gi 386768435 1284 L 1284
Cdd:COG0488 495 V 495
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
453-950 |
3.08e-04 |
|
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: 45.10 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 453 QEKQRESSKRESET--LGVEIKKIETSMQDLK-KLEKEINEVNELYESAtkNIDQQAIKDAIARK----------KASIA 519
Cdd:pfam05483 229 EEYKKEINDKEKQVslLLIQITEKENKMKDLTfLLEESRDKANQLEEKT--KLQDENLKELIEKKdhltkelediKMSLQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 520 ENQIQFKKLDEQLTFLGSMAKLVAEcslkqkELDKKNQEVHRVRSRHSDHFGKLfkEPITCNYRRSMQVvyEKLRREIQE 599
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTE------EKEAQMEELNKAKAAHSFVVTEF--EATTCSLEELLRT--EQQRLEKNE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 600 LNEKANTQKLKEQSYEIK-----RKNLISDISRMEKELKDSEELIYQKCRSTPYDD-----------LLERSKTTISKLQ 663
Cdd:pfam05483 377 DQLKIITMELQKKSSELEemtkfKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEelkgkeqelifLLQAREKEIHDLE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 664 FDHGALKSSEALYKKYIQKMDEEPSCP-------LCHHNMTS-------DEACDLTSELTDEIQKLPDNITRAEKALKAE 729
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEklknielTAHCDKLLlenkeltQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 730 QIKYENLLQLKPTILKVK--------ELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELANSMMGDMSLL 801
Cdd:pfam05483 537 ENLEEKEMNLRDELESVReefiqkgdEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 802 DEALKDSARL-----------TKDLDLQKGQLPASYDSSVSMDDLQAEKSKVSKE--LETERKELESAQNAVQQQMDALN 868
Cdd:pfam05483 617 NKALKKKGSAenkqlnayeikVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEklLEEVEKAKAIADEAVKLQKEIDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 869 R----------LREKKNSLKDRQIHLREglQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKK 938
Cdd:pfam05483 697 RcqhkiaemvaLMEKHKHQYDKIIEERD--SELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
570
....*....|..
gi 386768435 939 SESEKLAQLNSK 950
Cdd:pfam05483 775 EAKENTAILKDK 786
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-686 |
3.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 186 IFGITEYNKALD------KIIKLRKEAMEELKIKEANIKhvaylkqemevktlnlqkaqrkcDAIKAQCSECEEEMKPIE 259
Cdd:PRK03918 154 ILGLDDYENAYKnlgeviKEIKRRIERLEKFIKRTENIE-----------------------ELIKEKEKELEEVLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 260 ARLVEIRNVEFEIGKYQAQKVEMDTKhkncKDQISTLTLKIKKpFRGTLDELDQEISNFDQRMLEMRQKRTEVEGDLSQI 339
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEEL----KEEIEELEKELES-LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 340 K--RSSVAEQEKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRELhipidcdlveqpEKMGEVLRDIEAMIITKHCE 417
Cdd:PRK03918 286 KelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL------------EEKEERLEELKKKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 418 ITEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINE-VNELYE 496
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaIEELKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 497 SATK------NIDQQAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAECSLKQKELDKKNQEVHRVRSRHSDhF 570
Cdd:PRK03918 434 AKGKcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEK-L 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 571 GKLFKEPITCNYRRsmqvvYEKLRREIQELneKANTQKLKEqsyEIKRKN-LISDISRMEKELKDSEELiyqkcRSTPYD 649
Cdd:PRK03918 513 KKYNLEELEKKAEE-----YEKLKEKLIKL--KGEIKSLKK---ELEKLEeLKKKLAELEKKLDELEEE-----LAELLK 577
|
490 500 510
....*....|....*....|....*....|....*..
gi 386768435 650 DLLERSKTTISKLQfdhGALKSSEALYKKYIQKMDEE 686
Cdd:PRK03918 578 ELEELGFESVEELE---ERLKELEPFYNEYLELKDAE 611
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
899-1068 |
4.02e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.24 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 899 EKLNSFLTTVASEISELKAKIQPLKlNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDhdiqrLNKeaedyakldLRN 978
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEEELRQLKQLEDELEDCDPTE-----LDR---------AKE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 979 EIKKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQT----VERDLKDNRelKQLEDKEAKLRESCQVLdKQLGN 1054
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTeiaeAEKKLEQCR--GFTFKEIEKLKEQLKLL-QSLTG 288
|
170
....*....|....
gi 386768435 1055 LDFHSVSKEKVNLT 1068
Cdd:smart00787 289 WKITKLSGNTLSMT 302
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1209-1285 |
5.32e-04 |
|
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: 42.17 E-value: 5.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEalncIVEERQSQSNFMLIIITHDENFVSSLG 1285
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALDPITRREVRA----LLKSLQAQLGITVVLVTHDLDEAARLA 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-637 |
5.34e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 424 QNEKADRSRQvKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEI----KKIETSMQDLKKLEKEINEVNELYESAT 499
Cdd:COG4942 18 QADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalaRRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 500 KNIDQQaiKDAIARKKASIAENQIQ-----------FKKLDEQLTFLGSMA----KLVAECSLKQKELDKKNQEVHRVRS 564
Cdd:COG4942 97 AELEAQ--KEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAparrEQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386768435 565 RHSDHFGKLFKEpitcnyRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEE 637
Cdd:COG4942 175 ELEALLAELEEE------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
836-1119 |
5.51e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 836 QAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDrQIHLREGLQS-----LPQLKERLEKLNSFLTTVAS 910
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN-KIKILEQQIKdlndkLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 911 EISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDY--AKLDLRNEIKKLDEIIM 988
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELenELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 989 ASKDKLRKLATEISL------KTDELETIKTECSNQQTVerdLKDNRELKQ--LEDKEAKLRESCQVLdKQLGNLDFHsV 1060
Cdd:TIGR04523 191 KIKNKLLKLELLLSNlkkkiqKNKSLESQISELKKQNNQ---LKDNIEKKQqeINEKTTEISNTQTQL-NQLKDEQNK-I 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768435 1061 SKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDE---PRFKESLKNFRKANYEIE 1119
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnKELKSELKNQEKKLEEIQ 327
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1209-1276 |
5.62e-04 |
|
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: 41.98 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERqsqsnfMLIIITH 1276
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK------TVIVIAH 153
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1184-1256 |
5.94e-04 |
|
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: 40.30 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1184 DRRKTYNYRV-VQSKNYSEIE---MRGRCSAGQR-VLASLIIRLALAETFSSN------CGVLALDEPTTNLDRANINSL 1252
Cdd:pfam13558 5 DYRNWLSFEVeVRDEDGSEVEtyrRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTA 84
|
....
gi 386768435 1253 CEAL 1256
Cdd:pfam13558 85 LELL 88
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1201-1276 |
7.19e-04 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 42.58 E-value: 7.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768435 1201 EIEMRGR-CSAGQRVLasliirLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERqsqsnfMLIIITH 1276
Cdd:cd03245 133 QIGERGRgLSGGQRQA------VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK------TLIIITH 197
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
21-80 |
7.58e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 42.83 E-value: 7.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 21 DLQSIKFSSPVTLILGENGCGKTTVVECLKYALtGECPPGSDRGKSFVHDPKIFGLNEVL 80
Cdd:COG3910 29 NLEGLEFHPPVTFFVGENGSGKSTLLEAIAVAA-GFNPEGGSKNFRFSTRESESALGEYL 87
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
173-496 |
7.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 173 LDESKKLKEKF-DAIFGITEYNKALDKIIKLRKEAMEELK---------------------IKE--ANIKHVAYLKQEME 228
Cdd:PRK03918 393 LEELEKAKEEIeEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteehrkelLEEytAELKRIEKELKEIE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 229 VKTLNLQKAQRKCDAIKAQcsecEEEMKPIEARLVEIRNVEFEIGKYQAQKVEMDTKHKnckDQISTLTLKIKKPFRGTL 308
Cdd:PRK03918 473 EKERKLRKELRELEKVLKK----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLKGEIKSLK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 309 DELdQEISNFDQRMLEMRQKRTEVEGDLSQIKRssvaEQEKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRELHIP 388
Cdd:PRK03918 546 KEL-EKLEELKKKLAELEKKLDELEEELAELLK----ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 389 IDcDLVEQPEKMGEVLRDIEAMIITKHCEITEI-VEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETL 467
Cdd:PRK03918 621 LK-KLEEELDKAFEELAETEKRLEELRKELEELeKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
330 340
....*....|....*....|....*....
gi 386768435 468 GVEIKKIETSMQDLKKLEKEINEVNELYE 496
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELRE 728
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
426-642 |
8.58e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 426 EKADRSRQVKIDE----------LRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKietsMQDLKKLEKEINEVNE-- 493
Cdd:pfam17380 319 EEAEKARQAEMDRqaaiyaeqerMAMERERELERIRQEERKRELERIRQEEIAMEISR----MRELERLQMERQQKNErv 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 494 ------------LYESATKNIDQQAIKDAIARKKASIAEnQIQFKKLDEQLTflgsmaklvAECSLKQKELDKKNQEVHR 561
Cdd:pfam17380 395 rqeleaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEAR-QREVRRLEEERA---------REMERVRLEEQERQQQVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 562 VRSRHSDHfgklFKEPITCNYRRSMQVVYEKLRREIQELNEKANTQKLKEQsyEIKRKNLisdisrmEKELKDSEELIYQ 641
Cdd:pfam17380 465 LRQQEEER----KRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE--ERKRKLL-------EKEMEERQKAIYE 531
|
.
gi 386768435 642 K 642
Cdd:pfam17380 532 E 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-973 |
9.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 791 ANSMMGDMSLLDEALKDSARLTKDLDLQKGQLPASydssvsMDDLQAEKSKVSKELETERKELeSAQNAVQQQMDALNRL 870
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAE------LAELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 871 REKKNS------------LKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKE---- 934
Cdd:COG4942 123 ALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQklla 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 386768435 935 RLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAK 973
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK09841 |
PRK09841 |
tyrosine-protein kinase; |
803-969 |
9.72e-04 |
|
tyrosine-protein kinase;
Pssm-ID: 182106 [Multi-domain] Cd Length: 726 Bit Score: 43.74 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 803 EALKDSARLTKDLDLQKGQLPASYDSSVSMDDLQA----EKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLk 878
Cdd:PRK09841 222 ERSKESGMLELTMTGDDPQLITRILNSIANNYLQQniarQAAQDSQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSV- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 879 DRQIHLREGLQSLPQLKERLEKLnsflTTVASEISELKAKIQPlklNLRAAIEEKERLkksESEKLaQLNSKYNSYKSTD 958
Cdd:PRK09841 301 DLNLEAKAVLEQIVNVDNQLNEL----TFREAEISQLYKKDHP---TYRALLEKRQTL---EQERK-RLNKRVSAMPSTQ 369
|
170
....*....|.
gi 386768435 959 HDIQRLNKEAE 969
Cdd:PRK09841 370 QEVLRLSRDVE 380
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
423-1035 |
9.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 423 EQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIEtsmQDLKKLEKEINEVNELYESATKNI 502
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 503 DQqaIKDAIARKKASIAENQIQFKKLDEQLtflgsmAKLVAECSLKQKELDKKNQEVHRVRSRhsdhfgklfkepitcny 582
Cdd:COG1196 298 AR--LEQDIARLEERRRELEERLEELEEEL------AELEEELEELEEELEELEEELEEAEEE----------------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 583 RRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIYQKcrstpyDDLLERSKTTISKL 662
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL------LERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 663 QFDHGALKSSEALYKKYIQKMDEEpscplchhnmtsdEAcDLTSELTDEIQKLPDNITRAEKALKAEQIKYENLLQLKPT 742
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEE-------------EA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 743 ILKVKELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELANSMMGdmSLLDEALKDSARLTKDLDLQKGQL 822
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA--ALQNIVVEDDEVAAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 823 PAsydsSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLN 902
Cdd:COG1196 571 AG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 903 SFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKK 982
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 386768435 983 LDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKD-NRELKQLE 1035
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERlEREIEALG 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
908-1123 |
9.98e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 908 VASEISELKAKIQPLKLNLRAAIEEKERLkksesEKLAQLNSKYNSYKSTDHDIQRLNKEAE------DYAKLDL-RNEI 980
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQI-----ELLEPIRELAERYAAARERLAELEYLRAalrlwfAQRRLELlEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 981 KKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTveRDLKD-NRELKQLEDKEAKLRESCQVLDKQLGNLDFHS 1059
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQlEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768435 1060 VSKEKV------NLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRfKE--SLKNfRKANYEIEVTRL 1123
Cdd:COG4913 376 PASAEEfaalraEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEiaSLER-RKSNIPARLLAL 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-1114 |
1.01e-03 |
|
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: 43.51 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 596 EIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIYQ-KCRSTPYDDLLERSKTTISKLQFDHGALKSSEA 674
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 675 LYKKYIQKMDEEpscpLCHHNMTSDEACDLTSELTDEIQKLPDNITRAEKALKAEQIKYENLLQlkptilKVKELKDslp 754
Cdd:TIGR02168 313 NLERQLEELEAQ----LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES------RLEELEE--- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 755 qkkeelkkveellgdsvsEYETLIALIGEPTHNMELANSmmgDMSLLDEALKDSARLTKDLDLQKGQLPASYDSSvSMDD 834
Cdd:TIGR02168 380 ------------------QLETLRSKVAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEELLKKLEEA-ELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 835 LQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISE 914
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 915 LKAKIQPLK--------------------------LNLRAAIEEKERLKKSESEKLA----------QLNSKYNSYKSTD 958
Cdd:TIGR02168 518 LSGILGVLSelisvdegyeaaieaalggrlqavvvENLNAAKKAIAFLKQNELGRVTflpldsikgtEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 959 HDIQRLNKEAEDYAK------------------------------------------------------------LDLRN 978
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPklrkalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssiLERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 979 EIKKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLkdNRELKQLEDKEAKLRESCQVLDKQLGNLdfh 1058
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--SRQISALRKDLARLEAEVEQLEERIAQL--- 752
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 386768435 1059 svSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDepRFKESLKNFRKA 1114
Cdd:TIGR02168 753 --SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE--QLKEELKALREA 804
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
833-1027 |
1.14e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 833 DDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLReglQSLPQLKERLEKLNSFLTTVASEI 912
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT---KKISSLKEKIEKLESEKKEKESKI 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 913 SELKAKIQPLKLNLRAAIEEKERLKKseSEKLAQLNSKYNSYKSTDHDIQRLNKEAEDyAKLDLRNEI------------ 980
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEIDEK--NKEIEELKQTQKSLKKKQEEKQELIDQKEK-EKKDLIKEIeekekkisslek 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386768435 981 ---------KKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKD 1027
Cdd:TIGR04523 618 elekakkenEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
836-1008 |
1.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 836 QAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLkdRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISEL 915
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERELEERERRRARL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 916 KAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDyAKLDLRNEIKKLDE---IIMASKD 992
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR-ELRELEAEIASLERrksNIPARLL 443
|
170
....*....|....*..
gi 386768435 993 KLRK-LATEISLKTDEL 1008
Cdd:COG4913 444 ALRDaLAEALGLDEAEL 460
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1209-1276 |
1.40e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 41.40 E-value: 1.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANinslCEALNCIVEERQSQsNFMLIIITH 1276
Cdd:PRK13539 129 SAGQKR------RVALARLLVSNRPIWILDEPTAALDAAA----VALFAELIRAHLAQ-GGIVIAATH 185
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1209-1287 |
1.62e-03 |
|
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: 40.66 E-value: 1.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALnciveERQSQSNFMLIIITHDENFVSSLGKI 1287
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI-----AALKAAGATRIVIAHRPETLASADRI 165
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
12-64 |
1.70e-03 |
|
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: 40.42 E-value: 1.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 386768435 12 IRSFGTYADDlQSIKFSSP-VTLILGENGCGKTTVVECLKYALTGECPPGSDRG 64
Cdd:cd03227 4 LGRFPSYFVP-NDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-349 |
2.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 172 PLDESKKLKEKFDAIFGITEYNKALDKIIKLRKEAMEELKIKEANIKHVAYLKQEMEvKTLNLQKAQRKCDAIKAQCSEC 251
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 252 EEEMKPIEARLVEIRNVEFEIGKYQAQKVEMDTKHKNCKDQISTLTLKIKKPFRGTLDELDQEISNFDQRMLEMRQKRTE 331
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*...
gi 386768435 332 VEGDLSQIKRSSVAEQEK 349
Cdd:COG4717 225 LEEELEQLENELEAAALE 242
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1221-1276 |
2.90e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 41.75 E-value: 2.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 386768435 1221 RLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNcivEERQSQSNFMliiITH 1276
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN---AASRRQTTLM---VTH 542
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1209-1277 |
2.93e-03 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 40.95 E-value: 2.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386768435 1209 SAGQRVlasliiRLALAETFSSNCGVLALDEPTTNLD---RANInslceaLNCIVEErQSQSNFMLIIITHD 1277
Cdd:cd03257 147 SGGQRQ------RVAIARALALNPKLLIADEPTSALDvsvQAQI------LDLLKKL-QEELGLTLLFITHD 205
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
392-1118 |
3.34e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 392 DLVEQPEKMGEVLRDIEAMIitkHCEITEIVEQNEKADRSrqvKIDELRIE-LTKSEQSVTAQEKQRES---------SK 461
Cdd:TIGR01612 1030 DIEQKIEDANKNIPNIEIAI---HTSIYNIIDEIEKEIGK---NIELLNKEiLEEAEINITNFNEIKEKlkhynfddfGK 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 462 RESETLGVEIKKIETSMQDL-KKLEKEINEVNELYESATKNIDQ--------QAIKD-AIARKKASIAENQIQ--FKKLD 529
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLdQKIDHHIKALEEIKKKSENYIDEikaqindlEDVADkAISNDDPEEIEKKIEniVTKID 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 530 EQLTFLGSMAKLVAECSlkQKELDKKN-QEVHRVRSRHSDHFGKLFKEPITCNYRRSMQVVyEKLRREIQELNEkantqk 608
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIA--EIEKDKTSlEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMI-KAMEAYIEDLDE------ 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 609 LKEQSYEIKRKNLISDISRMEKELKDSEELIYQKcrstpYDDLLERSKTTISKLQfdHGALKSSEALYKKyiqkmdeeps 688
Cdd:TIGR01612 1255 IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKD-----HHIISKKHDENISDIR--EKSLKIIEDFSEE---------- 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 689 cplchhnmtsdeacdltSELTDEIQKLPDNITRAEKAlKAEQIKYENLLQLKPTILKVKELK---DSLPQKKEELKKVEE 765
Cdd:TIGR01612 1318 -----------------SDINDIKKELQKNLLDAQKH-NSDINLYLNEIANIYNILKLNKIKkiiDEVKEYTKEIEENNK 1379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 766 LLGDSVSEYETLIALIGEPThNMELANSMMgdMSLLDEalKDSARLTKDLDLQKGQLpasYDSSVSMDDLQAEKSKVSKE 845
Cdd:TIGR01612 1380 NIKDELDKSEKLIKKIKDDI-NLEECKSKI--ESTLDD--KDIDECIKKIKELKNHI---LSEESNIDTYFKNADENNEN 1451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 846 LETERKELESAQNAVQQQMDAlnrlrEKKNSLKDRQIHLREglqslpqLKERLEKLNSFLTTVASEiselkakiqplkln 925
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQHILKI-----KKDNATNDHDFNINE-------LKEHIDKSKGCKDEADKN-------------- 1505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 926 lRAAIEEKERLKKSESEKLAQLNSKY------NSYKSTDHDIQRLNKEAED-YAKLDLR--------NEIKKLDEII--- 987
Cdd:TIGR01612 1506 -AKAIEKNKELFEQYKKDVTELLNKYsalaikNKFAKTKKDSEIIIKEIKDaHKKFILEaekseqkiKEIKKEKFRIedd 1584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 988 MASKDKLRKLATEISLKTDELETIKTECSNQQTVERD-LKDNRELKQ------LEDKEAKLRESCQVLDKQLGNLDfhSV 1060
Cdd:TIGR01612 1585 AAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDcLKETESIEKkissfsIDSQDTELKENGDNLNSLQEFLE--SL 1662
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768435 1061 SKEKVNLTKQRDkatvrkgellgQLGEIHSQVNKLQREIDEprfkeslknfRKANYEI 1118
Cdd:TIGR01612 1663 KDQKKNIEDKKK-----------ELDELDSEIEKIEIDVDQ----------HKKNYEI 1699
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
422-1203 |
3.57e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 422 VEQNEKADRSRQVKIDELRieltkseqsvtaqeKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESatkn 501
Cdd:PTZ00440 486 KEKKESSDSNYQEKVDELL--------------QIINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKY---- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 502 iDQQAIKDAIARKKasiaENQIQFKKLDEQLTFLGSMAKLVAECSLKQKELDKKNQEVHRVRSrhSDHFGKLFKEPITCN 581
Cdd:PTZ00440 548 -YLQSIETLIKDEK----LKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELIN--EALFNKEKFINEKND 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 582 YRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIyQKCRSTPYDDLLERSKTTISK 661
Cdd:PTZ00440 621 LQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKL-EFMKSDNIDNIIKNLKKELQN 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 662 LQfdhgALKssEALYKKYIQKMDEEPSCPLchhNMTSDEACDLTSELTD---EIQKLPDN----ITRAEKALKAEQIKYE 734
Cdd:PTZ00440 700 LL----SLK--ENIIKKQLNNIEQDISNSL---NQYTIKYNDLKSSIEEykeEEEKLEVYkhqiINRKNEFILHLYENDK 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 735 NLLQLKPTILKVKELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMElANSMMGDMSLLDEALKDSarlTKD 814
Cdd:PTZ00440 771 DLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLE-AHTEKNDEELKQLLQKFP---TED 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 815 LDLQKGQLPASYDSSVS-MDDLQAEKSKVSKELETeRKELESAQNAVQQQMDALNRLREKKNSLKDRQ------------ 881
Cdd:PTZ00440 847 ENLNLKELEKEFNENNQiVDNIIKDIENMNKNINI-IKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLeqhmkiintdni 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 882 IHLREGLQSLPQLKERLEKLNSFLTTvaSEISELKAKIQPLklnLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDI 961
Cdd:PTZ00440 926 IQKNEKLNLLNNLNKEKEKIEKQLSD--TKINNLKMQIEKT---LEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEI 1000
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 962 QRLNKEAEDYAKLDLRNEIKKLDEIIMASKDKLRKLATEISLKTDE----LETIKTECSNQQTVE-----RDLKDNRELK 1032
Cdd:PTZ00440 1001 DKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKEKGKEIEEKVDQyislLEKMKTKLSSFHFNIdikkyKNPKIKEEIK 1080
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1033 QLEDKEAKLRESCQVLDKQLGNLDFHSvSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRfKESLKNFR 1112
Cdd:PTZ00440 1081 LLEEKVEALLKKIDENKNKLIEIKNKS-HEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMN-LEDITLNE 1158
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1113 KANYEIEVTRLCIEDLGQyrlalewaLIQFHSEKMEMINRLIREYWRkiyrgnDIDYIQVKtdevSSDASADRRKTYNYR 1192
Cdd:PTZ00440 1159 VNEIEIEYERILIDHIVE--------QINNEAKKSKTIMEEIESYKK------DIDQVKKN----MSKERNDHLTTFEYN 1220
|
810
....*....|....
gi 386768435 1193 VVQSK---NYSEIE 1203
Cdd:PTZ00440 1221 AYYDKataSYENIE 1234
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
801-973 |
3.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 801 LDEALKDSARLTKDLDLQKGQLPASYDS-SVSMDDLQAEKSKVSKELETERKELESAQNAVQQQM--------------- 864
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNElQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyrsggsvsyldv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 865 --------DALNRLrEKKNSLKDRQihlREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERL 936
Cdd:COG3883 108 llgsesfsDFLDRL-SALSKIADAD---ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 386768435 937 KKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAK 973
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-50 |
4.02e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 4.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 386768435 4 IESLSIQGIRSFGTYADDLqsikfsSPVTLILGENGCGKTTVVECLK 50
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPL------GPLTVLIGANGSGKSNLLDALR 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
522-976 |
4.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 522 QIQFKKLDEQLTFLGSMAKLVAECSLKQKELDKKNQEVHRVRSRHSDHFGKLFKEPITCNYRRSMQvVYEKLRREIQELN 601
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 602 EKANTQKLKEQSYEikrkNLISDISRMEKELKDSEELIYQKCRSTPYDDLLErskttISKLQFDHGALKSSEALYKKYIQ 681
Cdd:COG4717 146 ERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEE-----LQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 682 KMDEEPscplchhnmtsdeacdltSELTDEIQKLPDNITRAEKALKAEQIKYenLLQLKPTILKVKELKDSLPQKKEELK 761
Cdd:COG4717 217 EAQEEL------------------EELEEELEQLENELEAAALEERLKEARL--LLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 762 -KVEELLGDSVSEYETLIALIGEPTHNMELANSMMGDMSLLDEALKD-SARLTKDLDLQKGQLPASYDSSVSMDDLQAEK 839
Cdd:COG4717 277 gVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 840 SKVSKELETERKELESAQNAVQQQMDALNRLR------EKKNSLKDRQIHLREGLQSL-PQLKERLEKLNsfLTTVASEI 912
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRaaleqaEEYQELKEELEELEEQLEELlGELEELLEALD--EEELEEEL 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768435 913 SELKAKIQPLKLNLRAAIEEKERLKK-----SESEKLAQLNSKYNSYKstdhdiQRLNKEAEDYAKLDL 976
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAeleqlEEDGELAELLQELEELK------AELRELAEEWAALKL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
417-987 |
4.54e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 417 EITEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEvnELYE 496
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE--ALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 497 SATKNIDQQAIKDAIARKKASIAENQIQFKKLDEQL-TFLGSMAKLVAECSLKQKELDKKNQEVHRVRSRHSDHFGKLfk 575
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELeEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA-- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 576 epitcnyRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISR--MEKELKDSEELIYQkcrstpyDDLLE 653
Cdd:COG1196 448 -------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLE-------GVKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 654 RSKTTISKLQFDHGALKSSEALYKKYIqkmdEEPSCPLCHHNMTSDEAcdltsELTDEIQKLPDNITRAEKALKAEQIKY 733
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAAL----EAALAAALQNIVVEDDE-----VAAAAIEYLKAAKAGRATFLPLDKIRA 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 734 ENLLQLKPTILKVKELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELANSMMGDMSLLDEALKDSARLTK 813
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 814 DLDLQKGQLPASYDSS-VSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLP 892
Cdd:COG1196 665 GSRRELLAALLEAEAElEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 893 QLKERLEKLNSF-----LTTVASEISELKAKIQPL-KLNLrAAIEEKERLKksesEKLAQLNSKYNsykstdhdiqrlnk 966
Cdd:COG1196 745 EELLEEEALEELpeppdLEELERELERLEREIEALgPVNL-LAIEEYEELE----ERYDFLSEQRE-------------- 805
|
570 580
....*....|....*....|.
gi 386768435 967 eaedyaklDLRNEIKKLDEII 987
Cdd:COG1196 806 --------DLEEARETLEEAI 818
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1212-1282 |
4.61e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.21 E-value: 4.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768435 1212 QRVLasliirlaLAETFSSNCGVLALDEPTTNLDRANINSLCEALNciveeRQSQSNFMLIIITHDENFVS 1282
Cdd:cd03235 139 QRVL--------LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-----ELRREGMTILVVTHDLGLVL 196
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
845-1002 |
5.00e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 845 ELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQplkl 924
Cdd:COG0497 210 ELEEERRRLSNAEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELR---- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 925 NLRAAIE-EKERLKKSEsEKLAQLNS---KYNsyKSTDHDIQRLNKEAEDYAKLDLRNE-IKKLDEIIMASKDKLRKLAT 999
Cdd:COG0497 286 RYLDSLEfDPERLEEVE-ERLALLRRlarKYG--VTVEELLAYAEELRAELAELENSDErLEELEAELAEAEAELLEAAE 362
|
...
gi 386768435 1000 EIS 1002
Cdd:COG0497 363 KLS 365
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
805-970 |
5.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 805 LKDSARLTKDLDLQKGQLPASYDS-SVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIH 883
Cdd:pfam01576 421 LSESERQRAELAEKLSKLQSELESvSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 884 LREGLQSLPQLKERLEKLnsfLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQR 963
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQ---LSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
....*..
gi 386768435 964 LNKEAED 970
Cdd:pfam01576 578 LQQELDD 584
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1234-1284 |
5.38e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 5.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 386768435 1234 VLALDEPTTNLDRANInslcEALNCIVEERQSQsnfmLIIITHDENFVSSL 1284
Cdd:PRK15064 459 VLVMDEPTNHMDMESI----ESLNMALEKYEGT----LIFVSHDREFVSSL 501
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
884-1148 |
6.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 884 LREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQR 963
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 964 LNKEAEdyaklDLRNEIKKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDKEAKLRE 1043
Cdd:COG4372 113 LQEELE-----ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 1044 SCQVLDKQLGNLDFHSVSKEK-----VNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRFKESLKNFRKANYEI 1118
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLieslpRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270
....*....|....*....|....*....|
gi 386768435 1119 EVTRLCIEDLGQYRLALEWALIQFHSEKME 1148
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1209-1280 |
7.06e-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: 39.56 E-value: 7.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386768435 1209 SAGQRVLASLIIRLALAETFSSNCGV----LALDEPTTNLDRANINSLCEALNCIVEErqsqsNFMLIIITHDENF 1280
Cdd:cd03279 125 SGGETFLASLSLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALELIRTE-----NRMVGVISHVEEL 195
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
835-1043 |
7.95e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 835 LQAEKSKVSKELETERKeLESAQNAVQQQMD------------------ALNRLREKKNSLKDRQIHLREGLQSLPQLKE 896
Cdd:pfam17380 301 LRQEKEEKAREVERRRK-LEEAEKARQAEMDrqaaiyaeqermamererELERIRQEERKRELERIRQEEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 897 rLEKLNSflttvaseisELKAKIQPLKLNLRAA----IEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYA 972
Cdd:pfam17380 380 -LERLQM----------ERQQKNERVRQELEAArkvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386768435 973 KLDLRNEIKKLDEIIMASKDKLRKLATEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDKEAKLRE 1043
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1221-1278 |
7.99e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 39.38 E-value: 7.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768435 1221 RLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERQSqsnfMLIIITHDE 1278
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGT----TLILVTHDL 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
417-605 |
8.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 417 EITEIVEQNEKADRSRQvKIDELRIELTKSEQsVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYE 496
Cdd:COG4913 625 ELAEAEERLEALEAELD-ALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 497 SATKNIDQqaIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAEcslkqkeldkknqevhrvrsrhsDHFGKLFKE 576
Cdd:COG4913 703 ELEEELDE--LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-----------------------ALLEERFAA 757
|
170 180
....*....|....*....|....*....
gi 386768435 577 PITCNYRRSMQvvyEKLRREIQELNEKAN 605
Cdd:COG4913 758 ALGDAVERELR---ENLEERIDALRARLN 783
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
918-1110 |
8.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 918 KIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEdyaklDLRNEIKKLDEIIMASKDKLRKL 997
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-----KLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 998 ATEI-----------------SLKT--DELETIKTECSNQQTVERDLKDNRElkQLEDKEAKLRESCQVLDKQLGNLDfh 1058
Cdd:COG3883 92 ARALyrsggsvsyldvllgseSFSDflDRLSALSKIADADADLLEELKADKA--ELEAKKAELEAKLAELEALKAELE-- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386768435 1059 svsKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRFKESLKN 1110
Cdd:COG3883 168 ---AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
843-948 |
9.06e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768435 843 SKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLnsfLTTVASEISELKAKIQPL 922
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQAL---LAELAGAGAAAEGRAGEL 121
|
90 100
....*....|....*....|....*.
gi 386768435 923 KlnlrAAIEEKERLKKSESEKLAQLN 948
Cdd:PRK09039 122 A----QELDSEKQVSARALAQVELLN 143
|
|
| |
