|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-806 |
1.50e-63 |
|
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: 232.27 E-value: 1.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 1 SKEERDKWIKkELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQ 80
Cdd:TIGR02169 404 LKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 81 SERNYLWRE-ENAEQQALAAKREdlekkqQLLRAATGKAILNGIDsinkvlehfrrkginqhvqnGYHGIVMNNFECEPA 159
Cdd:TIGR02169 483 KELSKLQRElAEAEAQARASEER------VRGGRAVEEVLKASIQ--------------------GVHGTVAQLGSVGER 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 160 FYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNPRFDKA 236
Cdd:TIGR02169 537 YATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDPKYEPA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 237 FKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNE--NL 314
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElsSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 315 RRNIERINNEIDQLMNQMQQIETQQRKfkasrdsILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAE 394
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 395 LG--TDLLSQLSLEDQKRVDALNDE-IRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELRETE 468
Cdd:TIGR02169 767 IEelEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLK 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 469 GGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLK 548
Cdd:TIGR02169 847 EQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 549 KKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKS 627
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 628 IMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLvPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF 707
Cdd:TIGR02169 1005 ILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPD-----------------------------DPF 1054
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 708 TGvGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITT 787
Cdd:TIGR02169 1055 AG-GLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVV 1133
|
810
....*....|....*....
gi 40226155 788 TFRPELLESADKFYGVKFR 806
Cdd:TIGR02169 1134 SLRSPMIEYADRAIGVTMR 1152
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
719-813 |
4.33e-58 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (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: 213239 [Multi-domain] Cd Length: 243 Bit Score: 198.64 E-value: 4.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 719 KQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 798
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
90
....*....|....*
gi 40226155 799 KFYGVKFRNKVSHID 813
Cdd:cd03272 229 KFYGVKFRNKVSTID 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-812 |
4.40e-55 |
|
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: 206.83 E-value: 4.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 3 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKyyEVKNKKDELQSE 82
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 83 RNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA--ILNGIDSINKVLEHFRRKGI-------NQHVQNGYHGIVMNN 153
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELaqLQARLDSLERLQENLEGFSEgvkallkNQSGLSGILGVLSEL 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 154 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLR----- 228
Cdd:TIGR02168 529 ISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakdl 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 229 --YNPRFDKAFKHVFGKTLICRSMEVSTQLARA--FTMDCITLEGDQVSHRGALTGGYYDTRKSRL-------ELQKDVR 297
Cdd:TIGR02168 608 vkFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrreieELEEKIE 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 298 KAEEELGELEAKLNEnLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTF-------MPK 370
Cdd:TIGR02168 688 ELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeiEEL 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 371 QRSLQSLEASLHAMESTRESLKAELgTDLLSQLSLEDqKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENL 450
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRL-EDL 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 451 RKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKsmerwKNMEKEHmdA 528
Cdd:TIGR02168 844 EEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-----KRSELRR--E 916
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 529 INHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQE---AFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFV 605
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 606 NFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqDEG 685
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPE-------DLL 1069
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 686 EgsgesergsgsqssvpsvdqfTGVGIRVSFTGKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDA 765
Cdd:TIGR02168 1070 E---------------------AGIEIFAQPPGKK--NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDD 1126
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 40226155 766 QHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNK-VSHI 812
Cdd:TIGR02168 1127 ANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKgVSKI 1174
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-811 |
3.32e-51 |
|
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: 194.81 E-value: 3.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 1 SKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQ 80
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 81 SERNYLWREE-NAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVQNGYHGIVMNNFECEPA 159
Cdd:pfam02463 467 LKKSEDLLKEtQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 160 FYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVrdtaypetndaipmisklryNPRFDKAFKH 239
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--------------------LEIDPILNLA 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 240 VFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIE 319
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 320 RINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMlKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDL 399
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL-LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 400 LSQLSLEDQKRVDALNDEIRQLQQEnrqllneriKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSE 479
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEE---------EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 480 LEAINK--RVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHdtKELEKMTNRQGMLLKKKEECMKKI 557
Cdd:pfam02463 837 ELALELkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES--KEEKEKEEKKELEEESQKLNLLEE 914
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 558 RELGSLPQEAFEK--------YQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIM 629
Cdd:pfam02463 915 KENEIEERIKEEAeillkyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 630 ELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPggkatlvMKKGDVEGSQSqDEGEGSGESErgsgsqssVPSVDQFTG 709
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS-------INKGWNKVFFY-LELGGSAELR--------LEDPDDPFS 1058
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 710 VGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTF 789
Cdd:pfam02463 1059 GGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISL 1138
|
810 820
....*....|....*....|...
gi 40226155 790 RPELLESADKFYGVKF-RNKVSH 811
Cdd:pfam02463 1139 REEMLEKADKLVGVTMvENGVST 1161
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
676-811 |
4.95e-38 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 139.75 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 676 VEGSQSQDEGEGSGESERGSGSQSSVPSVDqftgVGI----RVSFTgKQGEMREMqqLSGGQKSLVALALIFAIQKCDPA 751
Cdd:cd03239 45 VLGGKAAKLRRGSLLFLAGGGVKAGINSAS----VEItfdkSYFLV-LQGKVEQI--LSGGEKSLSALALIFALQEIKPS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40226155 752 PFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFRNKVSH 811
Cdd:cd03239 118 PFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVHGVST 178
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
393-803 |
4.13e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.05 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 393 AELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRE-TEGGT 471
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvTLEGE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 472 VLTATTSELEAINKRVKDT----MARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLL 547
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAAlleaEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 548 KKKEECMKKIRELgSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKS 627
Cdd:COG1196 735 EELLEELLEEEEL-LEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARET 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 628 IMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF 707
Cdd:COG1196 814 LEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTDPD-----------------------------DPL 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 708 -TGVGIRVSFTGKqgEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQ--HRkaVSDMIMELAVHAQF 784
Cdd:COG1196 865 eTGIEIMAQPPGK--KLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQF 940
|
410
....*....|....*....
gi 40226155 785 ITTTFRPELLESADKFYGV 803
Cdd:COG1196 941 IVITHNKRTMEAADRLYGV 959
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
144-256 |
1.39e-28 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 110.78 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 144 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYP 215
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 40226155 216 ETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 256
Cdd:smart00968 80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
728-807 |
1.77e-27 |
|
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: 108.99 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 728 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFR 806
Cdd:cd03227 77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 40226155 807 N 807
Cdd:cd03227 157 I 157
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
144-257 |
8.48e-24 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 96.95 E-value: 8.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 144 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAI 221
Cdd:pfam06470 2 KGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 40226155 222 PMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLA 257
Cdd:pfam06470 81 PLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
718-810 |
9.30e-24 |
|
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: 99.46 E-value: 9.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 718 GKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 797
Cdd:cd03278 105 GKK--VQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAA 182
|
90
....*....|....
gi 40226155 798 DKFYGVKFRNK-VS 810
Cdd:cd03278 183 DRLYGVTMQESgVS 196
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
728-813 |
2.64e-18 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (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: 213240 [Multi-domain] Cd Length: 251 Bit Score: 85.43 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 728 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRN 807
Cdd:cd03273 166 ELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVD 245
|
....*.
gi 40226155 808 KVSHID 813
Cdd:cd03273 246 GTSTVT 251
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
724-812 |
5.26e-17 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (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: 213242 [Multi-domain] Cd Length: 247 Bit Score: 81.46 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 724 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAV-HAQFITTTFRPELLESADKFYG 802
Cdd:cd03275 151 RDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADALVG 230
|
90
....*....|...
gi 40226155 803 VkFRNK---VSHI 812
Cdd:cd03275 231 V-YRDQecnSSKV 242
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
724-803 |
1.83e-15 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (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: 213241 [Multi-domain] Cd Length: 212 Bit Score: 76.18 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 724 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGV 803
Cdd:cd03274 123 KNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGI 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
728-804 |
2.24e-13 |
|
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: 68.43 E-value: 2.24e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40226155 728 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLE-SADKFYGVK 804
Cdd:cd00267 80 QLSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLK 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
315-623 |
4.80e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 315 RRNIERINNEIDQLMNQMQQIETQQRK------FKASRDSILSEMKMLKEKRQQSEktfmpkqrsLQSLEASLHAMESTR 388
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAE---------LEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 389 ESLKAELgtDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETyLNENLRKRLDQVEQELNELRETE 468
Cdd:COG1196 256 EELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 469 GG--TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 546
Cdd:COG1196 333 EEleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40226155 547 LKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQcNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDR 623
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
715-785 |
4.64e-09 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (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: 213243 [Multi-domain] Cd Length: 198 Bit Score: 56.84 E-value: 4.64e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40226155 715 SF-TGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFI 785
Cdd:cd03276 95 SFlTSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAkkqPGRQFI 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
312-678 |
5.27e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 312 ENLRRNIERINNEIDQLMNQMQQIETQqrKFKASRDSILSEMKmlkEKRQQSEKTfmpkqRSLQSLEASLHAMESTRESL 391
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEK---REYEGYELL-----KEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 392 KAELGtdllsqlslEDQKRVDALNDEIRQLQQENRQLlNERIKLEGIITRVEtylnenLRKRLDQVEQELNELRETeggt 471
Cdd:TIGR02169 250 EEELE---------KLTEEISELEKRLEEIEQLLEEL-NKKIKDLGEEEQLR------VKEKIGELEAEIASLERS---- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 472 vltattseLEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKK-- 549
Cdd:TIGR02169 310 --------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfa 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 550 ---------KEECMKKIRELGSLPQEAFEKYQTlsLKQLFRKLEQCNTELkkyshvnKKALDQFVNFSEQKEKLIKRQEE 620
Cdd:TIGR02169 382 etrdelkdyREKLEKLKREINELKRELDRLQEE--LQRLSEELADLNAAI-------AGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40226155 621 LDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL-------------VPGGKATLVMKKGDVEG 678
Cdd:TIGR02169 453 QEWKLEQLAADLSKYE-QELYDLKEEYDRVEKELSKLQRELaeaeaqaraseerVRGGRAVEEVLKASIQG 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
313-643 |
1.49e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 313 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 389
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 390 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 469
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 470 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 544
Cdd:PRK03918 318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 545 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 610
Cdd:PRK03918 396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474
|
330 340 350
....*....|....*....|....*....|...
gi 40226155 611 KEKLIKRQEELDrgyksiMELMNVLELRKYEAI 643
Cdd:PRK03918 475 ERKLRKELRELE------KVLKKESELIKLKEL 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
312-574 |
3.95e-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: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 312 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESL 391
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 392 KAELGTDLLSQLSLE-----DQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRE 466
Cdd:COG1196 315 EERLEELEEELAELEeeleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 467 TEggtvltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 546
Cdd:COG1196 395 AA------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260
....*....|....*....|....*...
gi 40226155 547 LKKKEECMKKIRELGSLPQEAFEKYQTL 574
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
409-827 |
4.55e-07 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 53.58 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 409 KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlrkrLDQVEQELNELRETEGGTVLTattSELEAINKRVK 488
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEE-----LEEADLQPGEDEALEAEQQRL---SNLEKLRELSQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 489 DTMAR-SEDLDNSIDKTEAGIKELQKSMErwknmekehmdaiNHDTKELEKMTNRQGMLLKKKEECMKKIRELGS----L 563
Cdd:TIGR00634 233 NALAAlRGDVDVQEGSLLEGLGEAQLALA-------------SVIDGSLRELAEQVGNALTEVEEATRELQNYLDelefD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 564 PQEAFEKYQTLS-LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYksIMELMNVLELRKYEA 642
Cdd:TIGR00634 300 PERLNEIEERLAqIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEEL--DKAAVALSLIRRKAA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 643 iqltfKQVSKNFSEVFQKLvpggkaTLVMKKGDVEGSQSQDEGEGSGESERGsgsqssvpsVDQftgvgIRVSFTGKQGE 722
Cdd:TIGR00634 378 -----ERLAKRVEQELKAL------AMEKAEFTVEIKTSLPSGAKARAGAYG---------ADQ-----VEFLFSANTGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 723 mrEMQQL----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 798
Cdd:TIGR00634 433 --PVKPLakvaSGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHAD 510
|
410 420
....*....|....*....|....*....
gi 40226155 799 KFYGVKfrnKVShIDVITAEMAKDFVEDD 827
Cdd:TIGR00634 511 AHFKVE---KEG-LDGRTATRVRPLSGEE 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
313-527 |
7.90e-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: 53.14 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 313 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLK 392
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 393 AELGTDL-----LSQLSLEDQKRVDALNDEIRQLQQENRQLLNE----RIKLEGIITRVETYLNENLRKRLDQVEQELNE 463
Cdd:TIGR02168 358 AELEELEaeleeLESRLEELEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40226155 464 LRET--EGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 527
Cdd:TIGR02168 438 LQAEleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
283-601 |
1.25e-06 |
|
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: 52.36 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 283 YDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 362
Cdd:TIGR00606 205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 363 SEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKL------- 435
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV-----DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrh 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 436 -EGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEA--INKRVKDTMARSEDLDNSIDKTEAGIKELQ 512
Cdd:TIGR00606 360 qEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 513 KSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEA----------FEKYQTLSLKQLFRK 582
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltetlkkevkSLQNEKADLDRKLRK 519
|
330
....*....|....*....
gi 40226155 583 LEQCNTELKKYSHVNKKAL 601
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQME 538
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
356-623 |
2.05e-06 |
|
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: 51.60 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 356 LKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLK--AELGTDL------LSQLSLEDQ-KRVDALNDEIRQLQQENR 426
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLErqAEKAERYkelkaeLRELELALLvLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 427 QLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEA 506
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKE-----LYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 507 GIKELQKSmerwknmekehmdaINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKyqtlsLKQLFRKLEQC 586
Cdd:TIGR02168 324 QLEELESK--------------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-----LEELEEQLETL 384
|
250 260 270
....*....|....*....|....*....|....*..
gi 40226155 587 NTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDR 623
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
718-799 |
7.85e-06 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 49.21 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 718 GKQGEMremqqLSGGQKSLVALALIFaiqkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 797
Cdd:TIGR02857 453 GEGGAG-----LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
..
gi 40226155 798 DK 799
Cdd:TIGR02857 524 DR 525
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
719-804 |
1.15e-05 |
|
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: 47.22 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 719 KQGE-----MREMQQLSGGQKSLVALALIFAIQK--CDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFITTT 788
Cdd:cd03240 101 HQGEsnwplLDMRGRCSGGEKVLASLIIRLALAEtfGSNCGILALDEPTTNLDEENIEESLAEIIEERksqKNFQLIVIT 180
|
90
....*....|....*.
gi 40226155 789 FRPELLESADKFYGVK 804
Cdd:cd03240 181 HDEELVDAADHIYRVE 196
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
714-779 |
1.22e-05 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (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: 213244 [Multi-domain] Cd Length: 213 Bit Score: 47.21 E-value: 1.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40226155 714 VSFtgKQGEmrEMQQL-----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 779
Cdd:cd03277 111 VKF--REGE--QLQELdphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETA 177
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
312-660 |
3.02e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 312 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEmkmlkeKRQQSEKTFmpKQRSLQSLEASLHAMESTRESL 391
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLID------KINELDKAF--KDASLNDYEAKNNELIKYFNDL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 392 KAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-----------KLEGIITRVETYLNENLRKRLDQVEQE 460
Cdd:TIGR01612 1006 KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniidEIEKEIGKNIELLNKEILEEAEINITN 1085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 461 LNELRETEGGTVLTATTSE-----LEAINKrVKDTMarsEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAI------ 529
Cdd:TIGR01612 1086 FNEIKEKLKHYNFDDFGKEenikyADEINK-IKDDI---KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLedvadk 1161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 530 ---NHDTKELE-KMTNRQGMLLKKK---EECMKKIRELGSLP--QEAFEKYQTL------SLKQLFrkLEQCNTELKKYS 594
Cdd:TIGR01612 1162 aisNDDPEEIEkKIENIVTKIDKKKniyDEIKKLLNEIAEIEkdKTSLEEVKGInlsygkNLGKLF--LEKIDEEKKKSE 1239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40226155 595 HVNKKALDQFVNFSEQKEK--LIKRQEELDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQK 660
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISH-DDDKDHHIISKKHDENISDIREK 1306
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
284-513 |
3.03e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 284 DTRKSRLELQKDVRKAEEELGELEAKLNEnLRRNIERINNEIDQLMnqmQQIETQQRKFKASRDSILSEMKMLKEKRQQS 363
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 364 EKTFMPKQRSLQSLEASLHamestreslkaelgtdLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 443
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQ----------------YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 444 TylnenLRKRLDQVEQELNELreteggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQK 513
Cdd:COG4942 185 E-----ERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
9-114 |
3.74e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 9 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYE---------VKNKKDEL 79
Cdd:COG4942 53 LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalLLSPEDFL 132
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 40226155 80 QSER-----NYLWREENAEQQALAAKREDLEKKQQLLRAA 114
Cdd:COG4942 133 DAVRrlqylKYLAPARREQAEELRADLAELAALRAELEAE 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9-517 |
6.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 9 IKKELKSLDQAINDKKRQIAAIHKDLED----TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERn 84
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 85 ylwREENAEQQALAAKREDLEKKQQLLRAATGKAIlnGIDSIN--------KVLEHFRRkginqhvqngyhgivmnnfeC 156
Cdd:COG4913 422 ---RELEAEIASLERRKSNIPARLLALRDALAEAL--GLDEAElpfvgeliEVRPEEER--------------------W 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 157 EPAfytcVEVTAGNRLFYHIVDS---DEVSTKIlmefNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPmiSKLRYNPrf 233
Cdd:COG4913 477 RGA----IERVLGGFALTLLVPPehyAAALRWV----NRLHLRGRLVYERVRTGLPDPERPRLDPDSLA--GKLDFKP-- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 234 dkafkHVFGktlicrsMEVSTQLARAFTMDC-------------ITLEGdQVSHRGALtgGYYDTRK---SRLELQKDVR 297
Cdd:COG4913 545 -----HPFR-------AWLEAELGRRFDYVCvdspeelrrhpraITRAG-QVKGNGTR--HEKDDRRrirSRYVLGFDNR 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 298 KAEeelgeleaklnENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSIlsemkmlkekRQQSEKTFMpkQRSLQSL 377
Cdd:COG4913 610 AKL-----------AALEAELAELEEELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 378 EASLHAMESTRESLKAelgtdllsqlsleDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVEtylnenlrKRLDQV 457
Cdd:COG4913 667 EREIAELEAELERLDA-------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------KELEQA 725
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40226155 458 EQELNELRETEGGTVLTATTSELEAINKRVKDTMAR------SEDLDNSIDKTEAGIKELQKSMER 517
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELER 791
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
729-801 |
7.87e-05 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 43.91 E-value: 7.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40226155 729 LSGGQKSLVALALIFaIQKcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFY 801
Cdd:cd03228 97 LSGGQRQRIAIARAL-LRD---PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
356-517 |
8.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 356 LKEKRQQSEKT--FMPKQrsLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI 433
Cdd:COG3206 166 LELRREEARKAleFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 434 KLEGIITRVETYLNE--------NLRKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARS-EDLDNSID 502
Cdd:COG3206 244 ALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSAryTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323
|
170
....*....|....*
gi 40226155 503 KTEAGIKELQKSMER 517
Cdd:COG3206 324 ALQAREASLQAQLAQ 338
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
312-633 |
8.12e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 312 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEM--KMLKEKRQQSEKtfmPKQRSLQSLEASLHAMESTRE 389
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKKRFSLLK---KETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 390 sLKAELGT-DLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-KLEGIITRVETylnENLRKRLDQVEQELNELRET 467
Cdd:COG5022 887 -LKIDVKSiSSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIaRLKKLLNNIDL---EEGPSIEYVKLPELNKLHEV 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 468 EGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH-------------MDAINHDTK 534
Cdd:COG5022 963 ESK--LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLkelpvevaelqsaSKIISSEST 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 535 ELEKMTNRQ---GMLLKKKEECMKKIRELG----SLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNF 607
Cdd:COG5022 1041 ELSILKPLQklkGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120
|
330 340
....*....|....*....|....*.
gi 40226155 608 SEQKEKLIKRQEELDRGYKSIMELMN 633
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVF 1146
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
724-786 |
1.74e-04 |
|
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: 43.61 E-value: 1.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40226155 724 REMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQFIT 786
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKL--KAEGKT 186
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
322-503 |
2.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 322 NNEIDQLMnQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLS 401
Cdd:COG1579 3 PEDLRALL-DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 402 QLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELREteggtvltATTSELE 481
Cdd:COG1579 82 LGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL-AELEAELAELEAELEEKKA--------ELDEELA 152
|
170 180
....*....|....*....|..
gi 40226155 482 AINKRVKDTMARSEDLDNSIDK 503
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
9-117 |
2.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 9 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKD--ELQSERNYL 86
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIESL 101
|
90 100 110
....*....|....*....|....*....|.
gi 40226155 87 WREENAEQQALAAKREDLEKKQQLLRAATGK 117
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
11-99 |
2.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 11 KELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREE 90
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....*....
gi 40226155 91 NAEQQALAA 99
Cdd:COG4942 100 EAQKEELAE 108
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
724-785 |
2.39e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.51 E-value: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40226155 724 REMQQLSGGQKSLVALAlIFAIQKCDpapFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 785
Cdd:cd03236 135 RNIDQLSGGELQRVAIA-AALARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
|
|
| F-BAR_CIP4-like |
cd07653 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ... |
2-96 |
2.97e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153337 [Multi-domain] Cd Length: 251 Bit Score: 43.40 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 2 KEERDKWIKkELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELdRKYYEVKNKKDElQS 81
Cdd:cd07653 104 RQERKKHLS-EGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNLTKADVEKA-KANANLKTQAAE-EA 180
|
90
....*....|....*..
gi 40226155 82 ERNY--LWREENAEQQA 96
Cdd:cd07653 181 KNEYaaQLQKFNKEQRQ 197
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
314-646 |
3.22e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 314 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMpkqRSLQSLEASLHAMESTRESLKa 393
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAK- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 394 ELGTDLLSQLsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlRKRLDQVEQELNEL---RETEGG 470
Cdd:pfam15921 338 RMYEDKIEEL----EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 471 TVLTATTSELEAINKRVKdtmaRSEDLDNSIDkteagiKELQKSMERwknmekeHMDAINHDTKELEKMTNRQGMLLKKK 550
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQ----RLEALLKAMK------SECQGQMER-------QMAAIQGKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 551 EECMKKIRELGS--LPQEAFEKY---QTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGY 625
Cdd:pfam15921 475 EMLRKVVEELTAkkMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
|
330 340
....*....|....*....|.
gi 40226155 626 KSIMELMNVLELRKYEAIQLT 646
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMT 575
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
311-633 |
3.61e-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: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 311 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 390
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 391 LKAELGTDLLS----QLSLEDQKR--------VDALNDEIRQLQQENRQL------LNERI-KLEGIITRVETYL----- 446
Cdd:TIGR04523 466 LETQLKVLSRSinkiKQNLEQKQKelkskekeLKKLNEEKKELEEKVKDLtkkissLKEKIeKLESEKKEKESKIsdled 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 447 ----------NENLRKRLDQVEQELNELRETEggTVLTATTSELEainKRVKDTMARSEDLDNSIDKTEAGIKELQKSME 516
Cdd:TIGR04523 546 elnkddfelkKENLEKEIDEKNKEIEELKQTQ--KSLKKKQEEKQ---ELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 517 rwkNMEKEHMDaINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSlpqEAFEKYQTLSLK-----QLFRK-LEQCNTEL 590
Cdd:TIGR04523 621 ---KAKKENEK-LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP---EIIKKIKESKTKiddiiELMKDwLKELSLHY 693
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 40226155 591 KKY--SHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMN 633
Cdd:TIGR04523 694 KKYitRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
9-118 |
3.65e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 9 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDEL------QSE 82
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLdvllgsESF 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 40226155 83 RNYLWR----------------EENAEQQALAAKREDLEKKQQLLRAATGKA 118
Cdd:COG3883 115 SDFLDRlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAEL 166
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
349-583 |
4.29e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 349 ILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG----TDLLSQLSLEDQKRVDALNDEIRQLQQE 424
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaeMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 425 NRQLLNERIKLEGIITRVETY-----LNENLRKRLDQVEQELNELR-----ETEGGTVLTATTSELEAInkRVKDTMARS 494
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMrelerLQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEMEQI--RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 495 EDLDNSIDKTEAGIKEL-QKSMERWKNMEKEHMDAINHDTKELEKmtNRQGMLLKKKEECMKKIRElgslpQEAFEKYQT 573
Cdd:pfam17380 435 REVRRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLEL--EKEKRDRKRAEEQRRKILE-----KELEERKQA 507
|
250
....*....|
gi 40226155 574 LSLKQLFRKL 583
Cdd:pfam17380 508 MIEEERKRKL 517
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
728-799 |
4.64e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.15 E-value: 4.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40226155 728 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 799
Cdd:PRK10851 136 QLSGGQKQRVALARALAVE----PQILLLDEPFGALDAQVRKELRRWLRQL--HEELkFTSVFvthdQEEAMEVADR 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
317-562 |
4.90e-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: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 317 NIERINNEIDQLMNQMQQIETQQRKFKAsrdsiLSEMKMLKEKRQQsektfmpkqrsLQSLEASLHAMESTRESLKAELG 396
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 397 TDLLsqlsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELREteggtvltat 476
Cdd:COG4913 290 LELL-------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 477 tsELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINhdtKELEKMTNRQGMLLKKKEECMKK 556
Cdd:COG4913 353 --ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAE 427
|
....*.
gi 40226155 557 IRELGS 562
Cdd:COG4913 428 IASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
406-620 |
8.30e-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: 42.44 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 406 EDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINK 485
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAE-----LAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 486 RVKDTMARSEDLDNSIDKT-EAGIKELQKSMERWKNMEK--EHMDAIN-HDTKELEKMTNRQGMLLKKKEECMKKIRELG 561
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRrlQYLKYLApARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40226155 562 SLPQEAFEKYQTLSLKQLFRK--LEQCNTELKKYshvnKKALDQFVNFSEQKEKLIKRQEE 620
Cdd:COG4942 178 ALLAELEEERAALEALKAERQklLARLEKELAEL----AAELAELQQEAEELEALIARLEA 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
312-661 |
8.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 312 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdsilSEMKMLKEKRQQSEKtFMPKQRSLQSLEASLHAMESTRESL 391
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 392 KAELGTdlLSQLSLEDQKRVDALND---EIRQLQQENRQLLNERIKLEgiiTRVETYlnenlrKRLDQVEQELNELRETE 468
Cdd:PRK03918 313 EKRLSR--LEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELE---ERHELY------EEAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 469 GGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNM------------EKEHMDAINHDTKEL 536
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 537 EKMTNRqgmlLKKKEECMKKIR-ELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYshvNKKALDQ-FVNFSEQKEKL 614
Cdd:PRK03918 462 KRIEKE----LKEIEEKERKLRkELRELEKVLKKESELIKLKELAEQLKELEEKLKKY---NLEELEKkAEEYEKLKEKL 534
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 40226155 615 IKRQEELdRGYKSIMELMNVLELRKyEAIQLTFKQVSKNFSEVFQKL 661
Cdd:PRK03918 535 IKLKGEI-KSLKKELEKLEELKKKL-AELEKKLDELEEELAELLKEL 579
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
311-621 |
9.88e-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: 42.70 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 311 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILsemKMLKEKRQQSEKTfmpkQRSLQSLEASLHAMESTRES 390
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQN----NKKIKELEKQLNQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 391 LKAELGTDLLSQlsledqkrvdaLNDEIRQLQQENRQLLNERIKLEGIITRVETYLNeNLRKRLDQVEQELNELRETegg 470
Cdd:TIGR04523 300 LNNQKEQDWNKE-----------LKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-QLKKELTNSESENSEKQRE--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 471 tvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSM----ERWKNMEKEHmDAINHDTKELEKMTNRQGM- 545
Cdd:TIGR04523 365 --LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEK-ELLEKEIERLKETIIKNNSe 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 546 ---LLKKKEECMKKIRELGSLPQEAFEKYQTLS---------LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEK 613
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
....*...
gi 40226155 614 LIKRQEEL 621
Cdd:TIGR04523 522 LKEKIEKL 529
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
312-661 |
1.02e-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: 42.70 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 312 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTresl 391
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 392 kaelgtdlLSQLSLEDQKRVDALNDEIRQLQQENRQLlneriklegiitrvetylnENLRKRLDQVEQELNELRETEGGT 471
Cdd:TIGR04523 255 --------LNQLKDEQNKIKKQLSEKQKELEQNNKKI-------------------KELEKQLNQLKSEISDLNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 472 VLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKE 551
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 552 ECMKKIRELGSLPQEAFEKYQTL-----SLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKrqeELDRGYK 626
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKdeqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK---NLDNTRE 464
|
330 340 350
....*....|....*....|....*....|....*
gi 40226155 627 SIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL 661
Cdd:TIGR04523 465 SLETQLKVLS-RSINKIKQNLEQKQKELKSKEKEL 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
340-664 |
1.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 340 RKFKASRDSILSEMKMLKEKRQQSEK------TFMPKQRSLQSLEASLHAMESTRESLKaelgtdllsQLSLEdqkrvda 413
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKelreleKVLKKESELIKLKELAEQLKELEEKLK---------KYNLE------- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 414 lndEIRQLQQENRQLLNERIKLEGIITRVETYLN--ENLRKRLDQVEQELNELREteggtvltattsELEAINKRVKdtm 491
Cdd:PRK03918 519 ---ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEklEELKKKLAELEKKLDELEE------------ELAELLKELE--- 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 492 arsEDLDNSIDKTEAGIKELQKSMERW---KNMEKEHMDAINHDTKELEKMTNRQGMLLKKK---EECMKKIRELGSL-P 564
Cdd:PRK03918 581 ---ELGFESVEELEERLKELEPFYNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEkrlEELRKELEELEKKyS 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 565 QEAFEKY--QTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEA 642
Cdd:PRK03918 658 EEEYEELreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
330 340
....*....|....*....|..
gi 40226155 643 IQLTFKQVSKNFSEVFQKLVPG 664
Cdd:PRK03918 738 KERALSKVGEIASEIFEELTEG 759
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
728-799 |
1.26e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). 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: 213263 [Multi-domain] Cd Length: 239 Bit Score: 41.17 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40226155 728 QLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 799
Cdd:cd03296 136 QLSGGQRQRVALARALAV---EPK-VLLLDEPFGALDAKVRKELRRWLRRL--HDELhVTTVFvthdQEEALEVADR 206
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
448-639 |
1.75e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 448 ENLRKRLDQVEQELNELRETEggtvlTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 527
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 528 AINHDTKELEKMTNRQG-MLLKKKEECMKKIRELGSLpqeafeKYQTLSLKQLFRKLEQCNTELKKyshVNKKALDQFVN 606
Cdd:COG4942 105 ELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYL------KYLAPARREQAEELRADLAELAA---LRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|...
gi 40226155 607 FSEQKEKLIKRQEELDRGYKSIMELMNVLELRK 639
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
727-799 |
1.92e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 41.74 E-value: 1.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40226155 727 QQLSGGQKSLVALA--LIfaiqkCDPaPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADK 799
Cdd:COG2274 610 SNLSGGQRQRLAIAraLL-----RNP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
284-498 |
2.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 284 DTRKSRLELQKDVRKAEEELGELEAKLNENLRRN-IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 362
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 363 SEKT--FMPKQRSLQSLEASLHAMESTRESLKAELGtdllsqlslEDQKRVDALNDEI----RQLQQENRQLLNE-RIKL 435
Cdd:COG3206 252 GPDAlpELLQSPVIQQLRAQLAELEAELAELSARYT---------PNHPDVIALRAQIaalrAQLQQEAQRILASlEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40226155 436 EGIITRVETylnenLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLD 498
Cdd:COG3206 323 EALQAREAS-----LQAQLAQLEARLAELPELE--AELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
258-815 |
2.01e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 258 RAFTMDCITLEGDQVSHRGALTG------GYYDTRKSRLELQKDVRKAEEELGELEAKLNE--NLRRNIERINNEIDQLM 329
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNidaeinKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQilELEGYEMDYNSYLKSIE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 330 NQMQQIETQQRKFKASRDSILSEMKM-------LKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLK---------- 392
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIqeidpdaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSrnmemlngqs 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 393 ------AELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLE--------GIITRVETYLN--ENLRKRLDQ 456
Cdd:PRK01156 454 vcpvcgTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNkiESARADLED 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 457 VEQELNELRETEG--------------GTVLTATTSELEAINKR----VKDTMARSEDLDNSIDKTEAGIKELQKSMERW 518
Cdd:PRK01156 534 IKIKINELKDKHDkyeeiknrykslklEDLDSKRTSWLNALAVIslidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 519 KNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSlpQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNK 598
Cdd:PRK01156 614 KSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKK--QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 599 KALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNvlELRKYEAIQLTFKQVSKNFSevfqklVPGGKATLVMKKGDVEG 678
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLE--SMKKIKKAIGDLKRLREAFD------KSGVPAMIRKSASQAMT 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 679 SQSQDegegsgeseRGSGSQSSVPSVDQFTGVGIRVSftgKQGEMREMQQLSGGQKSLVALALIFAIQK--CDPAPFYLF 756
Cdd:PRK01156 764 SLTRK---------YLFEFNLDFDDIDVDQDFNITVS---RGGMVEGIDSLSGGEKTAVAFALRVAVAQflNNDKSLLIM 831
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40226155 757 DEIDQALDAQHRKAVSDMI----MELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVI 815
Cdd:PRK01156 832 DEPTAFLDEDRRTNLKDIIeyslKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVIPL 894
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
724-800 |
2.14e-03 |
|
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: 40.15 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 724 REMQQLSGGQKSLVALALIFAIqkcdPAPFYLFDEIDQALDAQHRKAVSDMIMElavHAQ----FITTTFRPELLESADK 799
Cdd:COG4133 127 LPVRQLSAGQKRRVALARLLLS----PAPLWLLDEPFTALDAAGVALLAELIAA---HLArggaVLLTTHQPLELAAARV 199
|
.
gi 40226155 800 F 800
Cdd:COG4133 200 L 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
724-778 |
2.18e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 40.74 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 40226155 724 REMQQLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMEL 778
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLAL---NPE-IIIFDESTSMLDPKGKREIKKIMVDL 188
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
729-801 |
2.64e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 40.15 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 729 LSGGQKSLVALALifAI-QKCDpapFYLFDEIDQALDAQhrkaVSDMIME------LAVHAQFITTTFRPELLESADKFY 801
Cdd:cd03250 128 LSGGQKQRISLAR--AVySDAD---IYLLDDPLSAVDAH----VGRHIFEncilglLLNNKTRILVTHQLQLLPHADQIV 198
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
347-434 |
2.82e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 347 DSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENR 426
Cdd:smart00935 7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86
|
....*...
gi 40226155 427 QLLNERIK 434
Cdd:smart00935 87 KRQQEELQ 94
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
727-778 |
3.18e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 41.04 E-value: 3.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 40226155 727 QQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDQALDAQHRKAVSDMIMEL 778
Cdd:COG1123 141 HQLSGGQRQRVAIAMALA---LDPD-LLIADEPTTALDVTTQAEILDLLREL 188
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
9-119 |
3.31e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 9 IKKELKSLDQAINDKKRQIAAIHKDLEdTEAnKEKNLEQYNKLDQDLNEVKARVEELDRKyyeVKNKKDELQSERNYLWR 88
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEAL-LEA-KEEIHKLRNEFEKELRERRNELQKLEKR---LLQKEENLDRKLELLEK 107
|
90 100 110
....*....|....*....|....*....|....
gi 40226155 89 EEN---AEQQALAAKREDLEKKQQLLRAATGKAI 119
Cdd:PRK12704 108 REEeleKKEKELEQKQQELEKKEEELEELIEEQL 141
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
727-779 |
3.50e-03 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 39.55 E-value: 3.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 40226155 727 QQLSGGQKSLVALALIFAIQKcdpaPFYLFDEIDQALDAQHRKAVSDMIMELA 779
Cdd:cd03226 125 LSLSGGQKQRLAIAAALLSGK----DLLIFDEPTSGLDYKNMERVGELIRELA 173
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
724-779 |
3.58e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 3.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 40226155 724 REMQQLSGG--QKSLVALALIfaiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 779
Cdd:PRK13409 208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-120 |
3.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 3 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKE--KNLEQYNKLDQDLNEVKAR-----------------VE 63
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREiaeleaelerldassddLA 688
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 40226155 64 ELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAIL 120
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3-113 |
4.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 3 EERDKWIKKELKSLDQAINDKKRQIAAIHK--DLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQ 80
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110
....*....|....*....|....*....|...
gi 40226155 81 SERNYLwrEENAEQQALAAKREDLEKKQQLLRA 113
Cdd:COG3206 254 DALPEL--LQSPVIQQLRAQLAELEAELAELSA 284
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
726-775 |
4.70e-03 |
|
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: 38.20 E-value: 4.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 40226155 726 MQQLSGGQKSLVALALIFaIQKCDpapFYLFDEIDQALDAQHRKAVSDMI 775
Cdd:cd03221 68 FEQLSGGEKMRLALAKLL-LENPN---LLLLDEPTNHLDLESIEALEEAL 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-114 |
4.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 1 SKEERDKWIKKELKSLDQAINDKKRQIAA--IHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDE 78
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE 178
|
90 100 110
....*....|....*....|....*....|....*.
gi 40226155 79 LQSERNYLWREENAEQQALAAKREDLEKKQQLLRAA 114
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
724-786 |
5.20e-03 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 39.24 E-value: 5.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40226155 724 REMQQLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDQALDAQHRKAVSDMIMELavHAQFIT 786
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAME-----PEVLvLDEPTAGLDPRGRRELLELLKRL--NKEGKT 186
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
314-522 |
5.36e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 314 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKA 393
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 394 ELGTDLLSQLSLEDQKRVDALNdeiRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVL 473
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALD---ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 40226155 474 TATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNME 522
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
11-113 |
5.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 11 KELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLwREE 90
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL-RER 427
|
90 100
....*....|....*....|....
gi 40226155 91 NAEQQA-LAAKREDLEKKQQLLRA 113
Cdd:PRK02224 428 EAELEAtLRTARERVEEAEALLEA 451
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
317-630 |
5.68e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 317 NIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQsektfmpkqrslqsleaslhAMESTREsLKAELG 396
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE--------------------LNAQVKE-LREEAQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 397 tdllsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKR--LDQVEQELNELRETEGGTVLt 474
Cdd:COG1340 61 ---------ELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsIDKLRKEIERLEWRQQTEVL- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 475 aTTSELEAINKRVKDTMARSEDLDNSIDKTEAgIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECM 554
Cdd:COG1340 131 -SPEEEKELVEKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40226155 555 KKIRELGSLPQEAFEKyqtlsLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKlikrqEELDRGYKSIME 630
Cdd:COG1340 209 KEADELHKEIVEAQEK-----ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----EELEEKAEEIFE 274
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
320-524 |
5.77e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 320 RINNEIDQLMNQMQQIETQQRKFKASRD-----------------SILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLH 382
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDeadevleeheerreeleTLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 383 AMESTRESLKAELGTDLLSQLSLEDQ-----KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYlNENLRKRLDQV 457
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER-AEELREEAAEL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40226155 458 EQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKE 524
Cdd:PRK02224 369 ESELEEAREA-----VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
324-514 |
5.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 324 EIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG------- 396
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 397 -----TDLLSQL----SLED-QKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRE 466
Cdd:COG3883 97 rsggsVSYLDVLlgseSFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 40226155 467 TeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKS 514
Cdd:COG3883 176 Q-----QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
724-783 |
6.11e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 39.31 E-value: 6.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 724 REMQQLSGGQKSLVALALIFAiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQ 783
Cdd:cd03237 111 REVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
726-795 |
7.55e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 7.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40226155 726 MQQLSGGQKSLVALALIFAIQkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA-VHAQFITTTFRPELLE 795
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSA-LPKGGLLLIDEPESGLHPKLLRRLLELLKELSrNGAQLILTTHSPLLLD 303
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
292-543 |
7.55e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 292 LQKDVRKAEEELGELEAKLNENLrrNIERINNEI----DQLMNQMQQIETQQRKFKASRDSILSEMKMLKE-KRQQSEKT 366
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNM--STDALEQEIlqvsSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEaRRQLNEIE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 367 fmpkqRSLQSLEASLHAM-ESTRESLKAElgtdllsqlSLEDQKRVDALndEIRQLQQENRQllnERIKLegiitRVETY 445
Cdd:PRK10929 158 -----RRLQTLGTPNTPLaQAQLTALQAE---------SAALKALVDEL--ELAQLSANNRQ---ELARL-----RSELA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 446 --LNENLRKRLDQVEQELNELRETEGGTVLTATtsELEAINkrvkdtmarSEDLDNSIdkteagIKELQKSmerwknmeK 523
Cdd:PRK10929 214 kkRSQQLDAYLQALRNQLNSQRQREAERALEST--ELLAEQ---------SGDLPKSI------VAQFKIN--------R 268
|
250 260
....*....|....*....|
gi 40226155 524 EHMDAINHDTKELEKMTNRQ 543
Cdd:PRK10929 269 ELSQALNQQAQRMDLIASQQ 288
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
473-659 |
7.83e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 39.76 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 473 LTATTSELEAINKRVKDTMARSEDL----------------DNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKEL 536
Cdd:pfam18971 565 LTAKGLSLQEANKLIKDFLSSNKELagkalnfnkavaeaksTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNK 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 537 EKMTNRqGMLLKKKEECMKKIRELGSLPQEAFEKYQTLS--LKQLFRKLEQCNTELKKYShvnkKALDQFVNfseQKEKL 614
Cdd:pfam18971 645 NKMEAK-AQANSQKDEIFALINKEANRDARAIAYTQNLKgiKRELSDKLEKISKDLKDFS----KSFDEFKN---GKNKD 716
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 40226155 615 IKRQEELDRGYK-SIMEL-MNVLELRKYEAIQLTFKQV----SKNFSEVFQ 659
Cdd:pfam18971 717 FSKAEETLKALKgSVKDLgINPEWISKVENLNAALNEFkngkNKDFSKVTQ 767
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
344-466 |
8.45e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 344 ASRDSILSEM--KMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAElgTDLLSQLSLEDQKRVDALNDEIRQL 421
Cdd:COG2433 376 LSIEEALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE--VEELEAELEEKDERIERLERELSEA 453
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 40226155 422 QQENRQLLNERIKLEGIITRvetylNENLRKRLDQVEQELNELRE 466
Cdd:COG2433 454 RSEERREIRKDREISRLDRE-----IERLERELEEERERIEELKR 493
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
316-700 |
9.27e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 39.64 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 316 RNIERINNEIDQLMNQMQQI----ETQQRKFKASRDSILSEMKMLKEKR----QQSEKTFMPKQRSLQSLEASLHAMEST 387
Cdd:PTZ00108 999 YLLGKLERELARLSNKVRFIkhviNGELVITNAKKKDLVKELKKLGYVRfkdiIKKKSEKITAEEEEGAEEDDEADDEDD 1078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 388 RESLKAELGTD-LLSQ----LSLEdqkRVDALNDEIRQLQQENRQLLNeriklegiITRVETYLNEnlrkrLDQVEQELN 462
Cdd:PTZ00108 1079 EEELGAAVSYDyLLSMpiwsLTKE---KVEKLNAELEKKEKELEKLKN--------TTPKDMWLED-----LDKFEEALE 1142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 463 ELRETEggTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNR 542
Cdd:PTZ00108 1143 EQEEVE--EKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS 1220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 543 QGMLL----KKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVN---------KKALDQFVNFSE 609
Cdd:PTZ00108 1221 SGSDQeddeEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSavqysppppSKRPDGESNGGS 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 610 QKEKLIKRQeELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKlvPGGKATLVMKKGDVEGSQSQDEGEGSG 689
Cdd:PTZ00108 1301 KPSSPTKKK-VKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSS--RLLRRPRKKKSDSSSEDDDDSEVDDSE 1377
|
410
....*....|.
gi 40226155 690 ESERGSGSQSS 700
Cdd:PTZ00108 1378 DEDDEDDEDDD 1388
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
312-558 |
9.64e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 312 ENLRRNIERINNEI-------DQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQ---QSEKTFMPKQRSLQSLEASL 381
Cdd:COG1340 25 EELKEKRDELNEELkelaekrDELNAQVKELREEAQELREKRDELNEKVKELKEERDelnEKLNELREELDELRKELAEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 382 HAMESTRESLKAELG----TDLLSQLSLEDQKRvdaLNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQV 457
Cdd:COG1340 105 NKAGGSIDKLRKEIErlewRQQTEVLSPEEEKE---LVEKIKELEKELEKAKKALEKNEKLKELRAEL--KELRKEAEEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40226155 458 EQELNELRETEGGTV--LTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMerwKNMEKEHMDAINHDTKe 535
Cdd:COG1340 180 HKKIKELAEEAQELHeeMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL---RELRKELKKLRKKQRA- 255
|
250 260
....*....|....*....|...
gi 40226155 536 lEKMTNRQGMLLKKKEECMKKIR 558
Cdd:COG1340 256 -LKREKEKEELEEKAEEIFEKLK 277
|
|
| |
