|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-656 |
2.07e-60 |
|
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: 219.55 E-value: 2.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 7 EPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNPRF 83
Cdd:TIGR02169 534 GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDPKY 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 84 DKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNE- 162
Cdd:TIGR02169 613 EPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREl 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 163 -NLRRNIERINNEIDQLMNQMQQIETQQRKfkasrdsILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:TIGR02169 691 sSLQSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KAELG--TDLLSQLSLEDQKRVDALNDE-IRQLQQENRQLLNERIKLEGIITRVETYLN------ENLRKRLDQVEQELN 312
Cdd:TIGR02169 764 EARIEelEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQKLNrltlekEYLEKEIQELQEQRI 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 313 ELRETEggtvlTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNR 392
Cdd:TIGR02169 844 DLKEQI-----KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 393 QGMLLKKKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEEL 471
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL 998
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 472 DRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLvPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssv 551
Cdd:TIGR02169 999 EEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPD-------------------------- 1051
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 552 psvDQFTGvGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVH 631
Cdd:TIGR02169 1052 ---DPFAG-GLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGE 1127
|
650 660
....*....|....*....|....*
gi 34785382 632 AQFITTTFRPELLESADKFYGVKFR 656
Cdd:TIGR02169 1128 AQFIVVSLRSPMIEYADRAIGVTMR 1152
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
569-663 |
4.82e-59 |
|
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: 199.02 E-value: 4.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 569 KQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 648
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
90
....*....|....*
gi 34785382 649 KFYGVKFRNKVSHID 663
Cdd:cd03272 229 KFYGVKFRNKVSTID 243
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
49-661 |
1.42e-47 |
|
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: 181.32 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 49 VTFLPLNKLDVRDTAYPETNDAIPMISkLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGAL 128
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKS-IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 129 TGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMlKE 208
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL-LA 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 209 KRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQEnrqllneriKLEGI 288
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE---------EKEEK 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 289 ITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINK--RVKDTMARSEDLDNSIDKTEAGIKELQKSME 366
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 367 RWKNMEKEHMDAINHdtKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEK--------YQTLSLKQLFRKLEQCNT 438
Cdd:pfam02463 876 EEELEEQKLKDELES--KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAeillkyeeEPEELLLEEADEKEKEEN 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 439 ELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPggkat 518
Cdd:pfam02463 954 NKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS----- 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 519 lvMKKGDVEGSQSqDEGEGSGESErgsgsqssVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKC 598
Cdd:pfam02463 1029 --INKGWNKVFFY-LELGGSAELR--------LEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKY 1097
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34785382 599 DPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKF-RNKVSH 661
Cdd:pfam02463 1098 KPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMvENGVST 1161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-662 |
1.96e-47 |
|
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: 181.02 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLR----- 78
Cdd:TIGR02168 529 ISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakdl 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 79 --YNPRFDKAFKHVFGKTLICRSMEVSTQLARA--FTMDCITLEGDQVSHRGALTGGYYDTRKSRL-------ELQKDVR 147
Cdd:TIGR02168 608 vkFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrreieELEEKIE 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 148 KAEEELGELEAKLNEnLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTF-------MPK 220
Cdd:TIGR02168 688 ELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeiEEL 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 221 QRSLQSLEASLHAMESTRESLKAELgTDLLSQLSLEDqKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENL 300
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRL-EDL 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 301 RKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKsmerwKNMEKEHmdA 378
Cdd:TIGR02168 844 EEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-----KRSELRR--E 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 379 INHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQE---AFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFV 455
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 456 NFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqDEG 535
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPE-------DLL 1069
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 536 EgsgesergsgsqssvpsvdqfTGVGIRVSFTGKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDA 615
Cdd:TIGR02168 1070 E---------------------AGIEIFAQPPGKK--NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDD 1126
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 34785382 616 QHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNK-VSHI 662
Cdd:TIGR02168 1127 ANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKgVSKI 1174
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
526-661 |
6.89e-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: 138.98 E-value: 6.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 526 VEGSQSQDEGEGSGESERGSGSQSSVPSVDqftgVGI----RVSFTgKQGEMREMqqLSGGQKSLVALALIFAIQKCDPA 601
Cdd:cd03239 45 VLGGKAAKLRRGSLLFLAGGGVKAGINSAS----VEItfdkSYFLV-LQGKVEQI--LSGGEKSLSALALIFALQEIKPS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34785382 602 PFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFRNKVSH 661
Cdd:cd03239 118 PFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVHGVST 178
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-653 |
1.21e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.90 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 243 AELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRE-TEGGT 321
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvTLEGE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 322 VLTATTSELEAINKRVKDT----MARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLL 397
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAAlleaEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 398 KKKEECMKKIRELgSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKS 477
Cdd:COG1196 735 EELLEELLEEEEL-LEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARET 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 478 IMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF 557
Cdd:COG1196 814 LEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTDPD-----------------------------DPL 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 558 -TGVGIRVSFTGKqgEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQ--HRkaVSDMIMELAVHAQF 634
Cdd:COG1196 865 eTGIEIMAQPPGK--KLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQF 940
|
410
....*....|....*....
gi 34785382 635 ITTTFRPELLESADKFYGV 653
Cdd:COG1196 941 IVITHNKRTMEAADRLYGV 959
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
578-657 |
1.38e-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: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 578 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFR 656
Cdd:cd03227 77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 34785382 657 N 657
Cdd:cd03227 157 I 157
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
4-106 |
2.13e-25 |
|
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: 101.54 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYPETNDAIPMIS 75
Cdd:smart00968 11 ISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLPEPGFVGPAID 89
|
90 100 110
....*....|....*....|....*....|.
gi 34785382 76 KLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 106
Cdd:smart00968 90 LVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
568-660 |
9.52e-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: 99.08 E-value: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 568 GKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 647
Cdd:cd03278 105 GKK--VQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAA 182
|
90
....*....|....
gi 34785382 648 DKFYGVKFRNK-VS 660
Cdd:cd03278 183 DRLYGVTMQESgVS 196
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
4-107 |
1.65e-21 |
|
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: 90.01 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAIPMISKLRYNP 81
Cdd:pfam06470 12 IEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAGPLLDLVEYDD 90
|
90 100
....*....|....*....|....*.
gi 34785382 82 RFDKAFKHVFGKTLICRSMEVSTQLA 107
Cdd:pfam06470 91 EYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
578-663 |
2.59e-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: 85.04 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 578 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRN 657
Cdd:cd03273 166 ELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVD 245
|
....*.
gi 34785382 658 KVSHID 663
Cdd:cd03273 246 GTSTVT 251
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
574-662 |
4.30e-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: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 574 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAV-HAQFITTTFRPELLESADKFYG 652
Cdd:cd03275 151 RDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADALVG 230
|
90
....*....|...
gi 34785382 653 VkFRNK---VSHI 662
Cdd:cd03275 231 V-YRDQecnSSKV 242
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
574-653 |
1.23e-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: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 574 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGV 653
Cdd:cd03274 123 KNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGI 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
578-654 |
1.73e-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: 1.73e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34785382 578 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLE-SADKFYGVK 654
Cdd:cd00267 80 QLSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLK 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-473 |
7.26e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 165 RRNIERINNEIDQLMNQMQQIETQQRK------FKASRDSILSEMKMLKEKRQQSEktfmpkqrsLQSLEASLHAMESTR 238
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAE---------LEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 239 ESLKAELgtDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETyLNENLRKRLDQVEQELNELRETE 318
Cdd:COG1196 256 EELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 319 GG--TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 396
Cdd:COG1196 333 EEleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34785382 397 LKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQcNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDR 473
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-528 |
2.66e-10 |
|
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: 63.93 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQqrKFKASRDSILSEMKmlkEKRQQSEKTfmpkqRSLQSLEASLHAMESTRESL 241
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEK---REYEGYELL-----KEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KAELGtdllsqlslEDQKRVDALNDEIRQLQQENRQLlNERIKLEGIITRVEtylnenLRKRLDQVEQELNELRETeggt 321
Cdd:TIGR02169 250 EEELE---------KLTEEISELEKRLEEIEQLLEEL-NKKIKDLGEEEQLR------VKEKIGELEAEIASLERS---- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 322 vltattseLEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKK-- 399
Cdd:TIGR02169 310 --------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfa 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 400 ---------KEECMKKIRELGSLPQEAFEKYQTlsLKQLFRKLEQCNTELkkyshvnKKALDQFVNFSEQKEKLIKRQEE 470
Cdd:TIGR02169 382 etrdelkdyREKLEKLKREINELKRELDRLQEE--LQRLSEELADLNAAI-------AGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34785382 471 LDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL-------------VPGGKATLVMKKGDVEG 528
Cdd:TIGR02169 453 QEWKLEQLAADLSKYE-QELYDLKEEYDRVEKELSKLQRELaeaeaqaraseerVRGGRAVEEVLKASIQG 522
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
565-635 |
5.49e-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: 56.45 E-value: 5.49e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34785382 565 SF-TGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFI 635
Cdd:cd03276 95 SFlTSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAkkqPGRQFI 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-493 |
5.58e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 163 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 239
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 240 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 319
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 320 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 394
Cdd:PRK03918 318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 395 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 460
Cdd:PRK03918 396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474
|
330 340 350
....*....|....*....|....*....|...
gi 34785382 461 KEKLIKRQEELDrgyksiMELMNVLELRKYEAI 493
Cdd:PRK03918 475 ERKLRKELRELE------KVLKKESELIKLKEL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-492 |
5.72e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRK-----------FKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEAS 230
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaelRELELALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 231 LHAMESTRESLKAELGTdlLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKR------L 304
Cdd:TIGR02168 262 LQELEEKLEELRLEVSE--LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLdelaeeL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 305 DQVEQELNELRE---------TEGGTVLTATTS-------ELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERW 368
Cdd:TIGR02168 340 AELEEKLEELKEelesleaelEELEAELEELESrleeleeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 369 K-NMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLsLKQLFRKLEQCNTELkkysHVN 447
Cdd:TIGR02168 420 QqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA-LDAAERELAQLQARL----DSL 494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 34785382 448 KKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLElrKYEA 492
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE--GYEA 537
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-424 |
1.14e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KAELGTDLLSQLSLE-----DQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRE 316
Cdd:COG1196 315 EERLEELEEELAELEeeleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 317 TEggtvltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 396
Cdd:COG1196 395 AA------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260
....*....|....*....|....*...
gi 34785382 397 LKKKEECMKKIRELGSLPQEAFEKYQTL 424
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
259-677 |
1.15e-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: 55.12 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 259 KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlrkrLDQVEQELNELRETEGGTVLTattSELEAINKRVK 338
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEE-----LEEADLQPGEDEALEAEQQRL---SNLEKLRELSQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 339 DTMAR-SEDLDNSIDKTEAGIKELQKSMErwknmekehmdaiNHDTKELEKMTNRQGMLLKKKEECMKKIRELGS----L 413
Cdd:TIGR00634 233 NALAAlRGDVDVQEGSLLEGLGEAQLALA-------------SVIDGSLRELAEQVGNALTEVEEATRELQNYLDelefD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 414 PQEAFEKYQTLS-LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYksIMELMNVLELRKYEA 492
Cdd:TIGR00634 300 PERLNEIEERLAqIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEEL--DKAAVALSLIRRKAA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 493 iqltfKQVSKNFSEVFQKLvpggkaTLVMKKGDVEGSQSQDEGEGSGESERGsgsqssvpsVDQftgvgIRVSFTGKQGE 572
Cdd:TIGR00634 378 -----ERLAKRVEQELKAL------AMEKAEFTVEIKTSLPSGAKARAGAYG---------ADQ-----VEFLFSANTGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 573 mrEMQQL----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 648
Cdd:TIGR00634 433 --PVKPLakvaSGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHAD 510
|
410 420
....*....|....*....|....*....
gi 34785382 649 KFYGVKfrnKVShIDVITAEMAKDFVEDD 677
Cdd:TIGR00634 511 AHFKVE---KEG-LDGRTATRVRPLSGEE 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
206-473 |
2.78e-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: 53.91 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 206 LKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLK--AELGTDL------LSQLSLEDQ-KRVDALNDEIRQLQQENR 276
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLErqAEKAERYkelkaeLRELELALLvLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 277 QLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEA 356
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKE-----LYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 357 GIKELQKSmerwknmekehmdaINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKyqtlsLKQLFRKLEQC 436
Cdd:TIGR02168 324 QLEELESK--------------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-----LEELEEQLETL 384
|
250 260 270
....*....|....*....|....*....|....*..
gi 34785382 437 NTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDR 473
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
133-451 |
2.85e-07 |
|
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: 54.28 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 133 YDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 212
Cdd:TIGR00606 205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 213 SEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKL------- 285
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV-----DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrh 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 286 -EGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEA--INKRVKDTMARSEDLDNSIDKTEAGIKELQ 362
Cdd:TIGR00606 360 qEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 363 KSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEA----------FEKYQTLSLKQLFRK 432
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltetlkkevkSLQNEKADLDRKLRK 519
|
330
....*....|....*....
gi 34785382 433 LEQCNTELKKYSHVNKKAL 451
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQME 538
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
162-510 |
1.02e-06 |
|
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: 52.36 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEmkmlkeKRQQSEKTFmpKQRSLQSLEASLHAMESTRESL 241
Cdd:TIGR01612 934 EKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLID------KINELDKAF--KDASLNDYEAKNNELIKYFNDL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-----------KLEGIITRVETYLNENLRKRLDQVEQE 310
Cdd:TIGR01612 1006 KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniidEIEKEIGKNIELLNKEILEEAEINITN 1085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 311 LNELRETEGGTVLTATTSE-----LEAINKrVKDTMarsEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAI------ 379
Cdd:TIGR01612 1086 FNEIKEKLKHYNFDDFGKEenikyADEINK-IKDDI---KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLedvadk 1161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 380 ---NHDTKELE-KMTNRQGMLLKKK---EECMKKIRELGSLP--QEAFEKYQTL------SLKQLFrkLEQCNTELKKYS 444
Cdd:TIGR01612 1162 aisNDDPEEIEkKIENIVTKIDKKKniyDEIKKLLNEIAEIEkdKTSLEEVKGInlsygkNLGKLF--LEKIDEEKKKSE 1239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34785382 445 HVNKKALDQFVNFSEQKEK--LIKRQEELDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQK 510
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISH-DDDKDHHIISKKHDENISDIREK 1306
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
161-483 |
1.35e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 161 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 240
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 241 LKAELGTDLLS----QLSLEDQKR--------VDALNDEIRQLQQENRQL------LNERI-KLEGIITRVETYL----- 296
Cdd:TIGR04523 466 LETQLKVLSRSinkiKQNLEQKQKelkskekeLKKLNEEKKELEEKVKDLtkkissLKEKIeKLESEKKEKESKIsdled 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 297 ----------NENLRKRLDQVEQELNELRETEggTVLTATTSELEainKRVKDTMARSEDLDNSIDKTEAGIKELQKSME 366
Cdd:TIGR04523 546 elnkddfelkKENLEKEIDEKNKEIEELKQTQ--KSLKKKQEEKQ---ELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 367 rwkNMEKEHMDaINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSlpqEAFEKYQTLSLK-----QLFRK-LEQCNTEL 440
Cdd:TIGR04523 621 ---KAKKENEK-LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP---EIIKKIKESKTKiddiiELMKDwLKELSLHY 693
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 34785382 441 KKY--SHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMN 483
Cdd:TIGR04523 694 KKYitRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
568-649 |
6.03e-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: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 568 GKQGEMremqqLSGGQKSLVALALIFaiqkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 647
Cdd:TIGR02857 453 GEGGAG-----LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
..
gi 34785382 648 DK 649
Cdd:TIGR02857 524 DR 525
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
134-363 |
6.16e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 134 DTRKSRLELQKDVRKAEEELGELEAKLNEnLRRNIERINNEIDQLMnqmQQIETQQRKFKASRDSILSEMKMLKEKRQQS 213
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 214 EKTFMPKQRSLQSLEASLHamestreslkaelgtdLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 293
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQ----------------YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 294 TylnenLRKRLDQVEQELNELreteggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQK 363
Cdd:COG4942 185 E-----ERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
569-654 |
8.58e-06 |
|
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: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 569 KQGE-----MREMQQLSGGQKSLVALALIFAIQK--CDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFITTT 638
Cdd:cd03240 101 HQGEsnwplLDMRGRCSGGEKVLASLIIRLALAEtfGSNCGILALDEPTTNLDEENIEESLAEIIEERksqKNFQLIVIT 180
|
90
....*....|....*.
gi 34785382 639 FRPELLESADKFYGVK 654
Cdd:cd03240 181 HDEELVDAADHIYRVE 196
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
161-471 |
1.06e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 161 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILsemKMLKEKRQQSEKTfmpkQRSLQSLEASLHAMESTRES 240
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQN----NKKIKELEKQLNQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 241 LKAELGTDLLSQlsledqkrvdaLNDEIRQLQQENRQLLNERIKLEGIITRVETYLNeNLRKRLDQVEQELNELRETegg 320
Cdd:TIGR04523 300 LNNQKEQDWNKE-----------LKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-QLKKELTNSESENSEKQRE--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 321 tvLTATTSELEAINKR-------VKDTMARSEDLDNSIDKTEAGIKELQ---KSMERWKN-MEKEHMDAINHDTKELEKM 389
Cdd:TIGR04523 365 --LEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDeqiKKLQQEKElLEKEIERLKETIIKNNSEI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 390 TNrqgmLLKKKEECMKKIRELGSLPQEAFEKYQTLS---------LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQ 460
Cdd:TIGR04523 443 KD----LTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
330
....*....|.
gi 34785382 461 KEKLIKRQEEL 471
Cdd:TIGR04523 519 ISSLKEKIEKL 529
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
564-629 |
1.19e-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: 46.82 E-value: 1.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34785382 564 VSFtgKQGEmrEMQQL-----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 629
Cdd:cd03277 111 VKF--REGE--QLQELdphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETA 177
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
162-511 |
1.63e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLhamESTRESL 241
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTTEI---SNTQTQL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KaelgtdllsQLSLEDQKRVDALNDEIRQLQQENRQLlneriklegiitrvetylnENLRKRLDQVEQELNELRETEGGT 321
Cdd:TIGR04523 256 N---------QLKDEQNKIKKQLSEKQKELEQNNKKI-------------------KELEKQLNQLKSEISDLNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 322 VLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKE 401
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 402 ECMKKIRELGSLPQEAFEKYQTL-----SLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKrqeELDRGYK 476
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKdeqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK---NLDNTRE 464
|
330 340 350
....*....|....*....|....*....|....*
gi 34785382 477 SIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL 511
Cdd:TIGR04523 465 SLETQLKVLS-RSINKIKQNLEQKQKELKSKEKEL 498
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
162-483 |
1.96e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEM--KMLKEKRQQSEKtfmPKQRSLQSLEASLHAMESTRE 239
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKKRFSLLK---KETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 240 sLKAELGT-DLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-KLEGIITRVETylnENLRKRLDQVEQELNELRET 317
Cdd:COG5022 887 -LKIDVKSiSSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIaRLKKLLNNIDL---EEGPSIEYVKLPELNKLHEV 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 318 EGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH-------------MDAINHDTK 384
Cdd:COG5022 963 ESK--LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLkelpvevaelqsaSKIISSEST 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 385 ELEKMTNRQ---GMLLKKKEECMKKIRELG----SLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNF 457
Cdd:COG5022 1041 ELSILKPLQklkGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120
|
330 340
....*....|....*....|....*.
gi 34785382 458 SEQKEKLIKRQEELDRGYKSIMELMN 483
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVF 1146
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
190-667 |
2.02e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 190 RKFKASRDSILSEMKMLKEKRQQSEK------TFMPKQRSLQSLEASLHAMESTRESLKaelgtdllsQLSLEdqkrvda 263
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKelreleKVLKKESELIKLKELAEQLKELEEKLK---------KYNLE------- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 264 lndEIRQLQQENRQLLNERIKLEGIITRVETYLN--ENLRKRLDQVEQELNELREteggtvltattsELEAINKRVKdtm 341
Cdd:PRK03918 519 ---ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEklEELKKKLAELEKKLDELEE------------ELAELLKELE--- 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 342 arsEDLDNSIDKTEAGIKELQKSMERW---KNMEKEHMDAINHDTKELEKMTNRQGMLLKKK---EECMKKIRELGSL-- 413
Cdd:PRK03918 581 ---ELGFESVEELEERLKELEPFYNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEkrlEELRKELEELEKKys 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 414 ---PQEAFEKYQTLSlKQLFRKLEQCNtELKKYSHVNKKALDqfvNFSEQKEKLIKRQEELDRGYKSIMELMNVLE-LRK 489
Cdd:PRK03918 658 eeeYEELREEYLELS-RELAGLRAELE-ELEKRREEIKKTLE---KLKEELEEREKAKKELEKLEKALERVEELREkVKK 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 490 YEAI--QLTFKQVSKNFSEVFQKLVPGGKATLVMKKgdvegsqsqdegegsgESERgsgsqssvpsvdqftgvgIRVsFT 567
Cdd:PRK03918 733 YKALlkERALSKVGEIASEIFEELTEGKYSGVRVKA----------------EENK------------------VKL-FV 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 568 GKQGEMREMQQLSGGQKslVALALIF----AIQKCDPAPFYLFDEIDQALDAQHRKAVSDmIME--LAVHAQFITTTFRP 641
Cdd:PRK03918 778 VYQGKERPLTFLSGGER--IALGLAFrlalSLYLAGNIPLLILDEPTPFLDEERRRKLVD-IMEryLRKIPQVIIVSHDE 854
|
490 500
....*....|....*....|....*.
gi 34785382 642 ELLESADKFYGVKFRNKVSHIDVITA 667
Cdd:PRK03918 855 ELKDAADYVIRVSLEGGVSKVEVVSL 880
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-367 |
2.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSIlsemkmlkekRQQSEKTFMpkQRSLQSLEASLHAMESTRESL 241
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KAelgtdllsqlsleDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVEtylnenlrKRLDQVEQELNELRETEGGT 321
Cdd:COG4913 681 DA-------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------KELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 34785382 322 VLTATTSELEAINKRVKDTMAR------SEDLDNSIDKTEAGIKELQKSMER 367
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELER 791
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
172-360 |
2.42e-05 |
|
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: 46.07 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 172 NNEIDQLMnQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLS 251
Cdd:COG1579 3 PEDLRALL-DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 252 QLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIItrvetylnENLRKRLDQVEQELNELRETeggtvLTATTSELE 331
Cdd:COG1579 82 LGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERI--------EELEEELAELEAELAELEAE-----LEEKKAELD 148
|
170 180
....*....|....*....|....*....
gi 34785382 332 AInkrVKDTMARSEDLDNSIDKTEAGIKE 360
Cdd:COG1579 149 EE---LAELEAELEELEAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-511 |
2.80e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdsilSEMKMLKEKRQQSEKtFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KAELGTdlLSQLSLEDQKRVDALND---EIRQLQQENRQLLNERIKLEgiiTRVETYlnenlrKRLDQVEQELNELRETE 318
Cdd:PRK03918 313 EKRLSR--LEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELE---ERHELY------EEAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 319 GGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNM------------EKEHMDAINHDTKEL 386
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 387 EKMTNRqgmlLKKKEECMKKIR-ELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYshvNKKALDQ-FVNFSEQKEKL 464
Cdd:PRK03918 462 KRIEKE----LKEIEEKERKLRkELRELEKVLKKESELIKLKELAEQLKELEEKLKKY---NLEELEKkAEEYEKLKEKL 534
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 34785382 465 IKRQEELdRGYKSIMELMNVLELRKyEAIQLTFKQVSKNFSEVFQKL 511
Cdd:PRK03918 535 IKLKGEI-KSLKKELEKLEELKKKL-AELEKKLDELEEELAELLKEL 579
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
206-367 |
3.55e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 206 LKEKRQQSEKT--FMPKQrsLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI 283
Cdd:COG3206 166 LELRREEARKAleFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 284 KLEGIITRVETYLNE--------NLRKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARS-EDLDNSID 352
Cdd:COG3206 244 ALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSAryTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323
|
170
....*....|....*
gi 34785382 353 KTEAGIKELQKSMER 367
Cdd:COG3206 324 ALQAREASLQAQLAQ 338
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
579-651 |
5.81e-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: 5.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34785382 579 LSGGQKSLVALALIFaIQKcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFY 651
Cdd:cd03228 97 LSGGQRQRIAIARAL-LRD---PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
164-496 |
8.22e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 164 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMpkqRSLQSLEASLHAMESTRESLKa 243
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAK- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 244 ELGTDLLSQLsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlRKRLDQVEQELNEL---RETEGG 320
Cdd:pfam15921 338 RMYEDKIEEL----EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 321 TVLTATTSELEAINKRVKdtmaRSEDLDNSIDkteagiKELQKSMERwknmekeHMDAINHDTKELEKMTNRQGMLLKKK 400
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQ----RLEALLKAMK------SECQGQMER-------QMAAIQGKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 401 EECMKKIRELGS--LPQEAFEKY---QTLSLKQLFRKLEQCNTELKKY-SHVNKKaLDQFVNFSEQKEKLIKRQEELDRG 474
Cdd:pfam15921 475 EMLRKVVEELTAkkMTLESSERTvsdLTASLQEKERAIEATNAEITKLrSRVDLK-LQELQHLKNEGDHLRNVQTECEAL 553
|
330 340
....*....|....*....|..
gi 34785382 475 YKSIMELMNVLELRKYEAIQLT 496
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMT 575
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
108-665 |
9.94e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 108 RAFTMDCITLEGDQVSHRGALTG------GYYDTRKSRLELQKDVRKAEEELGELEAKLNE--NLRRNIERINNEIDQLM 179
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNidaeinKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQilELEGYEMDYNSYLKSIE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 180 NQMQQIETQQRKFKASRDSILSEMKM-------LKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLK---------- 242
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIqeidpdaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSrnmemlngqs 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 243 ------AELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLE--------GIITRVETYLN--ENLRKRLDQ 306
Cdd:PRK01156 454 vcpvcgTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNkiESARADLED 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 307 VEQELNELRETEG--------------GTVLTATTSELEAINKR----VKDTMARSEDLDNSIDKTEAGIKELQKSMERW 368
Cdd:PRK01156 534 IKIKINELKDKHDkyeeiknrykslklEDLDSKRTSWLNALAVIslidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 369 KNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSlpQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNK 448
Cdd:PRK01156 614 KSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKK--QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 449 KALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNvlELRKYEAIQLTFKQVSKNFSevfqklVPGGKATLVMKKGDVEG 528
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLE--SMKKIKKAIGDLKRLREAFD------KSGVPAMIRKSASQAMT 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 529 SQSQDegegsgeseRGSGSQSSVPSVDQFTGVGIRVSftgkQGEMRE-MQQLSGGQKSLVALALIFAIQK--CDPAPFYL 605
Cdd:PRK01156 764 SLTRK---------YLFEFNLDFDDIDVDQDFNITVS----RGGMVEgIDSLSGGEKTAVAFALRVAVAQflNNDKSLLI 830
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34785382 606 FDEIDQALDAQHRKAVSDMIM----ELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVI 665
Cdd:PRK01156 831 MDEPTAFLDEDRRTNLKDIIEyslkDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVIPL 894
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
167-480 |
1.04e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 167 NIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQsektfmpkqrslqsleaslhAMESTREsLKAELG 246
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE--------------------LNAQVKE-LREEAQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 247 tdllsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKR--LDQVEQELNELRETEGGTVLt 324
Cdd:COG1340 61 ---------ELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsIDKLRKEIERLEWRQQTEVL- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 325 aTTSELEAINKRVKDTMARSEDLDNSIDKTEAgIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECM 404
Cdd:COG1340 131 -SPEEEKELVEKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34785382 405 KKIRELGSLPQEAFEKyqtlsLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKlikrqEELDRGYKSIME 480
Cdd:COG1340 209 KEADELHKEIVEAQEK-----ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----EELEEKAEEIFE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-412 |
1.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 167 NIERINNEIDQLMNQMQQIETQQRKFKAsrdsiLSEMKMLKEKRQQsektfmpkqrsLQSLEASLHAMESTRESLKAELG 246
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 247 TDLLsqlsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELREteggtvltat 326
Cdd:COG4913 290 LELL-------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 327 tsELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINhdtKELEKMTNRQGMLLKKKEECMKK 406
Cdd:COG4913 353 --ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAE 427
|
....*.
gi 34785382 407 IRELGS 412
Cdd:COG4913 428 IASLER 433
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
574-636 |
1.31e-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: 1.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34785382 574 REMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQFIT 636
Cdd:cd03225 130 RSPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKL--KAEGKT 186
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
256-470 |
1.41e-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: 44.75 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 256 EDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINK 335
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAE-----LAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 336 RVKDTMARSEDLDNSIDKT-EAGIKELQKSMERWKNMEK--EHMDAIN-HDTKELEKMTNRQGMLLKKKEECMKKIRELG 411
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRrlQYLKYLApARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34785382 412 SLPQEAFEKYQTLSLKQLFRK--LEQCNTELKKYshvnKKALDQFVNFSEQKEKLIKRQEE 470
Cdd:COG4942 178 ALLAELEEERAALEALKAERQklLARLEKELAEL----AAELAELQQEAEELEALIARLEA 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
574-635 |
1.42e-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: 43.89 E-value: 1.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34785382 574 REMQQLSGGQKSLVALAlIFAIQKCDpapFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 635
Cdd:cd03236 135 RNIDQLSGGELQRVAIA-AALARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
199-433 |
1.48e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 199 ILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG----TDLLSQLSLEDQKRVDALNDEIRQLQQE 274
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaeMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 275 NRQLLNERIKLEGIITRVETY-----LNENLRKRLDQVEQELNELR-----ETEGGTVLTATTSELEAInkRVKDTMARS 344
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMrelerLQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEMEQI--RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 345 EDLDNSIDKTEAGIKEL-QKSMERWKNMEKEHMDAINHDTKELEKmtNRQGMLLKKKEECMKKIRElgslpQEAFEKYQT 423
Cdd:pfam17380 435 REVRRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLEL--EKEKRDRKRAEEQRRKILE-----KELEERKQA 507
|
250
....*....|
gi 34785382 424 LSLKQLFRKL 433
Cdd:pfam17380 508 MIEEERKRKL 517
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
164-372 |
2.39e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 164 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKA 243
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 244 ELGTDLLSQLSLEDQKRVDALNdeiRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVL 323
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALD---ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 34785382 324 TATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNME 372
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
162-408 |
2.61e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEI-------DQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQ---QSEKTFMPKQRSLQSLEASL 231
Cdd:COG1340 25 EELKEKRDELNEELkelaekrDELNAQVKELREEAQELREKRDELNEKVKELKEERDelnEKLNELREELDELRKELAEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 232 HAMESTRESLKAELG----TDLLSQLSLEDQKRvdaLNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQV 307
Cdd:COG1340 105 NKAGGSIDKLRKEIErlewRQQTEVLSPEEEKE---LVEKIKELEKELEKAKKALEKNEKLKELRAEL--KELRKEAEEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 308 EQELNELRETEGGTV--LTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMerwKNMEKEHMDAINHDTKe 385
Cdd:COG1340 180 HKKIKELAEEAQELHeeMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL---RELRKELKKLRKKQRA- 255
|
250 260
....*....|....*....|...
gi 34785382 386 lEKMTNRQGMLLKKKEECMKKIR 408
Cdd:COG1340 256 -LKREKEKEELEEKAEEIFEKLK 277
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
578-649 |
3.62e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.15 E-value: 3.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34785382 578 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 649
Cdd:PRK10851 136 QLSGGQKQRVALARALAVE----PQILLLDEPFGALDAQVRKELRRWLRQL--HEELkFTSVFvthdQEEAMEVADR 206
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
298-489 |
4.05e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 298 ENLRKRLDQVEQELNELRETEggtvlTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 377
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 378 AINHDTKELEKMTNRQG-MLLKKKEECMKKIRELGSLpqeafeKYQTLSLKQLFRKLEQCNTELKKyshVNKKALDQFVN 456
Cdd:COG4942 105 ELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYL------KYLAPARREQAEELRADLAELAA---LRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|...
gi 34785382 457 FSEQKEKLIKRQEELDRGYKSIMELMNVLELRK 489
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
197-298 |
7.34e-04 |
|
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: 40.26 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 197 DSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENR 276
Cdd:smart00935 7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86
|
90 100
....*....|....*....|..
gi 34785382 277 QLLNERIKleGIITRVETYLNE 298
Cdd:smart00935 87 KRQQEELQ--KILDKINKAIKE 106
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
174-364 |
9.06e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 174 EIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG------- 246
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 247 -----TDLLSQL----SLED-QKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRE 316
Cdd:COG3883 97 rsggsVSYLDVLlgseSFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 34785382 317 TeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKS 364
Cdd:COG3883 176 Q-----QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
578-649 |
9.62e-04 |
|
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: 41.56 E-value: 9.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34785382 578 QLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 649
Cdd:cd03296 136 QLSGGQRQRVALARALAV---EPK-VLLLDEPFGALDAKVRKELRRWLRRL--HDELhVTTVFvthdQEEALEVADR 206
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
134-348 |
1.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 134 DTRKSRLELQKDVRKAEEELGELEAKLNENLRRN-IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 212
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 213 SEKT--FMPKQRSLQSLEASLHAMESTRESLKAELGtdllsqlslEDQKRVDALNDEI----RQLQQENRQLLNE-RIKL 285
Cdd:COG3206 252 GPDAlpELLQSPVIQQLRAQLAELEAELAELSARYT---------PNHPDVIALRAQIaalrAQLQQEAQRILASlEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34785382 286 EGIITRVETylnenLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLD 348
Cdd:COG3206 323 EALQAREAS-----LQAQLAQLEARLAELPELE--AELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
574-628 |
1.16e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.51 E-value: 1.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 34785382 574 REMQQLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMEL 628
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLAL---NPE-IIIFDESTSMLDPKGKREIKKIMVDL 188
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
323-509 |
1.54e-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: 41.68 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 323 LTATTSELEAINKRVKDTMARSEDL----------------DNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKEL 386
Cdd:pfam18971 565 LTAKGLSLQEANKLIKDFLSSNKELagkalnfnkavaeaksTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNK 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 387 EKMTNRqGMLLKKKEECMKKIRELGSLPQEAFEKYQTLS--LKQLFRKLEQCNTELKKYShvnkKALDQFVNfseQKEKL 464
Cdd:pfam18971 645 NKMEAK-AQANSQKDEIFALINKEANRDARAIAYTQNLKgiKRELSDKLEKISKDLKDFS----KSFDEFKN---GKNKD 716
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34785382 465 IKRQEELDRGYK-SIMEL-MNVLELRKYEAIQLTFKQV----SKNFSEVFQ 509
Cdd:pfam18971 717 FSKAEETLKALKgSVKDLgINPEWISKVENLNAALNEFkngkNKDFSKVTQ 767
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
178-575 |
1.61e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.63 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 178 LMNQMQQIETQQRKFKASRDSILSEmkmLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGtdlLSQLSLED 257
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAE---FNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLA---LARAEMEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 258 QKRVDALNDEIRQ--LQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETeggtvltaTTSELEAINK 335
Cdd:pfam03528 80 IKAVATVSENTKQeaIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYRES--------AEREIADLRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 336 RVKDTMaRSEDLDNSIDKTEAGIKELQK---SMERWKNMEKEHMDAINHDTKELE--KMTNRQGMLLKKK------EECM 404
Cdd:pfam03528 152 RLSEGQ-EEENLEDEMKKAQEDAEKLRSvvmPMEKEIAALKAKLTEAEDKIKELEasKMKELNHYLEAEKscrtdlEMYV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 405 KKIRELGSLPQEAFEKYQTlSLKQLFRKLEQCNTELKKYSHVNKKALDQFVnfseQKEKLIKRQEELDRGYKSIMELMNV 484
Cdd:pfam03528 231 AVLNTQKSVLQEDAEKLRK-ELHEVCHLLEQERQQHNQLKHTWQKANDQFL----ESQRLLMRDMQRMESVLTSEQLRQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 485 LELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSGESERGsgsqsSVPSVDQFTGVGIRV 564
Cdd:pfam03528 306 EEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAHG-----SVHSLDTDVVLGAGD 380
|
410
....*....|.
gi 34785382 565 SFTGKQGEMRE 575
Cdd:pfam03528 381 SFNKQEDPFKE 391
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
162-491 |
1.65e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLmnQMQQIETQQR--------KFKASRDSILSEMK--------MLKEKRQ-----------QSE 214
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQL--KIITMELQKKsseleemtKFKNNKEVELEELKkilaedekLLDEKKQfekiaeelkgkEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 215 KTFM--PKQRSLQSLEASLHAMESTRE-------SLKAELGTDLL---------SQLSLEDQKRVDALNDEIRQLQQENR 276
Cdd:pfam05483 441 LIFLlqAREKEIHDLEIQLTAIKTSEEhylkeveDLKTELEKEKLknieltahcDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 277 QLLNERIKLEGIITRVETYLNE--NLRKRLDQVEQELNELREteggtvltattseleainkRVKDTMARSEDLDNSIDKT 354
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEEKemNLRDELESVREEFIQKGD-------------------EVKCKLDKSEENARSIEYE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 355 EAGIKELQKSMERWKNMEKEHMDAINHDTKELEKmtnrQGMLLKKKEECMKKIRELGSLPQEAFEkYQTLSLKQLFRKLE 434
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ----ENKALKKKGSAENKQLNAYEIKVNKLE-LELASAKQKFEEII 656
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34785382 435 ---QCNTELKKYSHvnKKALDQFVNFSEQKEKLIKRQEELD-RGYKSIMELMNVLELRKYE 491
Cdd:pfam05483 657 dnyQKEIEDKKISE--EKLLEEVEKAKAIADEAVKLQKEIDkRCQHKIAEMVALMEKHKHQ 715
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
574-650 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 574 REMQQLSGGQKSLVALALIFAIqkcdPAPFYLFDEIDQALDAQHRKAVSDMIMElavHAQ----FITTTFRPELLESADK 649
Cdd:COG4133 127 LPVRQLSAGQKRRVALARLLLS----PAPLWLLDEPFTALDAAGVALLAELIAA---HLArggaVLLTTHQPLELAAARV 199
|
.
gi 34785382 650 F 650
Cdd:COG4133 200 L 200
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-374 |
1.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 170 RINNEIDQLMNQMQQIETQQRKFKASRD-----------------SILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLH 232
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDeadevleeheerreeleTLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 233 AMESTRESLKAELGTDLLSQLSLEDQ-----KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYlNENLRKRLDQV 307
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER-AEELREEAAEL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34785382 308 EQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKE 374
Cdd:PRK02224 369 ESELEEAREA-----VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
577-649 |
1.82e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 41.36 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34785382 577 QQLSGGQKSLVALA--LIfaiqkCDPaPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADK 649
Cdd:COG2274 610 SNLSGGQRQRLAIAraLL-----RNP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
140-492 |
1.95e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 140 LELQKDVRKAEEELGELEAKLNENLRRNIERINNEID--QLMNQMQQIETQQRKFKASRDSILSEMKMLKEkRQQSEKTF 217
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqDVRLHLQQCSQELALKLTALHALQLTLTQERV-REHALSIR 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 218 MPKQRSLQSLEASLHAMESTRESLKAElgtdllsqlsLEDQKRVDALNDEIRQLQQENRQLLNEriklegiITRVETYLN 297
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYW----------KEMLAQCQTLLRELETHIEEYDREFNE-------IENASSSLG 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 298 ENLRKRLDQVEQELNELREtEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 377
Cdd:TIGR00618 732 SDLAAREDALNQSLKELMH-QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 378 AINHDTKELEKmtnrqgmllkkkeECMKKIRELGSLPQEAFEKYQTL-SLKQLFRKLEQCntelkkyshvnKKALDQFVn 456
Cdd:TIGR00618 811 EIPSDEDILNL-------------QCETLVQEEEQFLSRLEEKSATLgEITHQLLKYEEC-----------SKQLAQLT- 865
|
330 340 350
....*....|....*....|....*....|....*.
gi 34785382 457 fseQKEKLIKRQEELDRGYKSIMELMNVLELRKYEA 492
Cdd:TIGR00618 866 ---QEQAKIIQLSDKLNGINQIKIQFDGDALIKFLH 898
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
579-651 |
2.09e-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: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 579 LSGGQKSLVALALifAI-QKCDpapFYLFDEIDQALDAQhrkaVSDMIME------LAVHAQFITTTFRPELLESADKFY 651
Cdd:cd03250 128 LSGGQKQRISLAR--AVySDAD---IYLLDDPLSAVDAH----VGRHIFEncilglLLNNKTRILVTHQLQLLPHADQIV 198
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
207-482 |
2.13e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 207 KEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGtdllSQLSLEDQKRVDALNDEIRQLQQEnRQLLNERIK-L 285
Cdd:pfam15905 25 KSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKK----SQKNLKESKDQKELEKEIRALVQE-RGEQDKRLQaL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 286 EGIITRVETYLNENLRKRLD------QVEQELNELreTEGGTVLTATTSE--------------LEAINKR---VKDTMA 342
Cdd:pfam15905 100 EEELEKVEAKLNAAVREKTSlsasvaSLEKQLLEL--TRVNELLKAKFSEdgtqkkmsslsmelMKLRNKLeakMKEVMA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 343 RSEDLDNSIDKTEAGIKELQKSM----ERWKNMEKEHMDAiNHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAF 418
Cdd:pfam15905 178 KQEGMEGKLQVTQKNLEHSKGKVaqleEKLVSTEKEKIEE-KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKN 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34785382 419 EKYQTLSLkqlfrKLEQCNTELKKyshvNKKALDQFVNFSE-QKEKLIKRQEELDRGYKSIMELM 482
Cdd:pfam15905 257 DEIESLKQ-----SLEEKEQELSK----QIKDLNEKCKLLEsEKEELLREYEEKEQTLNAELEEL 312
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
574-629 |
2.27e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 2.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 34785382 574 REMQQLSGG--QKSLVALALIfaiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 629
Cdd:PRK13409 208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
577-629 |
2.56e-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: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 34785382 577 QQLSGGQKSLVALALIFAIQKcdpaPFYLFDEIDQALDAQHRKAVSDMIMELA 629
Cdd:cd03226 125 LSLSGGQKQRLAIAAALLSGK----DLLIFDEPTSGLDYKNMERVGELIRELA 173
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
205-401 |
2.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 205 MLKEK-RQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTdllsqlSLEDQKRVDALNDEIRQLQQENRQLLNERI 283
Cdd:COG4717 46 MLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE------YAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 284 KLEGIITRVETYL-NENLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLDNSID-KTEAGIKEL 361
Cdd:COG4717 120 KLEKLLQLLPLYQeLEALEAELAELPERLEELEERL--EELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 34785382 362 QKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKE 401
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
577-628 |
2.75e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 40.66 E-value: 2.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 34785382 577 QQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDQALDAQHRKAVSDMIMEL 628
Cdd:COG1123 141 HQLSGGQRQRVAIAMALA---LDPD-LLIADEPTTALDVTTQAEILDLLREL 188
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
166-550 |
3.12e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 166 RNIERINNEIDQLMNQMQQI----ETQQRKFKASRDSILSEMKMLKEKR----QQSEKTFMPKQRSLQSLEASLHAMEST 237
Cdd:PTZ00108 999 YLLGKLERELARLSNKVRFIkhviNGELVITNAKKKDLVKELKKLGYVRfkdiIKKKSEKITAEEEEGAEEDDEADDEDD 1078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 238 RESLKAELGTD-LLSQ----LSLEdqkRVDALNDEIRQLQQENRQLLNeriklegiITRVETYLNEnlrkrLDQVEQELN 312
Cdd:PTZ00108 1079 EEELGAAVSYDyLLSMpiwsLTKE---KVEKLNAELEKKEKELEKLKN--------TTPKDMWLED-----LDKFEEALE 1142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 313 ELRETEggTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNR 392
Cdd:PTZ00108 1143 EQEEVE--EKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS 1220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 393 QGMLL----KKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVN---------KKALDQFVNFSE 459
Cdd:PTZ00108 1221 SGSDQeddeEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSavqysppppSKRPDGESNGGS 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 460 QKEKLIKRQeELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKlvPGGKATLVMKKGDVEGSQSQDEGEGSG 539
Cdd:PTZ00108 1301 KPSSPTKKK-VKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSS--RLLRRPRKKKSDSSSEDDDDSEVDDSE 1377
|
410
....*....|.
gi 34785382 540 ESERGSGSQSS 550
Cdd:PTZ00108 1378 DEDDEDDEDDD 1388
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
576-625 |
3.18e-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: 38.58 E-value: 3.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 34785382 576 MQQLSGGQKSLVALALIFaIQKCDpapFYLFDEIDQALDAQHRKAVSDMI 625
Cdd:cd03221 68 FEQLSGGEKMRLALAKLL-LENPN---LLLLDEPTNHLDLESIEALEEAL 113
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
194-316 |
3.47e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 194 ASRDSILSEM--KMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAElgTDLLSQLSLEDQKRVDALNDEIRQL 271
Cdd:COG2433 376 LSIEEALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE--VEELEAELEEKDERIERLERELSEA 453
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 34785382 272 QQENRQLLNERIKLEGIITRvetylNENLRKRLDQVEQELNELRE 316
Cdd:COG2433 454 RSEERREIRKDREISRLDRE-----IERLERELEEERERIEELKR 493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
302-471 |
3.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 302 KRLDQVEQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWknmeKEHMDAINh 381
Cdd:COG1579 17 SELDRLEHRLKELPAE-----LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY----EEQLGNVR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 382 DTKELEKMTNRQGMLLKKKEECMKKIRELgslpQEAFEKYQTlSLKQLFRKLEQCNTELKKYshvnKKALDQFVNFSEQK 461
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILEL----MERIEELEE-ELAELEAELAELEAELEEK----KAELDEELAELEAE 157
|
170
....*....|.
gi 34785382 462 -EKLIKRQEEL 471
Cdd:COG1579 158 lEELEAEREEL 168
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
166-387 |
3.80e-03 |
|
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: 40.49 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 166 RNIERINNEIDQLMNQMqqietqqRKFKASRDSILSEMKMLKEK-RQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAE 244
Cdd:pfam15921 646 RAVKDIKQERDQLLNEV-------KTSRNELNSLSEDYEVLKRNfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 245 LGTDLLS-QLSLEDQKRVDALNDEIRQLQQEnRQLLNERIKlegiitrvetylNENLRKRLdqVEQELNELREtEGGTVL 323
Cdd:pfam15921 719 EGSDGHAmKVAMGMQKQITAKRGQIDALQSK-IQFLEEAMT------------NANKEKHF--LKEEKNKLSQ-ELSTVA 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 324 T---ATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERwknMEKEHMD-AINH--DTKELE 387
Cdd:pfam15921 783 TeknKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQR---QEQESVRlKLQHtlDVKELQ 849
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
574-636 |
3.96e-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: 3.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34785382 574 REMQQLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDQALDAQHRKAVSDMIMELavHAQFIT 636
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAME-----PEVLvLDEPTAGLDPRGRRELLELLKRL--NKEGKT 186
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
576-645 |
4.56e-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: 39.68 E-value: 4.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34785382 576 MQQLSGGQKSLVALALIFAIQkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA-VHAQFITTTFRPELLE 645
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSA-LPKGGLLLIDEPESGLHPKLLRRLLELLKELSrNGAQLILTTHSPLLLD 303
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
161-389 |
4.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 161 NENLRRNIErinnEIDQLMNQMQQIETQQRKFKASRDSILSEmkmLKEKRQQSEKTfmpkQRSLQSLEASLHAMESTRES 240
Cdd:COG4372 30 SEQLRKALF----ELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQL----EEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 241 LKAELGTdlLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETEGG 320
Cdd:COG4372 99 AQEELES--LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE-LEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34785382 321 TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKM 389
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
574-633 |
4.66e-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: 4.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 574 REMQQLSGGQKSLVALALIFAiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQ 633
Cdd:cd03237 111 REVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-366 |
5.53e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 162 ENLRRNIERINNEIDQLMNQMQQIETQQRKF-------KASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAM 234
Cdd:pfam01576 780 KELEAQIDAANKGREEAVKQLKKLQAQMKDLqreleeaRASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 235 ESTRESLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQllnERIKLEgiitrvetYLNENLRKRLDQVEQELNEL 314
Cdd:pfam01576 860 QQERDELADEIASGASGKSALQDEKR--RLEARIAQLEEELEE---EQSNTE--------LLNDRLRKSTLQVEQLTTEL 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 34785382 315 R-ETEGGTVLTATTSELEAINKRVKDTMARSE-----DLDNSIDKTEAGIKELQKSME 366
Cdd:pfam01576 927 AaERSTSQKSESARQQLERQNKELKAKLQEMEgtvksKFKSSIAALEAKIAQLEEQLE 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-333 |
5.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 136 RKSRLELQKDVRKAEEELGELEAKLnENLRRNIERINNEIDQL--MNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQs 213
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEE- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 214 ektfmpkqrsLQSLEASLHAMESTRESLKAELgTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 293
Cdd:COG4717 158 ----------LRELEEELEELEAELAELQEEL-EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 34785382 294 TYLNENLRKRLDQveQELNELRETEGGTVLTATTSELEAI 333
Cdd:COG4717 227 EELEQLENELEAA--ALEERLKEARLLLLIAAALLALLGL 264
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
168-393 |
5.94e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 168 IERINNEI----DQLMNQMQQIETQQRKFKASRDSILSEMKMLKE-KRQQSEKTfmpkqRSLQSLEASLHAM-ESTRESL 241
Cdd:PRK10929 104 TDALEQEIlqvsSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEaRRQLNEIE-----RRLQTLGTPNTPLaQAQLTAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 242 KAElgtdllsqlSLEDQKRVDALndEIRQLQQENRQllnERIKLegiitRVETY--LNENLRKRLDQVEQELNELRETEG 319
Cdd:PRK10929 179 QAE---------SAALKALVDEL--ELAQLSANNRQ---ELARL-----RSELAkkRSQQLDAYLQALRNQLNSQRQREA 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34785382 320 GTVLTATtsELEAINkrvkdtmarSEDLDNSIdkteagIKELQKSmerwknmeKEHMDAINHDTKELEKMTNRQ 393
Cdd:PRK10929 240 ERALEST--ELLAEQ---------SGDLPKSI------VAQFKIN--------RELSQALNQQAQRMDLIASQQ 288
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
165-367 |
6.78e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 165 RRNIERINNEIDQLMNQMQQIETQQRKFKaSRDSILSEMKMLKEKRQQSEKTfMPKQRSLQSLEASLhamestreSLKAE 244
Cdd:COG3206 63 PQSSDVLLSGLSSLSASDSPLETQIEILK-SRPVLERVVDKLNLDEDPLGEE-ASREAAIERLRKNL--------TVEPV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 245 LGTDLLsQLSLED------QKRVDALndeIRQLQQENRQLLNERIKlegiitRVETYLNE---NLRKRLDQVEQELNELR 315
Cdd:COG3206 133 KGSNVI-EISYTSpdpelaAAVANAL---AEAYLEQNLELRREEAR------KALEFLEEqlpELRKELEEAEAALEEFR 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 34785382 316 ETEGgtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMER 367
Cdd:COG3206 203 QKNG---LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
164-428 |
7.17e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 164 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEaslhamestRESLKA 243
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIE---------YEVLKK 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 244 ELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETEGGTVL 323
Cdd:pfam05483 586 EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKFEEIIDNYQKEIE 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 324 TATTSE---LEAINKrVKDTMARSEDLDNSIDK-TEAGIKELQKSMER------------------WKNMEKEHMDAINH 381
Cdd:pfam05483 665 DKKISEeklLEEVEK-AKAIADEAVKLQKEIDKrCQHKIAEMVALMEKhkhqydkiieerdselglYKNKEQEQSSAKAA 743
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 34785382 382 DTKELEKMTNrQGMLLKKKEECMKKIRElgSLPQEAFEKYQTLSLKQ 428
Cdd:pfam05483 744 LEIELSNIKA-ELLSLKKQLEIEKEEKE--KLKMEAKENTAILKDKK 787
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
169-350 |
7.52e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 169 ERINNEIDQLMNQMQQIETQqrkfkasrdsilsemkmlKEKRQQSEKTFMPKQRSLqsLEASLHAMESTRESLKAEL-GT 247
Cdd:PRK11281 159 ERAQAALYANSQRLQQIRNL------------------LKGGKVGGKALRPSQRVL--LQAEQALLNAQNDLQRKSLeGN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 248 DLLSQLsleDQKRVDALNDEIRQLQQENrQLLNERIklegiitrvetylNEnlrKRLDQVEQELNELRETEGGTVLTATT 327
Cdd:PRK11281 219 TQLQDL---LQKQRDYLTARIQRLEHQL-QLLQEAI-------------NS---KRLTLSEKTVQEAQSQDEAARIQANP 278
|
170 180
....*....|....*....|....*.
gi 34785382 328 ---SELEaINKRVKDTMARSEDLDNS 350
Cdd:PRK11281 279 lvaQELE-INLQLSQRLLKATEKLNT 303
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
574-629 |
8.17e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 38.28 E-value: 8.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 34785382 574 REMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELA 629
Cdd:cd03235 128 RQIGELSGGQQQRVLLARALVQD----PDLLLLDEPFAGVDPKTQEDIYELLRELR 179
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
579-649 |
8.66e-03 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 37.58 E-value: 8.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34785382 579 LSGGQKSLVALALifAIQKcdpAPFYLF-DEIDQALDAQHRKAVSDMIMEL-AVHAQFITTTFRPELLESADK 649
Cdd:cd03246 97 LSGGQRQRLGLAR--ALYG---NPRILVlDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADR 164
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
574-629 |
8.83e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 39.38 E-value: 8.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 34785382 574 REMQQLSGG--QKSLVALALIfaiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 629
Cdd:COG1245 208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPSSYLDIYQRLNVARLIRELA 259
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
161-488 |
8.87e-03 |
|
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: 39.57 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 161 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 240
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 241 LKAELGTDLLSQLSLEDQ------KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETyLNENLRKRLDQVEQELNEL 314
Cdd:pfam02463 262 KEEEKLAQVLKENKEEEKekklqeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK-EKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 315 rETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMER-WKNMEKEHMDAINHDT-KELEKMTNR 392
Cdd:pfam02463 341 -EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLkEEELELKSEEEKEAQLlLELARQLED 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34785382 393 QGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELD 472
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
330
....*....|....*.
gi 34785382 473 RGYKSIMELMNVLELR 488
Cdd:pfam02463 500 QKESKARSGLKVLLAL 515
|
|
| |
