|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1005-1110 |
3.22e-60 |
|
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: 205.14 E-value: 3.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 1005 VEIRVAFRKSESLQVLDNHRQSGGERAVSTILYLQSMQHMVSAPFRVVDEINQGMDQSNERMIHEIVVNTACRAGSSQYF 1084
Cdd:cd03277 107 IELLVKFREGEQLQELDPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYF 186
|
90 100
....*....|....*....|....*.
gi 2421156680 1085 LITPKLLPDLSYHPMMKVLCIFNGEW 1110
Cdd:cd03277 187 LITPKLLPGLNYHEKMTVLCVYNGPH 212
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
50-195 |
9.36e-54 |
|
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: 186.65 E-value: 9.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 50 GSITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHERGSIEItlasa 129
Cdd:cd03277 1 GSIVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEI----- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2421156680 130 gtevkvrreivregnksiwkingrsasfaEVQKTTKNlcVQVDNLCQFLPQDRVVEFSKMSPQELL 195
Cdd:cd03277 76 -----------------------------ELYGNPGN--IQVDNLCQFLPQDRVGEFAKLSPIELL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-1087 |
2.40e-30 |
|
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: 130.19 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTP-GPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHERGS-----IEIT 125
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPfSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSgneayVTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 126 LASAGT------EVKVRREIVREGNKSIWKINGRSASFAEVQKTTKNLCVQVDNLcQFLPQDRVVEFSKMSPQELLK--- 196
Cdd:TIGR02169 82 FKNDDGkfpdelEVVRRLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGY-NVVLQGDVTDFISMSPVERRKiid 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 197 --------ETQKAVGREDLLQLQVELAEHRLKERQTMGELHRLAQDVDS------------------LRKQNEVLERDVE 250
Cdd:TIGR02169 161 eiagvaefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqallkekreyegyeLLKEKEALERQKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 251 RWQAR-EAAESQLRVLEALVPVVRYTDTKAEHDR---AKEARKHAHAHYLEVKNAVSDgVEEEIEQLESQIALNERQRRQ 326
Cdd:TIGR02169 241 AIERQlASLEEELEKLTEEISELEKRLEEIEQLLeelNKKIKDLGEEEQLRVKEKIGE-LEAEIASLERSIAEKERELED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 327 VQ-----------------DELSTEQRATQQR----TSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLED 385
Cdd:TIGR02169 320 AEerlakleaeidkllaeiEELEREIEEERKRrdklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 386 ahpEEKPQEGDSRELMQVASELSKQKLELKNEI-------IQLQDSQKGLLRSNRQLTTDMNSNDRQLRDLDDVAVRRRE 458
Cdd:TIGR02169 400 ---EINELKRELDRLQEELQRLSEELADLNAAIagieakiNELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 459 TLRRFNEdtfhalEWLEKNRSMFKQHVFAPVCLEASVANPQVALMIEAIVP-VSTLKMFVTQCDEDYHTfTREVNDRQRL 537
Cdd:TIGR02169 477 EYDRVEK------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgVHGTVAQLGSVGERYAT-AIEVAAGNRL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 538 RVDVV----------------RFNR----PLDSFRPQMSQSDVRAL-GFDGYALEFID-----APApVLAAMCSRDKVHE 591
Cdd:TIGR02169 550 NNVVVeddavakeaiellkrrKAGRatflPLNKMRDERRDLSILSEdGVIGFAVDLVEfdpkyEPA-FKYVFGDTLVVED 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 592 IPIA---VGKVNNERIESEKLFKEYV----SDGTRFIITVGRYGSRSATVMTTRVRSDIRLLSS--------EGESDEVR 656
Cdd:TIGR02169 629 IEAArrlMGKYRMVTLEGELFEKSGAmtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSlqselrriENRLDELS 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 657 ATRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSMV 736
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 737 S--------------EEQRGEDGGRVQA-----------------ERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVH 785
Cdd:TIGR02169 789 ShsripeiqaelsklEEEVSRIEARLREieqklnrltlekeylekEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 786 RLALVGLGGQSEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQAVRDEQARR 865
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 866 GRVTLEDLEIELSTCRQRLSmaANSGLSSRIMEQYEERKQRLARMESSVLELELALRQTRKRKSRLRERWEKPLDEIVQK 945
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIR--ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEA 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 946 IGTKFSEMFdqigcmGEVSlqrSGDGvvatdaeqpdddddddeQRITEPRDDQDYGnwGVEIRV-----AFRKSESLqvl 1020
Cdd:TIGR02169 1027 INENFNEIF------AELS---GGTG-----------------ELILENPDDPFAG--GLELSAkpkgkPVQRLEAM--- 1075
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 1021 dnhrqSGGERAVSTILYLQSMQHMVSAPFRVVDEINQGMDQSN-ERMIHEIvvntACRAGSSQYFLIT 1087
Cdd:TIGR02169 1076 -----SGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNvERVAKLI----REKAGEAQFIVVS 1134
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
52-953 |
3.39e-23 |
|
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: 106.98 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTP-GPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFV----KHGHERGSIEIT- 125
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPfSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEITf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 126 ------LASAGTEVKVRREIVReGNKSIWKINGRSASFAEVQKTTKNLCVQVDNLcQFLPQDRVVEFSKMSPQELLKETQ 199
Cdd:pfam02463 82 dnedheLPIDKEEVSIRRRVYR-GGDSEYYINGKNVTKKEVAELLESQGISPEAY-NFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 200 KAVGR----EDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAREAAE-------------SQL 262
Cdd:pfam02463 160 EEAAGsrlkRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEeyllyldylklneERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 263 RVLEALVPVVRYTDTKAEHDRAKEARKHAHAH-YLEVKNAVSDGVEEEIEQLESQIALNERQRRQVQ---DELSTEQRAT 338
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLkENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErrkVDDEEKLKES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 339 QQRTSRLERFETRQRDLSAELEEIGKRVQRRREqiaKLRTEISKLEDAHPEEKPQEGDSRELMQVASELSKQKLELKNEI 418
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKRE---AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 419 IQLQD----SQKGLLRSNRQLTTDMNSNDRQLRDLDDVAVRRRETLRRFNEDTFHALEWLEKNRSMFKQHVFAPVCLEAS 494
Cdd:pfam02463 397 LELKSeeekEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 495 VANPQVALMIEAIVPVSTLkmfvtqcDEDYHTFTREVNDRQRLRVDVVRFN-RPLDSFRPQMSQSDVRALGFDGYALEFI 573
Cdd:pfam02463 477 TQLVKLQEQLELLLSRQKL-------EERSQKESKARSGLKVLLALIKDGVgGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 574 DAPAPVLAAMC--SRDKVHEIPIAVGKVNNERIESEKLFKEYVSDGTRFIITVGRYGSRSATVMTTRVRSDIRLLSSEGE 651
Cdd:pfam02463 550 IVEVSATADEVeeRQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIL 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 652 SDEVRA-TRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRA 730
Cdd:pfam02463 630 KDTELTkLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 731 QLSSMVSEEQRGEDGGRVQAERQKIEQQLRDNAQERAEALAEIADSlttmtdlvhrlalvglggQSEARQLAELKAEASR 810
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS------------------RLKKEEKEEEKSELSL 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 811 QREAIIE---AQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQAVRDEQARRGRVTLEDLEIELSTCRQRLSMa 887
Cdd:pfam02463 772 KEKELAEereKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK- 850
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2421156680 888 ANSGLSSRIMEQYEERKQRLARMESSVLELELALRQTRKRKSRLRERWEKPLDEIVQKIGTKFSEM 953
Cdd:pfam02463 851 LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-937 |
1.06e-22 |
|
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: 105.52 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 77 IIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHE------RGSIEITLASAG--------TEVKVRREIVRE 142
Cdd:TIGR02168 28 IVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSEtrkplsLAEVELVFDNSDgllpgadySEISITRRLYRD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 143 GnKSIWKINGRSASFAEVQ---------KTTKNLCVQ--VDNLCQFLPQDRVVEFS--------KMSPQELLK---ETQK 200
Cdd:TIGR02168 108 G-ESEYFINGQPCRLKDIQdlfldtglgKRSYSIIEQgkISEIIEAKPEERRAIFEeaagiskyKERRKETERkleRTRE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 201 AVGR-EDL----------LQLQVELAE--HRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQA-REAAESQLRVLE 266
Cdd:TIGR02168 187 NLDRlEDIlnelerqlksLERQAEKAEryKELKAELRELELALLVLRLEELREELEELQEELKEAEEeLEELTAELQELE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 267 AlvpvvRYTDTKAEHDRAKEARKHAHAHYLEVKNAVSD-------------GVEEEIEQLESQIALNERQRRQVQ----- 328
Cdd:TIGR02168 267 E-----KLEELRLEVSELEEEIEELQKELYALANEISRleqqkqilrerlaNLERQLEELEAQLEELESKLDELAeelae 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 329 -----DELSTEQRATQQRTSRLER----FETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLED-------------- 385
Cdd:TIGR02168 342 leeklEELKEELESLEAELEELEAeleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerledrrerlqq 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 386 --AHPEEKPQEGDSRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRDLDDvAVRRRETLRRF 463
Cdd:TIGR02168 422 eiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLERLQEN 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 464 NEDTFHALEWLEKNRSMFKQHVfaPVCLEASVANPQVALMIEAIVPvSTLKMFVTQCDEDYhtftrevndrqRLRVDVVR 543
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGIL--GVLSELISVDEGYEAAIEAALG-GRLQAVVVENLNAA-----------KKAIAFLK 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 544 FNR-------PLDSFRPQMSQSDVRAL-----GFDGYALEFIDAPA---PVLAAMCSRDKVheipiavgkVNNERIESEK 608
Cdd:TIGR02168 567 QNElgrvtflPLDSIKGTEIQGNDREIlknieGFLGVAKDLVKFDPklrKALSYLLGGVLV---------VDDLDNALEL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 609 LfKEYvsdgtrfiitvgRYGSRSATVMTTRVRSDIRLLsseGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREQ 688
Cdd:TIGR02168 638 A-KKL------------RPGYRIVTLDGDLVRPGGVIT---GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALA 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 689 KVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSMVseEQRGEDGGRVQAERQKIEQQLRDNAQERAE 768
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--AQLSKELTELEAEIEELEERLEEAEEELAE 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 769 ALAEIADSLTTMTDLVHRLALVGLGGQSEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTD 848
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 849 EMTDDERQAVRDEQArrgrvtLEDLEIELSTCRQRLsmaansglsSRIMEQYEERKQRLARMESSVLELELALRQTRKRK 928
Cdd:TIGR02168 860 EIEELEELIEELESE------LEALLNERASLEEAL---------ALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
....*....
gi 2421156680 929 SRLRERWEK 937
Cdd:TIGR02168 925 AQLELRLEG 933
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
55-234 |
9.39e-19 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 85.63 E-value: 9.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 55 ISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDIS------EFVKHGHERGSIEITLAS 128
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGfvkgdiRIGLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 129 AGTE----VKVRREIVREGNKSIWKINGRSASFAEVQKTTKNLCVQVD---NLCQFLPQDRVVEFSKMSPQELLKETQKA 201
Cdd:pfam13476 81 NDGRytyaIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKiilPLLVFLGQEREEEFERKEKKERLEELEKA 160
|
170 180 190
....*....|....*....|....*....|...
gi 2421156680 202 VgreDLLQLQVELAEHRLKERQTMGELHRLAQD 234
Cdd:pfam13476 161 L---EEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
52-126 |
4.58e-18 |
|
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: 83.13 E-value: 4.58e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGP-HMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAK---DISEFVKHGHERGSIEITL 126
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSnSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSllfLAGGGVKAGINSASVEITF 79
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
52-130 |
1.19e-17 |
|
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: 82.26 E-value: 1.19e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHERGSIEITLASAG 130
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTLKNQG 79
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1007-1104 |
8.77e-17 |
|
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: 79.27 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 1007 IRVAFRKSESL--QVLDNHRQSGGERAVSTILYLQSMQHMVSAPFRVVDEINQGMDQSNERMIHEIVVNTACRagSSQYF 1084
Cdd:cd03239 75 VEITFDKSYFLvlQGKVEQILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKH--TSQFI 152
|
90 100
....*....|....*....|
gi 2421156680 1085 LITPKLLPDLSYHPMMKVLC 1104
Cdd:cd03239 153 VITLKKEMFENADKLIGVLF 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
192-760 |
5.59e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 192 QELLKETQKAVGREDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQlrvlealvpv 271
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---------- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 272 vRYTDTKAEHDRAKEARKHAHAHYLEVKNAVSDgVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETR 351
Cdd:COG1196 317 -RLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 352 QRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKPQEgdsRELMQVASELSKQKLELKNEIIQLQDSQKGLLRS 431
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE---EEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 432 NRQLttdmNSNDRQLRDLDDVAVRRRETLRRFNEDTFHALE-WLEKNRSMFKQHVFAPVCLEASVANPQVALMIEAIVPV 510
Cdd:COG1196 472 AALL----EAALAELLEELAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 511 StlkmfvtqcdEDYHTFTREVNDRQRLRVDVVRFNR----PLDSFRPQMSQSDVRALGFDGYALEFIDAPAPVLAAmcsR 586
Cdd:COG1196 548 L----------QNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADA---R 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 587 DKVHEIPIAVGKVNNERIESEKLFKEyVSDGTRFIITVGRYGSRSATVMTTRVRSDIRLLSSEGESDEVRATRDRLRQEI 666
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAV-TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 667 DDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEvatWERQKVHIETRRAQLSSMVSEEQrgedgg 746
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL---LEEEELLEEEALEELPEPPDLEE------ 764
|
570
....*....|....
gi 2421156680 747 rVQAERQKIEQQLR 760
Cdd:COG1196 765 -LERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
653-933 |
9.59e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 653 DEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQL 732
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 733 SsmvseeqrgEDGGRVQAERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVhrlalvglggQSEARQLAELKAEASRQR 812
Cdd:COG1196 315 E---------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----------AELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 813 EAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDER--QAVRDEQARRGRVTLEDLEIELSTCRQRLSMAANS 890
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2421156680 891 GLSSRIMEQYEERKQRLARMESSVLELELALRQTRKRKSRLRE 933
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-815 |
9.95e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 64 DRMEVTPGPHMNMIIGPNGTGKSTIVCAI--ALGLGGRPSLlgRAKDISEFVKHGHE------RGSIEIT-------LAS 128
Cdd:COG1196 16 DPTTIPFEPGITAIVGPNGSGKSNIVDAIrwVLGEQSAKSL--RGGKMEDVIFAGSSsrkplgRAEVSLTfdnsdgtLPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 129 AGTEVKVRREIVREGnKSIWKINGRSASFAEVQKttknlcvqvdnlcQFL-----P-------QDRVVEFSKMSPQEL-- 194
Cdd:COG1196 94 DYDEVTITRRLYRSG-ESEYYINGKPCRLKDIQD-------------LFLdtglgPesysiigQGMIDRIIEAKPEERra 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 195 ---------------------LKETQKAVGR-EDL----------LQLQVELAE--HRLKERQTMGELHRLAQDVDSLRK 240
Cdd:COG1196 160 iieeaagiskykerkeeaerkLEATEENLERlEDIlgelerqlepLERQAEKAEryRELKEELKELEAELLLLKLRELEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 241 QNEVLERDVERWQAR-EAAESQLRVLEAlvpvvRYTDTKAEHDRAKEARKHAHAHYLEvknavsdgVEEEIEQLESQIAL 319
Cdd:COG1196 240 ELEELEAELEELEAElEELEAELAELEA-----ELEELRLELEELELELEEAQAEEYE--------LLAELARLEQDIAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 320 NERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDahpEEKPQEGDSRE 399
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA---ELAEAEEELEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 400 LMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRDLDDVAVRRRETLRRFNEDTFHALEWLEKNRS 479
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 480 MFKQHVFAPVCLEASVAnpQVALMIEAIVPVSTLKmfvtqcdedyhtftREVNDRQRLRVDVVRFNRPLDSFRPQmsQSD 559
Cdd:COG1196 464 LLAELLEEAALLEAALA--ELLEELAEAAARLLLL--------------LEAEADYEGFLEGVKAALLLAGLRGL--AGA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 560 VRALGFDGYALEfiDAPAPVLAAMCSRDKVHEIPIAVgkvnnERIESEKLFKEyvSDGTRF-IITVGRYGSRSATVMTTR 638
Cdd:COG1196 526 VAVLIGVEAAYE--AALEAALAAALQNIVVEDDEVAA-----AAIEYLKAAKA--GRATFLpLDKIRARAALAAALARGA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 639 VRSDIRLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQ-RKLSVREQKVRDGHRNIEAREEELRIERQRISKEVAT 717
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRaVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 718 WERQKVHIETRRAQLSSMVSEEQRGEDGGRVQAERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLAL--VGLGGQ 795
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeeEALEEL 756
|
810 820
....*....|....*....|
gi 2421156680 796 SEARQLAELKAEASRQREAI 815
Cdd:COG1196 757 PEPPDLEELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-957 |
2.58e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 208 LQLQVELAE--HRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAR-EAAESQLRVLEAlvpvvRYTDTKAEHDRA 284
Cdd:COG1196 205 LERQAEKAEryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAElEELEAELAELEA-----ELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 285 KEARKHAHAHYLEVknavsdgvEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGK 364
Cdd:COG1196 280 ELELEEAQAEEYEL--------LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 365 RVQRRREQIAKLRTEISKLEDahpEEKPQEGDSRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDR 444
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEA---ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 445 QLRDLDDVAVRRRETLRRFNEDTFHALEWLEKNRSMFKQHVFAPVCLEASVAnpQVALMIEAIVPVSTLKmfvtqcdedy 524
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA--ELLEELAEAAARLLLL---------- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 525 htftREVNDRQRLRVDVVRFNRPLDSFRPQmsQSDVRALGFDGYALEfiDAPAPVLAAMCSRDKVHEIPIAVgkvnnERI 604
Cdd:COG1196 497 ----LEAEADYEGFLEGVKAALLLAGLRGL--AGAVAVLIGVEAAYE--AALEAALAAALQNIVVEDDEVAA-----AAI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 605 ESEKLFKEyvsdgtrfiitvGRygsrsatvmTTRVRSDIRLLSSEGESDEVRATRDRLRQEIDDirskldenegkqrkls 684
Cdd:COG1196 564 EYLKAAKA------------GR---------ATFLPLDKIRARAALAAALARGAIGAAVDLVAS---------------- 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 685 vreqkvrdghrniEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSmVSEEQRGEDGGRVQAERQKIEQQLRDNAQ 764
Cdd:COG1196 607 -------------DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA-GRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 765 ERAEALAEIADslttmtdLVHRLALVGLGGQSEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETR 844
Cdd:COG1196 673 ALLEAEAELEE-------LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 845 KLTDEMTDDERQAVRDEqarrgrvtlEDLEIELSTCRQRLS------MAAnsglssriMEQYEERKQRLARMESSVLELE 918
Cdd:COG1196 746 ELLEEEALEELPEPPDL---------EELERELERLEREIEalgpvnLLA--------IEEYEELEERYDFLSEQREDLE 808
|
730 740 750
....*....|....*....|....*....|....*....
gi 2421156680 919 LALRQTRKRksrlrerwekpLDEIVQKIGTKFSEMFDQI 957
Cdd:COG1196 809 EARETLEEA-----------IEEIDRETRERFLETFDAV 836
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-466 |
7.45e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 193 ELLKETQKAVGREDLLQLQVELAEHRLKERQTMGE-----LHRLAQDVDSLRKQNEVLERDVERWQAReAAESQLRVLEA 267
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrkeLEELSRQISALRKDLARLEAEVEQLEER-IAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 268 LVPVVRYTDTKAEHDRAKEARKhahahylevknAVSDGVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLER 347
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 348 FETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKPQ-EGDSRELMQVASELSKQKLELKNEIIQLQDSQK 426
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESElEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2421156680 427 GLLRSNRQLTTDMNSNDRQLRDLDDVAVRRRETLRRFNED 466
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
52-137 |
1.41e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 67.73 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTY-DRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSllGRAKDISEFVKHGHERGSIEITLASAG 130
Cdd:COG0419 2 LLRLRLENFRSYrDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKAR--SRSKLRSDLINVGSEEASVELEFEHGG 79
|
....*..
gi 2421156680 131 TEVKVRR 137
Cdd:COG0419 80 KRYRIER 86
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
52-408 |
1.61e-12 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 71.64 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSllgrakdiSEFVKHGHERGSIEIT------ 125
Cdd:COG0497 2 LTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRAD--------ASLVRHGADKAEVEAVfdlsdd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 126 ------LASAGTEVK-----VRREIVREGnKSIWKINGRSASFAEVQKTTKNLC-----------VQVDNLCQFLpqDRV 183
Cdd:COG0497 74 pplaawLEENGLDLDdgeliLRREISADG-RSRAFINGRPVTLSQLRELGELLVdihgqhehqslLDPDAQRELL--DAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 184 VEfskmsPQELLKETQKAVG---------------------REDLLQLQV-ELAEHRLKErqtmGELHRLAQDVDSLRKQ 241
Cdd:COG0497 151 AG-----LEELLEEYREAYRawralkkeleelradeaerarELDLLRFQLeELEAAALQP----GEEEELEEERRRLSNA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 242 NEVLErDVErwQAREA-AESQLRVLEALVPVVRYTDTKAEHD-RAKEARKHAHAHYLEVKNAVS------DGVE---EEI 310
Cdd:COG0497 222 EKLRE-ALQ--EALEAlSGGEGGALDLLGQALRALERLAEYDpSLAELAERLESALIELEEAASelrrylDSLEfdpERL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 311 EQLESQI-ALNERQRR---------QVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRV-QRRREQIAKLRTE 379
Cdd:COG0497 299 EEVEERLaLLRRLARKygvtveellAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLsAARKKAAKKLEKA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 380 ISK------LEDA------HPEEKPQE---------------GDSRELMQVAS--ELS 408
Cdd:COG0497 379 VTAeladlgMPNArfevevTPLEEPGPngadqveflfsanpgEPPKPLAKVASggELS 436
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
54-129 |
2.50e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 63.15 E-value: 2.50e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 54 QISLKNFVTYDRMEVTPG--PHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDisefVKHGHERGSIEITLASA 129
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFgeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSG----VKAGCIVAAVSAELIFT 74
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
656-934 |
1.17e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 656 RATRDRLrQEIDDIRSKLDEN-------------------EGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVA 716
Cdd:COG1196 182 EATEENL-ERLEDILGELERQleplerqaekaeryrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 717 TWERQKVHIETRRAQLSSMVSE-EQRGEDGGRVQAERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLALvglggq 795
Cdd:COG1196 261 ELAELEAELEELRLELEELELElEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE------ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 796 sEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQAVRDEQARRG-RVTLEDLE 874
Cdd:COG1196 335 -LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEElEEAEEALL 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 875 IELSTCRQRLSMAANSGLSSRimEQYEERKQRLARMESSVLELELALRQTRKRKSRLRER 934
Cdd:COG1196 414 ERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1026-1103 |
2.81e-10 |
|
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: 61.07 E-value: 2.81e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 1026 SGGERAVSTILYLQSMQHMVSAPFRVVDEINQGMDQSNERMIHEIVVNTACRAGSSQYFLITPKLLPDLSYHPMMKVL 1103
Cdd:cd03276 111 SGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGLASSDDVKVF 188
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
52-162 |
3.30e-10 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (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 including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 62.22 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSllgrakdiSEFVKHGHERGSIEIT------ 125
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRAS--------ADLIRSGAEKAVVEGVfdisde 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2421156680 126 ----------LASAGTEVKVRREIVREGnKSIWKINGRSASFAEVQK 162
Cdd:cd03241 73 eeakalllelGIEDDDDLIIRREISRKG-RSRYFINGQSVTLKLLRE 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-426 |
5.13e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 225 MGELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQLRVLEALVPVVRY--------------TDTKAEHDRAKEARKH 290
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLwfaqrrlelleaelEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 291 AHAHYlevknavsDGVEEEIEQLESQIALNERQRR-QVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRR 369
Cdd:COG4913 314 LEARL--------DALREELDELEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2421156680 370 REQIAKLRTEISKLEDAHPEEKpqegdsRELMQVASELSKQKLELKNEIIQLQDSQK 426
Cdd:COG4913 386 RAEAAALLEALEEELEALEEAL------AEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
52-455 |
9.32e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.00 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPsllgRAKDISEFVKHGHERGSIEITLASAGT 131
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 132 EVKVRREIVREG----NKSIWKINGR--SASFAEVQKT------TKNLCV----------QVDNLCQFLPQDRVVEFSKM 189
Cdd:PRK01156 79 VYQIRRSIERRGkgsrREAYIKKDGSiiAEGFDDTTKYieknilGISKDVflnsifvgqgEMDSLISGDPAQRKKILDEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 190 SPQELLKETQKAVgREDLLQLQVELAEHRLKERqtmgELHRLAQDVDSLRKQ---NEVLERDVERWQAREAAEsqlrvle 266
Cdd:PRK01156 159 LEINSLERNYDKL-KDVIDMLRAEISNIDYLEE----KLKSSNLELENIKKQiadDEKSHSITLKEIERLSIE------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 267 alvpvvrYTDTKAEHDRAKEARKHAHAhylevknavsdgVEEEIEQLESQIALNErQRRQVQDELSTEQRATQQRTSRLE 346
Cdd:PRK01156 227 -------YNNAMDDYNNLKSALNELSS------------LEDMKNRYESEIKTAE-SDLSMELEKNNYYKELEERHMKII 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 347 RFET-RQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKPQEGDSRELMqvasELSKQKLELKNEIIQL---Q 422
Cdd:PRK01156 287 NDPVyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI----KKKSRYDDLNNQILELegyE 362
|
410 420 430
....*....|....*....|....*....|...
gi 2421156680 423 DSQKGLLRSNRQLTTDMNSNDRQLRDLDDVAVR 455
Cdd:PRK01156 363 MDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
51-156 |
1.13e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 61.71 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 51 SITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIalglggrpSLLG------RAKDiSEFVKHGHERGSIEI 124
Cdd:PRK00064 2 YLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAI--------YLLApgrshrTARD-KELIRFGAEAAVIHG 72
|
90 100 110
....*....|....*....|....*....|..
gi 2421156680 125 TLASAGTEVKVRREIVREGNKSIwKINGRSAS 156
Cdd:PRK00064 73 RVEKGGRELPLGLEIDKKGGRKV-RINGEPQR 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
304-466 |
1.79e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 304 DGVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKL 383
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 384 EDA--------------HPEEKPQEGDSRELMQ-VASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRD 448
Cdd:COG4942 110 LRAlyrlgrqpplalllSPEDFLDAVRRLQYLKyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170
....*....|....*...
gi 2421156680 449 LDDVAVRRRETLRRFNED 466
Cdd:COG4942 190 LEALKAERQKLLARLEKE 207
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
52-159 |
2.25e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 59.63 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVT--PGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHERGSIEItLASA 129
Cdd:COG3950 3 IKSLTIENFRGFEDLEIDfdNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKL-ILYY 81
|
90 100 110
....*....|....*....|....*....|
gi 2421156680 130 GTEVKVRREIVREGNKSIWKINGRSASFAE 159
Cdd:COG3950 82 GTSRLLLDGPLKKLERLKEEYFSRLDGYDS 111
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
52-167 |
7.65e-09 |
|
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: 57.58 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYdRMEVTPGPHMNM--IIGPNGTGKSTIVCAIALGLGGRPSLLgRAKDISEFVkHGHERGSIEITLAS- 128
Cdd:cd03275 1 LKRLELENFKSY-KGRHVIGPFDRFtcIIGPNGSGKSNLMDAISFVLGEKSSHL-RSKNLKDLI-YRARVGKPDSNSAYv 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2421156680 129 -------AGTEVKVRREIVREGnkSIWKINGRSASFAEVQKTTKNL 167
Cdd:cd03275 78 tavyeddDGEEKTFRRIITGGS--SSYRINGKVVSLKEYNEELEKI 121
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1023-1097 |
2.76e-08 |
|
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: 54.29 E-value: 2.76e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2421156680 1023 HRQSGGERAVSTILYLQSMQHMVSAPFRVVDEINQGMDQSNERMIHEIVVNTACraGSSQYFLITPK----LLPDLSYH 1097
Cdd:cd03227 76 LQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLV--KGAQVIVITHLpelaELADKLIH 152
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-441 |
5.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHERGSIEITLASAGT 131
Cdd:PRK03918 3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 132 EVKVRREIVRegNKSIWKINGRSASFAEVQKTTKNLcvqVDNLCQFLPQDRVVEFSKMSPQELLK--ETQKAVGREDLLQ 209
Cdd:PRK03918 83 KYRIVRSFNR--GESYLKYLDGSEVLEEGDSSVREW---VERLIPYHVFLNAIYIRQGEIDAILEsdESREKVVRQILGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 210 LQVELAEHRLKERQTmgELHRLAQDVDSLRKQNEVLERDVErwQAREAAESQLRVLEALVPVVRYTDTKAEHDRAKEARK 289
Cdd:PRK03918 158 DDYENAYKNLGEVIK--EIKRRIERLEKFIKRTENIEELIK--EKEKELEEVLREINEISSELPELREELEKLEKEVKEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 290 HAHAHYLEVKNAVSDGVEEEIEQLESQIALNERQRRQVQDELStEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRR 369
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2421156680 370 REQIAKLRTEISKLedahpEEKPQEGDSRElmQVASELSKQKLELKNEIIQLQDSQKgLLRSNRQLTTDMNS 441
Cdd:PRK03918 313 EKRLSRLEEEINGI-----EERIKELEEKE--ERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELER 376
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
52-187 |
5.74e-08 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 55.38 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRpSLlgRAKDISEFVKHGHERGSIEITLASAGT 131
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGK-SH--RTSRDKELIRWGAEEAKISAVLERQGG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2421156680 132 EVKVRREIVREGNKSIwKINGrsasfAEVQKTTknlcvqvdnlcQFLPQDRVVEFS 187
Cdd:cd03242 78 ELALELTIRSGGGRKA-RLNG-----IKVRRLS-----------DLLGVLNAVWFA 116
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
52-128 |
1.70e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 54.62 E-value: 1.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHERGSIEITLAS 128
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGS 79
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
645-857 |
1.83e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 645 LLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVR----EQKVRDGHRNIEAREEELRIERQRISKEVATWER 720
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 721 QKVHIETRRAQLSSMVSEEQRGEDGGRVQ--------AERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLalvgl 792
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL----- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2421156680 793 ggQSEARQLAELKAEASRQRE----AIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQA 857
Cdd:COG4942 170 --EAERAELEALLAELEEERAaleaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-395 |
2.69e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 200 KAVGREDLLQL-QVELAEHRLKE-RQTMGELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQLrvLEALVPVVRYTDT 277
Cdd:COG4717 60 KPQGRKPELNLkELKELEEELKEaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 278 KAEHDRAKEARKHAHAHYLEVKNAvsdgvEEEIEQLESQIALNERQRRQVQDELSTEQRAT-QQRTSRLERFETRQRDLS 356
Cdd:COG4717 138 EAELAELPERLEELEERLEELREL-----EEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELE 212
|
170 180 190
....*....|....*....|....*....|....*....
gi 2421156680 357 AELEEIGKRVQRRREQIAKLRTEiskLEDAHPEEKPQEG 395
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENE---LEAAALEERLKEA 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
644-873 |
3.23e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 644 RLLSSEGESDEVRATRDRLR------QEIDDIRSKLDENEGKQRKLSVREQKVRdgHRNIEAREEELRIERQRISKEVAT 717
Cdd:COG4913 236 DLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 718 WERQKVHIETRRAQLssmvsEEQRGEDGGRvqaERQKIEQQLRDNAQERAEALAEIADslttmtdLVHRLALVGLGGQSE 797
Cdd:COG4913 314 LEARLDALREELDEL-----EAQIRGNGGD---RLEQLEREIERLERELEERERRRAR-------LEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 798 ARQLAELKAEASRQREAIIEAQKLYEQAESSynlAKAKAKQCLEETRKLTDEMT---------DDERQAVRDEQARRGRV 868
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAEIAslerrksniPARLLALRDALAEALGL 455
|
....*
gi 2421156680 869 TLEDL 873
Cdd:COG4913 456 DEAEL 460
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
52-950 |
3.45e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEV---TPGPHMNMIIGPNGTGKSTIVCAIALGLGGRpslLGRAKDISEfVKHGHERGSIEITLAS 128
Cdd:TIGR00618 3 PLRLTLKNFGSYKGTHTidfTALGPIFLICGKTGAGKTTLLDAITYALYGK---LPRRSEVIR-SLNSLYAAPSEAAFAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 129 agTEVKVRREIVREGNKSIWKINGRSaSFAEVQKTTKNLCVQVDNLCQFL--PQDRVVEFSKMSPQELLKETQKAVGRED 206
Cdd:TIGR00618 79 --LEFSLGTKIYRVHRTLRCTRSHRK-TEQPEQLYLEQKKGRGRILAAKKseTEEVIHDLLKLDYKTFTRVVLLPQGEFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 207 llQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAReaaeSQLRVLEALVPVVRYTDTKAEHDRake 286
Cdd:TIGR00618 156 --QFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLR----SQLLTLCTPCMPDTYHERKQVLEK--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 287 arkhahahylEVKNAVsdgvEEEIEQLESQIALneRQRRQVQDELSTEQRATQQRTSRLERFETrqrdLSAELEEIGKRV 366
Cdd:TIGR00618 227 ----------ELKHLR----EALQQTQQSHAYL--TQKREAQEEQLKKQQLLKQLRARIEELRA----QEAVLEETQERI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 367 QRRReQIAKLRTEISKLEdaHPEEKPQEgdsrelmqVASELSKQKLELKNEIIQLQDSQK--GLLRSNRQLTTDMNSNDR 444
Cdd:TIGR00618 287 NRAR-KAAPLAAHIKAVT--QIEQQAQR--------IHTELQSKMRSRAKLLMKRAAHVKqqSSIEEQRRLLQTLHSQEI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 445 QLRDLDDVAVRRRETLRRFNEDTFHALEW-------LEKNRSMFK--------QHVFAPVCLEASVANPQVALMIEAIVP 509
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLqqqkttlTQKLQSLCKeldilqreQATIDTRTSAFRDLQGQLAHAKKQQEL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 510 VstlKMFVTQCDEDYHTFTREVNDRQRLrvdVVRFNRPLDSFRPQMSQSDVRALGFD-------GYALEFIDAPAPvLAA 582
Cdd:TIGR00618 436 Q---QRYAELCAAAITCTAQCEKLEKIH---LQESAQSLKEREQQLQTKEQIHLQETrkkavvlARLLELQEEPCP-LCG 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 583 MCSRDKVHEIPIAVGKVNN---ERIESEKLFKEYVSDGTRFIITVGRYGSRSATVMTTRVRSDIRLLSSEgeSDEVRATR 659
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC--DNRSKEDI 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 660 DRLRQEIDDIRSKLDENEGKQRKLSVrEQKVRDGHRNIEAREEELRIERQRISKEVA----TWERQKVHIETRRAQLSSM 735
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLAC-EQHALLRKLQPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHAL 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 736 VSEEQRGEDGGRVQAERQKIEQQLRDNAQERA------EALAEIADSLTTMTDLVHRLALVGLGGQSEARQ----LAELK 805
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlaqcqTLLRELETHIEEYDREFNEIENASSSLGSDLAAredaLNQSL 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 806 AEASRQREAIIEAQKLYEQAESSYNLAK-------AKAKQCLEETRKLTDE------MTDDERQAVRDEQARRGRVTLED 872
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAAlqtgaelSHLAAEIQFFNRLREEdthllkTLEAEIGQEIPSDEDILNLQCET 825
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2421156680 873 LEIELSTCRQRLSMAANS-GLSSRIMEQYEERKQRLARmessvlelelaLRQTRKRKSRLRERWEKPLDEIVQKIGTKF 950
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATlGEITHQLLKYEECSKQLAQ-----------LTQEQAKIIQLSDKLNGINQIKIQFDGDAL 893
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
52-139 |
5.64e-07 |
|
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: 51.45 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVT-YDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGG--RPSLLGRAKDISEFVKhGHERGSIEITLAS 128
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGelPPNSKGGAHDPKLIRE-GEVRAQVKLAFEN 79
|
90
....*....|..
gi 2421156680 129 A-GTEVKVRREI 139
Cdd:cd03240 80 AnGKKYTITRSL 91
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
52-325 |
6.28e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRpsLLGRAKDIseFVKHGHERGSIEITLASAGT 131
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLER--LEKEADEL--FKPQGRKPELNLKELKELEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 132 EVKVRREIVREGNKSIWKINGRSASFAEVQKTTKNLCVQVDNLCQFLpqdrvvefskmSPQELLKETQKAvgREDLLQLQ 211
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----------QLLPLYQELEAL--EAELAELP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 212 VELAEHRLKERqtmgELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQLRVlealvpvvryTDTKAEHDRAKEARKHA 291
Cdd:COG4717 146 ERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEEL----------QDLAEELEELQQRLAEL 211
|
250 260 270
....*....|....*....|....*....|....
gi 2421156680 292 HAHYLEVKNAVSDgVEEEIEQLESQIALNERQRR 325
Cdd:COG4717 212 EEELEEAQEELEE-LEEELEQLENELEAAALEER 244
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
75-439 |
7.00e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.48 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 75 NMIIGPNGTGKSTIVCAIALGLGGRPsllgrAKDIS--EFVKHGHERGSI-EITLASAGTEVKVRR-------EIVREGN 144
Cdd:PHA02562 30 TLITGKNGAGKSTMLEALTFALFGKP-----FRDIKkgQLINSINKKDLLvELWFEYGEKEYYIKRgikpnvfEIYCNGK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 145 K---------------SIWKINgrSASFAEVqkttknLCVQVDNLCQFL----PQDR-VVE-------FSKMSpqELLKE 197
Cdd:PHA02562 105 LldesasskdfqkyfeQMLGMN--YKSFKQI------VVLGTAGYVPFMqlsaPARRkLVEdlldisvLSEMD--KLNKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 198 TQKAVGRE-DLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNeVLERDVERWQAREAAESQL--RVLEALVPVVRY 274
Cdd:PHA02562 175 KIRELNQQiQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQN-KYDELVEEAKTIKAEIEELtdELLNLVMDIEDP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 275 TD--TKAEHDRAKEARKHAH----AHYLEvKNAVSDGVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERF 348
Cdd:PHA02562 254 SAalNKLNTAAAKIKSKIEQfqkvIKMYE-KGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 349 ETRQR---DLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKpqegdsrelmqvaSELSKQKLELKNEIIQLQDSQ 425
Cdd:PHA02562 333 NEQSKkllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA-------------EELAKLQDELDKIVKTKSELV 399
|
410
....*....|....
gi 2421156680 426 KGLLRsnRQLTTDM 439
Cdd:PHA02562 400 KEKYH--RGIVTDL 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-934 |
9.55e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 215 AEHRLkeRQTMGELHRLAQDVDSLRKQNEVLERDVErwQAREAAE--SQLRVLEALVPVVRYTDTKAEHDRAKEARKHAH 292
Cdd:COG1196 177 AERKL--EATEENLERLEDILGELERQLEPLERQAE--KAERYRElkEELKELEAELLLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 293 AHyLEVKNAVSDGVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQ 372
Cdd:COG1196 253 AE-LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 373 IAKLRTEISKLEDAHPEEKPQEgdsRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRDLDDV 452
Cdd:COG1196 332 LEELEEELEELEEELEEAEEEL---EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 453 AVRRRETLRRFNEDTFHALEWLEKNRSMfKQHVFAPVCLEASVANPQVALMIEAIVPVSTLKmfvtqcdedyhtftREVN 532
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEE-EEEEEEALEEAAEEEAELEEEEEALLELLAELL--------------EEAA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 533 DRQRLRVDVVRFNRPLDSFRPQMSQSDVRALGFDGYALEFIDAPAPVLAAmcsrdKVHEIPIAVGKVnnerieseklfke 612
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA-----GAVAVLIGVEAA------------- 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 613 yvsdgtrfiitvgrygsrsatvmttrVRSDIRLLSSEGESDEVRATRDRLRQEIDDIRskldenegkqrklsvreqkvrd 692
Cdd:COG1196 536 --------------------------YEAALEAALAAALQNIVVEDDEVAAAAIEYLK---------------------- 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 693 ghRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSMVSEEQRGEDGGRVQAERQkIEQQLRDNAQERAEALAE 772
Cdd:COG1196 568 --AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT-LVAARLEAALRRAVTLAG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 773 IADSLTtmtdlvhRLALVGLGGQSEARQLAELKAEASRQREAIIEAQklyEQAESSYNLAKAKAKQCLEETRKLTDEMTD 852
Cdd:COG1196 645 RLREVT-------LEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL---AERLAEEELELEEALLAEEEEERELAEAEE 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 853 DERQAVRDEQARRGRVTLEDLEIElstcrqrlsmaansglssrimEQYEERKQRLARMESSVLELELALRQTRKRKSRLR 932
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELL---------------------EELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
..
gi 2421156680 933 ER 934
Cdd:COG1196 774 RE 775
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
52-482 |
1.28e-06 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 52.82 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQI-SLKNFVTY-DRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAK------------DI----SEFV 113
Cdd:COG4694 2 ITKIkKLKNVGAFkDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEfeieaggsapnpSVrvfnRDFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 114 K---HGHERGSIEITLASAGTEVKvrrEIVREGNKsiwKINGRSASFAEVQKTTKNLCVQVDNLCQFLPQDRVVEFSKMS 190
Cdd:COG4694 82 EenlRSGEEIKGIFTLGEENIELE---EEIEELEK---EIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 191 PQEL-------LKETQKAVGREDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERwQAREAAESQLR 263
Cdd:COG4694 156 ASSGrnyrkanLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAVS-SAIEELAALIQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 264 VLEALVPVVR---YTDTKAE-----------HDRAKEARKHAHAHYLEVKNAVSD---GVEEEIEQLESQ-IALNERQRR 325
Cdd:COG4694 235 NPGNSDWVEQglaYHKEEEDdtcpfcqqelaAERIEALEAYFDDEYEKLLAALKDlleELESAINALSALlLEILRTLLP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 326 QVQDELSTEQRATQQRTSRL-ERFETRQRDLS---------------AELEEIGKRVQRRREQIAKLRTEISKLedahpE 389
Cdd:COG4694 315 SAKEDLKAALEALNALLETLlAALEEKIANPStsidlddqelldelnDLIAALNALIEEHNAKIANLKAEKEEA-----R 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 390 EKPQEGDSRELMQVASELSKQKLELKNEIIQLQDSQKGLlrsnRQLTTDMNSNDRQLRDLDDVAVRRRETLRRFNEDTFH 469
Cdd:COG4694 390 KKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKAL----EDLKTEISELEAELSSVDEAADEINEELKALGFDEFS 465
|
490
....*....|...
gi 2421156680 470 aLEWLEKNRSMFK 482
Cdd:COG4694 466 -LEAVEDGRSSYR 477
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
641-946 |
7.44e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 641 SDIRLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQR---------KLSVREQKVRDGhrNIEAREEELRIERQRI 711
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaealleagKCPECGQPVEGS--PHVETIEEDRERVEEL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 712 SKEVATWERQKVHIETRRAQLSSMVSEEQRGEDggrvQAERQKIEQQLRDNAQERAEALAEIADSLTTmtdlvhrlalvg 791
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDRIER----LEERREDLEELIAERRETIEEKRERAEELRE------------ 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 792 lggqsearQLAELKAEASRQREAiieAQKLYEQAESsynlakakakqCLEETRKLtdemtDDERQAVRDEQARRGRV--- 868
Cdd:PRK02224 545 --------RAAELEAEAEEKREA---AAEAEEEAEE-----------AREEVAEL-----NSKLAELKERIESLERIrtl 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 869 --TLEDLEIELSTCRQRLSMAAnsglssrimEQYEERKQRLARMESSVLELELALRQTRKRKSRL-RERWEKPLDEIVQK 945
Cdd:PRK02224 598 laAIADAEDEIERLREKREALA---------ELNDERRERLAEKRERKRELEAEFDEARIEEAREdKERAEEYLEQVEEK 668
|
.
gi 2421156680 946 I 946
Cdd:PRK02224 669 L 669
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
52-218 |
8.91e-06 |
|
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: 48.41 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTY-DRMEVTP-GPHMNMIIGPNGTGKSTIVCAIALGL---------GGRPSLL--GR-AKDISEFVkhgh 117
Cdd:cd03272 1 IKQVIIQGFKSYkDQTVIEPfSPKHNVVVGRNGSGKSNFFAAIRFVLsdeythlreEQRQALLheGSgPSVMSAYV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 118 ergsiEITLASA-------GTEVKVRREIvrEGNKSIWKINGRSASFAEVQKTTKNLCVQVDNLCQFLPQDRVVEFSKMS 190
Cdd:cd03272 77 -----EIIFDNSdnrfpidKEEVRLRRTI--GLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMK 149
|
170 180
....*....|....*....|....*...
gi 2421156680 191 PQELLKETQKAVGREDLLQLQVELAEHR 218
Cdd:cd03272 150 QDEQQEMQQLSGGQKSLVALALIFAIQK 177
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
200-482 |
1.93e-05 |
|
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: 48.89 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 200 KAVGREDLLQLQV-ELAEHRLKERQTMGELHRLAQDvdsLRKQNEVLERDVERWQAREAAESQLRVLEALVPVVRYTDTK 278
Cdd:TIGR00606 731 LAPGRQSIIDLKEkEIPELRNKLQKVNRDIQRLKND---IEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERK 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 279 AEHDRAKEARKHAHAHYLEVKNAVSDGvEEEIEQLESQIALN----ERQRRQVQ------DELSTEQRATQQRTSRLERF 348
Cdd:TIGR00606 808 IAQQAAKLQGSDLDRTVQQVNQEKQEK-QHELDTVVSKIELNrkliQDQQEQIQhlksktNELKSEKLQIGTNLQRRQQF 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 349 ETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKPQEGDSRELMQvaSELSKQKLELKNEIIQLQD----S 424
Cdd:TIGR00606 887 EEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ--DKVNDIKEKVKNIHGYMKDienkI 964
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2421156680 425 QKGLLRSNRQLTTDMNSNDRQLRDLDDVAVRRRETLR--RFNEDTFHALE-WLEKNRSMFK 482
Cdd:TIGR00606 965 QDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRlmRQDIDTQKIQErWLQDNLTLRK 1025
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-386 |
2.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 197 ETQKAVGREDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQLRVLEALvpvvryTD 276
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL------DA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 277 TKAEHDRAKEARKHAHAHYLEVKNAVsDGVEEEIEQLESQIALNERQRRQVQDELstEQRATQQRTSRLERFETRQRDLS 356
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEEL-DELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|.
gi 2421156680 357 AelEEIGKRVQRR-REQIAKLRTEISKLEDA 386
Cdd:COG4913 760 G--DAVERELRENlEERIDALRARLNRAEEE 788
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
185-483 |
2.65e-05 |
|
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: 48.58 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 185 EFSKMSPQELLKETQKAVGREDLLQLQVELAEHR--LKERQTMGELHRLAQDvdSLRKQNEVLERDVERWQAREAAES-- 260
Cdd:pfam17380 248 DVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQkaVSERQQQEKFEKMEQE--RLRQEKEEKAREVERRRKLEEAEKar 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 261 -------------QLRVL---EALVPVVRYTDTKAEHDR------AKEARKHAHAHYLEV-KNAVSDGVEEEIEQLESQ- 316
Cdd:pfam17380 326 qaemdrqaaiyaeQERMAmerERELERIRQEERKRELERirqeeiAMEISRMRELERLQMeRQQKNERVRQELEAARKVk 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 317 IALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEIS-----KLEDAHPEEK 391
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEerkrkKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 392 PQEGDSRELMQVASELSKQKL-----ELKNEII--QLQDSQKGLLRSNRQlttdmNSNDRQLRDLDDVAVRRR--ETLRR 462
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQamieeERKRKLLekEMEERQKAIYEEERR-----REAEEERRKQQEMEERRRiqEQMRK 560
|
330 340
....*....|....*....|.
gi 2421156680 463 FNEDTfHALEWLEKNRSMFKQ 483
Cdd:pfam17380 561 ATEER-SRLEAMEREREMMRQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
192-388 |
2.73e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 192 QELLKETQKAVG--REDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAREAaesqlRVLEALV 269
Cdd:COG4942 40 EKELAALKKEEKalLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA-----ELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 270 PVVRYTDTK----AEHDRAKEARKHAHAHYLEVKNAVSDGVEEEIEQLESQIALNERQRRQVQDELSTEQ-------RAT 338
Cdd:COG4942 115 RLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEeeraaleALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2421156680 339 QQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHP 388
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
52-126 |
3.48e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 45.92 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTY-DRMEVTPGPHMNMIIGPNGTGKSTIVCAI--ALGLGGRPSLlgRAKDISEFVKHGHE----RGSIEI 124
Cdd:cd03278 1 LKKLELKGFKSFaDKTTIPFPPGLTAIVGPNGSGKSNIIDAIrwVLGEQSAKSL--RGEKMSDVIFAGSEtrkpANFAEV 78
|
..
gi 2421156680 125 TL 126
Cdd:cd03278 79 TL 80
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
209-465 |
8.51e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 209 QLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNE-------VLERDVE--------RWQAREAAESQLRVLEALV---P 270
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelreeaaELESELEeareavedRREEIEELEEEIEELRERFgdaP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 271 VVR------YTDTKAEHDRAKEARKHAHAHYLEVKNAVSDG---------------------------VEEEIEQLESQI 317
Cdd:PRK02224 405 VDLgnaedfLEELREERDELREREAELEATLRTARERVEEAealleagkcpecgqpvegsphvetieeDRERVEELEAEL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 318 ALNERQRRQVQDELSTEQRATQQRtSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLE----DAHPEEKPQ 393
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAE-DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaeEKREAAAEA 563
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2421156680 394 EGDSRELMQVASELSKQKLELKNEIIQLQDSQKgLLRSNRQLTTDMNSNDRQLRDLDDVAVRRRETLRRFNE 465
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLERIRT-LLAAIADAEDEIERLREKREALAELNDERRERLAEKRE 634
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
355-845 |
9.03e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 355 LSAELEEIGKRVQRRREQIAKlrtEISKLEDAHPEEKPQEGDSRELMQVASELSKQKLELKNEIIQLQDSQKGL--LRSN 432
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 433 RQLTTDMNSNDRQLRDLDDVAVRRRETLRRFNEdTFHALEWLEKNRSMFKQHVFApvcLEASVANPQVALMIEAIVPVST 512
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 513 LKMFVTQCDEDYHTFTREVNDRQRlRVDVVRFNRPLDSFRPQMSQSDVRA------LGFDGYALEFIDAPAPVLAAMCSR 586
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLliaaalLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 587 DKVheIPIAVGKVNNERIESEKLFKEYVSDGTRFIItvgrygsrsATVMTTRVRSDIRLlSSEGESDEVRATRDRLrQEI 666
Cdd:COG4717 283 LGL--LALLFLLLAREKASLGKEAEELQALPALEEL---------EEEELEELLAALGL-PPDLSPEELLELLDRI-EEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 667 DDIRSKLDENEgKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSMVSEEQRGEDGG 746
Cdd:COG4717 350 QELLREAEELE-EELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 747 RVQAERQKIEQQLRDNAQERAEALAEIAdslttmtDLVHRLALVGlggqsEARQLAELKAEASRQREAIIEAQKLYeqae 826
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELA-------ELEAELEQLE-----EDGELAELLQELEELKAELRELAEEW---- 492
|
490
....*....|....*....
gi 2421156680 827 SSYNLAKAKAKQCLEETRK 845
Cdd:COG4717 493 AALKLALELLEEAREEYRE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-421 |
9.67e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 193 ELLKETQKAVGR--------EDLLQLQVELaeHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAR--------- 255
Cdd:PRK03918 345 KKLKELEKRLEEleerhelyEEAKAKKEEL--ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigelkkeik 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 256 --EAAESQLRVLEALVPVVRYTDTkaEHDRAKEARKHAhahyLEVKNavsdgVEEEIEQLESQIALNERQRRQVQDELST 333
Cdd:PRK03918 423 elKKAIEELKKAKGKCPVCGRELT--EEHRKELLEEYT----AELKR-----IEKELKEIEEKERKLRKELRELEKVLKK 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 334 EQRATQQRT--SRLERFETRQRDLSAE-LEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKPQEGDSRELMQVASELSKQ 410
Cdd:PRK03918 492 ESELIKLKElaEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
250
....*....|.
gi 2421156680 411 KLELKNEIIQL 421
Cdd:PRK03918 572 LAELLKELEEL 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-373 |
1.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 192 QELLKETQKAVGREDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQN---EVLERDVERWQAR-EAAESQLRVLEA 267
Cdd:COG4913 634 EALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAElEELEEELDELKG 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 268 lvpvvRYTDTKAEHDRAKEARKHAHAhylEVKNAVSDGVEEEIEQLESQI--ALNERQRRQVQDELSTEQRATQQRTSRL 345
Cdd:COG4913 714 -----EIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEERFaaALGDAVERELRENLEERIDALRARLNRA 785
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2421156680 346 E------------RFETRQRDLSAELEEIGKrVQRRREQI 373
Cdd:COG4913 786 EeeleramrafnrEWPAETADLDADLESLPE-YLALLDRL 824
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
308-451 |
1.44e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 308 EEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAH 387
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 388 PEEKPQ---------------EGDSRELMQVASELSK---QKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRDL 449
Cdd:TIGR04523 464 ESLETQlkvlsrsinkikqnlEQKQKELKSKEKELKKlneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
..
gi 2421156680 450 DD 451
Cdd:TIGR04523 544 ED 545
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-387 |
1.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 227 ELHRLAQDVDSLRKQNEVLERDVERWQAR-EAAESQLRVLEAlvpvvRYTDTKAEHDRAKEARKHAHAHYLEVKNA-VSD 304
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARlEAAKTELEDLEK-----EIKRLELEIEEVEARIKKYEEQLGNVRNNkEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 305 GVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLE 384
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
...
gi 2421156680 385 DAH 387
Cdd:COG1579 173 PPE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
637-934 |
1.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 637 TRVRSDIRLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRIS---- 712
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlate 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 713 -------KEVATWERQKVHIETRRAQLSSMVSEEQRGEDGGRVQAERQKIEQQLRDNAQERAEA-----LAEIADSLTTM 780
Cdd:COG4717 192 eelqdlaEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallaLLGLGGSLLSL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 781 TDLVHRLALVGLG------------------GQSEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAK----AKAKQ 838
Cdd:COG4717 272 ILTIAGVLFLVLGllallflllarekaslgkEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELldriEELQE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 839 CLEETRKLTDEMTDDERQA----------VRDEQARRGRVT----LEDLEIELSTCRQRLSMAANSGLSSRIMEQYEERK 904
Cdd:COG4717 352 LLREAEELEEELQLEELEQeiaallaeagVEDEEELRAALEqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
330 340 350
....*....|....*....|....*....|
gi 2421156680 905 QRLARMESSVLELELALRQTRKRKSRLRER 934
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAE 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
692-934 |
2.32e-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: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 692 DGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSMVSEEQRGEDggRVQAERQKIEQQLRDNAQERAEALA 771
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR--ALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 772 EIADSLTTMtdlvhrlalvglggqseARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMT 851
Cdd:COG4942 98 ELEAQKEEL-----------------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 852 DDERQAVRDEQARRgrvTLEDLEIELSTCRQRLS--MAANSGLSSRIMEQYEERKQRLARMESSVLELELALRQTRKRKS 929
Cdd:COG4942 161 ELAALRAELEAERA---ELEALLAELEEERAALEalKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 2421156680 930 RLRER 934
Cdd:COG4942 238 AAAER 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
285-420 |
2.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 285 KEARKHAHAHyleVKNAVSDgVEEEIEQLESQIalnERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGK 364
Cdd:PRK12704 45 EEAKKEAEAI---KKEALLE-AKEEIHKLRNEF---EKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2421156680 365 RVQRRREQIAKLRTEISKLEDAHpeekpqegdsRELMQVASELSKQklELKNEIIQ 420
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQ----------LQELERISGLTAE--EAKEILLE 161
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
699-933 |
2.43e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 699 AREEELRIERQRISKEVATWERQKVHIETRRAQLSSMVSEEQRGEDGGRvQAERQKIEQQLRDNAQERAEAL-------A 771
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR-TALKNARLDLRRLFDEKQSEKDkknkalaE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 772 EIADSLTTMTDLVHRLALVGLGGQS----EARQLAELKAEASRQREAIIEAQK-----LYEQAESSYNLAKAKAKQCLEE 842
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQLDKKHQAwleeQKEQKREARTEKQAYWQVVEGALDaqlalLKAAIAARRSGAKAELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 843 TRKLTDEMTDDERQAVRDEQARRgrvtleDLEIELSTCRQRLSMAAN--SGLSSRIMEQYEERKQRLARMESSVLELELA 920
Cdd:pfam12128 756 YKRDLASLGVDPDVIAKLKREIR------TLERKIERIAVRRQEVLRyfDWYQETWLQRRPRLATQLSNIERAISELQQQ 829
|
250
....*....|....
gi 2421156680 921 L-RQTRKRKSRLRE 933
Cdd:pfam12128 830 LaRLIADTKLRRAK 843
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
52-189 |
2.58e-04 |
|
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: 44.21 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTY-DRMEVTP-GPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFV-KHGHE---RGSIEIT 125
Cdd:cd03273 3 IKEIILDGFKSYaTRTVISGfDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIyKRGQAgitKASVTIV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2421156680 126 L-------ASAGTE----VKVRREIVrEGNKSIWKINGRSASFAEVQKTTKNLCVQVDNLCQFLPQDRVVEFSKM 189
Cdd:cd03273 83 FdnsdksqSPIGFEnypeITVTRQIV-LGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNM 156
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
53-93 |
3.27e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.89 E-value: 3.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2421156680 53 TQISLKNFVTYDRMEVTPGPHMNM-IIGPNGTGKSTIVCAIA 93
Cdd:pfam13555 2 TRLQLINWGTFDGHTIPIDPRGNTlLTGPSGSGKSTLLDAIQ 43
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
660-936 |
3.54e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 660 DRLRQEID-DIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLssmvse 738
Cdd:pfam10174 453 ERLKEQRErEDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV------ 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 739 EQRGEDGGRVQAERQKIEqqlrdNAQERAEALAEIADSLTTMTDLVHRLALVGLGGQSEARQL----------------- 801
Cdd:pfam10174 527 EQKKEECSKLENQLKKAH-----NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLlgilrevenekndkdkk 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 802 -AELKAEASRQreaIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQavrdeqarrgrVTLEDLEIELSTC 880
Cdd:pfam10174 602 iAELESLTLRQ---MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQ-----------LQLEELMGALEKT 667
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2421156680 881 RQRLsmaansglssrimeqyEERKQRLARMESSVLELELALRQTR-KRKSRLRERWE 936
Cdd:pfam10174 668 RQEL----------------DATKARLSSTQQSLAEKDGHLTNLRaERRKQLEEILE 708
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
54-139 |
3.64e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 54 QISLKNFVTYDRMEV---TPGPHMNM--IIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDISEFVKHGHERGSIEITLAS 128
Cdd:cd03279 5 KLELKNFGPFREEQVidfTGLDNNGLflICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQL 84
|
90
....*....|.
gi 2421156680 129 AGTEVKVRREI 139
Cdd:cd03279 85 GGKKYRVERSR 95
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
306-437 |
3.67e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 306 VEEEIEQLESQIALNERQRRQVQDELSTEQRATQQ--RTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKL 383
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2421156680 384 EDAHPEEKPQ-----EGDSRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTT 437
Cdd:COG3206 304 RAQLQQEAQRilaslEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
310-435 |
3.71e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 310 IEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDaHPE 389
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES-KIS 541
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2421156680 390 EKPQEGDSRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQL 435
Cdd:TIGR04523 542 DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
195-451 |
3.76e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 195 LKETQKAVGREDLLQLQVE--LAEHRLKERQTMGELHRLAQdvdslrkqnevlerdveRWQAREAAESQL-RVLEALVPV 271
Cdd:COG3096 422 LEKARALCGLPDLTPENAEdyLAAFRAKEQQATEEVLELEQ-----------------KLSVADAARRQFeKAYELVCKI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 272 VRYTDTKAEHDRAKEARKHAHAHYLEVKNAVSdgVEEEIEQLESQIALNERQRRQvQDELSteQRATQQRTSR------L 345
Cdd:COG3096 485 AGEVERSQAWQTARELLRRYRSQQALAQRLQQ--LRAQLAELEQRLRQQQNAERL-LEEFC--QRIGQQLDAAeeleelL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 346 ERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPE--------EKPQE------GDSRELMQVASELSKQK 411
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaaqdalERLREqsgealADSQEVTAAMQQLLERE 639
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2421156680 412 LELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRDLDD 451
Cdd:COG3096 640 REATVERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
52-934 |
3.96e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAIALGLGGRPSLLGRAKDIsefVKHGHERGSIEITLASAGT 131
Cdd:PRK02224 3 FDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALDDTLDDV---ITIGAEEAEIELWFEHAGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 132 EVKVRREIVREGNKSIW----------KINGRSASFAEVQKTTKNLCVQVDNlCQFLPQDRVVEFSKMSPqellKETQKA 201
Cdd:PRK02224 80 EYHIERRVRLSGDRATTakcvletpegTIDGARDVREEVTELLRMDAEAFVN-CAYVRQGEVNKLINATP----SDRQDM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 202 VgrEDLLQLQvELAEHRlkERQTMGelhRLAQDvDSLRKQNEVLERDVERWQAREAAESQLRvLEALVPVVRYTDTKAEH 281
Cdd:PRK02224 155 I--DDLLQLG-KLEEYR--ERASDA---RLGVE-RVLSDQRGSLDQLKAQIEEKEEKDLHER-LNGLESELAELDEEIER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 282 -----DRAKEARKHAH---AHYLEVKNAVSDgVEEEIEQLESQIALNERQRRQVQDELSTeqratqqRTSRLERFETRQR 353
Cdd:PRK02224 225 yeeqrEQARETRDEADevlEEHEERREELET-LEAEIEDLRETIAETEREREELAEEVRD-------LRERLEELEEERD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 354 DLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKPQegdsrelmqvASELSKQKLELKNEIIQLQDSQKGLLRSNR 433
Cdd:PRK02224 297 DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA----------AQAHNEEAESLREDADDLEERAEELREEAA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 434 QLTTDMNSNDRQLRDlddvavrRRETLRRFNEDtfhalewLEKNRSMFKqhvFAPVCLEASvanpqvalmieaivpvstl 513
Cdd:PRK02224 367 ELESELEEAREAVED-------RREEIEELEEE-------IEELRERFG---DAPVDLGNA------------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 514 kmfvtqcdEDYHTFTREvnDRQRLRVDVVRFNRPLDSFRPQMSQSdvRALGFDGYALE----FIDAPApVLAAMCSRDKV 589
Cdd:PRK02224 411 --------EDFLEELRE--ERDELREREAELEATLRTARERVEEA--EALLEAGKCPEcgqpVEGSPH-VETIEEDRERV 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 590 HEIPIAVGKVNNERIESEKlfkeyvsdgtrfiitvgrygsrsatvmttRVRSDIRLLSSEGESDEVRATRDRLRQEIDDI 669
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEE-----------------------------RLERAEDLVEAEDRIERLEERREDLEELIAER 528
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 670 RSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSMVSeeqrgedggrVQ 749
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT----------LL 598
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 750 AERQKIEQQLrDNAQERAEALAEIADslttmtdlvhrlalvglggqsEARQLAELKAEASRQREAIIEAQKLyEQAESSy 829
Cdd:PRK02224 599 AAIADAEDEI-ERLREKREALAELND---------------------ERRERLAEKRERKRELEAEFDEARI-EEARED- 654
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 830 nlaKAKAKQCLEETRKLTDEMTDDerqavRDE-QARRGRVTLEdLEiELSTCRQRLsmaansglssrimEQYEERKQRLA 908
Cdd:PRK02224 655 ---KERAEEYLEQVEEKLDELREE-----RDDlQAEIGAVENE-LE-ELEELRERR-------------EALENRVEALE 711
|
890 900
....*....|....*....|....*.
gi 2421156680 909 RMESSVLELELALRQTRkrkSRLRER 934
Cdd:PRK02224 712 ALYDEAEELESMYGDLR---AELRQR 734
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
311-437 |
4.14e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 311 EQLESQI-ALNERQrrqvqdELSTEQRATQQR-TSRLERFETRQRdLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHP 388
Cdd:PRK11281 39 ADVQAQLdALNKQK------LLEAEDKLVQQDlEQTLALLDKIDR-QKEETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2421156680 389 EEKPQEGDSRELMQVASELSKQKlelkneiIQLQDSQKGLLRSNRQLTT 437
Cdd:PRK11281 112 EETRETLSTLSLRQLESRLAQTL-------DQLQNAQNDLAEYNSQLVS 153
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
52-94 |
4.33e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.15 E-value: 4.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPhMNMIIGPNGTGKSTIVCAIAL 94
Cdd:COG4637 2 ITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRF 43
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-462 |
4.34e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 253 QAREAAESQLRVLEALVpvvryTDTKAEHDRAKEARKHAHAHYLEVKNAVSDgVEEEIEQLESQIALNERQRRQVQDELS 332
Cdd:COG4942 27 AELEQLQQEIAELEKEL-----AALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 333 TEQRATQQRTSRLERFETRQR-----------DLSAELEEIGKRVQRRREQIAKLRTEISKLEDAhpeEKPQEGDSRELM 401
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPlalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2421156680 402 QVASELSKQKLELKNEIIQLQDSQKGL---LRSNRQLTTDMNSNDRQLRDLDDVAVRRRETLRR 462
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLekeLAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
644-837 |
5.98e-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: 43.60 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 644 RLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLsvrEQKVRDGHRNIEAREEELRIERQRISKEVATWERQ-- 721
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAELRAELEAQKEELAELLRALYRLgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 722 -----------------------KVHIETRRAQLSSMVSEEQRGED-GGRVQAERQKIEQQLRDNAQERAEALAEIADSL 777
Cdd:COG4942 119 qpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAAlRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2421156680 778 TTMTDLVHRLAlvglggqSEARQLAELKAEASRQREAI---IEAQKLYEQAESSYNLAKAKAK 837
Cdd:COG4942 199 KLLARLEKELA-------ELAAELAELQQEAEELEALIarlEAEAAAAAERTPAAGFAALKGK 254
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
632-863 |
6.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 632 ATVMTTRVRSDIRLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVReqkvrdghrnIEAREEELRIERQRI 711
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE----------LEALQAEIDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 712 skevatwERQKVHIETRRAQLSSMVSEEQRGedGGRVQAerqkieqqlrdnaqerAEALAEiADSLTTMTDLVHRLALVG 791
Cdd:COG3883 75 -------AEAEAEIEERREELGERARALYRS--GGSVSY----------------LDVLLG-SESFSDFLDRLSALSKIA 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2421156680 792 LGGQSEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQAVRDEQA 863
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
654-968 |
6.79e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 654 EVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRI---------------------- 711
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVdlklqelqhlknegdhlrnvqt 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 712 ---SKEVATWERQKVhIETRRAQLSSMVS-EEQRGEDGGRVQAERQKIEQQLRDNAQERAE-------ALAEIADSLTTM 780
Cdd:pfam15921 549 eceALKLQMAEKDKV-IEILRQQIENMTQlVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkilkdkKDAKIRELEARV 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 781 TDL-VHRLALVGLGGQsEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMtdderqavr 859
Cdd:pfam15921 628 SDLeLEKVKLVNAGSE-RLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKL--------- 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 860 deqarrgRVTLEDLEIELSTCRQRL-SMAANSGLSSRI----MEQYEERKQRLARMESSVLELELALRQTRKRKSRLRER 934
Cdd:pfam15921 698 -------KMQLKSAQSELEQTRNTLkSMEGSDGHAMKVamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
330 340 350
....*....|....*....|....*....|....
gi 2421156680 935 WEKpLDEIVQKIGTKFSEMfdqigcMGEVSLQRS 968
Cdd:pfam15921 771 KNK-LSQELSTVATEKNKM------AGELEVLRS 797
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
52-104 |
7.44e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.65 E-value: 7.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPhMNMIIGPNGTGKSTIVCAIALGLGGRPSLLG 104
Cdd:COG4938 1 IKSISIKNFGPFKEAELELKP-LTLLIGPNGSGKSTLIQALLLLLQSNFIYLP 52
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
304-418 |
7.64e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 304 DGVEEEIEQLESQIALNERQRrqvqDELSTEQRATQQRtsRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKL 383
Cdd:COG0542 407 DSKPEELDELERRLEQLEIEK----EALKKEQDEASFE--RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|....*
gi 2421156680 384 EDAHPEEKPQEgdsRELMQVASELSKQKLELKNEI 418
Cdd:COG0542 481 EQRYGKIPELE---KELAELEEELAELAPLLREEV 512
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-439 |
8.34e-04 |
|
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: 43.63 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 197 ETQKAVGREDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQ-NEVLERDVERWQAREAAESQLRVLEAlvpvvRYT 275
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQLED-----ERN 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 276 DTKAEHDRAKEARKHAHAHYLEVKNAVSDgVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDL 355
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSD-MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 356 SAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEK---PQEGDSRELMQV-ASELSKQKLELKNEIIQLQDSQKGLLRS 431
Cdd:pfam01576 579 QQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKaisARYAEERDRAEAeAREKETRALSLARALEEALEAKEELERT 658
|
....*...
gi 2421156680 432 NRQLTTDM 439
Cdd:pfam01576 659 NKQLRAEM 666
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
670-945 |
9.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 670 RSKLDENEGKQRKLSVREQKVRDGHRNIEA---------REEELRIERQRISKEVAtwERQKVHIETRRAQLSSMVSEEQ 740
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAakkkaeekkKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEK 1430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 741 RGEDGGRVQAERQKIEQQLRDNAQE--RAEALAEIADSLTTMTDLVHRlalvglggQSEARQLAELKAEASRQREAIIEA 818
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKK--------AEEAKKADEAKKKAEEAKKKADEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 819 QKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDE-------------------RQAVRDEQARRGRVTLEDLEIELSt 879
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadelkkaeelKKAEEKKKAEEAKKAEEDKNMALR- 1581
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 880 cRQRLSMAANSGLSSRIMEQYEERKQRLARMESSVLELELALRQTRKRKS--RLRERWEKPLDEIVQK 945
Cdd:PTZ00121 1582 -KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekKKVEQLKKKEAEEKKK 1648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
747-953 |
9.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 747 RVQAERQKIE--QQLRDNAQERAEALAEIA--DSLTTMTDL---VHRLALVGLGGQSEARQLAELKAEASRQREAIIEAQ 819
Cdd:COG4913 243 ALEDAREQIEllEPIRELAERYAAARERLAelEYLRAALRLwfaQRRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 820 KLYEQAESSYNLAKAKAKQCLE-ETRKLTDEMTDDERQAVR-DEQARRGRVTLEDLEIELSTCRQRLSMAAN--SGLSSR 895
Cdd:COG4913 323 EELDELEAQIRGNGGDRLEQLErEIERLERELEERERRRARlEALLAALGLPLPASAEEFAALRAEAAALLEalEEELEA 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 896 IMEQYEERKQRLARMESSVLELELALRQTRKRKSRLRERWEKPLDEIVQKIGTKFSEM 953
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
240-384 |
9.76e-04 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 42.63 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 240 KQNEVLERDVErwqareAAESQL---RVLEALVPVVRyTDTK---AEHDRAKEARKHAHAHYLEVKNAVSDGVEEEIEQL 313
Cdd:pfam10498 184 KPREIIESNVD------AAEWKLeleRVLPQLKVTIK-ADAKdwrAHLEQMKQHKKSIEESLPDTKSQLDKLHTDISKTL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 314 E----------SQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRR-------------R 370
Cdd:pfam10498 257 EkiesrekyinSQLEPLIQEYREAQDELSEVQEKYKQLSEGVTERTRELAEITEELEKVKQEMEERgssmtdgsplvkiK 336
|
170
....*....|....
gi 2421156680 371 EQIAKLRTEISKLE 384
Cdd:pfam10498 337 QALTKLKEEIKQMD 350
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
307-438 |
9.85e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 307 EEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDa 386
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ- 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2421156680 387 hpEEKPQEGDSRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTD 438
Cdd:COG4372 130 --QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
638-829 |
1.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 638 RVRSDIRLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEElrierqRISKEVAT 717
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE------QLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 718 WERQKVHIETRRAQLSSMVseeqrgedggrvqaerQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLalvglggQSE 797
Cdd:COG4913 350 LERELEERERRRARLEALL----------------AALGLPLPASAEEFAALRAEAAALLEALEEELEAL-------EEA 406
|
170 180 190
....*....|....*....|....*....|..
gi 2421156680 798 ARQLAELKAEASRQREAIIEAQKLYEQAESSY 829
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
640-826 |
1.28e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.36 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 640 RSDIRLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWE 719
Cdd:pfam19220 45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 720 RQKVHiETRRAQlssMVSEEQRGEDGGRVQAE--RQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLAlvglggqSE 797
Cdd:pfam19220 125 RQLAA-ETEQNR---ALEEENKALREEAQAAEkaLQRAEGELATARERLALLEQENRRLQALSEEQAAELA-------EL 193
|
170 180 190
....*....|....*....|....*....|.
gi 2421156680 798 ARQLAELK--AEASRQREAIIEAQKLYEQAE 826
Cdd:pfam19220 194 TRRLAELEtqLDATRARLRALEGQLAAEQAE 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
647-838 |
1.48e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 647 SSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLsvreqKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIE 726
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 727 TRRAQLSSMVSEEQRGEDGGRVQAERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLA-LVGLGGQSEARQLAELK 805
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAaLRAQLQQEAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|...
gi 2421156680 806 AEASRQREAIIEAQKLYEQAESSYNLAKAKAKQ 838
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
205-430 |
1.49e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 205 EDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAR-EAAESQLRVLEAlvpvvRYTDTKAEHDR 283
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiRALEQELAALEA-----ELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 284 AKEARKHAHAHYLE-VKNAVSDGVEEEIEQLESQIALNERQRRqvqdeLSTEQRATQQRTSRLERFETRQRDLSAELEEI 362
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 363 GKRVQRRREQIAKLRTEISKLEDAHPEEKpqegdsrelmQVASELSKQKLELKNEIIQLQDSQKGLLR 430
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQ----------KLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
712-955 |
1.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 712 SKEVATWERQKVHIETRRAQLSSMVSEEQRGEDGGRVQAERQKIEQQLRD--NAQERAEALAEIADSLTTMTDLVHRLAL 789
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREAEELEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 790 VGLGGQSEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQAVRDEqarrgrvt 869
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE-------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 870 LEDLEIELSTCRQRLSMAANSGLSSRIMEQYEERKQRLARMESSVLELELALRQTRKRKSRLRERWEKPLDEIVQKIgtk 949
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEY--- 524
|
....*.
gi 2421156680 950 FSEMFD 955
Cdd:COG4717 525 FSRLTD 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
663-865 |
1.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 663 RQEIDDIRSKLDEN---EGKQRKLSVREQKVRDGHRNIEAR---EEELRIERQRISKEVATWERQKVHIETRRAQLSSMV 736
Cdd:PTZ00121 1469 AKKADEAKKKAEEAkkaDEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 737 SEEQRGEDGGRVQ----AERQKIEQQLRDNAQERAEALAEIADSlttmtdlvhRLALVGLGGQSEARQLAElkaEASRQR 812
Cdd:PTZ00121 1549 DELKKAEELKKAEekkkAEEAKKAEEDKNMALRKAEEAKKAEEA---------RIEEVMKLYEEEKKMKAE---EAKKAE 1616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2421156680 813 EAIIEAQKLYEQAESSYNLAKAKAKQClEETRKLTDEMTDDERQAVRDEQARR 865
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAEELKKAEEENKIKAAEEAK 1668
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-358 |
1.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 197 ETQKAVGREDLLQLQVELAEHRLKERQTMGELHRL-AQDVDSLRKQNEVLERDVERW-QAREAAESQLRVLEALVPvvry 274
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEEReRRRARLEALLAALGLPLP---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 275 tdtkAEHDRAKEARKHAHAHylevknavSDGVEEEIEQLESQIALNERQRRQVQ---DELSTEQRATQQRTSRLERFETR 351
Cdd:COG4913 377 ----ASAEEFAALRAEAAAL--------LEALEEELEALEEALAEAEAALRDLRrelRELEAEIASLERRKSNIPARLLA 444
|
....*..
gi 2421156680 352 QRDLSAE 358
Cdd:COG4913 445 LRDALAE 451
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
52-92 |
1.84e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.20 E-value: 1.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2421156680 52 ITQISLKNFVTYDRMEVTPGPHMNMIIGPNGTGKSTIVCAI 92
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEAL 43
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
204-417 |
2.08e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 204 REDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAR-EAAESQLRVLEAlvpvvRYTDTKAEHD 282
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElAALEAELAELEK-----EIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 283 RAKE--------ARKHAHAHYLEVKNAvSDGVEEEIEQLESQIALNERQRRQVqDELSTEQRATQQRTSRLERFETRQRD 354
Cdd:COG4942 101 AQKEelaellraLYRLGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQA-EELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2421156680 355 LSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKPQ-EGDSRELMQVASELSKQKLELKNE 417
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAElQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
307-483 |
2.29e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 307 EEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRR--------------EQ 372
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeleKQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 373 IAKLRTEISKLEDahpeEKpQEGDSRELMQVASELSKQKLELKNE-------IIQLQDSQKGLLRSNRQLTTDMNSNDRQ 445
Cdd:TIGR04523 290 LNQLKSEISDLNN----QK-EQDWNKELKSELKNQEKKLEEIQNQisqnnkiISQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190
....*....|....*....|....*....|....*...
gi 2421156680 446 LRDlddvAVRRRETLRRFNEDTFHALEWLEKNRSMFKQ 483
Cdd:TIGR04523 365 LEE----KQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-383 |
2.81e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 197 ETQKAVGREDLLQLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAR-EAAESQLRVLEALVPVVRyt 275
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEELEELIEELE-- 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 276 dtkAEHDRAKEARKHAHAHYLEVKNAVSDgVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDL 355
Cdd:TIGR02168 873 ---SELEALLNERASLEEALALLRSELEE-LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
170 180 190
....*....|....*....|....*....|....*.
gi 2421156680 356 -SAELEEIGKRVQRR-------REQIAKLRTEISKL 383
Cdd:TIGR02168 949 ySLTLEEAEALENKIeddeeeaRRRLKRLENKIKEL 984
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
282-454 |
3.12e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 282 DRAKEARKHAHAHYLEVKNAVsDGVEEEIEQLESQIALNERQRRQVQDELsteqratQQRTSRLERFETRQ--------- 352
Cdd:COG1579 20 DRLEHRLKELPAELAELEDEL-AALEARLEAAKTELEDLEKEIKRLELEI-------EEVEARIKKYEEQLgnvrnnkey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 353 RDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPEEKpqegdsRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSN 432
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELE------AELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
170 180
....*....|....*....|....*..
gi 2421156680 433 RQLTTDMNSN-----DRQLRDLDDVAV 454
Cdd:COG1579 166 EELAAKIPPEllalyERIRKRKNGLAV 192
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
154-384 |
3.68e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 154 SASFaEVQKTTKnlcvQVDNLCQFLPQDRVVEFSKmSPQELLKETqkavgREDLLQLQVELAEHRLKERQTMGELHRLAQ 233
Cdd:COG3096 803 KASF-DVQKLQR----LHQAFSQFVGGHLAVAFAP-DPEAELAAL-----RQRRSELERELAQHRAQEQQLRQQLDQLKE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 234 DVDSLRK-------------QNEVLERDVERWQAREAAES------QLRVLEALVPVVR-----YTDTKAEHDRAKEARK 289
Cdd:COG3096 872 QLQLLNKllpqanlladetlADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQsdpeqFEQLQADYLQAKEQQR 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 290 HAHA------------HYLEVKNAVSDGVE--EEIEQLESQIALNERQRRQVQDELSTEQ----RATQQRTSRLERFETR 351
Cdd:COG3096 952 RLKQqifalsevvqrrPHFSYEDAVGLLGEnsDLNEKLRARLEQAEEARREAREQLRQAQaqysQYNQVLASLKSSRDAK 1031
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2421156680 352 QRDLSA---ELEEIG------------KRVQRRREQIAKLRTEISKLE 384
Cdd:COG3096 1032 QQTLQEleqELEELGvqadaeaeerarIRRDELHEELSQNRSRRSQLE 1079
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
197-451 |
3.90e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 197 ETQKAVGREDLLQLQVELAEH--RLKERQTMGELHRlaQDVDSLRKQNEVLERD------VERWQAREAAESQLRVLEAL 268
Cdd:PRK04863 382 EARAEAAEEEVDELKSQLADYqqALDVQQTRAIQYQ--QAVQALERAKQLCGLPdltadnAEDWLEEFQAKEQEATEELL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 269 VPVVRYTDTKAEHDRAKEARKHAHAHYLEV-KNAVSDGVEEEIEQLESQIALNER--QRRQVQDELstEQRATQQRTSR- 344
Cdd:PRK04863 460 SLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsRSEAWDVARELLRRLREQRHLAEQlqQLRMRLSEL--EQRLRQQQRAEr 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 345 ----------------------LERFETRQRDLSAELEEIGKRVQRRREQIAKLRTEISKLEDAHPE--------EKPQE 394
Cdd:PRK04863 538 llaefckrlgknlddedeleqlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaaqdalARLRE 617
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2421156680 395 ------GDSRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRDLDD 451
Cdd:PRK04863 618 qsgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
132-932 |
4.25e-03 |
|
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: 41.57 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 132 EVKVRREIVREGNKSIWKINGRSASFAEVQKttknlcvQVDNLCQFLPQDRVVEFskMSPQELLKETQKAVGREDLlqlq 211
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKIMKLDNEIKALKSRKK-------QMEKDNSELELKMEKVF--QGTDEQLNDLYHNHQRTVR---- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 212 vELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQLRVLEALVPVVRYTDTKAEHDRAKEAR-KH 290
Cdd:TIGR00606 316 -EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQiKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 291 AHAHYLEVKNAVSDGVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEI---GKRVQ 367
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLegsSDRIL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 368 RRREQIAKLRTEISKLE-DAHPEEKPQEGDSRELMQVASELSKQKLELKNEiiqLQDSQKGLLRSNRQLTTDMNSNDRQL 446
Cdd:TIGR00606 475 ELDQELRKAERELSKAEkNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME---QLNHHTTTRTQMEMLTKDKMDKDEQI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 447 RDLDDVAVRRRETLRRFNEDTFHALEWLEKNRSMFKQhvfapvcLEASVA--NPQVALMIEAIVPVSTLKMFVTQCDEDY 524
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQ-------TRDRLAklNKELASLEQNKNHINNELESKEEQLSSY 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 525 HTFTREVNDRQRLRVDVVRFNRPLDSFRPQMSQSDVRALGFDGYALEFIDAPAPVlAAMCSRDkvheipiavgkvnnerI 604
Cdd:TIGR00606 625 EDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSC-CPVCQRV----------------F 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 605 ESEKLFKEYVSD-GTRFIITVGRYGSRSATVMTTRVRSDIRLLSSEG----------ESDEVRATRDRLRQEIDDIRSKL 673
Cdd:TIGR00606 688 QTEAELQEFISDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGrqsiidlkekEIPELRNKLQKVNRDIQRLKNDI 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 674 DENEGKQRKLSVREQKVRDGHRN---IEAREEELRIERQRISKEVAtwERQKVHIETRRAQLSSMVSEEQ--------RG 742
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQheldtvvsKI 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 743 EDGGRVQAERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLALVGLGGQSEARQLAELKAEASRQREAIIEAQKLY 822
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 823 EQAESSYNLAKAKAKQCLEETRKLTDE----MTDDER--QAVRDEQARRGRVTLEDLEIELSTCRQR-------LSMAAN 889
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNihgyMKDIENkiQDGKDDYLKQKETELNTVNAQLEECEKHqekinedMRLMRQ 1005
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2421156680 890 SGLSSRIMEQYEERKQRLARMESSVLELELALRQTRKRKSRLR 932
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
235-445 |
4.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 235 VDSLRKQNEVLER-----DVERWQAREAAESQLRVLEalvpvvrytDTKAEHDRAKEARKHAHAHYLEVKNAVSDgVEEE 309
Cdd:COG4717 48 LERLEKEADELFKpqgrkPELNLKELKELEEELKEAE---------EKEEEYAELQEELEELEEELEELEAELEE-LREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 310 IEQLESQIALNE--RQRRQVQDELSTEQRatqqrtsRLERFETRQRdlsaELEEIGKRVQRRREQIAKLRTEISKLEDAH 387
Cdd:COG4717 118 LEKLEKLLQLLPlyQELEALEAELAELPE-------RLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2421156680 388 PEEKPQEGdsRELMQVASELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQ 445
Cdd:COG4717 187 SLATEEEL--QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
653-777 |
4.52e-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: 39.91 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 653 DEVRATRDRLRQEIDDIRSKLdenEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRI-------------------SK 713
Cdd:COG1579 20 DRLEHRLKELPAELAELEDEL---AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkyeeqlgnvrnnkeyealQK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2421156680 714 EVATWERQKVHIETRRAQLssMVSEEQRGEDGGRVQAERQKIEQQLRDNAQERAEALAEIADSL 777
Cdd:COG1579 97 EIESLKRRISDLEDEILEL--MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
204-422 |
4.69e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 204 REDLLQLQVEL-AEHRLKERQTMGELHRLAQDVDSLRKQNEVLERDVERW---QAREAAESQLRVLEALVPVVRYTDTK- 278
Cdd:pfam12128 652 RLDLRRLFDEKqSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWleeQKEQKREARTEKQAYWQVVEGALDAQl 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 279 AEHDRAKEARKHAHAHYLE--------------VKNAVSDGVEEEIEQLESQIAlNERQRRQVQDELSTEQRAT-----Q 339
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKaletwykrdlaslgVDPDVIAKLKREIRTLERKIE-RIAVRRQEVLRYFDWYQETwlqrrP 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 340 QRTSRLERFETRQRDLSAELEEIGKRVQRRREQI------------------AKLRTEISKLEDAHpEEKPQEGDSRELM 401
Cdd:pfam12128 811 RLATQLSNIERAISELQQQLARLIADTKLRRAKLemerkasekqqvrlsenlRGLRCEMSKLATLK-EDANSEQAQGSIG 889
|
250 260
....*....|....*....|.
gi 2421156680 402 QVASELSKQKLELKNEIIQLQ 422
Cdd:pfam12128 890 ERLAQLEDLKLKRDYLSESVK 910
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
654-770 |
4.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 654 EVRATRDRLRQEID-DIRSKLDENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQ- 731
Cdd:PRK12704 61 EAKEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEq 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2421156680 732 ------LSSMVSEEQRG------EDGGRVQAER--QKIEQQLRDNAQERAEAL 770
Cdd:PRK12704 141 lqelerISGLTAEEAKEillekvEEEARHEAAVliKEIEEEAKEEADKKAKEI 193
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
650-865 |
5.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 650 GESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREqkVRDGHRNIEAREEELRiERQRISKEVATWERQKVHIETRR 729
Cdd:COG4717 35 GKSTLLAFIRAMLLERLEKEADELFKPQGRKPELNLKE--LKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 730 AQLSSMVSEEQRGEDGGRVQAERQKIEQQLRDNAQERAEALAEIADSLTTMTDLVHRLALVglggQSEARQLAELKAEAS 809
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL----AELQEELEELLEQLS 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2421156680 810 -RQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQAVRDEQARR 865
Cdd:COG4717 188 lATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
651-865 |
5.29e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 651 ESDEVRATRDRLRQEIDDIRSKLD----ENEGKQRKLSVREQKVR-DGHRNIEAREEELRIERQRISKEVATWERQKVHI 725
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEaakaEAEAAADEAEAAEEKAEaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 726 ETRRAQLSSMVSEEQRGEDGGRVQAERQKIEQQLRDNAQE--RAEALAEIADSLTTMTDLVHRlalvglggQSEARQLAE 803
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKK--------AEEAKKADE 1474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2421156680 804 LKAEASRQREAiIEAQKLYEQAESSYNLAK--AKAKQCLEETRKLTDEMTDDErqAVRDEQARR 865
Cdd:PTZ00121 1475 AKKKAEEAKKA-DEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAKKADE--AKKAEEAKK 1535
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
637-865 |
6.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 637 TRVRSDIRLLSSEGESDEVRATRDRLRQEIDDIRSKLDENEGKQRKLSVREQKVRDGHRNIE-AR--EEELRIERQRISK 713
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEdARkaEEARKAEDARKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 714 EVATWERQKVHIETRRAQLSSMVSEEQRGEDGGRVQAERQKIEQQlrdnaqeRAEALAEIADSlttmtdlvhRLALVGLG 793
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR-------KAEELRKAEDA---------RKAEAARK 1207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2421156680 794 GQSEARQLAELKAEASRQREAIIEAQKLYEQAESSYNLAKAKAKQCLEETRKLTDEMTDDERQAVRDEQARR 865
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
215-367 |
6.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 215 AEHRLKERQTmgELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQLRvlealvpvvRYTDTKAEHDRAKEARKHAHAH 294
Cdd:COG4913 608 NRAKLAALEA--ELAELEEELAEAEERLEALEAELDALQERREALQRLA---------EYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2421156680 295 YLEVKNAVSDgveeeIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQ 367
Cdd:COG4913 677 LERLDASSDD-----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
227-387 |
7.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 227 ELHRLAQDVDSLRKQNEVLERDVERWQAREAAESQLRVLEALVPVVRYTDTKAEHDRAKEARKHAHAHYLEVKNAV---S 303
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 304 DGVEEE------IEQLESQIALNERqRRQVQDELSTEQRATQQRTSRLERFETRQR--DLSAELEEIGKRVQRRREQIAK 375
Cdd:COG4717 379 AGVEDEeelraaLEQAEEYQELKEE-LEELEEQLEELLGELEELLEALDEEELEEEleELEEELEELEEELEELREELAE 457
|
170
....*....|..
gi 2421156680 376 LRTEISKLEDAH 387
Cdd:COG4717 458 LEAELEQLEEDG 469
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
663-837 |
8.34e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 663 RQEIDDIRSKLD-ENEGKQRKLSVREQKVRDGHRNIEAREEELRIERQRISKEVATWERQKVHIETRRAQLSSMVSEEQr 741
Cdd:PRK12704 63 KEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 742 gedggrvqaerqkieqqlrdnaqeraEALAEIAdSLTtmtdlvhrlalvglggQSEARQ--LAELKAEASRQREAIIeaQ 819
Cdd:PRK12704 142 --------------------------QELERIS-GLT----------------AEEAKEilLEKVEEEARHEAAVLI--K 176
|
170
....*....|....*...
gi 2421156680 820 KLYEQAESSynlAKAKAK 837
Cdd:PRK12704 177 EIEEEAKEE---ADKKAK 191
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-381 |
9.01e-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: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 209 QLQVELAEHRLKERQTMGELHRLAQDVDSLRKQNEVLERdverwqAREAAESQLRVLEALVpvvryTDTKAEHDRAKEAR 288
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANK------GREEAVKQLKKLQAQM-----KDLQRELEEARASR 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 289 KHAHAHYLEVKNAvSDGVEEEIEQLESQIALNERQRRQVQ---DELSTEQRATQQRTSRLE----RFETRQRDLSAELEE 361
Cdd:pfam01576 822 DEILAQSKESEKK-LKNLEAELLQLQEDLAASERARRQAQqerDELADEIASGASGKSALQdekrRLEARIAQLEEELEE 900
|
170 180
....*....|....*....|....*..
gi 2421156680 362 -------IGKRVQRRREQIAKLRTEIS 381
Cdd:pfam01576 901 eqsntelLNDRLRKSTLQVEQLTTELA 927
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
297-449 |
9.38e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2421156680 297 EVKNAVSDgVEEEIEQLESQIALNERQRRQVQDELSTEQRATQQRTSRLERFETRQRDLSAELEEIGKRVQRRREQIAKL 376
Cdd:TIGR04523 339 QLNEQISQ-LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2421156680 377 RTEISKLEDAHPEEKPQEGDSRELMqvaSELSKQKLELKNEIIQLQDSQKGLLRSNRQLTTDMNSNDRQLRDL 449
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEI---KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
|
| |
