|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1155 |
1.64e-120 |
|
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: 401.27 E-value: 1.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 3 YLKLLLLENFKSWRGRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTA-NLRVKNVRELIHgaHVGKPFSSTASVK 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 82 IVYCEENGEEKTFS-------RIIRGSCSEFLFNDKAVSRSVYTAELEKIGIIVKARNCMVFQGAVESIAMKKPKERTQL 154
Cdd:pfam02463 79 ITFDNEDHELPIDKeevsirrRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 155 FEQISNSWEFAEEYDRKKKKMQQAEGDAQFNYNKKKHVAVERKHAKLEKEEAERYQMLLEELKENRIQLQLFRLYHNEKK 234
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 235 IDFLNNKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVDM 314
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 315 AKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEKKVEEEMLQRRADVELEASQLDRYKELKELARKKVATLTQQLE 394
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 395 KLQWEQKADLERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKKQQEKVLIDEMENSRVQIAQVN 474
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 475 EELNKIVGELQNARIDYHEGRRQQKRAEMLESLKRLYPDSVFGRLLDLCHPIHKKYQLAVTKVFGKYMSAIVVATEKIAR 554
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 555 DCIRFLKEERAEPETFLALDYLDIKPINEKLREIKGSKMMIDVVQTPFTPLKKVIQFVCGNGLVCETVKEARQIAFDgav 634
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT--- 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 635 rlKELMKIKRKETDLKQLQAQCQGTQTRLKYSQSELENIKKKHLANFYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIE 714
Cdd:pfam02463 636 --KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 715 EFQKKMNEVEDAVFQDFCEEIGVENIRVFEQERVKQQEETDRKRLEFENQKTRLSIQLEYSRGQLQKLVNKIHMLKEAVR 794
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 795 KDEAEIVRLKKDEEEFLLMVNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEAISIETSLEQKR 874
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELL 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 875 LERHNMLLECKVQDLRISVLLGSLDEISEVEL----GTEAESTEATADIYERERAIQIDYSSLTDDLTDLQSDKEIEAHL 950
Cdd:pfam02463 874 LKEEELEEQKLKDELESKEEKEKEEKKELEEEsqklNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 951 TRLQQQIVSKENVLFKTAAPNLRALEKLQTAKDKFQESVDAFEASRREARICRQEFEQMKKRRYERFSQCFEHVSVAIDQ 1030
Cdd:pfam02463 954 NKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1031 IYKKLCRNSCAQAFLSPENPEEPYLEGISYNCVAPGKRFMPMDNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALD 1110
Cdd:pfam02463 1034 NKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALD 1113
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*
gi 2092133180 1111 NTNIGKVSSFIKEQaQEQCQMIVISLKEEFYSRADALIGVCPEQD 1155
Cdd:pfam02463 1114 DQNVSRVANLLKEL-SKNAQFIVISLREEMLEKADKLVGVTMVEN 1157
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1167 |
1.85e-81 |
|
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: 290.82 E-value: 1.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 3 YLKLLLLENFKSWRGRQSIgPFMK-FNCIIGPNGSGKSNIMDALSFVMGERTAN-LRVKNVRELIHGAHVGKPfSSTASV 80
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKgFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQS-GNEAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 81 KIVYCEENG---EEKTFSRIIR----GSCSEFLFNDKAVSRSVYTAELEKIGIIVKARNcMVFQGAVESIAMKKPKERTQ 153
Cdd:TIGR02169 79 TVTFKNDDGkfpDELEVVRRLKvtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYN-VVLQGDVTDFISMSPVERRK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 154 LFEQISNSWEFAEEYDRKKKKMQQAEGDAQFNYNKKKHVAVERKHAKLEKEEAERYQMLLEELKENRIQLQLFRLYHNEK 233
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 234 KIDFLNNKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHM-EKEMKTLEASLNQKRPQYIKAKENTSHQIKKV 312
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 313 DMAKKSSKDNEKHLAKQEQNIKELDTELTDVER---SWRAYEKKVEEEMLQRRADVELEASQLDRYKELKELARKKVATL 389
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 390 TQQLEKLQWEQKADLERMtlderkqKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKKQQEKVLIDEMENSRVQ 469
Cdd:TIGR02169 398 KREINELKRELDRLQEEL-------QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 470 IAQVNEELNKIVGELQNAR--IDYHEGRRQQKRAEMLES-----LKRLYPDSVFGRLLDLCHpIHKKYQLAVTKVFGKYM 542
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQreLAEAEAQARASEERVRGGraveeVLKASIQGVHGTVAQLGS-VGERYATAIEVAAGNRL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 543 SAIVVATEKIARDCIRFLKEERAEPETFLALDYLDIKPIN-EKLREIKGSKMMIDVVQtpFTP-LKKVIQFVCGNGLVCE 620
Cdd:TIGR02169 550 NNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDlSILSEDGVIGFAVDLVE--FDPkYEPAFKYVFGDTLVVE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 621 TVKEARQIA------------FD-------GAVRLKELMKIKRKETD-LKQLQAQCQGTQTRLKYSQSELENIkKKHLAN 680
Cdd:TIGR02169 628 DIEAARRLMgkyrmvtlegelFEksgamtgGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRI-ENRLDE 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 681 FYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEEFQKKMNEVEDAvfqdfceeigvenIRVFEQERVKQQEETDRKRLE 760
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE-------------IENVKSELKELEARIEELEED 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 761 FENQKTRL-SIQLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEEFLLMVNEIMEEQQHLKDRLITLKTEVTKAQ 839
Cdd:TIGR02169 774 LHKLEEALnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 840 NAVEESRKKLLTLNREMGKLQKEAISIETSLEQKRLERHNMLLECKVQDLRISVLLGSLDEISEV--ELGTEAESTEATA 917
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlsELKAKLEALEEEL 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 918 DIYERERAIQIDYSSLTDDLTDLQSDKEieahltRLQQQIVSKENVlfktaapNLRALEKLQTAKDKFQESVDAFEASRR 997
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEEELSLEDVQAELQ------RVEEEIRALEPV-------NMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 998 EARICRQEFEQMKKRRYERFSQCFEHVSVAIDQIYKKLcrnSCAQAFLSPENPEEPYLEGISYNCVAPGKRFMPMDNLSG 1077
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL---SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSG 1077
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1078 GEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAQEqCQMIVISLKEEFYSRADALIGVCPEQDDY 1157
Cdd:TIGR02169 1078 GEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGE-AQFIVVSLRSPMIEYADRAIGVTMRRNGE 1156
|
1210
....*....|
gi 2092133180 1158 mfSQVLTLDL 1167
Cdd:TIGR02169 1157 --SQVFGLKL 1164
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-148 |
3.92e-80 |
|
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: 262.89 E-value: 3.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 4 LKLLLLENFKSWRGRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVRELIHGAHVGKPFSSTASVKIV 83
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092133180 84 YCEENGEEKTFSRIIRGSCSEFLFNDKAVSRSVYTAELEKIGIIVKARNCMVFQGAVESIAMKKP 148
Cdd:cd03275 81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-1150 |
2.45e-70 |
|
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: 257.68 E-value: 2.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 3 YLKLLLLENFKSWRGRQSIGpfmkFN----CIIGPNGSGKSNIMDALSFVMGERTA-NLRVKNVRELIHGAHVGKPFSST 77
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTIN----FDkgitGIVGPNGCGKSNIVDAIRWVLGEQSAkALRGGKMEDVIFNGSETRKPLSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 78 ASVKIVYCEENGEEKTFS--------RIIRGSCSEFLFNDKAVSRSVYTAELEKIGIIVKARNcMVFQGAVESIAMKKPK 149
Cdd:TIGR02168 77 AEVELVFDNSDGLLPGADyseisitrRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYS-IIEQGKISEIIEAKPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 150 ERTQLFEQ---ISnswefaeEYDRKKKKMQQAEGDAQFNYNKKKHVAVER----KHAKLEKEEAERYQMLLEELKENRIQ 222
Cdd:TIGR02168 156 ERRAIFEEaagIS-------KYKERRKETERKLERTRENLDRLEDILNELerqlKSLERQAEKAERYKELKAELRELELA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 223 LQLFRLYHNEKKIDFLNNKLGEKN--------------MDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLE 288
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEeeleeltaelqeleEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 289 ASLNQKRPQYIKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEKKVEEemlqRRADVELE 368
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 369 ASQLDRYKELKELARKKVATLTQQLEKLQWEQKADLERMTLDERKQKEIEesIKQVVEQIEDHKKRIQKLEEYTKSCIEL 448
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 449 LAEKKQQEKVLIDEMENSRVQIAQVNEELNKIVGELQNARiDYHEGRRQQKraemlesLKRLYPDSVFGRLLDLCHpIHK 528
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE-GFSEGVKALL-------KNQSGLSGILGVLSELIS-VDE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 529 KYQLAVTKVFGKYMSAIVVATEKIARDCIRFLKEERAEPETFLALDYLDIKPINEKLREIKGSK-----MMIDVVQTPfT 603
Cdd:TIGR02168 534 GYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgVAKDLVKFD-P 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 604 PLKKVIQFVCGNGLVCETVKEARQIA-----------FDG-----------------AVRLKELMKIKRKETDLKQLQAQ 655
Cdd:TIGR02168 613 KLRKALSYLLGGVLVVDDLDNALELAkklrpgyrivtLDGdlvrpggvitggsaktnSSILERRREIEELEEKIEELEEK 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 656 CQGTQTRLKYSQSELENIK------KKHLANFYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEEFQKKMNEVEDAVFQ 729
Cdd:TIGR02168 693 IAELEKALAELRKELEELEeeleqlRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 730 DFCEEIGVENIRVFEQERVKQQEE---TDRKRL-EFENQKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKK 805
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEelkALREALdELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 806 DEEEFLLMVNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEAISIETSLEQKRLERHNMLLECK 885
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 886 VQDLRISVLLGSLDEISEVELGtEAESTEATADIYEREraiqidyssltddltdlqsdkeIEAHLTRLQQQIVSKENVlf 965
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLE-EAEALENKIEDDEEE----------------------ARRRLKRLENKIKELGPV-- 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 966 ktaapNLRALEKLQTAKDKFQEsVDAFEASRREAR-ICRQEFEQMKKRRYERFSQCFEHVSVAIDQIYKKLCRNscAQAF 1044
Cdd:TIGR02168 988 -----NLAAIEEYEELKERYDF-LTAQKEDLTEAKeTLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGG--GEAE 1059
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1045 LSPENPEEPYLEGISYNCVAPGKRFMPMDNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQ 1124
Cdd:TIGR02168 1060 LRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEF 1139
|
1210 1220
....*....|....*....|....*.
gi 2092133180 1125 AqEQCQMIVISLKEEFYSRADALIGV 1150
Cdd:TIGR02168 1140 S-KNTQFIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1064-1167 |
4.36e-62 |
|
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: 212.05 E-value: 4.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1064 APGKRFMPMDNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAQEQCQMIVISLKEEFYSR 1143
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224
|
90 100
....*....|....*....|....
gi 2092133180 1144 ADALIGVCPEQdDYMFSQVLTLDL 1167
Cdd:cd03275 225 ADALVGVYRDQ-ECNSSKVLTLDL 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-1167 |
1.04e-50 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 195.16 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 3 YLKLLLLENFKSWRGRQSIgPFMK-FNCIIGPNGSGKSNIMDALSFVMGERTA-NLRVKNVRELIH-GAHVGKPfSSTAS 79
Cdd:COG1196 2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEQSAkSLRGGKMEDVIFaGSSSRKP-LGRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 80 VKIVYCEENG------EEKTFSRII-RGSCSEFLFNDKAVSRSVYTAELEKIGIIVKARNcMVFQGAVESIAMKKPKERT 152
Cdd:COG1196 80 VSLTFDNSDGtlpidyDEVTITRRLyRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYS-IIGQGMIDRIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 153 QLFEQ---ISnswefaeEYDRKKKKmqqAEgdaqfnyNKKKHVA------------VERKHAKLEK--EEAERYQMLLEE 215
Cdd:COG1196 159 AIIEEaagIS-------KYKERKEE---AE-------RKLEATEenlerledilgeLERQLEPLERqaEKAERYRELKEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 216 LKENRIQLQLFRLYHNEKKIDFLNNKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKR 295
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 296 PQYIKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEKKVEEEMLQRRADVELEASQLDRY 375
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 376 KELKELARKKVATLTQQLEKLQWEQKADLERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKKQQ 455
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 456 EKVLIDEMENSRVQIAQVNEELNKI-----VGELQNARIDYHEGRRQQKRAEMLESLKRLYPDSVFGRLLDLchpihKKY 530
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELaeaaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE-----AAY 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 531 QLAVTKVFGKYMSAIVVATEKIARDCIRFLKEERAEPETFLALDyldikpineklreikgskmmidvvqtpftplkkviq 610
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD------------------------------------ 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 611 fvcgnglvcetvkearqiafdgavrlkelmKIKRKETDLKQLQAqcqgtqtrlkysqselenikkkhlanfykekskles 690
Cdd:COG1196 581 ------------------------------KIRARAALAAALAR------------------------------------ 594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 691 elvniksqyamlneGLLQRAEKIEEFQKKMNEVEDAVFQDFCEEIGVENIRvfEQERVKQQEETDRKRLEFENQKTRLSI 770
Cdd:COG1196 595 --------------GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR--LEAALRRAVTLAGRLREVTLEGEGGSA 658
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 771 QLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEEfllmvneimeeqqhlkdrlitlktevtkaqnAVEESRKKLL 850
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE-------------------------------ALLAEEEEER 707
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 851 TLNREMGKLQKEAISIETSLEQKRLERHNmlleckvqdlrisvllgSLDEISEVELGTEAESTEATADIYEREraiqidy 930
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREE-----------------LLEELLEEEELLEEEALEELPEPPDLE------- 763
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 931 ssltddltdlqsdkEIEAHLTRLQQQIVSKENVlfktaapNLRALEKLQTAKDKFQESVDAF---EASRR--EARIcrqe 1005
Cdd:COG1196 764 --------------ELERELERLEREIEALGPV-------NLLAIEEYEELEERYDFLSEQRedlEEAREtlEEAI---- 818
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1006 fEQMKKRRYERFSQCFEHVSVAIDQIYKKLCRNScaQAFLSPENPEEPyLE-GISYNCVAPGKRFMPMDNLSGGEKSVAA 1084
Cdd:COG1196 819 -EEIDRETRERFLETFDAVNENFQELFPRLFGGG--EAELLLTDPDDP-LEtGIEIMAQPPGKKLQRLSLLSGGEKALTA 894
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1085 LALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAqEQCQMIVISLKEEFYSRADALIGVCPEQDDYmfSQVLT 1164
Cdd:COG1196 895 LALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMS-EDTQFIVITHNKRTMEAADRLYGVTMQEPGV--SRVVS 971
|
...
gi 2092133180 1165 LDL 1167
Cdd:COG1196 972 VDL 974
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1064-1151 |
3.15e-30 |
|
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: 118.72 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1064 APGKRFMPMDNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAqEQCQMIVISLKEEFYSR 1143
Cdd:cd03278 103 APGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS-KETQFIVITHRKGTMEA 181
|
....*...
gi 2092133180 1144 ADALIGVC 1151
Cdd:cd03278 182 ADRLYGVT 189
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
513-628 |
1.13e-26 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 105.78 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 513 DSVFGRLLDLCHpIHKKYQLAVTKVFGKYMSAIVVATEKIARDCIRFLKEERAEPETFLALDYLDIKPI-NEKLREIK-- 589
Cdd:smart00968 1 PGVLGRVADLIS-VDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPaGSKLREALlp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2092133180 590 ---GSKMMIDVVQTPfTPLKKVIQFVCGNGLVCETVKEARQI 628
Cdd:smart00968 80 epgFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1075-1150 |
6.53e-24 |
|
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: 100.08 E-value: 6.53e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133180 1075 LSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAQEQCQMIVISLKEEFYSRADALIGV 1150
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGV 170
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1065-1150 |
4.40e-23 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 98.52 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1065 PGKRFMPMDNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAqEQCQMIVISLKEEFYSRA 1144
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERT-KNAQFIVISLRNNMFELA 196
|
....*.
gi 2092133180 1145 DALIGV 1150
Cdd:cd03274 197 DRLVGI 202
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
7-160 |
6.70e-22 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 95.06 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 7 LLLENFKSWRGRQSIGPFMK-FNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVRELIHGAHvGKPFSSTASVKIvyc 85
Cdd:cd03274 6 LVLENFKSYAGEQVIGPFHKsFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSA-GHPNLDSCSVEV--- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092133180 86 eengeekTFSRIIrgscseflfnDKAVsrsvytaeLEKIGIIVKARNCMVFQGAVESIAMkKPKERtqlFEQISN 160
Cdd:cd03274 82 -------HFQEII----------DKPL--------LKSKGIDLDHNRFLILQGEVEQIAQ-MPKKS---WKNISN 127
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1075-1155 |
2.19e-21 |
|
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: 92.04 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1075 LSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAQEQCQMIVISLKEEFYSRADALIGVCPEQ 1154
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157
|
.
gi 2092133180 1155 D 1155
Cdd:cd03227 158 T 158
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
513-629 |
4.08e-20 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 86.93 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 513 DSVFGRLLDLCHpIHKKYQLAVTKVFGKYMSAIVVATEKIARDCIRFLKEERAEPETFLALDYLDIKPINEKLREIKGSK 592
Cdd:pfam06470 2 KGVLGRLADLIE-VDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAG 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2092133180 593 MMIDVVQTPfTPLKKVIQFVCGNGLVCETVKEARQIA 629
Cdd:pfam06470 81 PLLDLVEYD-DEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-86 |
8.25e-20 |
|
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: 88.13 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 4 LKLLLLENFKSWRGRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVRELIHGAhvGKPFSSTASVKIV 83
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEIT 78
|
...
gi 2092133180 84 YCE 86
Cdd:cd03239 79 FDK 81
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-106 |
1.14e-19 |
|
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: 88.29 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 4 LKLLLLENFKSWRGRQSIgPFMK-FNCIIGPNGSGKSNIMDALSFVMGERTA-NLRVKNVRELIHGAHVGKPFSSTASVK 81
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPgLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVT 79
|
90 100
....*....|....*....|....*
gi 2092133180 82 IVYCEENGeekTFSRIIRGSCSEFL 106
Cdd:cd03278 80 LTFDNSDG---RYSIISQGDVSEII 101
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1075-1147 |
2.92e-17 |
|
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: 82.73 E-value: 2.92e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133180 1075 LSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALD--NT-NIGKVssfIKEQAqEQCQMIVISLKEEFYSRADAL 1147
Cdd:cd03273 167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlsHTqNIGRM---IKTHF-KGSQFIVVSLKEGMFNNANVL 238
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
3-140 |
3.66e-17 |
|
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: 82.35 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 3 YLKLLLLENFKSWRGRQSIGPF-MKFNCIIGPNGSGKSNIMDALSFVMG-ERTANLRVKNVRELIHgaHVGKPFSSTASV 80
Cdd:cd03273 2 HIKEIILDGFKSYATRTVISGFdPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIY--KRGQAGITKASV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092133180 81 KIVYCE----------ENGEEKTFSRIIR-GSCSEFLFNDKAVSRSVYTAELEKIGIIVKARNCMVFQGAV 140
Cdd:cd03273 80 TIVFDNsdksqspigfENYPEITVTRQIVlGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1072-1150 |
9.33e-16 |
|
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: 78.07 E-value: 9.33e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092133180 1072 MDNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTNIGKVSSFIKEQAqEQCQMIVISLKEEFYSRADALIGV 1150
Cdd:cd03272 156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELS-DGAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
4-159 |
8.67e-14 |
|
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: 72.29 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 4 LKLLLLENFKSWRGRQSIGPFM-KFNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVRELIHgaHVGKPFSSTASVKI 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSpKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLH--EGSGPSVMSAYVEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 83 V------YCEENGEEKTFSRIIRGSCSEFLFNDKAVSRSVYTAELEKIGI-------IVKarncmvfQGAVESIAMKKPK 149
Cdd:cd03272 79 IfdnsdnRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFsrsnpyyIVP-------QGKINSLTNMKQD 151
|
170
....*....|
gi 2092133180 150 ErTQLFEQIS 159
Cdd:cd03272 152 E-QQEMQQLS 160
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
298-904 |
6.81e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 298 YIKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEKKvEEEMLQRRADVELEASQLDRYKE 377
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE-LPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 378 LKELARKKVATLTQQLEKLqweqkadlermtldERKQKEIEESIKQVVEQIEDHK---KRIQKLEEYTKSCIELLAEKKQ 454
Cdd:PRK03918 239 EIEELEKELESLEGSKRKL--------------EEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 455 QEKVLID---EMENSRVQIAQVNEELNKIvgELQNARIDYHEGRRQ--QKRAEMLESLKRLYPDSVfgRLLDLCHPIHKK 529
Cdd:PRK03918 305 YLDELREiekRLSRLEEEINGIEERIKEL--EEKEERLEELKKKLKelEKRLEELEERHELYEEAK--AKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 530 YQLAVTKVFGKYMSAIVVATEKIARDcIRFLKEERAEPETflaldylDIKPINEKLREIKGSKMMIDVVQTPFTPLKK-- 607
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEE-ISKITARIGELKK-------EIKELKKAIEELKKAKGKCPVCGRELTEEHRke 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 608 -VIQFVCGNGLVCETVKEARQIAFDGAVRLKELMKIKRKETDLKQLQAqcqgTQTRLKYSQSELENIKKKHLANFYKEKS 686
Cdd:PRK03918 453 lLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE----LAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 687 KLESELVNIKSQYamlnEGLLQRAEKIEEFQKKMNEVEDAV---------FQDFCEEIGVENIRVFEqERVKQQEETDRK 757
Cdd:PRK03918 529 KLKEKLIKLKGEI----KSLKKELEKLEELKKKLAELEKKLdeleeelaeLLKELEELGFESVEELE-ERLKELEPFYNE 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 758 RLEFENQKTRLSIQLEysrgQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEEFLLMVNEimEEQQHLKDRLITLKTEVTK 837
Cdd:PRK03918 604 YLELKDAEKELEREEK----ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAG 677
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092133180 838 AQNAVEESRKKLLTLNREMGKLQKEAISIETSLEQ-----KRLERHNMLLEcKVQDLRISVLLGSLDEISEV 904
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEEREKAKKElekleKALERVEELRE-KVKKYKALLKERALSKVGEI 748
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
9-59 |
2.73e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 57.37 E-value: 2.73e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2092133180 9 LENFKSWRGRQSIGPF-MKFNCIIGPNGSGKSNIMDALSFVMGERTANLRVK 59
Cdd:cd03227 4 LGRFPSYFVPNDVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRR 55
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1075-1144 |
3.59e-09 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 56.87 E-value: 3.59e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1075 LSGGEKSVAALALVFAihsfRPAPFFILDEVDAALDNTNIGKVSSFIKEQAQEQCQMIVISLKEEFYSRA 1144
Cdd:cd00267 81 LSGGQRQRVALARALL----LNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-509 |
2.53e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 144 AMKKPKERTQLFEQISNSWEFAEEYDRKKKKMQQAEGDAQFNynKKKHVAVERKHAKLEKEEAERYQMLLEELKENRIQL 223
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 224 QLFRLYHNEKKIDFLNNKLGE---KNMDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIK 300
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEakkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 301 AKE-NTSHQIKKVDMAKKSSKDNEKHLAKQEQnIKELDTELTDVERSWRAYEKKVEEEMLQRRADVELEASQLDRYKELK 379
Cdd:PTZ00121 1554 AEElKKAEEKKKAEEAKKAEEDKNMALRKAEE-AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 380 ---ELARKKVATLTQQLEKLQWEQ------KADLERMTLDERKQ----KEIEESIKQVVEQIEDHKKRIQKLEEYTKSCI 446
Cdd:PTZ00121 1633 kkvEQLKKKEAEEKKKAEELKKAEeenkikAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092133180 447 EllaEKKQQEKVLIDEMENS---------------RVQIAQVNEELNKIVGELQNARIDYHEGRRQQKRAEMLESLKR 509
Cdd:PTZ00121 1713 E---EKKKAEELKKAEEENKikaeeakkeaeedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-214 |
2.88e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.40 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 9 LENFKSWRGRQSIgPFMK-FNCIIGPNGSGKSNIMDALSFVMGERTANlRVKNVRELIHGAhvgkpfSSTASVKIVYcEE 87
Cdd:COG0419 7 LENFRSYRDTETI-DFDDgLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVG------SEEASVELEF-EH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 88 NGEEKtfsRIIRgscseflfndkavsrsvytaelekigiivkarncmvFQGAVESIAMKKPKERTQLFEQISNswefAEE 167
Cdd:COG0419 78 GGKRY---RIER------------------------------------RQGEFAEFLEAKPSERKEALKRLLG----LEI 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2092133180 168 YDRKKKKMQQAEGDAQFNYNKKkhvaverkhAKLEKEEAERYQMLLE 214
Cdd:COG0419 115 YEELKERLKELEEALESALEEL---------AELQKLKQEILAQLSG 152
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-114 |
5.09e-08 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 56.32 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 3 YLKLLLLENFKSWRgRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMgeRTANLRVKNVRELI-HGAhvgkpfsSTASVK 81
Cdd:COG1195 1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLA--TGRSFRTARDAELIrFGA-------DGFRVR 70
|
90 100 110
....*....|....*....|....*....|...
gi 2092133180 82 IVYCEENGEEKTFSRIIRGSCSEFLFNDKAVSR 114
Cdd:COG1195 71 AEVERDGREVRLGLGLSRGGKKRVRINGKPVRR 103
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
287-828 |
2.07e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 287 LEASLNQKRPQYIKAK----ENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSwrayekkvEEEMLQRR 362
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--------LEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 363 ADVELEASQLDRYKELKELaRKKVATLTQQLEKLQWEQKAdlermtlderkQKEIEESIKQVVEQIEDHKKRIQKLEEyt 442
Cdd:COG4717 119 EKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLEE-----------LRELEEELEELEAELAELQEELEELLE-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 443 ksciELLAEKKQQEKVLIDEMENSRVQIAQVNEELNKIVGELQNARIDYHEGRRQQKRAEMLESLKRLYPDS-VFGRLLD 521
Cdd:COG4717 185 ----QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLlIAAALLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 522 LchpihkkyQLAVTKVFGKYMSAIVVATEKIARDCIRFLKEERAEPETFLALDYLDIKPINEKLREIkgskmmidvvqtp 601
Cdd:COG4717 261 L--------LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 602 ftplkkviqfvcgnglvcETVKEARQIAFDGAVRLKELMKIKRKETDLKQLQAQCQGTQTRLKYSQSELENIKKKHLANF 681
Cdd:COG4717 320 ------------------ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 682 ykeksklESElvniksqyamlnEGLLQRAEKIEEFQKKMNEVEDAvfqdfceeigvenirvfeQERVKQQEETDRKRLEF 761
Cdd:COG4717 382 -------EDE------------EELRAALEQAEEYQELKEELEEL------------------EEQLEELLGELEELLEA 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133180 762 ENqKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEefllmVNEIMEEQQHLKDRL 828
Cdd:COG4717 425 LD-EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAEL 485
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-179 |
2.64e-07 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 52.11 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 7 LLLENFKSWRGrQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVREL-IHGAHVGKPFSSTASVKIVYC 85
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFvKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 86 EENGE-----EKTFSRIIRGSCSEFLFNDKAVSRSVYTAELEKIGIIVKARNCMVFQGAVESIAMKKPKERTQLFEQISN 160
Cdd:pfam13476 80 NNDGRytyaiERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELEK 159
|
170
....*....|....*....
gi 2092133180 161 SWEFAEEYDRKKKKMQQAE 179
Cdd:pfam13476 160 ALEEKEDEKKLLEKLLQLK 178
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-48 |
5.12e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 53.40 E-value: 5.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2092133180 4 LKLLLLENFKSWRG-RQSIGPFmkfNCIIGPNGSGKSNIMDALSFV 48
Cdd:COG4637 2 ITRIRIKNFKSLRDlELPLGPL---TVLIGANGSGKSNLLDALRFL 44
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-862 |
1.21e-06 |
|
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: 53.05 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 7 LLLENFKSWRGRQSI--GPFMKFNCIIGPNGSGKSNIMDALSFVM----GERTANLRVKNVRELIHGAHVGKPF------ 74
Cdd:TIGR00618 6 LTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALygklPRRSEVIRSLNSLYAAPSEAAFAELefslgt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 75 SSTASVKIVYCEENGEEKTFSRIIRGSCSEF---LFNDKAVSRSVYTAELEKIGIIVKARNCMVFQGAVESIAMKKPKER 151
Cdd:TIGR00618 86 KIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGrgrILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 152 TQLFEQISNSWEFAEEYDRKKKKMQQAEGDAqfNYNKKKHVAVERKHAKLEKEEAERYQMLLEELKENRIQLQLFRLYHN 231
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKA--ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 232 EKKidflnnKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKK 311
Cdd:TIGR00618 244 YLT------QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 312 VDMAKKSS-KDNEKHLAKQEQNIKELDTELTDVERswrayekkvEEEMLQRRADVELE-ASQLDRYKELkelaRKKVATL 389
Cdd:TIGR00618 318 SKMRSRAKlLMKRAAHVKQQSSIEEQRRLLQTLHS---------QEIHIRDAHEVATSiREISCQQHTL----TQHIHTL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 390 TQQLEKL-QWEQKADLERMTLDERKQKEIEESIKQVVEQIedHKKRIQKLEEYTKSCIELLAEKKQQEKVLIDEMENSRV 468
Cdd:TIGR00618 385 QQQKTTLtQKLQSLCKELDILQREQATIDTRTSAFRDLQG--QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 469 QIAQVNEELNKIVGELQNarIDYHEGRRQQKRAEMLESLKRLyPDSVFGRLLdlcHPIHKKYQLAVTKVFGKYMSAI--- 545
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQ--IHLQETRKKAVVLARLLELQEE-PCPLCGSCI---HPNPARQDIDNPGPLTRRMQRGeqt 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 546 VVATEKIARDCIRFLKEERAEPETFLALDYLDIKPINEKLREIKGSKMMIDVVQTPFTPLKKVIQfvcgnglvcETVKEA 625
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE---------KLSEAE 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 626 RQIAFDGAVRLKELmKIKRKETDLKQLQAQCQ-----------GTQTRLKYSQSE-----LENIKKKHLANFYKEKSKLE 689
Cdd:TIGR00618 608 DMLACEQHALLRKL-QPEQDLQDVRLHLQQCSqelalkltalhALQLTLTQERVRehalsIRVLPKELLASRQLALQKMQ 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 690 SE---LVNIKSQYAMLNEGLLQRAEKIEEFQKKMNEVEDAVFQDFCEEIGVENIRVFEQERVKQQEETDRKRLEFENQKT 766
Cdd:TIGR00618 687 SEkeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 767 RLSIQLEYSRG-QLQKLVNKIHMLKEAVRKD-------EAEI-VRLKKDEEEFLLMVNEIMEEQQHLKDRLITLKT---E 834
Cdd:TIGR00618 767 NEEVTAALQTGaELSHLAAEIQFFNRLREEDthllktlEAEIgQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAtlgE 846
|
890 900
....*....|....*....|....*...
gi 2092133180 835 VTKAQNAVEESRKKLLTLNREMGKLQKE 862
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-96 |
1.50e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.30 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 4 LKLLLLENFKSWRGRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVM-GERTANLRvknvreliHGAHVGKPFSST---AS 79
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSK--------GGAHDPKLIREGevrAQ 72
|
90
....*....|....*..
gi 2092133180 80 VKIVYCEENGEEKTFSR 96
Cdd:cd03240 73 VKLAFENANGKKYTITR 89
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1071-1150 |
2.97e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1071 PMDNLSGGEKSVAALALVFAIHSFRPA--PFFILDEVDAALDNTNI-GKVSSFIKEQ-AQEQCQMIVISLKEEFYSRADA 1146
Cdd:cd03240 112 MRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERkSQKNFQLIVITHDEELVDAADH 191
|
....
gi 2092133180 1147 LIGV 1150
Cdd:cd03240 192 IYRV 195
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-259 |
3.09e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 50.47 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 27 FNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVRELIHGAHVGKPFSSTASVKIVYCEENGEEKTFSRIIRgscSEFL 106
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYR---YGLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 107 FNDKAVSRSVYTAELEKIGIIVKARNcmvfqgaVESIAMKKPKERTQLFEQISNSWE---FAEEYDRKKKKMQQAEGDAQ 183
Cdd:pfam13304 78 LEREDVEEKLSSKPTLLEKRLLLRED-------SEEREPKFPPEAEELRLGLDVEERielSLSELSDLISGLLLLSIISP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133180 184 FNYnkkkhvaVERKHAKLEKEEAERYQMLLEELKENRIQLQLFRLYHNEKKIDFLNNKLGEKNMDVNTKKDSLSSA 259
Cdd:pfam13304 151 LSF-------LLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRER 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
323-493 |
6.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 323 EKHLAKQEQNIKELDTELTDVERSWRAYEKKVE-EEMLQRRADVELEASQLDRYKELKELARKKVATLTQQLEKLQWEQK 401
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEySWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 402 ADLERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKK----QQEKVLIDEMENSRVQIAQVNEEL 477
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaaaLGDAVERELRENLEERIDALRARL 782
|
170
....*....|....*.
gi 2092133180 478 NKIVGELQNARIDYHE 493
Cdd:COG4913 783 NRAEEELERAMRAFNR 798
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-55 |
7.72e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 49.62 E-value: 7.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2092133180 3 YLKLLLLENFKSWRgRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTAN 55
Cdd:COG3593 2 KLEKIKIKNFRSIK-DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1072-1113 |
7.91e-06 |
|
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: 47.98 E-value: 7.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2092133180 1072 MDNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTN 1113
Cdd:cd03276 107 VKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN 148
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-865 |
8.99e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 101 SCSEFLFNDKAVSRSVYTAELEKiGIIVKARNCMVFQGAVESiamkKPKERTQLFEQISNSWEFAEEYD-RKKKKMQQAE 179
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAF-GKAEEAKKTETGKAEEAR----KAEEAKKKAEDARKAEEARKAEDaRKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 180 GDAQFNYNKK----KHVAVERKHAKLEKEEAERYQMLLEELKENRI-----QLQLFRLYHNEKKIDFLNNKLGEKNMDVN 250
Cdd:PTZ00121 1150 DAKRVEIARKaedaRKAEEARKAEDAKKAEAARKAEEVRKAEELRKaedarKAEAARKAEEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 251 TKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKE-NTSHQIKKVDMAKKSSK----DNEKH 325
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAEEKKKADEAKKAEEkkkaDEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 326 LAKQEQNIKELDTELTDVERSWRAYEKKVEEEMLQ---RRADVELEASQLDRYKELKELARKKVATLTQQLEKLQweQKA 402
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK--KKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 403 DlERMTLDERKQKEieESIKQVVEQIEDHKKRIQKLEEYTKSCIELL----AEKKQQEKVLIDEMENsRVQIAQVNEELN 478
Cdd:PTZ00121 1388 E-EKKKADEAKKKA--EEDKKKADELKKAAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADEAKK-KAEEAKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 479 KIVGELQNAridyHEGRRQQKRAEMLESLKRLYPDSVfgrlldlchpiHKKYQLAVTKVFGKYMSAIVVATEKIARDCIR 558
Cdd:PTZ00121 1464 KKAEEAKKA----DEAKKKAEEAKKADEAKKKAEEAK-----------KKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 559 FLKEERAEPETFLALDYLDIKPInEKLREIKGSKMMIDVVQTPFTPLKKviqfvcgnGLVCETVKEARQIAfdgAVRLKE 638
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADEL-KKAEELKKAEEKKKAEEAKKAEEDK--------NMALRKAEEAKKAE---EARIEE 1596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 639 LMKIKRKETDLKQLQAQcQGTQTRLKYSQSELENIKKKHLANFYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEEFQK 718
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 719 KmnevedavfqdfceeigvenirvfeQERVKQQEETDRKRLEFENQKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKDEA 798
Cdd:PTZ00121 1676 K-------------------------AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092133180 799 EIVRLKKDEEEFLLMVNEIMEEQ------QHLKDRLITLKTEVTKAQNAV--EESRKKLLTLNREMGKLQKEAIS 865
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
9-48 |
1.01e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 48.89 E-value: 1.01e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2092133180 9 LENFKSWRGRQSI------GPFMKFNCIIGPNGSGKSNIMDALSFV 48
Cdd:COG1106 7 IENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
814-1019 |
1.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 814 VNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEaisIETSleQKRLERHNMLLECKVQDLRISv 893
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEA--EAEIEERREELGERARALYRS- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 894 llGSLDEISEVELGteAESTeatADIYERERAIQIDYSSLTDDLTDLQSDKEIeahLTRLQQQIVSKENVLFKTAAPNLR 973
Cdd:COG3883 99 --GGSVSYLDVLLG--SESF---SDFLDRLSALSKIADADADLLEELKADKAE---LEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2092133180 974 ALEKLQTAKDKFQESVDAFEASRREARICRQEFEQMKKRRYERFSQ 1019
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-476 |
1.73e-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: 48.61 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 273 LNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEK 352
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 353 KVEE--------------EMLQRRADVELEASQLDRYKELKELARKKVATL---TQQLEKLQWEQKADLERMtldERKQK 415
Cdd:COG4942 105 ELAEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELradLAELAALRAELEAERAEL---EALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092133180 416 EIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKKQQEKVLIDEMENSRVQIAQVNEE 476
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
326-844 |
2.23e-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: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 326 LAKQEQNIKELDTELTDVeRSWRAYEKK--VEEEMLQRRADVELEASQLDRYKELKELARKKVATLTQQLEKLQWEQKAD 403
Cdd:COG4913 264 YAAARERLAELEYLRAAL-RLWFAQRRLelLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 404 LERM------TLDERKQK--EIEESIKQVVEQIEDHKKRiqkLEEYTKSCIELLAEKKQQEKVLIDEMENSRVQIAQVNE 475
Cdd:COG4913 343 LEREierlerELEERERRraRLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 476 ELNKIVGELQN--ARIDYHEGRRQQKRAEMLESLKrLYPDSV--FGRLLDLcHPIHKKYQLAVTKVFGKYMSAIVVATE- 550
Cdd:COG4913 420 ELRELEAEIASleRRKSNIPARLLALRDALAEALG-LDEAELpfVGELIEV-RPEEERWRGAIERVLGGFALTLLVPPEh 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 551 -KIARDCIRFLKEERaepetflALDYLDIKPINEKLREIKGSK----MMIDVVQTPFTP-----LKKVIQFVCgnglvCE 620
Cdd:COG4913 498 yAAALRWVNRLHLRG-------RLVYERVRTGLPDPERPRLDPdslaGKLDFKPHPFRAwleaeLGRRFDYVC-----VD 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 621 TVKE-------------------ARQIAFDGAVRLKELM------KIKRKETDLKQLQAQCQGTQTRLKYSQSELENIKK 675
Cdd:COG4913 566 SPEElrrhpraitragqvkgngtRHEKDDRRRIRSRYVLgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 676 KHLAnfYKEKSKLESELVNIKSQyamlnegllqrAEKIEEFQKKMNEVEDAVFQdfceeigvenIRVFEQERVKQQEETD 755
Cdd:COG4913 646 RREA--LQRLAEYSWDEIDVASA-----------EREIAELEAELERLDASSDD----------LAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 756 RKRLEFENQKTRLSiQLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEEFLLMVNEIMEE-QQHLKDRLITLKTE 834
Cdd:COG4913 703 ELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElRENLEERIDALRAR 781
|
570
....*....|
gi 2092133180 835 VTKAQNAVEE 844
Cdd:COG4913 782 LNRAEEELER 791
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-877 |
2.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 141 ESIAMKKPKERTQLFEQISNSWEFAEEYDRKKKKMQQAEGDAQFNYNKKKHVAVERKHAKLEKEEAERYQMLLEELKENR 220
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 221 IQLQlfRLYHNEKKIDFLNNKLGEKNMDVNTKKDSLSSAEDTFKAK--KKVLGILNRDQQHMEKEMKTLEASLNQKRPQY 298
Cdd:PTZ00121 1166 AEEA--RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEeeRKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 299 IKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKEldTELTDVERSWRAYEKKVEEEM-----LQRRADvelEASQLD 373
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA--DELKKAEEKKKADEAKKAEEKkkadeAKKKAE---EAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 374 RYKELKELARKKVATLTQQLEklqweqkadlERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIEllAEKK 453
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAE----------EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA--AKKK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 454 QQEKVLIDEMENSRVQIAQVNEELNKIVGELQNAridyHEGRRQQKRAEMLESLKRLYPDSVFGRLLDLCHPIHKKYQLA 533
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA----DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 534 VTKvfgkymsaivvATEKIARDCIRFLKEERAEPETfLALDYLDIKPINEKLREIKGSKMMIDVVQTPFTPLKKVIQFVC 613
Cdd:PTZ00121 1463 KKK-----------AEEAKKADEAKKKAEEAKKADE-AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 614 GNGLVCETVKEARQIAfdGAVRLKELMKIKRKETDLKQLQAQCQGTQTRLKYSQSE-LENIKKKHLanfyKEKSKLESEL 692
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKK--KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARI----EEVMKLYEEE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 693 VNIKSQYAMLNEGLLQRAEKIEEFQKKMNEVEDAVFQDFCEEIGVENIRVFEQERVKQQEETDRKRLEFENQKTRLSIQL 772
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 773 EYSRGQLQKLVNKIHMLK--EAVRKDEAEIVR----LKKDEEEFLLMVNEIMEEQQHLKDRLITLKT---EVTKAQNAVE 843
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKkaEELKKKEAEEKKkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKK 1764
|
730 740 750
....*....|....*....|....*....|....
gi 2092133180 844 ESRKKLLTLNREMGKLQKEAISIETSLEQKRLER 877
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
166-874 |
2.56e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 166 EEYDRKKKKMQQAEGDAQFNYNKKK---HVAVERKHAKLEKEEAERYQMLLEELKENRIQLQLfrlyHNEkkidfLNNKL 242
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKfylRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL----RNQ-----LQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 243 GEKNMDVNTKKDSLSSAedtfkakkkvlgilNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVD-MAKKSSKD 321
Cdd:pfam15921 152 HELEAAKCLKEDMLEDS--------------NTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDsMSTMHFRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 322 NEKHLAKQeqnIKELDTELTDVERSWRAYEKKVEEEMLQRRADVELEASQ-LDRYKEL--------------KELARKKV 386
Cdd:pfam15921 218 LGSAISKI---LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhQDRIEQLiseheveitgltekASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 387 ATLTQQLEKLQwEQKADLERMTLdeRKQKEIEESIKQVVEQIEDHKKRIQ-KLEEYTKSCIelLAEKkqqekvlidEMEN 465
Cdd:pfam15921 295 NSIQSQLEIIQ-EQARNQNSMYM--RQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLV--LANS---------ELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 466 SRVQIAQVNEELNKIVGELQNARIDYHegRRQQKRAEMLESLKRLYpDSVFGRLLDLchpIHKKYQLAVTKVFGKYMSAI 545
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLLADLH--KREKELSLEKEQNKRLW-DRDTGNSITI---DHLRRELDDRNMEVQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 546 VVATEKIARDCI-RFLKEERAEPETFLALDYL--DIKPINEKLR----EIKGSKMMIDVVQTPFTPLKKVIQFvcGNGLV 618
Cdd:pfam15921 435 LKAMKSECQGQMeRQMAAIQGKNESLEKVSSLtaQLESTKEMLRkvveELTAKKMTLESSERTVSDLTASLQE--KERAI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 619 CETVKEARQIAFDGAVRLKELMKIKRKETDLKQLQAQCQGTQTRLKYSQSELEnIKKKHLANFYKEKSKLESELVNIKSQ 698
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE-ILRQQIENMTQLVGQHGRTAGAMQVE 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 699 YAMLNEGLLQRAEKIEEFqKKMNEVEDAVFQDFceEIGVENIRVFEQERVKQQEETDRKRLEFENQKTRLSIQLEYSRGQ 778
Cdd:pfam15921 592 KAQLEKEINDRRLELQEF-KILKDKKDAKIREL--EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 779 LQKLVNKIHMLKEAVRkdeaeivrlKKDEEefllmvneiMEEQQHlkdrliTLKTEVTKAQNAVEESRKKLLTLNREMGK 858
Cdd:pfam15921 669 LNSLSEDYEVLKRNFR---------NKSEE---------METTTN------KLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
730
....*....|....*.
gi 2092133180 859 LQKEAISIETSLEQKR 874
Cdd:pfam15921 725 AMKVAMGMQKQITAKR 740
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
323-484 |
2.57e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 323 EKHLAKQEQNIKELDTELTDVERSWRAYEKKVEEemlqRRADVELEASQLDRYKELKELARKKVATLTQQLEKL--QWEQ 400
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 401 KADLERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKKQQekvLIDEMENSRVQIAQVNEELNKI 480
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREEL 168
|
....
gi 2092133180 481 VGEL 484
Cdd:COG1579 169 AAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
258-503 |
3.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 258 SAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKEntshqikKVDMAKKSSKDNEKHLAKQEQNIKELD 337
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-------ELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 338 TELTDVERSwrAYEKKVEEEMLqrraDVELEASQLdrykelkelarkkvATLTQQLEKLQWEQKADLERMTLDERKQKEI 417
Cdd:COG3883 86 EELGERARA--LYRSGGSVSYL----DVLLGSESF--------------SDFLDRLSALSKIADADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 418 EESIKQVVEQIEDHKKRIQKLEEYTKsciELLAEKKQQEKvLIDEMENSRVQIAQVNEELNKIVGELQNARIDYHEGRRQ 497
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKA---ELEAQQAEQEA-LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
....*.
gi 2092133180 498 QKRAEM 503
Cdd:COG3883 222 AAAAAA 227
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
163-860 |
3.15e-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: 48.50 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 163 EFAEEYDRKKKKMQQAEGDAQFNYNKKKHVAVERKHAKLEKEEAERYQMLLE-ELKENRIQLQLFRLYHN---EKKID-F 237
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDsLIQSLATRLELDGFERGpfsERQIKnF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 238 LNNKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLgilnrdqQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVDMAKK 317
Cdd:TIGR00606 396 HTLVIERQEDEAKTAAQLCADLQSKERLKQEQA-------DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 318 SSKD---NEKHLAKQEQNIKELD-TELTDVERSWRAYEKKVEEEMLQRRADVELEASQLDRYKELK---ELARKKVATLT 390
Cdd:TIGR00606 469 SSDRileLDQELRKAERELSKAEkNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRtqmEMLTKDKMDKD 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 391 QQLEKLQWEQKADLERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYtkscielLAEKKQQEKVLIDEMENSRVQI 470
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE-------LASLEQNKNHINNELESKEEQL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 471 AQVNEELNKIVG------ELQNARIDYHEGRRQQKraeMLESLKRLYpDSVFGRLLDL---CHPIHK---KYQLAVTKVF 538
Cdd:TIGR00606 622 SSYEDKLFDVCGsqdeesDLERLKEEIEKSSKQRA---MLAGATAVY-SQFITQLTDEnqsCCPVCQrvfQTEAELQEFI 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 539 GKYMSAIVVATEKIaRDCIRFLKEERAEPETFLALDYLDIKPINEKLREIKGSKMMIDVVQTPFTPLKKVIQfvcGNGLV 618
Cdd:TIGR00606 698 SDLQSKLRLAPDKL-KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE---EQETL 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 619 CETV----KEARQIAFDGAVRLKELMKIKRKETDLKQLQAQCQGTQTRLKYSQSELENIKKKH---------------LA 679
Cdd:TIGR00606 774 LGTImpeeESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHeldtvvskielnrklIQ 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 680 NFYKEKSKLESELVNIKSQYAMLNEGLLQRA-------EKIEEFQKKMNEVEDAVFQDFCEEIGVENIRVFEQERVKQQE 752
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELKSEKLQIGTNLQRRQqfeeqlvELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 753 ETDRKRlefENQKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKD-EAEIVRL-----------KKDEEEFLLMVNEImeE 820
Cdd:TIGR00606 934 TSNKKA---QDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQkETELNTVnaqleecekhqEKINEDMRLMRQDI--D 1008
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2092133180 821 QQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQ 860
Cdd:TIGR00606 1009 TQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-510 |
4.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 149 KERTQLFEQISNSWEFAEEYDRKKKKMQQAEGDAQfnynKKKHVAVERKHAKLEKEEAERyqmllEELKENRIQLqlfrl 228
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKK----RLTGLTPEKLEKELEELEKAK-----EEIEEEISKI----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 229 yhnEKKIDFLNNKLGEKNMDVNTKKDS-----LSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKake 303
Cdd:PRK03918 411 ---TARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE--- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 304 ntshqIKKVdMAKKSSKDNEKHLAKQEQNIKELDTE--LTDVERSWRAYEkKVEEEMLQRRADVELEASQLDRYKELKel 381
Cdd:PRK03918 485 -----LEKV-LKKESELIKLKELAEQLKELEEKLKKynLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELK-- 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 382 arKKVATLTQQLEKLQwEQKADLErmtlderkqKEIEEsikQVVEQIEDHKKRIQKLEEYTKSCIEL------LAEKKQQ 455
Cdd:PRK03918 556 --KKLAELEKKLDELE-EELAELL---------KELEE---LGFESVEELEERLKELEPFYNEYLELkdaekeLEREEKE 620
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2092133180 456 EKVLIDEMENSRVQIAQVNEELNKIVGELQNARIDYHEGRRQQKRAEMLESLKRL 510
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
3-66 |
4.67e-05 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 47.08 E-value: 4.67e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133180 3 YLKLLLLENFKSWRgRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVM---GERTANLrvknvRELIH 66
Cdd:PRK00064 2 YLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYLLApgrSHRTARD-----KELIR 62
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1001-1157 |
5.10e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.01 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1001 ICRQEFEQMKKRRYERFSQCFEHVS-VAIDQIyKKLCRNscaqaflspenpeepyleGISYncVAPGKrfmPMDNLSGGE 1079
Cdd:cd03238 37 LVNEGLYASGKARLISFLPKFSRNKlIFIDQL-QFLIDV------------------GLGY--LTLGQ---KLSTLSGGE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092133180 1080 KSVAALALVFAIHSFRPapFFILDEVDAALDNTNIGKVSSFIKEQAQEQCQMIVISLKEEFYSRADALIGVCPEQDDY 1157
Cdd:cd03238 93 LQRVKLASELFSEPPGT--LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKS 168
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
28-727 |
1.03e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 28 NCIIGPNGSGKSNIMDALSFVMGERTanlRVKNVRELIhgahvgKPFSSTASVKIVYCEENGEEKTFSRIIR-----GSC 102
Cdd:PRK01156 26 NIITGKNGAGKSSIVDAIRFALFTDK---RTEKIEDMI------KKGKNNLEVELEFRIGGHVYQIRRSIERrgkgsRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 103 SEFLFNDKAVSRSVYTA----ELEKIGII--VKARNCMVFQGAVESIAMKKPKERTQLFEQISNSWEFAEEYDRKKK--K 174
Cdd:PRK01156 97 AYIKKDGSIIAEGFDDTtkyiEKNILGISkdVFLNSIFVGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDviD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 175 MQQAEGDaqfNYN------KKKHVAVERKHAKLEKEEAeRYQMLLEELKENRIQLQLfrlyhNEKKIDFLNNKLGEKNMD 248
Cdd:PRK01156 177 MLRAEIS---NIDyleeklKSSNLELENIKKQIADDEK-SHSITLKEIERLSIEYNN-----AMDDYNNLKSALNELSSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 249 VNTKKdSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVdmaKKSSKDNEKHLAK 328
Cdd:PRK01156 248 EDMKN-RYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK---KQILSNIDAEINK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 329 QEQNIKeldtELTDVERSWRAYEKKVE--EEMLQRRADVELEASQLDRYKELKELARKKVATLTQQLEKLQWEQKADLER 406
Cdd:PRK01156 324 YHAIIK----KLSVLQKDYNDYIKKKSryDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 407 MTLDERKQKEIEESIKQVVEQIEdhkKRIQKLEEYTKSCIELLAEKKQQEKVLIDE-----------MENSRVQIAQVNE 475
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDIS---SKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 476 ELNKI---VGELQNARIDYHEGRRQQ-KRAEMLESLKRLYPDSVFGRLLDLCHPIhKKYQLAVTKVFGKYMSAiVVATEK 551
Cdd:PRK01156 477 KKSRLeekIREIEIEVKDIDEKIVDLkKRKEYLESEEINKSINEYNKIESARADL-EDIKIKINELKDKHDKY-EEIKNR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 552 IARDCIRFLKEERAEPETFLA-LDYLDIKPI----NEKLREIKGSKMMIDVVQTPFTPLKKVIQFVCG---------NGL 617
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAvISLIDIETNrsrsNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIReieneannlNNK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 618 VCETVKEARQI-AFDGAVR--LKELMKIKRKETDLKQLQAQCQGTQTRLKYSQSELENIKkkhlANFYKEKSKLESELVN 694
Cdd:PRK01156 635 YNEIQENKILIeKLRGKIDnyKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK----ANRARLESTIEILRTR 710
|
730 740 750
....*....|....*....|....*....|...
gi 2092133180 695 iksqyamlNEGLLQRAEKIEEFQKKMNEVEDAV 727
Cdd:PRK01156 711 --------INELSDRINDINETLESMKKIKKAI 735
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
651-962 |
1.63e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 651 QLQAQCQGTQTRLKYSQSELENIK--KKHLANFYKEKSKLE-------SELVNIKSQYAMLNEGLLQRAEKIEEFQKKMN 721
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRqeKEEKAREVERRRKLEeaekarqAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 722 EVEDAVFQDfcEEIGVENIRVFEQERVK--QQEETDRKRLEFENQKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKDEAE 799
Cdd:pfam17380 359 KRELERIRQ--EEIAMEISRMRELERLQmeRQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 800 IVRLKKDEEEFLLMVNEIMEEQQHLKDRLitlktevtkaQNAVEESRKKLLTLNREMGKLQKEAISIETSLEQKRLERHN 879
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERL----------RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 880 MLLEckvQDLRISVLLGSLDE----ISEVELGTEAESTEATADIYERERAIQIDYSSLTDDLTDLQS-DKEIEahltrLQ 954
Cdd:pfam17380 507 AMIE---EERKRKLLEKEMEErqkaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAmERERE-----MM 578
|
....*...
gi 2092133180 955 QQIVSKEN 962
Cdd:pfam17380 579 RQIVESEK 586
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
315-486 |
2.97e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 315 AKKSSKDNEKHLAKQEQNIKELDTELTDVERSW----------RAYEKKVEEEMLQRRADVELEASQLDRYKELKELARK 384
Cdd:PRK04778 308 VEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYtlneselesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 385 KVATLTQqLEKLQWEQKADLERMTLDERkqkEIEESIKQVVEQIEDHKKRIQKL------EEYtkscIELLAEKKQQEKV 458
Cdd:PRK04778 388 ILKQLEE-IEKEQEKLSEMLQGLRKDEL---EAREKLERYRNKLHEIKRYLEKSnlpglpEDY----LEMFFEVSDEIEA 459
|
170 180
....*....|....*....|....*...
gi 2092133180 459 LIDEMENSRVQIAQVNEELNKIVGELQN 486
Cdd:PRK04778 460 LAEELEEKPINMEAVNRLLEEATEDVET 487
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
3-66 |
3.66e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 44.27 E-value: 3.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092133180 3 YLKLLLLENFKSW-RGRQSIGPfmKFNCIIGPNGSGKSNIMDALSFVMGERTanLRVKNVRELIH 66
Cdd:TIGR00611 2 YLSRLELTDFRNYdAVDLELSP--GVNVIVGPNGQGKTNLLEAIYYLALGRS--HRTSRDKPLIR 62
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
7-106 |
4.06e-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: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 7 LLLENFKSWRGRQSIGpFMKFN-----CIIGPNGSGKSNIMDALSFVM-GERTANLRVKNVRELIHGAHvgkpfsSTASV 80
Cdd:cd03279 6 LELKNFGPFREEQVID-FTGLDnnglfLICGPTGAGKSTILDAITYALyGKTPRYGRQENLRSVFAPGE------DTAEV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2092133180 81 KIVYcEENG-----------EEKTFSRII---RGSCSEFL 106
Cdd:cd03279 79 SFTF-QLGGkkyrversrglDYDQFTRIVllpQGEFDRFL 117
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
360-1035 |
4.90e-04 |
|
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: 44.57 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 360 QRRADVELEASQLDRYKELKELARKKVATLTQQLEKLQweqkADLERMTLDERKQKEIEESIKQVVE----QIEDHKKRI 435
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLT----LRSQLLTLCTPCMPDTYHERKQVLEkelkHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 436 QKLEEYTKSCIELLAEKKQQEKVL---IDEMENSRVQIAQVNEELNKIVGELQNARIDYHEGRRQQKRAEMLESLKRLyp 512
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLkqlRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 513 dsvfgrlldlchpihKKYQLAVTKVFGKYMSAIVVATEKIARDCIR---FLKEERAEPETFLALDYLDIKPINEKLREik 589
Cdd:TIGR00618 317 ---------------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtlHSQEIHIRDAHEVATSIREISCQQHTLTQ-- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 590 gskmMIDVVQTPFTPLKKVIQFVCGNgLVCETVKEARQIAFDGAVR-LKELMKIKRKETDLKQLQAQCQGTQTRLKYSQS 668
Cdd:TIGR00618 380 ----HIHTLQQQKTTLTQKLQSLCKE-LDILQREQATIDTRTSAFRdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 669 ELENIKKKHLANFYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEE----FQKKMNEVEDAVFQDFCEEIGVENIRVFE 744
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEepcpLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 745 QERVKQQEE---TDRKRLEFENQKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEEFLLMVNEIMEEQ 821
Cdd:TIGR00618 535 QTYAQLETSeedVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 822 QHLKDRL---ITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEAISIE---TSLEQKRLERHNMLLECKVQDLRISV-- 893
Cdd:TIGR00618 615 HALLRKLqpeQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsIRVLPKELLASRQLALQKMQSEKEQLty 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 894 -------LLGSLDEISEVELGTEAESTEATADIYERERAIQIDYSSLTDDLTDLQSD-KEIEAHLTRLQQQIVSKENVLF 965
Cdd:TIGR00618 695 wkemlaqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQaRTVLKARTEAHFNNNEEVTAAL 774
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 966 KTAAPNLRALEKLQTAKDKFQESVDAFEASRREARICRQEFEQMKKRRYERFSQCFEHVSVAIDQIYKKL 1035
Cdd:TIGR00618 775 QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATL 844
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
9-132 |
5.17e-04 |
|
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: 42.58 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 9 LENFKSWrGRQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTANL-RVKNVRELI-HGahvgkpfSSTASVKI-VYC 85
Cdd:cd03277 8 LENFVTY-DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKVGEFVkRG-------CDEGTIEIeLYG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2092133180 86 EENgeektfsRIIRGSCSEFLFNDKAVSrsvyTAELEKIGIIVKARN 132
Cdd:cd03277 80 NPG-------NIQVDNLCQFLPQDRVGE----FAKLSPIELLVKFRE 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-435 |
5.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 191 HVAVERKHAKLE-----KEEAERYQMLLEELKENRIQLQLFRLYHNEKKIDFLNNKLGEknmdvntkkdslssaedtfka 265
Cdd:COG4913 241 HEALEDAREQIEllepiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--------------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 266 kkkvlgiLNRDQQHMEKEMKTLEASLNQKRPQYIKAKEntshQIKKVDmakkssKDNEKHLAKQeqnIKELDTELTDVER 345
Cdd:COG4913 300 -------LRAELARLEAELERLEARLDALREELDELEA----QIRGNG------GDRLEQLERE---IERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 346 SWRAYEKKVeeemlqRRADVELEASQlDRYKELKELARKKVATLTQQLEKLQwEQKADLERmtlDERKQKEIEESIKQVV 425
Cdd:COG4913 360 RRARLEALL------AALGLPLPASA-EEFAALRAEAAALLEALEEELEALE-EALAEAEA---ALRDLRRELRELEAEI 428
|
250
....*....|
gi 2092133180 426 EQIEDHKKRI 435
Cdd:COG4913 429 ASLERRKSNI 438
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
30-49 |
6.26e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 6.26e-04
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
310-510 |
6.72e-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: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 310 KKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEKKVEE-EMLQRRADVELEASQLDRYKELKELARKKvAT 388
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAlEQELAALEAELAELEKEIAELRAELEAQK-EE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 389 LTQQLEKLQWEQKADLERMTLD-------ERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKScielLAEKKQQEKVLID 461
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSpedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAE----LEAERAELEALLA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2092133180 462 EMENSRVQIAQVNEELNKIVGELQNARIDYHEGRRQQKRAEmlESLKRL 510
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA--EELEAL 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-476 |
7.52e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 167 EYDRKKKKMQQAEGDAQFNYNKKKHV--AVERKHAKLEKEEAERYQMLLEELK---ENRIQLQLFRLYHNEKKidfLNNK 241
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEEAKkaeEAKIKAEELKKAEEEKK---KVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 242 LGEKNMDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKEntshQIKKVDMAKKSSKD 321
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE----EAKKAEELKKKEAE 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 322 NEKhlaKQEQNIKELDTELTDVERSwrayeKKVEEEMLQRRADVELEASQLDRYKELKELARKKVATLTQQLEKLQWE-- 399
Cdd:PTZ00121 1714 EKK---KAEELKKAEEENKIKAEEA-----KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEel 1785
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133180 400 QKADLERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKKQQEKVLIDEMENSRVQIAQVNEE 476
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1065-1135 |
7.94e-04 |
|
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: 42.96 E-value: 7.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133180 1065 PGKRFMPM-DNLSGGEKSVAALALVFAIHSFRPAPFFILDEVDaaldnTNIG-----KVSSFIKEQAQEqCQMIVIS 1135
Cdd:cd03241 160 PGEPLKPLaKIASGGELSRLMLALKAILARKDAVPTLIFDEID-----TGISgevaqAVGKKLKELSRS-HQVLCIT 230
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-65 |
9.57e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.68 E-value: 9.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092133180 3 YLKLLLLENFKSWRGRQ-SIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVRELI 65
Cdd:COG3950 2 RIKSLTIENFRGFEDLEiDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
736-1016 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 736 GVENIRVFEQERVKQQEETDRKRLEFENQKTRLS---IQLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEEFLL 812
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAREELEQLEEELEqarSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 813 MVNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEAISIETSLEQKRLERHNMLLECKVQDLRIS 892
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 893 VLLGSLDEISEVELGTEAESTEATADIYERERAIQIDYSSLTDDLTDLQSDKEIEAHLTRLQQQIVSKENVLFKTAAPNL 972
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2092133180 973 RALEKLQTAKDKFQESVDAFEASRREARICRQEFEQMKKRRYER 1016
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
273-485 |
1.04e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 273 LNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEK 352
Cdd:pfam05557 39 LKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 353 KVEeemlqrRADVELEA--SQLDRYKELKELARKKVATLTQQLEKLQWEQKA---------DLERMTLDERKQKEIEESI 421
Cdd:pfam05557 119 QIQ------RAELELQStnSELEELQERLDLLKAKASEAEQLRQNLEKQQSSlaeaeqrikELEFEIQSQEQDSEIVKNS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 422 KQVVEQIEDHKKRIQKLEEY------TKSCIELLAEKKQQEKVLIDEMENSRVQIAQVNEELNKIVGELQ 485
Cdd:pfam05557 193 KSELARIPELEKELERLREHnkhlneNIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQ 262
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
274-500 |
1.20e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 274 NRDQQHMEKEMKTLEasLNQKRPQYIKAKENTSHQIKKVDMAK--KSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYE 351
Cdd:pfam17380 347 ERELERIRQEERKRE--LERIRQEEIAMEISRMRELERLQMERqqKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 352 KKVEEEMLQRRADVELE---ASQLDRYKElKELARKKVATLTQQLEKLQWEQKADLERmtlDERKQKEIEESIKQVVEqi 428
Cdd:pfam17380 425 IRAEQEEARQREVRRLEeerAREMERVRL-EEQERQQQVERLRQQEEERKRKKLELEK---EKRDRKRAEEQRRKILE-- 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092133180 429 edhkkriQKLEEYTKSCIellaEKKQQEKVLIDEMENSRVQIAQvnEELNKIVGELQNARIDYHEGRRQQKR 500
Cdd:pfam17380 499 -------KELEERKQAMI----EEERKRKLLEKEMEERQKAIYE--EERRREAEEERRKQQEMEERRRIQEQ 557
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
665-918 |
1.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 665 YSQSELENIKKKhLANFYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEEFQKKMNEVEdavfqdfceeigvENIRVFE 744
Cdd:COG3883 13 FADPQIQAKQKE-LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-------------AEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 745 QERVKQQEE-TDRKRLEFENQKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKDeaeivrlkkdeeefllmvNEIMEEQQH 823
Cdd:COG3883 79 AEIEERREElGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADAD------------------ADLLEELKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 824 LKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEAISIETSLEQKRLERHNMLLECKVQDLRISVLLGSLDEISE 903
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
250
....*....|....*
gi 2092133180 904 VELGTEAESTEATAD 918
Cdd:COG3883 221 AAAAAAAAAAAAAAA 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-438 |
1.22e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 193 AVERKHAKLEKEEAERYQMLLEELKENRIQL--QLFRLYHNEKKIDFLNNKLGEKNMDVNTKKDSLSsaedtfKAKKKVL 270
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELA------ELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 271 GILNRDQQHMEKEMKTLEASLNqkrpQYIKAKEntshqikkvdmAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAY 350
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYN----EYLELKD-----------AEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 351 EKKVEEemLQRRADVELEASQLDRYKEL-KELARKKvaTLTQQLEKLQWEQKADLERMT--LDERKQKEIE-ESIKQVVE 426
Cdd:PRK03918 646 RKELEE--LEKKYSEEEYEELREEYLELsRELAGLR--AELEELEKRREEIKKTLEKLKeeLEEREKAKKElEKLEKALE 721
|
250
....*....|..
gi 2092133180 427 QIEDHKKRIQKL 438
Cdd:PRK03918 722 RVEELREKVKKY 733
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
4-65 |
1.25e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 42.28 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092133180 4 LKLLLLENFKSW-RGRQSIGPfmKFNCIIGPNGSGKSNIMDALSFVMGERTanLRVKNVRELI 65
Cdd:cd03242 1 LKSLELRNFRNYaELELEFEP--GVTVLVGENAQGKTNLLEAISLLATGKS--HRTSRDKELI 59
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
281-488 |
1.57e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 281 EKEMKTLEASLNQKRPQYIKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSwrayEKKVEEEMLQ 360
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL----RETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 361 RRADVELEASQLDRYKELKELARKKVATLtqQLEKLQWEqKADLERMTLDERKQkEIEESIKQVVEQIEDHKKRIQKLEE 440
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEA--GLDDADAE-AVEARREELEDRDE-ELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2092133180 441 YTKSCIELLAEKKQQEKVLIDEMENSRVQIAQVNEELNKIVGELQNAR 488
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
18-487 |
1.60e-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: 42.73 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 18 RQSIGPFMKFNCIIGPNGSGKSNIMDALSFVMGERTANLRVKNVreLIHGAHVGKPFSSTASVKIVYCEENGEEKTFSRI 97
Cdd:TIGR00606 21 KQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNT--FVHDPKVAQETDVRAQIRLQFRDVNGEECAVVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 98 I----RGSCSEFLFNDKAVSR--------------SVYTAELEKIGIIVKARNCMVFQGAVESI-AMKKPKERTQLFEQI 158
Cdd:TIGR00606 99 MvctqKTKKTEFKTLEGVITRykhgekvslsskcaEIDREMISHLGVSKAVLNNVIFCHQEDSNwPLSEGKALKQKFDEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 159 SNSWEFAEEYDRKKKKMQqaegdaqfnyNKKKHVAVERKHAKLEKEEAERYQMLLEELKENRIQLQLFR--LYHNEKKID 236
Cdd:TIGR00606 179 FSATRYIKALETLRQVRQ----------TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSReiVKSYENELD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 237 FLNNKLGEknmdVNTKKDSLSSAEDTFKAKKKvlgilnrdqqhMEKEMKTLEASLNQKRpqyIKAKENTSHQIKKVDMAK 316
Cdd:TIGR00606 249 PLKNRLKE----IEHNLSKIMKLDNEIKALKS-----------RKKQMEKDNSELELKM---EKVFQGTDEQLNDLYHNH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 317 KSS-KDNEKHLAKQEQNIKELDTELTDVERSwrayekkvEEEMLQRRADVELEASQLDRYKELKELARKKVATltqQLEK 395
Cdd:TIGR00606 311 QRTvREKERELVDCQRELEKLNKERRLLNQE--------KTELLVEQGRLQLQADRHQEHIRARDSLIQSLAT---RLEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 396 LQWEQKADLERmtlderkqkEIEESIKQVVEQIEDHKKRIQK----LEEYTKSCIELLAEKKQQEKVLIDEMENSRVQIA 471
Cdd:TIGR00606 380 DGFERGPFSER---------QIKNFHTLVIERQEDEAKTAAQlcadLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
490
....*....|....*.
gi 2092133180 472 QVNEELNKIVGELQNA 487
Cdd:TIGR00606 451 KKQEELKFVIKELQQL 466
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1071-1135 |
1.61e-03 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 41.31 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092133180 1071 PMDNLSGGEKSVAALALVFAihsfRPAPFFILDEVDAALDNTNIGKVSSFIKEQAQeQCQMIVIS 1135
Cdd:COG4133 128 PVRQLSAGQKRRVALARLLL----SPAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLT 187
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
296-440 |
1.76e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 296 PQYI--KAKENTSHQIKKVDMAKKSSKDNEKhlaKQEQNIKELDTELTDVERSWRAYEKKvEEEMLQRRADVELEASQld 373
Cdd:PRK00409 500 PENIieEAKKLIGEDKEKLNELIASLEELER---ELEQKAEEAEALLKEAEKLKEELEEK-KEKLQEEEDKLLEEAEK-- 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133180 374 RYKELKELARKKVATLTQQLEKLQWEQKADLERMTLDErKQKEIEESIKQVVEQIEDHKKRIQKLEE 440
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIE-ARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-1012 |
1.85e-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: 42.06 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 791 EAVRKDEAEIVRLKKDEEEFLLMVNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEAISIETSL 870
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 871 EQKRLERHNML--LECKVQDLRISVLLGS------------LDEISEVELGTEAESTEATADIYERERAIQIDYSSLTDD 936
Cdd:COG4942 100 EAQKEELAELLraLYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133180 937 LTDLQSDKEIEAHLTRLQQQIVSKENVLFKTAAPNLRALEKLQTAKDKFQESVDAfEASRREARICRQEFEQMKKR 1012
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA-EAAAAAERTPAAGFAALKGK 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
242-876 |
1.92e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 242 LGEKNMDVNTKKDSLSSAEDTFKAKK-----KVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVDMAK 316
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKsesqnKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 317 KSSKDNE----KHLAKQEQNIKELDTELTDVERSwraYEKKVEEEMLQrradVELEASQLDRYKELKELARKKVATLTQQ 392
Cdd:pfam15921 306 EQARNQNsmymRQLSDLESTVSQLRSELREAKRM---YEDKIEELEKQ----LVLANSELTEARTERDQFSQESGNLDDQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 393 LEKLQWEQKADLERMTLDERKQKEIEE-------SIKQVVEQIEDHKKRIQKLEEYTKSC-IELLAEKKQQEKVL----- 459
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMkSECQGQMERQMAAIqgkne 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 460 -IDEMENSRVQIAQVNEELNKIVGELQNARIdyhegrrqqkraeMLESLKRlypdsvfgRLLDLCHPIHKKYQL--AVTK 536
Cdd:pfam15921 459 sLEKVSSLTAQLESTKEMLRKVVEELTAKKM-------------TLESSER--------TVSDLTASLQEKERAieATNA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 537 VFGKYMSAIVVATEKiardcIRFLKEERaepetflalDYL-DIKPINEKLR-EIKGSKMMIDVVQtpfTPLKKVIQFVCG 614
Cdd:pfam15921 518 EITKLRSRVDLKLQE-----LQHLKNEG---------DHLrNVQTECEALKlQMAEKDKVIEILR---QQIENMTQLVGQ 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 615 NG-----LVCETVKEARQIAfDGAVRLKELMKIK-RKETDLKQLQAqcqgtqtrlKYSQSELENIK-------------- 674
Cdd:pfam15921 581 HGrtagaMQVEKAQLEKEIN-DRRLELQEFKILKdKKDAKIRELEA---------RVSDLELEKVKlvnagserlravkd 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 675 -KKHLANFYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEEFQKKMN-EVEDAVFQdfceeigvenirvFEQER--VKQ 750
Cdd:pfam15921 651 iKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSE-------------LEQTRntLKS 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 751 QEETDRKRLEFenqKTRLSIQLEYSRGQLQKLVNKIHMLKEAVRKDEAEIVRLKkdeeefllmvneimEEQQHLKDRLIT 830
Cdd:pfam15921 718 MEGSDGHAMKV---AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLK--------------EEKNKLSQELST 780
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2092133180 831 LKTEVTKAQNAVEesrkkllTLNREMGKLQKEAISIETSLEQKRLE 876
Cdd:pfam15921 781 VATEKNKMAGELE-------VLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1076-1113 |
2.10e-03 |
|
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: 41.04 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2092133180 1076 SGGEKSVAALALVFAIHSFRPAPFFILDEVDAALDNTN 1113
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTN 165
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
637-1046 |
2.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 637 KELMKIKRKETDLKQLQAQCQGTQTRLKYSQSELENIKKKH--------LANFYKEKSKLESELVNIKSQYamlnEGLLQ 708
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELeklekllqLLPLYQELEALEAELAELPERL----EELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 709 RAEKIEEFQKKMNEVEDAVFQdfcEEIGVENIRVFEQERVKQQEETDRKRLEfenqktRLSIQLEYSRGQLQKLVNKIHM 788
Cdd:COG4717 154 RLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELE------ELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 789 LKEAVRKDEAEIVRLKK----DEEEFLLMVNEIMEEQQHLKDRLITLKTEVTKAQNAV--------EESRKKLLTLNREM 856
Cdd:COG4717 225 LEEELEQLENELEAAALeerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallfLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 857 GKLQKEAISIETSLEQKRLERHNMLLECKVQDLRISVLLGSLDEISEVELGTEAESTEATADIYERERAIQIDYSSLTDD 936
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 937 ------LTDLQSDKEIEAHLTRLQQQIVSKENVLFKTAAPNLRA--LEKLQTAKDKFQESVDAFEASRREARICRQEFEQ 1008
Cdd:COG4717 385 eelraaLEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430
....*....|....*....|....*....|....*....
gi 2092133180 1009 MKK-RRYERFSQCFEHVSVAIDQIYKKLCRNSCAQAFLS 1046
Cdd:COG4717 465 LEEdGELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
641-847 |
2.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 641 KIKRKETDLKQLQAQCQGTQTRLKYSQSELENIKkkhlanfyKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEEFQKKM 720
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELN--------EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 721 NEVEDAV------------------FQDFCEEIG-VENIRVFEQERVKQQEEtDRKRLefENQKTRLSIQLEYSRGQLQK 781
Cdd:COG3883 89 GERARALyrsggsvsyldvllgsesFSDFLDRLSaLSKIADADADLLEELKA-DKAEL--EAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133180 782 LVNKIHMLKEAVRKDEAEIVRLKKDEEEFLLMVNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRK 847
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
356-488 |
3.29e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 356 EEMLQRRADV--ELEASQLDRYKELKELARKK------VATLTQQLEKLQWEQKADLERMTLDERKQKEIEESIKQVVE- 426
Cdd:pfam07888 37 EECLQERAELlqAQEAANRQREKEKERYKRDReqwerqRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEe 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 427 ------QIEDHKKRIQKLEEYTKSCIELLAE--------KKQQEKVLI------DEMENSRVQIAQVNEELNKIVGELQN 486
Cdd:pfam07888 117 kdallaQRAAHEARIRELEEDIKTLTQRVLEretelermKERAKKAGAqrkeeeAERKQLQAKLQQTEEELRSLSKEFQE 196
|
..
gi 2092133180 487 AR 488
Cdd:pfam07888 197 LR 198
|
|
| retron_eff_Eco8 |
NF038234 |
retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner ... |
20-47 |
3.43e-03 |
|
retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner next to a reverse transcriptase in Eco8 type retron systems, is a predicted OLD family endonuclease.
Pssm-ID: 468422 [Multi-domain] Cd Length: 679 Bit Score: 41.55 E-value: 3.43e-03
10 20
....*....|....*....|....*...
gi 2092133180 20 SIGPFMKFNCIIGPNGSGKSNIMDALSF 47
Cdd:NF038234 18 EIDDLKDINCIIGKNNVGKSNLLKALKF 45
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
299-483 |
3.54e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 41.53 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 299 IKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTEltdvERSWRAYEKKVEEEMLQRRADVEleASQLDRYKEL 378
Cdd:pfam05262 169 VSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQ----EDAKRAQQLKEELDKKQIDADKA--QQKADFAQDN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 379 KELARKKVAtltqqlEKLQWEQKADLERMTLDERKQKEIEESIKQVVE--QIEDHKKRIQKLEEYTKSCIELLAEKKQQE 456
Cdd:pfam05262 243 ADKQRDEVR------QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEkaQIEIKKNDEEALKAKDHKAFDLKQESKASE 316
|
170 180
....*....|....*....|....*..
gi 2092133180 457 KVLIDEMENSRVQIAQVNEELNKIVGE 483
Cdd:pfam05262 317 KEAEDKELEAQKKREPVAEDLQKTKPQ 343
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
351-471 |
3.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 351 EKKVE--EEMLQRRADVELEASQldRYKELKELARK---KVATLTQQLEKLQWEQKADLERMTLDERKQKEIEESIKQVV 425
Cdd:PRK12704 57 EALLEakEEIHKLRNEFEKELRE--RRNELQKLEKRllqKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELE 134
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2092133180 426 EQIEDHKKRIQKLEEYTKSciellaEKKQQekvLIDEMEN-SRVQIA 471
Cdd:PRK12704 135 ELIEEQLQELERISGLTAE------EAKEI---LLEKVEEeARHEAA 172
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
197-468 |
4.24e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 197 KHAKLEKEEaERYQMLLEELKENRIQLQLFRLYHNEKKIDF--LNNKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLGILN 274
Cdd:pfam05483 368 EQQRLEKNE-DQLKIITMELQKKSSELEEMTKFKNNKEVELeeLKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 275 -----------------RDQQHMEKEMKTLEASLNQKRPQYIKAK--------ENTSHQIKKVDMA---KKSSKDNEKHL 326
Cdd:pfam05483 447 arekeihdleiqltaikTSEEHYLKEVEDLKTELEKEKLKNIELTahcdklllENKELTQEASDMTlelKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 327 AKQEQNIKELDTeLTDVERSWRAYEKKVEEEMLQRRADVE------------LEASQLDRYKELKELA------RKKVAT 388
Cdd:pfam05483 527 KQEERMLKQIEN-LEEKEMNLRDELESVREEFIQKGDEVKckldkseenarsIEYEVLKKEKQMKILEnkcnnlKKQIEN 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 389 LTQQLEKLQWEQKADLERMTLDERKQKEIEESIKQVVEQIEDHKkriQKLEEYTKSCIELLAEKKQQEKVLIDEMENSRV 468
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK---QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
222-386 |
4.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 222 QLQLFRLYHNEKKIDFLNNKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLGILNRDQQHMEKEMKTLEASLNQKR---PQY 298
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 299 IKAKENTSHQiKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEKKVEEEMLQRRADVELEASQLDRYKEL 378
Cdd:COG1579 86 RNNKEYEALQ-KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*...
gi 2092133180 379 KELARKKV 386
Cdd:COG1579 165 REELAAKI 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
640-1013 |
4.58e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 640 MKIKRKETDLKQLQAQCQGTQTR--------------LKYSQSELENIK---KKHLANFYKEKSKLESELVNIKSQYAML 702
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERqmaaiqgkneslekVSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASL 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 703 NE-------------GLLQRAE-KIEEFQKKMNEVEDavFQDFCEEIGVENIRVFEQERV----KQQEEtDRKRLEFENQ 764
Cdd:pfam15921 506 QEkeraieatnaeitKLRSRVDlKLQELQHLKNEGDH--LRNVQTECEALKLQMAEKDKVieilRQQIE-NMTQLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 765 KTRLSIQLEysRGQLQKLVN------------------KIHMLKEAVRKDEAEIVRLKKDEEEFLLMVNEIMEEQQHLKD 826
Cdd:pfam15921 583 RTAGAMQVE--KAQLEKEINdrrlelqefkilkdkkdaKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 827 RLITLKTEVTKAQNAVEESRKKLLTLNREM----GKLQKEAISIETSLEQKRLERHNMlleckvqdlrisvlLGSLDEIS 902
Cdd:pfam15921 661 EVKTSRNELNSLSEDYEVLKRNFRNKSEEMetttNKLKMQLKSAQSELEQTRNTLKSM--------------EGSDGHAM 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 903 EVELGTEAESTEATADIYERERAIQIDYSSLTDDLTDLQSDKEIEAHLTRLQQQIVSKENvlfKTAApnlrALEKLQTAK 982
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN---KMAG----ELEVLRSQE 799
|
410 420 430
....*....|....*....|....*....|.
gi 2092133180 983 DKFQESVDAFEASRREARICRQEFEQMKKRR 1013
Cdd:pfam15921 800 RRLKEKVANMEVALDKASLQFAECQDIIQRQ 830
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-85 |
4.85e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.15 E-value: 4.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 26 KFNCIIGPNGSGKSNIMDALSFVmgertanLRVKNVRELIHGAHVGKPFSSTASVKIVYC 85
Cdd:cd00267 26 EIVALVGPNGSGKSTLLRAIAGL-------LKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
193-414 |
5.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 193 AVERKHAKLEKEEAERYQMLLEELKENRIQLQlfRLYHNEKKIDFLNNKLGEKNMDVNTKKDSLSSAEDTFKAKKKVLgi 272
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELK--EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 273 lnrDQQHMEKEMKTLEASLNQKRPQYIKAKEntshqikkvdmAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAYEK 352
Cdd:COG4717 126 ---QLLPLYQELEALEAELAELPERLEELEE-----------RLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092133180 353 KVEEEMLQRRADVEleaSQLDRYKELKELARKKVATLTQQLEKLQWEQKADLERMTLDERKQ 414
Cdd:COG4717 192 EELQDLAEELEELQ---QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
637-859 |
5.45e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 637 KELMKIKRKETDLKQLQAQCQGT----QTRLKYSQSELENikkkhlANFYKEKSKLESELVNIKSQ----YAMLNEGLLQ 708
Cdd:pfam06160 186 EETDALEELMEDIPPLYEELKTElpdqLEELKEGYREMEE------EGYALEHLNVDKEIQQLEEQleenLALLENLELD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 709 RAEKIEEfqkKMNEVEDAVFQDFCEEIG-----VENIRVFEQ--ERVKQQ-----EETDRKRLEFENQKTRLSIQLEYSR 776
Cdd:pfam06160 260 EAEEALE---EIEERIDQLYDLLEKEVDakkyvEKNLPEIEDylEHAEEQnkelkEELERVQQSYTLNENELERVRGLEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 777 gQLQKLVNKIHMLKEAVRKDEAEIVRLKKDEEEFLLMVNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREM 856
Cdd:pfam06160 337 -QLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLV 415
|
...
gi 2092133180 857 GKL 859
Cdd:pfam06160 416 EKS 418
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1075-1123 |
6.08e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 6.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2092133180 1075 LSGGEKSVA-----ALALVFAIHSF---RPAP-FFILDEVDAALDNTNIGKVSSFIKE 1123
Cdd:pfam13558 33 LSGGEKQLLaylplAAALAAQYGSAegrPPAPrLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
328-503 |
6.12e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 328 KQEQNIKELDTELTDVERswrayEKKVEEEMLQRRADVELEAS--------QLDRYKEL---------KELARKKVATLT 390
Cdd:pfam17380 297 EQERLRQEKEEKAREVER-----RRKLEEAEKARQAEMDRQAAiyaeqermAMERERELerirqeerkRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 391 QQLEKLQWEQKADLERMTLDERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKscIELLAEKKQQEKVLIDEMENSRVQI 470
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ--IRAEQEEARQREVRRLEEERAREME 449
|
170 180 190
....*....|....*....|....*....|...
gi 2092133180 471 AQVNEELNKivgELQNARIDYHEGRRQQKRAEM 503
Cdd:pfam17380 450 RVRLEEQER---QQQVERLRQQEEERKRKKLEL 479
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
183-500 |
7.59e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 183 QFNYNKKKHVAVERKHAKLEKEEAERYQMLLEELKENRIQLqlfrlyhneKKIDFLNNKLgeknmdvNTKKDSLSSAEDT 262
Cdd:pfam05557 42 QLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK---------KYLEALNKKL-------NEKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 263 FKAKKKVLGILNRDQQHMEKEMKTLEASLNQKRPQYIKAKENTSHQIKKVDMAKKSSKDnekhLAKQEQNIKELDTELTD 342
Cdd:pfam05557 106 ISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS----LAEAEQRIKELEFEIQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 343 VErSWRAYEKKVEEEmLQRRADVELEASQL-DRYKELKELARKKvATLTQQLE----KLQWEQKADLERMTLDERKQKeI 417
Cdd:pfam05557 182 QE-QDSEIVKNSKSE-LARIPELEKELERLrEHNKHLNENIENK-LLLKEEVEdlkrKLEREEKYREEAATLELEKEK-L 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 418 EESIKQVVEQIEDHKKRIQKLEEYTKSCIELLaekkQQEKVLIDE----------MENSRVQIAQVNEELNKIVGELQNA 487
Cdd:pfam05557 258 EQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQ----QREIVLKEEnssltssarqLEKARRELEQELAQYLKKIEDLNKK 333
|
330
....*....|....
gi 2092133180 488 RIDYHE-GRRQQKR 500
Cdd:pfam05557 334 LKRHKAlVRRLQRR 347
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
646-1011 |
8.58e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 646 ETDLKQLQAQCQGTQTRLKYSQSELENIKKKHLANFYKEKSKLESELVNIKSQYAMLNEGLLQRAEKIEEFQKKMNEVED 725
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 726 AVFQDFCEEIGVENIRVFEQERVKQ---------------QEETDRKRLEFENQKTRLSIQLEYSRGQLQKLVNKIHMLK 790
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQNKRlwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 791 EAVRKDEAEIVRLKKDEEefllMVNEIMEEQQHLKDRLITLKTEVTKAQNAVEESRKKLLTLNREMGKLQKEA-ISIETS 869
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKE----MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVdLKLQEL 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 870 LEQKRLERH--NMLLECKV-------QDLRISVLLGSLDEISEV--ELGTEAESTEATADIYERE---RAIQIDYSSLTD 935
Cdd:pfam15921 534 QHLKNEGDHlrNVQTECEAlklqmaeKDKVIEILRQQIENMTQLvgQHGRTAGAMQVEKAQLEKEindRRLELQEFKILK 613
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133180 936 DLTDLQSdKEIEAHLTRLQQQIVSkenvLFKTAAPNLRALEKLQTAKDKFQESVdafEASRREARICRQEFEQMKK 1011
Cdd:pfam15921 614 DKKDAKI-RELEARVSDLELEKVK----LVNAGSERLRAVKDIKQERDQLLNEV---KTSRNELNSLSEDYEVLKR 681
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
195-509 |
9.46e-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: 40.42 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 195 ERKHAKLEKEEAERYQML-LEELKENRIQLQlfrlyhnEKKIDFLNNKLGEKNMDVNTKKDSLSSAE---DTFKAKKKVL 270
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLgLAPGRQSIIDLK-------EKEIPELRNKLQKVNRDIQRLKNDIEEQEtllGTIMPEEESA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 271 GILNRDQQHMEKEMKTLEAslNQKRPQYIKAKENTSHQIKKVDMAKKSSKDNEKHLAKQEQNIKELDTELTDVERSWRAY 350
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKD--VERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 351 EKKVEE---------EMLQRRADVELEASQLDR-----YKELKElARKKVATLTQQLEKLQWEQKA-------------- 402
Cdd:TIGR00606 863 KSKTNElkseklqigTNLQRRQQFEEQLVELSTevqslIREIKD-AKEQDSPLETFLEKDQQEKEElissketsnkkaqd 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 403 -----------------DLERMTLD--ERKQKEIEESIKQVVEQIEDHKKRIQKLEEYTKSCIELLAEKKQQEKVLIDEM 463
Cdd:TIGR00606 942 kvndikekvknihgymkDIENKIQDgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2092133180 464 ENSRV--QIAQVNEELNKIVGELQNARIdYHEGRRQQKRAEMLESLKR 509
Cdd:TIGR00606 1022 TLRKRenELKEVEEELKQHLKEMGQMQV-LQMKQEHQKLEENIDLIKR 1068
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
824-1019 |
9.54e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 824 LKDRLITLKTEVTKAQNAVEE--SRKKLLTLNREMGKLQKEAISIETSLEQKRLERhnMLLECKVQDLRiSVLLGSLDEI 901
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL--AEAEARLAALR-AQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 902 SEVelgteaESTEATADIYERERAIQIDYSSLTDDLTDLQSD-KEIEAHLTRLQQQIVSKENVLFKTAAPNLRALEK--- 977
Cdd:COG3206 257 PEL------LQSPVIQQLRAQLAELEAELAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQArea 330
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2092133180 978 -LQTAKDKFQESVDAFEASRREARICRQEFEqMKKRRYERFSQ 1019
Cdd:COG3206 331 sLQAQLAQLEARLAELPELEAELRRLEREVE-VARELYESLLQ 372
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1067-1155 |
9.67e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133180 1067 KRFM--PMDNLSGGEKSVAALALVFA----IHSFRPAP--FFILDEVDAALDNTNIGKVSSFIKEQAQEQCQMIVISLKE 1138
Cdd:cd03279 114 DRFLarPVSTLSGGETFLASLSLALAlsevLQNRGGARleALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVE 193
|
90
....*....|....*..
gi 2092133180 1139 EFYSRADALIGVCPEQD 1155
Cdd:cd03279 194 ELKERIPQRLEVIKTPG 210
|
|
| |
