|
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 ... |
2-1185 |
1.35e-92 |
|
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: 323.46 E-value: 1.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 2 KIKEVRITGFRSYKDnTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSD-EYAHLKEEQRLGLLHESTGPKVAHARVEI 80
Cdd:pfam02463 1 YLKRIEIEGFKSYAK-TVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 81 TFDNSEKRLmAFENSEVKIVRQVGKKKD-QYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINELATSPDAYKLKL 159
Cdd:pfam02463 80 TFDNEDHEL-PIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 160 LREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKE 239
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 240 KTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTR 319
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 320 ERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQFSSVDDRDKFLRNE 399
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 400 IRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKA 479
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 480 IRDKIGNTEQDISAANDQLRRIVARPVYNGITGVRKVIEEFKHDNRNGQHDDviNGYYGTVIELAEVPDMFRTAVEVIAQ 559
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR--LGDLGVAVENYKVAISTAVIVEVSAT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 560 NRLFYHVVETDRIATKILRKFNEMQLPGEINFFPmnrvsaprqrdlsNNSNARPMSDVIDYEVQYDKvfksitanVIIVR 639
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLP-------------LKSIAVLEIDPILNLAQLDK--------ATLEA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 640 TLDQAARDLRNEGFDVVSVDGDQMSKKGVMTGGFIDKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIR 719
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 720 NRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQ 799
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKE 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 800 TVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKESLTARVDDISDNERRHKLENANAQLTS------- 872
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLeklaeee 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 873 LLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSLKKMRLLGA 952
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 953 LPTDtFSKWQNVKPRELEKKllecvneLKKYENVNKKALDQYMTASSQKEELTKRMAEQKKSEDSIEELLKVLENRKYEA 1032
Cdd:pfam02463 936 EPEE-LLLEEADEKEKEENN-------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1033 IDLTFKQVKKNFEQVFKQLVPHGRGKMQMRAREQRDDEEGINSVELYEGISVLVSFVSDDGDSETREMTQLSGGQKSLVA 1112
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVA 1087
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896701 1113 LAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRF-RNKVSH 1185
Cdd:pfam02463 1088 LALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMvENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1177 |
3.82e-91 |
|
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: 319.32 E-value: 3.82e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 3 IKEVRITGFRSYKDNTNVSgFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLL--HESTGPKVAHARVEI 80
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIP-FSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLisNGKNGQSGNEAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 81 TFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSrSNPYYIVKQGKINELATSPDAYKLKLL 160
Cdd:TIGR02169 81 TFKNDDGKFPDELEVVRRLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVERRKII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 161 REVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEK 240
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 241 TKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKtdkKKLESLGRGLREDKETLQAEETKMVEEkmtLKLEIDSL------N 314
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIE---QLLEELNKKIKDLGEEEQLRVKEKIGE---LEAEIASLersiaeK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 315 EENTRERQGR-QNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQ-RSQFSSVDDR 392
Cdd:TIGR02169 314 ERELEDAEERlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtRDELKDYREK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 393 DKFLRNEIRRISGLIADNKEREETIQKELADveredekLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEydaayvAQQT 472
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELAD-------LNAAIAGIEAKINELEEEKEDKALEIKKQEWK------LEQL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 473 AAREEKAiRDKIGNTEQDISAANDQLRRivARPVYNGITGVRKVIEEFKHDNRNGQH--DDVINGYYGTVIELAEVPDMF 550
Cdd:TIGR02169 461 AADLSKY-EQELYDLKEEYDRVEKELSK--LQRELAEAEAQARASEERVRGGRAVEEvlKASIQGVHGTVAQLGSVGERY 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 551 RTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLpGEINFFPMNRVSAPRqRDLSNNSNARPMS---DVIDYEVQYDKV 627
Cdd:TIGR02169 538 ATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDER-RDLSILSEDGVIGfavDLVEFDPKYEPA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 628 FKSITANVIIVRTLDqAARDLRNEgFDVVSVDGDQMSKKGVMTGGFIDKKRSKLelhtqkdRFTKELAELQKSLAEAEKM 707
Cdd:TIGR02169 616 FKYVFGDTLVVEDIE-AARRLMGK-YRMVTLEGELFEKSGAMTGGSRAPRGGIL-------FSRSEPAELQRLRERLEGL 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 708 VRERT---QEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQE 784
Cdd:TIGR02169 687 KRELSslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 785 IGSnMSSQLTSDEEQTVK--------KLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLY--KTKESLTARVDDI 854
Cdd:TIGR02169 767 IEE-LEEDLHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYleKEIQELQEQRIDL 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 855 SD--NERRHKLENANAQLTSLLTRMESTRKQLATAISELQDyetkekaLQINIDNVLEQQRDLEKQQADFQLQYDKITAK 932
Cdd:TIGR02169 846 KEqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 933 EDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKPRE-LEKKLLECVNELKKYENVNKKALDQYMTASSQKEELTKRMAEQ 1011
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1012 KKSEDSIEELLKVLENRKYEAIDLTFKQVKKNFEQVFKQLvPHGRGKMQMrarEQRDDEeginsvelyegISVLVSFVSD 1091
Cdd:TIGR02169 999 EEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELIL---ENPDDP-----------FAGGLELSAK 1063
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1092 DGDSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATA 1171
Cdd:TIGR02169 1064 PKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYA 1143
|
....*.
gi 392896701 1172 EKFYGV 1177
Cdd:TIGR02169 1144 DRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1189 |
3.20e-88 |
|
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: 310.84 E-value: 3.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 2 KIKEVRITGFRSYKDNTNVsGFSPRSNVVVGRNGSGKSNFFHAIQFVLSdeyahlkeEQRLGLLHESTGPKV-------- 73
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTI-NFDKGITGIVGPNGCGKSNIVDAIRWVLG--------EQSAKALRGGKMEDVifngsetr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 74 ---AHARVEITFDNSEKRLMAFENSEVKIVRQVGKKKD-QYYIDNKMVPRAEVVNLMESAGFSRSNpYYIVKQGKINELA 149
Cdd:TIGR02168 72 kplSLAEVELVFDNSDGLLPGADYSEISITRRLYRDGEsEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 150 TSPDAYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMY 229
Cdd:TIGR02168 151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 230 DNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLE 309
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 310 IDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQrsqfssv 389
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 390 ddrdkfLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENryEMDTFAAKSTSLKQEYDAAYVA 469
Cdd:TIGR02168 384 ------LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 470 QQTAAREEKAIRDKIGNTEQDISAANDQLRRIVARpvyngITGVRKVIEEFKHDNRNG----QHDDVINGYYGTVIELAE 545
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQAR-----LDSLERLQENLEGFSEGVkallKNQSGLSGILGVLSELIS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 546 VPDMFRTAVEVIAQNRLFYHVVETDRIATKILrKFNEMQLPGEINFFPMNRVSA------PRQRDLSNNSNARPMSDVID 619
Cdd:TIGR02168 531 VDEGYEAAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGteiqgnDREILKNIEGFLGVAKDLVK 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 620 YEVQYDKVFKSITANVIIVRTLDQAARDLR--NEGFDVVSVDGDQMSKKGVMTGGF-------IDKKRSKLELHTQKDRF 690
Cdd:TIGR02168 610 FDPKLRKALSYLLGGVLVVDDLDNALELAKklRPGYRIVTLDGDLVRPGGVITGGSaktnssiLERRREIEELEEKIEEL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 691 TKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGD-------FHRKHRELTEAKNAISQQFYMVTSTKEPKKDQ 763
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 764 LLGIKNHLRELLAQKENFEQEIGsNMSSQLTSDEEQtVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTkKLYKT 843
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIE-QLKEELKALREA-LDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQ 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 844 KESLTARVDDISD--NERRHKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQAD 921
Cdd:TIGR02168 847 IEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 922 FQLQYDKITAKEDEVKQK-REDSLKKMRLLGALPTDTFSkwqnvKPRELEKKLLECVNELKKYENVNKKALDQYMTASSQ 1000
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIED-----DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1001 KEELTKRMAEQKKS----EDSIEELLKVLENRKYEaidlTFKQVKKNFEQVFKQLVPHGRGKMQMrareqrDDEEGInsv 1076
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAketlEEAIEEIDREARERFKD----TFDQVNENFQRVFPKLFGGGEAELRL------TDPEDL--- 1068
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1077 eLYEGISVlvsFVSDDGdSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQA 1156
Cdd:TIGR02168 1069 -LEAGIEI---FAQPPG-KKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNT 1143
|
1210 1220 1230
....*....|....*....|....*....|....
gi 392896701 1157 QFVTTTFRPELLATAEKFYGVRFRNK-VSHIDSV 1189
Cdd:TIGR02168 1144 QFIVITHNKGTMEVADQLYGVTMQEKgVSKIVSV 1177
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-151 |
1.37e-79 |
|
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: 261.43 E-value: 1.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 3 IKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEITF 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896701 83 DNSEKRLMAFeNSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINELATS 151
Cdd:cd03272 81 DNSDNRFPID-KEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNM 148
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1177 |
2.15e-56 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 212.87 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDNTNVSgFSPRSNVVVGRNGSGKSNFFHAIQFVLSdeyahlkeEQRLGLL-----------HEST 69
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLG--------EQSAKSLrggkmedvifaGSSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 70 GPKVAHARVEITFDNSEKRLmAFENSEVKIVRQVGKKKD-QYYIDNKMVPRAEVVNLMESAGFSRsNPYYIVKQGKINEL 148
Cdd:COG1196 72 RKPLGRAEVSLTFDNSDGTL-PIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGP-ESYSIIGQGMIDRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 149 ATS-PDAyKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYT 227
Cdd:COG1196 150 IEAkPEE-RRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 228 MYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLK 307
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 308 LEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQrsqfs 387
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 388 svddrdkfLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAY 467
Cdd:COG1196 384 --------LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 468 VAQQTAAREEKAIRDKIGNTEQDISAANDQLRRivARPVYNGITGVRKVIEEFKHDNRNGQHDDVINGYYGTVIELAEVP 547
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAE--AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 548 DMFRTAVEVIAQNRLFYHVVETDRIATKiLRKFNEMQLPGEINFFPMNRVSAPRQRDLSNNSNAR-PMSDVIDYEVQYDK 626
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAA-AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgAAVDLVASDLREAD 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 627 VFKSITANVIIVRTLDQAARDLRN-------EGFDVVSVDGDQMSKKGVMTGGFIDKKRSKLElhtqkdrftkelAELQK 699
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALrravtlaGRLREVTLEGEGGSAGGSLTGGSRRELLAALL------------EAEAE 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 700 SLAEAEKMVRERTQEAEKIRNRMQQHENQigdfhrkhrelteaknaisqqfymvtstkepkkdqllgiknhlrellaqke 779
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEEREL--------------------------------------------------- 709
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 780 nfeqeigsnmssqltsdeeqtvkklrkkvdemtkqlatvsrrrmdlmhrknaienlltkklyktkesltarvddisdner 859
Cdd:COG1196 --------------------------------------------------------------------------------
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 860 rhklenanaqltslltrmestRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQK 939
Cdd:COG1196 710 ---------------------AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 940 REDSLKKMRLLGAlptdtfskwqnvkprelekkllecvnelkkyenVNKKALDQYMTASSQKEELTKRMAEQKKSEDSIE 1019
Cdd:COG1196 769 LERLEREIEALGP---------------------------------VNLLAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1020 ELLKVLENRKYEAIDLTFKQVKKNFEQVFKQLVPHGRGKMQMrareqRDDEEGINSvelyeGISVLVSFvsddGDSETRE 1099
Cdd:COG1196 816 EAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLL-----TDPDDPLET-----GIEIMAQP----PGKKLQR 881
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1100 MTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQ--HRksVADMIQSLSDQAQFVTTTFRPELLATAEKFYGV 1177
Cdd:COG1196 882 LSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQFIVITHNKRTMEAADRLYGV 959
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1093-1187 |
6.22e-54 |
|
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: 188.62 E-value: 6.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1093 GDSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAE 1172
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228
|
90
....*....|....*
gi 392896701 1173 KFYGVRFRNKVSHID 1187
Cdd:cd03272 229 KFYGVKFRNKVSTID 243
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1066-1185 |
1.01e-29 |
|
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: 116.64 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1066 QRDDEEGINSVELYEGISVLvsfvsddGDSETREMtqLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSV 1145
Cdd:cd03239 67 KAGINSASVEITFDKSYFLV-------LQGKVEQI--LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRV 137
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 392896701 1146 ADMIQSLSD-QAQFVTTTFRPELLATAEKFYGVRFRNKVSH 1185
Cdd:cd03239 138 SDMIKEMAKhTSQFIVITLKKEMFENADKLIGVLFVHGVST 178
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
534-646 |
1.22e-25 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 102.69 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 534 NGYYGTVIELAEVPDMFRTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLpGEINFFPMNRVSA-------PRQRDLS 606
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRL-GRATFLPLDKIKPrspagskLREALLP 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 392896701 607 NNSNARPMSDVIDYEVQYDKVFKSITANVIIVRTLDQAAR 646
Cdd:smart00968 80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARR 119
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
533-644 |
8.72e-25 |
|
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: 100.41 E-value: 8.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 533 INGYYGTVIELAEVPDMFRTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLpGEINFFPMNRVSAPRQRDLSNNSN-A 611
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADLKGgA 79
|
90 100 110
....*....|....*....|....*....|...
gi 392896701 612 RPMSDVIDYEVQYDKVFKSITANVIIVRTLDQA 644
Cdd:pfam06470 80 GPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEA 112
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-145 |
8.69e-23 |
|
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: 98.91 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLS-DEYAHLKEEQRLGLLHESTGPKVAHARVE 79
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 80 ITFDNSEKR--LMAFENS-EVKIVRQVGK-KKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKI 145
Cdd:cd03273 81 IVFDNSDKSqsPIGFENYpEITVTRQIVLgGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1100-1184 |
9.48e-23 |
|
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: 97.15 E-value: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1100 MTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRF 1179
Cdd:cd03278 111 LSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLYGVTM 190
|
....*.
gi 392896701 1180 RNK-VS 1184
Cdd:cd03278 191 QESgVS 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1102-1181 |
3.68e-22 |
|
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: 94.35 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1102 QLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQ-AQFVTTTFRPELLATAEKFYGVRFR 1180
Cdd:cd03227 77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 392896701 1181 N 1181
Cdd:cd03227 157 I 157
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-85 |
1.63e-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: 90.06 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 3 IKEVRITGFRSYKDNTNVSGFSPrSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEITF 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITF 79
|
...
gi 392896701 83 DNS 85
Cdd:cd03239 80 DKS 82
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1100-1187 |
1.18e-18 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 86.97 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1100 MTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRF 1179
Cdd:cd03273 164 LTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRF 243
|
....*...
gi 392896701 1180 RNKVSHID 1187
Cdd:cd03273 244 VDGTSTVT 251
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1098-1186 |
1.22e-15 |
|
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: 78.00 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1098 REMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQ-AQFVTTTFRPELLATAEKFYG 1176
Cdd:cd03275 151 RDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPnFQFIVISLKEEFFSKADALVG 230
|
90
....*....|...
gi 392896701 1177 VrFRNK---VSHI 1186
Cdd:cd03275 231 V-YRDQecnSSKV 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-444 |
2.93e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDNtnVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLsdeYAHLKEEQRLGLLHESTGPKVAHARVEI 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKSS--VVEFDDGINLIIGQNGSGKSSILEAILVGL---YWGHGSKPKGLKKDDFTRIGGSGTEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 81 TFDnsekrlmaFENSEVKIVRQVgKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYI------VKQGKINELATSpDA 154
Cdd:PRK03918 76 KFE--------KNGRKYRIVRSF-NRGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVflnaiyIRQGEIDAILES-DE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 155 YKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKY---IDERLQTLENEKED-LKEYQKLDKTKRSVEYTMyd 230
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEvLREINEISSELPELREEL-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 231 ntnKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKEtlQAEETKMVEEKMTLKLEI 310
Cdd:PRK03918 224 ---EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE--KVKELKELKEKAEEYIKL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 311 DSLNEE------NTRERQGRQNAE-HSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDEsrakEILAKQGQR 383
Cdd:PRK03918 299 SEFYEEyldelrEIEKRLSRLEEEiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE----EAKAKKEEL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896701 384 SQFSSvddrdKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDE 444
Cdd:PRK03918 375 ERLKK-----RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1098-1184 |
3.59e-13 |
|
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: 70.02 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1098 REMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGV 1177
Cdd:cd03274 123 KNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGI 202
|
....*..
gi 392896701 1178 RFRNKVS 1184
Cdd:cd03274 203 YKTNNCT 209
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-106 |
3.51e-12 |
|
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: 66.72 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 3 IKEVRITGFRSYKDNTNVSgFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAH-LKEEQRLGLLHESTG--PKVAHARVE 79
Cdd:cd03278 1 LKKLELKGFKSFADKTTIP-FPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAGSEtrKPANFAEVT 79
|
90 100
....*....|....*....|....*...
gi 392896701 80 ITFDNSEKRLMAFENSEV-KIVRQVGKK 106
Cdd:cd03278 80 LTFDNSDGRYSIISQGDVsEIIEAPGKK 107
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1102-1171 |
4.50e-12 |
|
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: 65.34 E-value: 4.50e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896701 1102 QLSGGQKSLVALAIIFSIQkcdpAPFYLFDEIDAALDAQHRKSVADMIQSLSDQ-AQFVTTTFRPELLATA 1171
Cdd:cd00267 80 QLSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELA 146
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-204 |
1.07e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 65.42 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 2 KIKEVRITGFRSYKDNTNVSgFSPRSNVVVGRNGSGKSNFFHAIQFVLsdeYAHLKEEQRLGLLHESTGPKvaHARVEIT 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYAL---YGKARSRSKLRSDLINVGSE--EASVELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 82 FDNSEKRLmafensevKIVRQvgkkkdqyyidnkmvpraevvnlmesagfsrsnpyyivkQGKINELATSPDAYKLKLLR 161
Cdd:COG0419 75 FEHGGKRY--------RIERR---------------------------------------QGEFAEFLEAKPSERKEALK 107
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 392896701 162 EVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTL 204
Cdd:COG0419 108 RLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQL 150
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-90 |
5.19e-11 |
|
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: 65.79 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDnTNVSgFSPRSNVVVGRNGSGKSNFFHAIQFVLS-DEYAHLKEEQrlglLHESTGPKVAHARVE 79
Cdd:COG3593 1 MKLEKIKIKNFRSIKD-LSIE-LSDDLTVLVGENNSGKSSILEALRLLLGpSSSRKFDEED----FYLGDDPDLPEIEIE 74
|
90
....*....|.
gi 392896701 80 ITFDNSEKRLM 90
Cdd:COG3593 75 LTFGSLLSRLL 85
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-172 |
6.43e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 62.64 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 2 KIKEVRITGFRSYKDnTNVSgFSPRsNVVVGRNGSGKSNFFHAIQFvLSDEYAH-----LKEEQRLG-LLHESTGPKVAH 75
Cdd:COG4637 1 MITRIRIKNFKSLRD-LELP-LGPL-TVLIGANGSGKSNLLDALRF-LSDAARGglqdaLARRGGLEeLLWRGPRTITEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 76 ARVEITFDNSEKRLMAFE--------NSEVKIVRQvgkkkdQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINE 147
Cdd:COG4637 77 IRLELEFAEEDERDLRYElelglpepGGRPEVKEE------RLWLKRGSGGRPFLDFRPKGRAVGGEPERLDSPESLLSQ 150
|
170 180
....*....|....*....|....*.
gi 392896701 148 LATSPDAYKLKLLRE-VAGTRVYDER 172
Cdd:COG4637 151 LGDPERFPELRALREaLRSWRFYDFH 176
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-130 |
9.07e-10 |
|
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: 60.66 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 3 IKEVRITGFRSYKDNTNVsGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLH--ESTGPKVAHARVEI 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVI-GPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYraRVGKPDSNSAYVTA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 392896701 81 TFDNSEKRLMAFEnsevKIVRQVGKkkdQYYIDNKMVPRAEVVNLMESAG 130
Cdd:cd03275 80 VYEDDDGEEKTFR----RIITGGSS---SYRINGKVVSLKEYNEELEKIN 122
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
10-56 |
1.10e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 58.53 E-value: 1.10e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 392896701 10 GFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHL 56
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSAT 52
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-277 |
3.52e-09 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 60.31 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDNTNVsgFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEI 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEID--LDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNIFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 81 TFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAG-------FSRSNPYYIVKQGKINELATSPD 153
Cdd:pfam13175 79 NISFSIDIEIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANkadllleLKISDLKKYLKQFKIYIYNNYYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 154 AYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTN 233
Cdd:pfam13175 159 DEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHENVLENLQIKKLLISADRNASDEDSEKIN 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 392896701 234 KEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKK 277
Cdd:pfam13175 239 SLLGALKQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELK 282
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-82 |
1.03e-07 |
|
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: 53.84 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 3 IKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTG-PKVAHARVEIT 81
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGhPNLDSCSVEVH 82
|
.
gi 392896701 82 F 82
Cdd:cd03274 83 F 83
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-50 |
1.17e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 55.05 E-value: 1.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 392896701 3 IKEVRITGFRSYKDNTNVS-----GFSPRSNVVVGRNGSGKSNFFHAIQFVLS 50
Cdd:COG1106 2 LISFSIENFRSFKDELTLSmvasgLRLLRVNLIYGANASGKSNLLEALYFLRN 54
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-927 |
1.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 254 DNNVKSQLNDVIAEMAKLK-------TDKKKLESLGRgLREDKETLQAeetkmveekmtLKLEIDSLNEEntRERQGRQN 326
Cdd:COG4913 220 EPDTFEAADALVEHFDDLErahealeDAREQIELLEP-IRELAERYAA-----------ARERLAELEYL--RAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 327 AEHSLQgvgdeifKNEEELDTIKPEYAKLLEEESRLKTdiRIDESRAKEILAKQgQRSQfsSVDDRDKFLRNEIRRISGL 406
Cdd:COG4913 286 AQRRLE-------LLEAELEELRAELARLEAELERLEA--RLDALREELDELEA-QIRG--NGGDRLEQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 407 IADNKEREETIQKELADVereDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKAIRDKIGN 486
Cdd:COG4913 354 LEERERRRARLEALLAAL---GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 487 TEQ---DISAANDQLRRIVARPvyngiTGVRKviEEFKhdnrngqhddvingYYGTVIELAEVPDMFRTAVEVIAQNRLF 563
Cdd:COG4913 431 LERrksNIPARLLALRDALAEA-----LGLDE--AELP--------------FVGELIEVRPEEERWRGAIERVLGGFAL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 564 YHVVETDRIAtKILRKFNEMQLPGEINFFPMN-RVSAPRQRDLSNNSNAR-------PMSDVIDYEVQYDkvfksitANV 635
Cdd:COG4913 490 TLLVPPEHYA-AALRWVNRLHLRGRLVYERVRtGLPDPERPRLDPDSLAGkldfkphPFRAWLEAELGRR-------FDY 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 636 IIVRTLDQaardLRNEGFdVVSVDGdQMSKKGVMtgGFIDKKRSKLELH-------TQKDRFTKELAELQKSLAEAEkmv 708
Cdd:COG4913 562 VCVDSPEE----LRRHPR-AITRAG-QVKGNGTR--HEKDDRRRIRSRYvlgfdnrAKLAALEAELAELEEELAEAE--- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 709 rERTQEAEKIRNRMQQHENQigdfHRKHRELTEAknaisqqfymvtstkepkKDQLLGIKNHLRELLAQKENFEQeiGSN 788
Cdd:COG4913 631 -ERLEALEAELDALQERREA----LQRLAEYSWD------------------EIDVASAEREIAELEAELERLDA--SSD 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 789 MSSQLtsdeEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLtkklyktkESLTARVDDISDNERRHKLENANA 868
Cdd:COG4913 686 DLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL--------DELQDRLEAAEDLARLELRALLEE 753
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896701 869 QLTSLLTRmESTRKQLATAISELQDYETKEKALqinidnvleqQRDLEKQQADFQLQYD 927
Cdd:COG4913 754 RFAAALGD-AVERELRENLEERIDALRARLNRA----------EEELERAMRAFNREWP 801
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
158-434 |
1.42e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 158 KLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKL--DKTKRSVEYTMYDNTNKE 235
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEleEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 236 AIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEET--KMVEEKMTLKLEIDSL 313
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErhELYEEAKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 314 NEENTRERQGRQNAEhsLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDI---------------RIDESRAKEILA 378
Cdd:PRK03918 378 KKRLTGLTPEKLEKE--LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrELTEEHRKELLE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896701 379 K-----QGQRSQFSSVDDRDKFLRNEIRRISGLIADNKE--REETIQKELADVEREDEKLNNE 434
Cdd:PRK03918 456 EytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLE 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-526 |
3.56e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 171 ERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKldktkrsveytmyDNTNKEAIKEKTKLDEQKVEL 250
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE-------------QDWNKELKSELKNQEKKLEEI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 251 NQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHS 330
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 331 LQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIR--IDESRAKEILAKqgqrsqfsSVDDRDKFLRNEIRRISGLIA 408
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdlTNQDSVKELIIK--------NLDNTRESLETQLKVLSRSIN 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 409 DNKEREETIQKELADVEREDEKLNNEIQSISRTIDEnryemdtfaakstsLKQEYDAAYVAQQTAAREEKAIRDKIGNTE 488
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD--------------LTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
330 340 350
....*....|....*....|....*....|....*...
gi 392896701 489 QDISAANDQLRRIVARPVyngITGVRKVIEEFKHDNRN 526
Cdd:TIGR04523 545 DELNKDDFELKKENLEKE---IDEKNKEIEELKQTQKS 579
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
158-448 |
8.75e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 158 KLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAI 237
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 238 KEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLRED-KETLQAEETKMVEEKMTLKLEIDSLNE- 315
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhRKELLEEYTAELKRIEKELKEIEEKERk 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 316 --------ENTRERQGRQNAEHSLQGVGDEIFK-----NEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEI------ 376
Cdd:PRK03918 478 lrkelrelEKVLKKESELIKLKELAEQLKELEEklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelkkk 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 377 -----------------LAKQGQRSQFSSVDDRDKFLR----------------NEIRRISGLIADNKEREETIQKELAD 423
Cdd:PRK03918 558 laelekkldeleeelaeLLKELEELGFESVEELEERLKelepfyneylelkdaeKELEREEKELKKLEEELDKAFEELAE 637
|
330 340
....*....|....*....|....*
gi 392896701 424 VEREDEKLNNEIQSISRTIDENRYE 448
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYE 662
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
692-920 |
1.90e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 692 KELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHL 771
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 772 RELL--AQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLtkklyKTKESLTA 849
Cdd:COG4942 107 AELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER-----AELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896701 850 RVddisdNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDyetKEKALQINIDNVLEQQRDLEKQQA 920
Cdd:COG4942 182 EL-----EEERAALEALKAERQKLLARLEKELAELAAELAELQQ---EAEELEALIARLEAEAAAAAERTP 244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
682-1081 |
2.21e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 682 ELHTQKDRFTKELA----ELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTK 757
Cdd:pfam15921 360 EARTERDQFSQESGnlddQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 758 EPKKDQLlgiKNHLRELLAQKENFEQeigsnmSSQLTSDEEQTVKKLRKKVDEMTKqlatvsrRRMDLMHRKNAIENLLT 837
Cdd:pfam15921 440 SECQGQM---ERQMAAIQGKNESLEK------VSSLTAQLESTKEMLRKVVEELTA-------KKMTLESSERTVSDLTA 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 838 kklyktkesltarvddiSDNERRHKLENANAQLTSLLTRMESTRKQLATAISE---LQDYETKEKALQINI---DNVLEQ 911
Cdd:pfam15921 504 -----------------SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMaekDKVIEI 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 912 QRDLEKQQADFQLQYDKiTAKEDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKPRELEKKLLECvnELKKYENVNKKAl 991
Cdd:pfam15921 567 LRQQIENMTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKLVNAGS- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 992 DQYMTASSQKEELTKRMAEQKKSEDSIEELlkvleNRKYEAIDLTFKQVKKNFEQVFKQLvphgrgKMQMRArEQRDDEE 1071
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSL-----SEDYEVLKRNFRNKSEEMETTTNKL------KMQLKS-AQSELEQ 710
|
410
....*....|
gi 392896701 1072 GINSVELYEG 1081
Cdd:pfam15921 711 TRNTLKSMEG 720
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-219 |
2.49e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 49.42 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 6 VRITGFRSYKDNT-NvsgFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHEStgpkvaharVEITFDN 84
Cdd:pfam13476 1 LTIENFRSFRDQTiD---FSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGD---------IRIGLEG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 85 SEKrlmafenSEVKIVRQVGKKKDQYYIDNKmvpRAEVVNLMESAGFSRSNPYYIVKQGKINELATSPDAYKLKLLREVA 164
Cdd:pfam13476 69 KGK-------AYVEITFENNDGRYTYAIERS---RELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 392896701 165 GTRVYDERKEESLKILKETKMKTEKIqgllKYIDERLQTLENEKEDLKEYQKLDK 219
Cdd:pfam13476 139 QEREEEFERKEKKERLEELEKALEEK----EDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-444 |
3.00e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 174 EESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLkEYQKLDKTKRSVEYTMYDNTnKEAIKEKTKLDEQKVELNQK 253
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQL-KELEEKLKKYNLEELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 254 D-NNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVE-EKMTLKLEIDSLNE--ENTRERQGRQNAEH 329
Cdd:PRK03918 526 EyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEEleERLKELEPFYNEYL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 330 SLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEIlakqgqRSQFSsvDDRDKFLRNEIRRISGLIAD 409
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL------EKKYS--EEEYEELREEYLELSRELAG 677
|
250 260 270
....*....|....*....|....*....|....*
gi 392896701 410 NKEREETIQKELADVEREDEKLNNEIQSISRTIDE 444
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
786-1173 |
3.12e-06 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 51.27 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 786 GSNMSSQLTSDEEQ-----TVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKT---------------KE 845
Cdd:TIGR00634 133 GQHDQQLLFRPDEQrqlldTFAGANEKVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQfqleeleeadlqpgeDE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 846 SLTARVDDISDNERRHKL---------ENANAQLTSLLTRMESTRKQLATAISElqdyetKEKALQINIDNVLEQQRDle 916
Cdd:TIGR00634 213 ALEAEQQRLSNLEKLRELsqnalaalrGDVDVQEGSLLEGLGEAQLALASVIDG------SLRELAEQVGNALTEVEE-- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 917 kqqADFQLQ--YDKITAKEDEVKQKREdslkKMRLLgalptdtfskwqnvkpRELEKKLLECVNELKKYENVNKKALDQY 994
Cdd:TIGR00634 285 ---ATRELQnyLDELEFDPERLNEIEE----RLAQI----------------KRLKRKYGASVEEVLEYAEKIKEELDQL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 995 MTASSQKEELTKRmaEQKKSEDSIEELLKVLENRKYEAIDLtfkqvKKNFEQVFKQL-VPHGRGKMQMRARE-----QRD 1068
Cdd:TIGR00634 342 DDSDESLEALEEE--VDKLEEELDKAAVALSLIRRKAAERL-----AKRVEQELKALaMEKAEFTVEIKTSLpsgakARA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1069 DEEGINSVELYegisvlvsFVSDDGDSETREMTQLSGGQKSLVALAI--IFSIQkcDPAPFYLFDEIDAALDAQHRKSVA 1146
Cdd:TIGR00634 415 GAYGADQVEFL--------FSANTGEPVKPLAKVASGGELSRVMLALkvVLSSS--AAVTTLIFDEVDVGVSGETAQAIA 484
|
410 420
....*....|....*....|....*..
gi 392896701 1147 DMIQSLSDQAQFVTTTFRPELLATAEK 1173
Cdd:TIGR00634 485 KKLAQLSERHQVLCVTHLPQVAAHADA 511
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-47 |
3.32e-06 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 50.93 E-value: 3.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 392896701 1 MKIKEVRITGFRSYKdNTNVSgFSPRSNVVVGRNGSGKSNFFHAIQF 47
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLE-LSPGVNVLVGENGQGKTNLLEAIYL 45
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
674-1169 |
4.66e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 674 IDKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAIS----QQ 749
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 750 FYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRK 829
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 830 N---------AIENLLTKKLYKTKESLTARVDDISDNERRHKLENA--NAQLTSL-------LTRMESTRKQLATAISEL 891
Cdd:COG4717 274 TiagvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEelEELLAALglppdlsPEELLELLDRIEELQELL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 892 QDYETKEKALQINiDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKPRELEK 971
Cdd:COG4717 354 REAEELEEELQLE-ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 972 KLLECVNELKKYENVNKKALDQYMTASSQKEELTK--RMAEQKKSEDSIEELLKVLENR--KYEAIDLTFKQVKKNFEQ- 1046
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEwaALKLALELLEEAREEYREe 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1047 ----VFKQLVPHGRGKMQMRAREQRDDEEGinsvelyegisvlvSFVSDDGDSETREMTQLSGGQKSLVALAIIFSI--- 1119
Cdd:COG4717 513 rlppVLERASEYFSRLTDGRYRLIRIDEDL--------------SLKVDTEDGRTRPVEELSRGTREQLYLALRLALael 578
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 392896701 1120 QKCDPAPFyLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLA 1169
Cdd:COG4717 579 LAGEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVE 627
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
690-892 |
4.79e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 690 FTKELAELQKSLAEAEKMVRE--RTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGI 767
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 768 KNH--LRELLAQKENFEQEIgSNMSSQLTsDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKE 845
Cdd:COG3206 260 LQSpvIQQLRAQLAELEAEL-AELSARYT-PNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392896701 846 SLTARVDDISDNERRH-----KLENANAQLTSLLTRMESTRKQLATAISELQ 892
Cdd:COG3206 338 QLEARLAELPELEAELrrlerEVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-504 |
6.21e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 171 ERKEESLKILKETKMKTEKIQGLLKYIDERLQTL---ENEKEDLKEyqKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQK 247
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEIEDLRETIaetEREREELAE--EVRDLRERLEELEEERDDLLAEAGLDDADAEA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 248 VELNQKD-NNVKSQLNDVIAEMA-----------KLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNE 315
Cdd:PRK02224 312 VEARREElEDRDEELRDRLEECRvaaqahneeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 316 ENTRERQGRQNAEHSLQGVgdeifknEEELDTIKPEYAKLLEEESRLKTDIRIDESR---AKEILAKQ-----GQRSQFS 387
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNA-------EDFLEELREERDELREREAELEATLRTARERveeAEALLEAGkcpecGQPVEGS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 388 SVDDRDKFLRNEIRRISGLIADNKEREETIQ------KELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSL-- 459
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELre 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 392896701 460 -KQEYDAAYVAQQTAAREEK----AIRDKIGNTEQDISAAN---DQLRRIVAR 504
Cdd:PRK02224 545 rAAELEAEAEEKREAAAEAEeeaeEAREEVAELNSKLAELKeriESLERIRTL 597
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-466 |
6.77e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 174 EESLKILKETKMKTEKIQGLLKYIDERL-------QTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQ 246
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLeeleerhELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 247 KVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLRED-KETLQAEETKMVEEKMTLKLEIDSLNE---------E 316
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhRKELLEEYTAELKRIEKELKEIEEKERklrkelrelE 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 317 NTRERQGRQNAEHSLQGVGDEIFK-----NEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQF-SSVD 390
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELeKKLD 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 391 DRDKFLRNEIRRISGL-IADNKEREETIQK---------ELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLK 460
Cdd:PRK03918 567 ELEEELAELLKELEELgFESVEELEERLKElepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
....*.
gi 392896701 461 QEYDAA 466
Cdd:PRK03918 647 KELEEL 652
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-534 |
6.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 144 KINELATSPDAYKLKLLREVAGTRVYDE-RKEESLKILKETKMKTEKiqgllKYIDERLQTLENEKEDLKeyqKLDKTKR 222
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEA-----KKAEEDKNMALRKAEEAK---KAEEARI 1594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 223 SVEYTMYDNTNKEAIKEKTKLDEQKVELNQ--KDNNVKSQLNDVI---------AEMAKLKTDKKKLESLGRGLREDKET 291
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKkkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 292 LQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHSLQGVGDEIfKNEEELDTIKPEYAKLLEEESRLKT-DIRIDE 370
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-KKAEEENKIKAEEAKKEAEEDKKKAeEAKKDE 1753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 371 SRAKEILAKQGQRSQFSS-------------VDDRDKFLRNEIRRISGLIADNKER-EETIQKELADVEREDEKLNNEIQ 436
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEeirkekeavieeeLDEEDEKRRMEVDKKIKDIFDNFANiIEGGKEGNLVINDSKEMEDSAIK 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 437 SISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKAIRDKIGN---TEQDISAANDQLRRIVA----RPVYNG 509
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEieeADEIEKIDKDDIEREIPnnnmAGKNND 1913
|
410 420
....*....|....*....|....*
gi 392896701 510 ITGVRKVIEEFKHDNRNGQHDDVIN 534
Cdd:PTZ00121 1914 IIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1102-1169 |
1.47e-05 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 47.46 E-value: 1.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896701 1102 QLSGGQKSLVALAIIFSIQkcdpAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQ-FVTTTFRPELLA 1169
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLL 198
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-500 |
1.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 162 EVAGTRVYDERKEESLKILKETKMKTEKIQgllKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKT 241
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 242 KLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRER 321
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 322 QGRQNAEHslqgvgdeiFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEilakqgQRSQFSSVDDRDKFLRNEIR 401
Cdd:PTZ00121 1617 EAKIKAEE---------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI------KAAEEAKKAEEDKKKAEEAK 1681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 402 RISgliADNKEREETIQKElADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKAiR 481
Cdd:PTZ00121 1682 KAE---EDEKKAAEALKKE-AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-K 1756
|
330
....*....|....*....
gi 392896701 482 DKIGNTEQDISAANDQLRR 500
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRK 1775
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-49 |
1.67e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 1.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 392896701 3 IKEVRITGFRSYKDNTNVSGFSPrSNVVVGRNGSGKSNFFHAIQFVL 49
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEALKYAL 46
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1087-1149 |
2.02e-05 |
|
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: 46.82 E-value: 2.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896701 1087 SFVSDDgDSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMI 1149
Cdd:cd03276 95 SFLTSN-KAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLL 156
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
977-1173 |
2.17e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 47.69 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 977 VNELKKYENVNKKALDQYMTASSQKEELtkrmaeqKKSEDSIEELLKVLENRKYEAIDLTFKQVKknfeQVFKQLVPHGR 1056
Cdd:COG3950 92 LKKLERLKEEYFSRLDGYDSLLDEDSNL-------REFLEWLREYLEDLENKLSDELDEKLEAVR----EALNKLLPDFK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1057 gkmQMRAREQRddeeginsvelyegisvlVSFVSDDGDSETREMTQLSGGQKSLVALA--IIFSIQKCDPAPFY------ 1128
Cdd:COG3950 161 ---DIRIDRDP------------------GRLVILDKNGEELPLNQLSDGERSLLALVgdLARRLAELNPALENplegeg 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392896701 1129 --LFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEK 1173
Cdd:COG3950 220 ivLIDEIDLHLHPKWQRRILPDLRKIFPNIQFIVTTHSPLILSSLED 266
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
697-920 |
2.99e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 697 LQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHR--ELTEAKNAISQQfyMVTSTkepkkDQLLGIKNHLREL 774
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQ--LSELE-----SQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 775 LAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRR-------RMDLMHRKNAIENLLTKKLYKTKESL 847
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896701 848 TARVDdiSDNERRHKLENANAQLTSLLTRMESTRKQLAtaisELQ-DYETKEKALqiniDNVLEQQRDLEKQQA 920
Cdd:COG3206 319 EAELE--ALQAREASLQAQLAQLEARLAELPELEAELR----RLErEVEVARELY----ESLLQRLEEARLAEA 382
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1098-1159 |
4.00e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.59 E-value: 4.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896701 1098 REMTQLSGGQKSLVALAIIFsIQKCDpapFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFV 1159
Cdd:cd03236 135 RNIDQLSGGELQRVAIAAAL-ARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
700-953 |
4.50e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 700 SLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQfyMVTSTKEpkkdqllgiknhLRELLAQKE 779
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARR------------IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 780 NFEQEIgsnmsSQLTSDEEQTVKKLRKKVDEMTKQLATVSRrrmdlMHRKNAIENLLtkklyktkesltaRVDDISDNER 859
Cdd:COG4942 80 ALEAEL-----AELEKEIAELRAELEAQKEELAELLRALYR-----LGRQPPLALLL-------------SPEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 860 R-HKLENANAQLTSLLTRMESTRKQLATAISELqdyETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQ 938
Cdd:COG4942 137 RlQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
250
....*....|....*
gi 392896701 939 KREDSLKKMRLLGAL 953
Cdd:COG4942 214 ELAELQQEAEELEAL 228
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-65 |
4.90e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.53 E-value: 4.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896701 1 MKIKEVRITGFRSYKDnTNVS-GFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLL 65
Cdd:COG3950 1 MRIKSLTIENFRGFED-LEIDfDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-500 |
6.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 96 EVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVK---QGKINELATSPDAYKLKLLREVAGTRVYDE- 171
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKaeeARKADELKKAEEKKKADEAKKAEEKKKADEa 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 172 -RKEESLKILKETKMKTE----KIQGLLKYIDERLQTLENEKEdlKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQ 246
Cdd:PTZ00121 1308 kKKAEEAKKADEAKKKAEeakkKADAAKKKAEEAKKAAEAAKA--EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 247 KVELNQKDNNVKSQLNDV---IAEMAKLKTDKKKLESLGRGLREDKetlQAEETKMVEEKMTLKLEIDSLNEENTRERQG 323
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDkkkADELKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 324 RQNAEHSLQG-----------VGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQFSSVDDR 392
Cdd:PTZ00121 1463 KKKAEEAKKAdeakkkaeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 393 DKFLR-NEIRRISGLiadnKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYE------MDTFAAKSTSLKQEYDA 465
Cdd:PTZ00121 1543 EEKKKaDELKKAEEL----KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmklyEEEKKMKAEEAKKAEEA 1618
|
410 420 430
....*....|....*....|....*....|....*.
gi 392896701 466 AYVAQQT-AAREEKAIRDKIGNTEQDISAANDQLRR 500
Cdd:PTZ00121 1619 KIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-504 |
7.26e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDNTNVsgFSPRSNVVVGRNGSGKSNFFHAIQFVLsdeyahlkeeqrlgllhestgpkvaharvei 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIE--FSPGLNVIYGPNEAGKSTLLAFIRAML------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 81 tfdnsekrlmafensevkiVRQVGKKKDQYYIDNKMVPRAEVVNLMEsagfsrsnpyyivKQGKINELATSPDAYKlKLL 160
Cdd:COG4717 48 -------------------LERLEKEADELFKPQGRKPELNLKELKE-------------LEEELKEAEEKEEEYA-ELQ 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 161 REVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTM--YDNTNKEAIK 238
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEeeLEELEAELAE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 239 EKTKLDEqkvELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLeidslnEENT 318
Cdd:COG4717 175 LQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL------EERL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 319 RERQGRQNAE---HSLQGVGDEIFKNEEELD---------TIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQF 386
Cdd:COG4717 246 KEARLLLLIAaalLALLGLGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 387 S----SVDDRDKFLRNEIRRISGLIADNKEREETIQK-ELADVEREDEKLNNEIQSIS----RTIDENRYEMDTFAAKST 457
Cdd:COG4717 326 AalglPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELE 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 392896701 458 SLKQEYDAAY--VAQQTAAREEKAIRDKIGNTEQDISAANDQLRRIVAR 504
Cdd:COG4717 406 ELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1103-1173 |
7.31e-05 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 46.90 E-value: 7.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896701 1103 LSGGQKSLVALAIIFsiqkCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEK 1173
Cdd:TIGR02857 459 LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
755-941 |
1.65e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 755 STKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEqtVKKLRKKVDEMTKQLATVSRRrmdLMHRKNAIEN 834
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE--LEALQAEIDKLQAEIAEAEAE---IEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 835 LLtKKLYKTKESLTA-----RVDDISD-NERRHKLENANAQLTSLLTRMESTRKQLATAISELQDyetKEKALQINIDNV 908
Cdd:COG3883 91 RA-RALYRSGGSVSYldvllGSESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEA---KLAELEALKAEL 166
|
170 180 190
....*....|....*....|....*....|...
gi 392896701 909 LEQQRDLEKQQADFQLQYDKITAKEDEVKQKRE 941
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
198-501 |
1.93e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 198 DERLQTLENEKEDLKE--YQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQKV-ELNQKDNNVKSQLNDVIAEMAK---- 270
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNelKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIkDLNDKLKKNKDKINKLNSDLSKinse 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 271 LKTDKK---KLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDT 347
Cdd:TIGR04523 112 IKNDKEqknKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 348 IKPEYAKLLEEESRLKTDIRIDESRAKEILAKQgqrSQFSSVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVERE 427
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELK---KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896701 428 DEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAY---VAQQTAAREEK--AIRDKIGNTEQDISAANDQLRRI 501
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWnkeLKSELKNQEKKleEIQNQISQNNKIISQLNEQISQL 347
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1102-1169 |
1.96e-04 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 44.25 E-value: 1.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1102 QLSGGQKSLVALAIIFSIQkcdpaPFYL-FDEIDAALDAQHRKSVADMIQSLSDQ-AQFVTTTFRPELLA 1169
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAME-----PEVLvLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVA 198
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
846-1028 |
2.15e-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: 45.14 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 846 SLTARVDDISDNERrhKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQ 925
Cdd:COG4942 14 AAAAQADAAAEAEA--ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 926 YDKITAKEDEVKQKREDSLKKMRLLGALPT--------------------DTFSKWQNVKPRELEKKLLEcVNELKKYEN 985
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylKYLAPARREQAEELRADLAE-LAALRAELE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392896701 986 VNKKALDQYMTA-SSQKEELTKRMAEQKKSEDSIEELLKVLENR 1028
Cdd:COG4942 171 AERAELEALLAElEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1077 |
2.45e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 675 DKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAiSQQFYMVT 754
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA-KKKAEEKK 1431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 755 STKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLmhRKNAIEN 834
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA--KKAAEAK 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 835 LLTKKLYKTKESLTA----------RVDDISDNERRHKLENA----NAQLTSLLTRMESTRKQLATAISELQDYETKEKA 900
Cdd:PTZ00121 1510 KKADEAKKAEEAKKAdeakkaeeakKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 901 LQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKqKREDSLKKMRLLGALPTDTFSKWQNVKPRElEKKLLECVNEL 980
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAE-EENKIKAAEEA 1667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 981 KKYENVNKKALDqymtaSSQKEELTKRMAEQKKSEDsiEELLKVLENRKYEAIDLTFKQVKKNFEQVFKQLVPHGRGKMQ 1060
Cdd:PTZ00121 1668 KKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
410 420
....*....|....*....|
gi 392896701 1061 ---MRAREQRDDEEGINSVE 1077
Cdd:PTZ00121 1741 edkKKAEEAKKDEEEKKKIA 1760
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-1071 |
3.13e-04 |
|
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: 45.04 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 2 KIKEVRITGFRSY----KDNTNVSGFSPRSnVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLglLHEstgPKVAH-- 75
Cdd:TIGR00606 2 KFLKMSILGVRSFgiedKDKQIIDFFSPLT-ILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTF--VHD---PKVAQet 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 76 ---ARVEITFDNSEKRLMAFENSevkIVRQVGKKKDQYYIDNKMVPRaevvnlmesagfsrsnpyyiVKQGKINELATSP 152
Cdd:TIGR00606 76 dvrAQIRLQFRDVNGEECAVVRS---MVCTQKTKKTEFKTLEGVITR--------------------YKHGEKVSLSSKC 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 153 DAYKLKLLREVAGTRV--------YDERKEESLKILKETKMKTEKIQGLLKYID--ERL-QTLENEKEDLKEYQkldktk 221
Cdd:TIGR00606 133 AEIDREMISHLGVSKAvlnnvifcHQEDSNWPLSEGKALKQKFDEIFSATRYIKalETLrQVRQTQGQKVQEHQ------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 222 rsVEYTMYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNdviaEMAKLKTDKKKLESLGRGLREDKETLQA-EETKMV 300
Cdd:TIGR00606 207 --MELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYEN----ELDPLKNRLKEIEHNLSKIMKLDNEIKAlKSRKKQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 301 EEKMTLKLEI----------DSLNE-ENTRERQGRQNaEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESR--LKTDIR 367
Cdd:TIGR00606 281 MEKDNSELELkmekvfqgtdEQLNDlYHNHQRTVREK-ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRlqLQADRH 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 368 IDESRAKEILAKQGQRSQFSSVDDRDKFLRNEI---------------RRISGLIADNKEREETIQKELADVEREDEKLN 432
Cdd:TIGR00606 360 QEHIRARDSLIQSLATRLELDGFERGPFSERQIknfhtlvierqedeaKTAAQLCADLQSKERLKQEQADEIRDEKKGLG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 433 NEIQSISRTIDENRYE--------------MDTFAAKSTSLKQEYDAAYVAQQTAAREEKAIRDKIGNTEQ--------D 490
Cdd:TIGR00606 440 RTIELKKEILEKKQEElkfvikelqqlegsSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKadldrklrK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 491 ISAANDQLRRIVARPVYNGITGVRKVIEEFKHDNRNGQHDDVINGYYGTVIELAEVPDMFRTAVEVIAQNRlfyhvvetD 570
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTR--------D 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 571 RIATKILRKFNEMQLPGEINffpmNRVSAPRQRDLSNNSNARPMSDVIDYEVQYDKVFKSITANVIIVRTLdqAARDLRN 650
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHIN----NELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAML--AGATAVY 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 651 EGFDVVSVDGDQ----MSKKGVMTGGFIDKKRSKLELHTQKdrFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHE 726
Cdd:TIGR00606 666 SQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRL--APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKE 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 727 NQIGDFHRK----HRELTEAKNAISQQFYMVTST--KEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQT 800
Cdd:TIGR00606 744 KEIPELRNKlqkvNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 801 VKKLRKKVDEMTKQLATVSRrrmdlmhrknaiENLLTKKLYKTKESLTARVDDISDNERRHKLenanaQLTSLLTRMEST 880
Cdd:TIGR00606 824 VQQVNQEKQEKQHELDTVVS------------KIELNRKLIQDQQEQIQHLKSKTNELKSEKL-----QIGTNLQRRQQF 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 881 RKQLATAISELQDYETKekalqinIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSL----KKMRLLGALPTD 956
Cdd:TIGR00606 887 EEQLVELSTEVQSLIRE-------IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVndikEKVKNIHGYMKD 959
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 957 TFSKWQNVKPRELEKK----------LLECVNELKKYENvNKKALDQYMTASSQKEELTKRMAEQKKSEDSIEELLKVLE 1026
Cdd:TIGR00606 960 IENKIQDGKDDYLKQKetelntvnaqLEECEKHQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELK 1038
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*
gi 392896701 1027 NRKYEAIDLTFKQVKKNFEQVFKQLVPHGRGKMQMRAREQRDDEE 1071
Cdd:TIGR00606 1039 QHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKE 1083
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-446 |
3.48e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 173 KEESLKILKETKMKTEK-IQGLLKYIDERLQT---LENEKEDLK-EYQKLDKTKRSVEyTMYDNTNKEAIKEKTKLDEQK 247
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKeIERLKETIIKNNSEikdLTNQDSVKElIIKNLDNTRESLE-TQLKVLSRSINKIKQNLEQKQ 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 248 VELNQKdnnvKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRErqgrqna 327
Cdd:TIGR04523 489 KELKSK----EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE------- 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 328 ehslqGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEIlakqgqRSQFSSVDDRDKFLRNEIRRIsgli 407
Cdd:TIGR04523 558 -----NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL------IKEIEEKEKKISSLEKELEKA---- 622
|
250 260 270
....*....|....*....|....*....|....*....
gi 392896701 408 adnKEREETIQKELADVEREDEKLNNEIQSISRTIDENR 446
Cdd:TIGR04523 623 ---KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
682-1051 |
5.20e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 682 ELHTQKDRFTKELAELQKSLAEA---EKMVRERTQEAEKIRNRMQQHenqigdfhrKHRELTEAKNAISQQFYMVTSTKE 758
Cdd:pfam05483 286 ELIEKKDHLTKELEDIKMSLQRSmstQKALEEDLQIATKTICQLTEE---------KEAQMEELNKAKAAHSFVVTEFEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 759 pkkdQLLGIKNHLRELLAQKENFEQEIGS-NMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLlT 837
Cdd:pfam05483 357 ----TTCSLEELLRTEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKI-A 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 838 KKLYKTKESLTARVddisdNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEK 917
Cdd:pfam05483 432 EELKGKEQELIFLL-----QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 918 QQADFQLQYDKITAKEDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKpRELEKKLLECVNELKKYENvnkkaldqymTA 997
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR-EEFIQKGDEVKCKLDKSEE----------NA 575
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 392896701 998 SSQKEELTKRMAEQKKSEDSIEELLKVLENRK--YEAIDLTFKQVKKNFEQVFKQL 1051
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNknIEELHQENKALKKKGSAENKQL 631
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
963-1169 |
6.26e-04 |
|
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: 43.15 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 963 NVKPRELEKKLLECVNELKKYENVNKKALDQYMTASSQKEELTKRMAEQKKSEDSIEELLKVLENRKYEAIDLTFKQVKK 1042
Cdd:pfam13304 77 DLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1043 NFEQVFKQLV------------PHGRGKMQMRAREQRDDEEGINSVELYEGISVLVSFVSDD--------GDSETREMTQ 1102
Cdd:pfam13304 157 LDEGLLLEDWavldlaadlalfPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRErglillenGGGGELPAFE 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896701 1103 LSGGQKSLVALAIIFSIQkCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSD-QAQFVTTTFRPELLA 1169
Cdd:pfam13304 237 LSDGTKRLLALLAALLSA-LPKGGLLLIDEPESGLHPKLLRRLLELLKELSRnGAQLILTTHSPLLLD 303
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-521 |
6.85e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDNTNVsgFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRlgllhestgpkvaharVEI 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEKIEDM----------------IKK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 81 TFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVpraEVVNLMESAGFSRSNPYY----------------IVKQGK 144
Cdd:PRK01156 63 GKNNLEVELEFRIGGHVYQIRRSIERRGKGSRREAYI---KKDGSIIAEGFDDTTKYIeknilgiskdvflnsiFVGQGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 145 INELATSPDAYKLKLLREVAGTrvydERKEESLKILKET-KMKTEKIQGLlKYIDERLQTLENEKEDLKEYQKLDKTKRS 223
Cdd:PRK01156 140 MDSLISGDPAQRKKILDEILEI----NSLERNYDKLKDViDMLRAEISNI-DYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 224 VeytmydntnkeAIKEKTKLDEQKVELNQKDNNVKSQLNdviaEMAKLKTDKKKLESlgrGLREDKETLQAEETKMVE-- 301
Cdd:PRK01156 215 I-----------TLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYES---EIKTAESDLSMELEKNNYyk 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 302 --EKMTLKLEIDSL--NEENTRE-----------RQGRQNAEHSLQGVgDEIFKNEEELDTIKPEYAKL---LEEESRLK 363
Cdd:PRK01156 277 elEERHMKIINDPVykNRNYINDyfkykndienkKQILSNIDAEINKY-HAIIKKLSVLQKDYNDYIKKksrYDDLNNQI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 364 TDIRIDESR----AKEILAKQGQRSQFSSVDDRDKFLRNEIRRISGLIAD--NKEREEtIQKELADVEREDEKLNNEIQS 437
Cdd:PRK01156 356 LELEGYEMDynsyLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDaiKKELNE-INVKLQDISSKVSSLNQRIRA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 438 ISRTIDENRYEMDTFAAKS------TSLKQEYDAAYVaqQTAAREEKAIRDKIGNTEQDISAANDQLRRIVARPVYNGIT 511
Cdd:PRK01156 435 LRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHII--NHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE 512
|
570
....*....|
gi 392896701 512 GVRKVIEEFK 521
Cdd:PRK01156 513 EINKSINEYN 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
285-445 |
7.01e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 285 LREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKP--EYAKLLEEESRL 362
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 363 KTDIRIDESRAKEILAKqgqrsqfssVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTI 442
Cdd:COG1579 102 KRRISDLEDEILELMER---------IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
...
gi 392896701 443 DEN 445
Cdd:COG1579 173 PPE 175
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-489 |
7.67e-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: 43.80 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKD-NTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVE 79
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGtHTIDFTALGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAFAELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 80 ITFDNSEKRLMAFEN-------SEVKIVRQVGKKKDQYYIDNKMVPRAEVVNL----MESAGFSRSnpyYIVKQGKINEL 148
Cdd:TIGR00618 81 FSLGTKIYRVHRTLRctrshrkTEQPEQLYLEQKKGRGRILAAKKSETEEVIHdllkLDYKTFTRV---VLLPQGEFAQF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 149 ATSPDAYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKI----QGLLKYIDERLQTLENEKEDL-KEYQKLDKTKRS 223
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLtlrsQLLTLCTPCMPDTYHERKQVLeKELKHLREALQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 224 VEYTmydntnKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLEslgrgLREDKETLqAEETKMVEek 303
Cdd:TIGR00618 238 TQQS------HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN-----RARKAAPL-AAHIKAVT-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 304 mtlklEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRlktdIRIDESRAKEILAkqgQR 383
Cdd:TIGR00618 304 -----QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH----IRDAHEVATSIRE---IS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 384 SQFSSVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISR---TIDENRYEMDTFAAKSTSLK 460
Cdd:TIGR00618 372 CQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHakkQQELQQRYAELCAAAITCTA 451
|
490 500
....*....|....*....|....*....
gi 392896701 461 QEYDAAYVAQQTAAREEKAIRDKIGNTEQ 489
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
674-1031 |
9.67e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 674 IDKKRSKLELHTQ-KDRFTKELAELQKSLAEAEKMVRERTQE---AEKIRNR-------MQQHENQIGDFHRKHRELTEA 742
Cdd:pfam05483 386 LQKKSSELEEMTKfKNNKEVELEELKKILAEDEKLLDEKKQFekiAEELKGKeqeliflLQAREKEIHDLEIQLTAIKTS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 743 KNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQEiGSNMSSQLTSDEEQtVKKLRKKVDEMTKQLATVSRRR 822
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE-ASDMTLELKKHQED-IINCKKQEERMLKQIENLEEKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 823 MDLMHRKNAI-------------------ENLLTKKLYKTKESLTARVDDISDNERRHKLENANAQLTSLLTRMESTRKQ 883
Cdd:pfam05483 544 MNLRDELESVreefiqkgdevkckldkseENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 884 LATAISELQDYETKEKALQINIDNVleqQRDLEKQQADFQlqydkitaKEDEVKQKREDSLKKMRLLGALPTDTFSKWQN 963
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASA---KQKFEEIIDNYQ--------KEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896701 964 VKPRELEKKLLECVNELKKYENVNKKALDQY-----MTASSQKEELTKRMAEQKKSEDSIEELLKVLENRKYE 1031
Cdd:pfam05483 693 EIDKRCQHKIAEMVALMEKHKHQYDKIIEERdselgLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIE 765
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1103-1155 |
1.02e-03 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 41.86 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 392896701 1103 LSGGQKSLVALAIIFsIQKCDpapFYLFDEIDAALDAQHRKSVADMIQSLSDQ 1155
Cdd:cd03226 127 LSGGQKQRLAIAAAL-LSGKD---LLIFDEPTSGLDYKNMERVGELIRELAAQ 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
234-446 |
1.06e-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: 42.83 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 234 KEAIKEKTKLDEQKVELNQKD-NNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDS 312
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEeKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 313 LNeeNTRERQGRQNAEHSLQGVGD--EIFKNEEELDTIKPEYAKLLEEesrLKTDI-RIDESRAKEILAKQGQRSQFSSV 389
Cdd:COG4942 109 LL--RALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEE---LRADLaELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392896701 390 DDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENR 446
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1101-1162 |
1.14e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 42.84 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896701 1101 TQLSGGQKSLVALAIIFS-----IQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAqFVTTT 1162
Cdd:PRK00064 272 DFGSTGQQKLLLLALKLAeaellKEETGEAPILLLDDVASELDDGRRAALLERLKGLGAQV-FITTT 337
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-464 |
1.16e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 171 ERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQ-KLDKTKRSVEYTMYDNTNKEAIKEKT-------- 241
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnLLEKEKLNIQKNIDKIKNKLLKLELLlsnlkkki 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 242 ----KLDEQKVELNQKDNNVKSQL----NDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSL 313
Cdd:TIGR04523 211 qknkSLESQISELKKQNNQLKDNIekkqQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 314 NEENTR-ERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRI-----------DESRAKEILAKQG 381
Cdd:TIGR04523 291 NQLKSEiSDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQlkkeltnseseNSEKQRELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 382 Q----RSQFSSVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKST 457
Cdd:TIGR04523 371 EieklKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
....*..
gi 392896701 458 SLKQEYD 464
Cdd:TIGR04523 451 VKELIIK 457
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
230-443 |
1.18e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 230 DNTNKEAIKEKTKLDEQKVELNQKD--NNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEE----K 303
Cdd:pfam05667 311 EAPAATSSPPTKVETEEELQQQREEelEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQykvkK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 304 MTLKLEIDSlnEENTRERQGR-QNAEHSLQGVG-----------DEIFKNEEELDTIKPEYAKLLEEESRLKTDIR--ID 369
Cdd:pfam05667 391 KTLDLLPDA--EENIAKLQALvDASAQRLVELAgqwekhrvpliEEYRALKEAKSNKEDESQRKLEEIKELREKIKevAE 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896701 370 ESRAKEILAKQGQrSQFSSVDdRDKfLRNE-IRRISGLIADNKEREETIQKELADVeREdekLNNEIQSISRTID 443
Cdd:pfam05667 469 EAKQKEELYKQLV-AEYERLP-KDV-SRSAyTRRILEIVKNIKKQKEEITKILSDT-KS---LQKEINSLTGKLD 536
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
682-1049 |
1.26e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 682 ELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENqigDFHRKHRELTEAKNAISQqfymVTSTKEPKK 761
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEK----LKKENQSYK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 762 DQLLGIKNHLRELLAQKENFEQEiGSNMSSQLTSDEEQtvKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLY 841
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKL-NQQKDEQIKKLQQE--KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 842 KTKESLTARVDDISD--NERRHKLENANAQLtslltrmESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKqq 919
Cdd:TIGR04523 461 NTRESLETQLKVLSRsiNKIKQNLEQKQKEL-------KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES-- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 920 adfqlqydKITAKEDEVKQKREDSLKKMRLL--GALPTDTFSKWQNVKPRELEKKLLECVNE-----LKKYENVNKKALD 992
Cdd:TIGR04523 532 --------EKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEekqelIDQKEKEKKDLIK 603
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896701 993 QYMTASSQKEELTKRMAEQKKSEDSIEELLKVLENRK------YEAIDLTFKQVKKNFEQVFK 1049
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKnklkqeVKQIKETIKEIRNKWPEIIK 666
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1103-1175 |
1.27e-03 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 40.83 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896701 1103 LSGGQKSLVALAIIFsIQKcdpAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFY 1175
Cdd:cd03228 97 LSGGQRQRIAIARAL-LRD---PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-110 |
1.30e-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: 41.49 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1 MKIKEVRITGFRSYKDNTNVSgFSPRSN----VVVGRNGSGKSNFFHAIQFVLsdeYAHLKEEQRLGLLHESTGPKVAHA 76
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVID-FTGLDNnglfLICGPTGAGKSTILDAITYAL---YGKTPRYGRQENLRSVFAPGEDTA 76
|
90 100 110
....*....|....*....|....*....|....
gi 392896701 77 RVEITFDNSEKRLmafensevKIVRQVGKKKDQY 110
Cdd:cd03279 77 EVSFTFQLGGKKY--------RVERSRGLDYDQF 102
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-462 |
1.30e-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: 43.18 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 121 EVVNLMESAGFSRSNPYYIVKQGKI-NELATSPDAYKLKLLREVAGT------------RVYDERKEESLKIL-----KE 182
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQLSDLESTvsqlrselreakRMYEDKIEELEKQLvlansEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 183 TKMKTEK-------------IQGLLKYIDERLQTLENEKEDLKEYQKLDkTKRSVeytMYDNTNKEAIKEKTKLDEQKVE 249
Cdd:pfam15921 359 TEARTERdqfsqesgnlddqLQKLLADLHKREKELSLEKEQNKRLWDRD-TGNSI---TIDHLRRELDDRNMEVQRLEAL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 250 LNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQaeetKMVEEKMTLKLEIDSLNEENTRERQGRQNAEH 329
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLR----KVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 330 SLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKtdiriDESRAKEILakqgqRSQFSSVDDRDKFLRNEIRRISGLIAD 409
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-----NVQTECEAL-----KLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 392896701 410 NKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQE 462
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1059-1163 |
1.35e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 41.94 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1059 MQMRAREQRDDEEginsvELYEGISVLVSFVSDDGdSETREMTQLSGGQKSLVALAIIFSIqkcDPApFYLFDEIDAALD 1138
Cdd:cd03296 99 LRVKPRSERPPEA-----EIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAV---EPK-VLLLDEPFGALD 168
|
90 100
....*....|....*....|....*
gi 392896701 1139 AQHRKSVADMIQSLSDQAQfVTTTF 1163
Cdd:cd03296 169 AKVRKELRRWLRRLHDELH-VTTVF 192
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1100-1151 |
1.49e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 40.12 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 392896701 1100 MTQLSGGQKSLVALAIIFSiqkcDPAPFYLFDEIDAALDAQHRKSVADMIQS 1151
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLL----ENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1098-1163 |
1.70e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 41.99 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896701 1098 REMTQLSGGQKSLVALAIIFSIQkcdpAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFvTTTF 1163
Cdd:PRK10851 132 RYPAQLSGGQKQRVALARALAVE----PQILLLDEPFGALDAQVRKELRRWLRQLHEELKF-TSVF 192
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
171-491 |
1.94e-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: 42.40 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 171 ERKEESLKILKETKMKTEKIQGLLKYIDERLQ-------TLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKeAIKEKTKL 243
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC-SLEELLRT 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 244 DEQKVELNQKDNNVKS----QLNDVIAEMAKLKTDKK-KLESLGRGLREDKETLqaEETKMVEEkmtLKLEIDSLNEENT 318
Cdd:pfam05483 368 EQQRLEKNEDQLKIITmelqKKSSELEEMTKFKNNKEvELEELKKILAEDEKLL--DEKKQFEK---IAEELKGKEQELI 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 319 RERQGRQNAEHSLqgvgdeifknEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRS-QFSSVDDRDKFLR 397
Cdd:pfam05483 443 FLLQAREKEIHDL----------EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLlENKELTQEASDMT 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 398 NEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKS--TSLKQEYDAAYVAQQTAAR 475
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSeeNARSIEYEVLKKEKQMKIL 592
|
330
....*....|....*...
gi 392896701 476 EEKA--IRDKIGNTEQDI 491
Cdd:pfam05483 593 ENKCnnLKKQIENKNKNI 610
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-461 |
2.11e-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: 42.42 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 115 KMVPRAEVVNLMESagFSRSNPYYIVKqgkINELATSPDAYKLKLLREVAGTRVYDERKEESlkilKETKMKTEKIQgll 194
Cdd:pfam17380 235 KMERRKESFNLAED--VTTMTPEYTVR---YNGQTMTENEFLNQLLHIVQHQKAVSERQQQE----KFEKMEQERLR--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 195 KYIDERLQTLENEKEdLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQlNDVIAEMAKLKT- 273
Cdd:pfam17380 303 QEKEEKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ-EEIAMEISRMREl 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 274 DKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLN-------EENTRERQGR---QNAEHSLQGVGDEIFKNEE 343
Cdd:pfam17380 381 ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEmeqiraeQEEARQREVRrleEERAREMERVRLEEQERQQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 344 ELDTIKPEyakllEEESRLKTDIRIDESRAKEILAKQGQRSQFSSVDDRDKFLRNEIRRISGLIADNKEREETI----QK 419
Cdd:pfam17380 461 QVERLRQQ-----EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeeeRR 535
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 392896701 420 ELADVEREDEKLNNE---IQSISRTIDENRYEMDTFAAKSTSLKQ 461
Cdd:pfam17380 536 REAEEERRKQQEMEErrrIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
265-552 |
2.27e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 265 IAEMAKLK--TDKKKLESLGRGLRE--------DKETLQAEETKMVEEKMT-LKLEIDSLNEENTRERQGRQ-NAEHSLQ 332
Cdd:PRK05771 3 PVRMKKVLivTLKSYKDEVLEALHElgvvhiedLKEELSNERLRKLRSLLTkLSEALDKLRSYLPKLNPLREeKKKVSVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 333 GVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEIlakqgqrSQFSSVDDRDKFLRNE--IRRISGLIADN 410
Cdd:PRK05771 83 SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-------EPWGNFDLDLSLLLGFkyVSVFVGTVPED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 411 KEREETIQKELADVEREDEKlnneiqsisrtidenrYEMDTFAAkSTSLKQEYDAAYVAQQTAAREEKaIRDKiGNTEQD 490
Cdd:PRK05771 156 KLEELKLESDVENVEYISTD----------------KGYVYVVV-VVLKELSDEVEEELKKLGFERLE-LEEE-GTPSEL 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896701 491 ISAANDQLRRIVARpvyngITGVRKVIEEFKhdNRNGQHDDVINGYYGTVIELAEVPDMFRT 552
Cdd:PRK05771 217 IREIKEELEEIEKE-----RESLLEELKELA--KKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
866-1033 |
2.45e-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: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 866 ANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSLK 945
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 946 KM-----------RLLGA-LPTDTFSKWQNVKP-RELEKKLLECVNELKKYENVNKKALDQYMT--------ASSQKEEL 1004
Cdd:COG3883 94 ALyrsggsvsyldVLLGSeSFSDFLDRLSALSKiADADADLLEELKADKAELEAKKAELEAKLAelealkaeLEAAKAEL 173
|
170 180
....*....|....*....|....*....
gi 392896701 1005 TKRMAEQKKSEDSIEELLKVLENRKYEAI 1033
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
2-444 |
2.80e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 42.03 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 2 KIKevRITGFRSYKDNTNVSGFSPRsNVVVGRNGSGKSNFFHAiqfvlsdeyahlkeeqrLGLLHESTGPKVAHARVEIT 81
Cdd:COG4694 4 KIK--KLKNVGAFKDFGWLAFFKKL-NLIYGENGSGKSTLSRI-----------------LRSLELGDTSSEVIAEFEIE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 82 FDNSE--KRLMAFENSEVKI-VRQVGKKKDQYYIDnkmvpraevvnlmesagfsrsnPYYIVKQGKINELATSPDAYKLK 158
Cdd:COG4694 64 AGGSApnPSVRVFNRDFVEEnLRSGEEIKGIFTLG----------------------EENIELEEEIEELEKEIEDLKKE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 159 LlrEVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERlQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIK 238
Cdd:COG4694 122 L--DKLEKELKEAKKALEKLLEDLAKSIKDDLKKLFASSGRN-YRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 239 EKTKLDEQKVELNQKDNNVKSQL-NDVIAEMAKLKTDKKKLE----------------------SLGRGLRED-----KE 290
Cdd:COG4694 199 PITPLPDLKALLSEAETLLEKSAvSSAIEELAALIQNPGNSDwveqglayhkeeeddtcpfcqqELAAERIEAleayfDD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 291 TLQAEETKMVEEKMTLKLEIDSLNEentrerQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESR-LKTDIRID 369
Cdd:COG4694 279 EYEKLLAALKDLLEELESAINALSA------LLLEILRTLLPSAKEDLKAALEALNALLETLLAALEEKIAnPSTSIDLD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 370 ESRAKEILAKQ------------GQRSQFSSV--DDRDKFLRNEIRRISGLIADNKE----------REETIQKELADVE 425
Cdd:COG4694 353 DQELLDELNDLiaalnalieehnAKIANLKAEkeEARKKLEAHELAELKEDLSRYKAeveelieelkTIKALKKALEDLK 432
|
490
....*....|....*....
gi 392896701 426 REDEKLNNEIQSISRTIDE 444
Cdd:COG4694 433 TEISELEAELSSVDEAADE 451
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1103-1193 |
3.08e-03 |
|
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: 41.03 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1103 LSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRFRNK 1182
Cdd:cd03241 171 ASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITHLPQVAAMADNHFLVEKEVE 250
|
90
....*....|....*
gi 392896701 1183 ----VSHIDSVTREQ 1193
Cdd:cd03241 251 ggrtVTKVRELDKEE 265
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1098-1154 |
3.41e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 392896701 1098 REMTQLSGG--QKSLVALAIIfsiqkcDPAPFYLFDEIDAALDAQHRKSVADMIQSLSD 1154
Cdd:PRK13409 208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPTSYLDIRQRLNVARLIRELAE 260
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
170-1052 |
3.56e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 170 DERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRS----VEYTMYDNTNKEAIKEK----- 240
Cdd:TIGR01612 1100 DFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINdledVADKAISNDDPEEIEKKieniv 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 241 TKLDEQKvelnqkdnNVKSQLNDVIAEMAKLKTDKKKLEslgrglredketlQAEETKMVEEKMTLKLEIDSLNEEntre 320
Cdd:TIGR01612 1180 TKIDKKK--------NIYDEIKKLLNEIAEIEKDKTSLE-------------EVKGINLSYGKNLGKLFLEKIDEE---- 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 321 rqgRQNAEHSLQGVGDEIfkneEELDTIKpEYAKLLEEESRLKTDIR-------IDESRAKEILAKQgQRSQFSSVDDRD 393
Cdd:TIGR01612 1235 ---KKKSEHMIKAMEAYI----EDLDEIK-EKSPEIENEMGIEMDIKaemetfnISHDDDKDHHIIS-KKHDENISDIRE 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 394 KFLRneirrisgLIADNKEREET--IQKELADVEREDEKLNNEIQSISRTIdENRYEMdtfaAKSTSLKQEYDAAYVAQQ 471
Cdd:TIGR01612 1306 KSLK--------IIEDFSEESDIndIKKELQKNLLDAQKHNSDINLYLNEI-ANIYNI----LKLNKIKKIIDEVKEYTK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 472 TAAREEKAIRDKIGNTEQDISAANDQLRrivarpvyngitgvrkvIEEFKHDNRNGQHDDVINGYYGTVIEL-------- 543
Cdd:TIGR01612 1373 EIEENNKNIKDELDKSEKLIKKIKDDIN-----------------LEECKSKIESTLDDKDIDECIKKIKELknhilsee 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 544 AEVPDMFRTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLPGEINFfpmNRVSAPRQRDLSNNsnarpmsdvidYEVQ 623
Cdd:TIGR01612 1436 SNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDF---NINELKEHIDKSKG-----------CKDE 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 624 YDKVFKSITANVIIVRTLDQAARDLRNegfdvvsvdgdqmskkgvmtggfidkKRSKLELHTQKDRFTKELAELQKSLAE 703
Cdd:TIGR01612 1502 ADKNAKAIEKNKELFEQYKKDVTELLN--------------------------KYSALAIKNKFAKTKKDSEIIIKEIKD 1555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 704 AEKMVRERTQEAEKIRNRMQQHENQIGDfhrkhrelTEAKNAISQQFYM-VTSTKEPKKDQLL---GIKNHLRELLAQKE 779
Cdd:TIGR01612 1556 AHKKFILEAEKSEQKIKEIKKEKFRIED--------DAAKNDKSNKAAIdIQLSLENFENKFLkisDIKKKINDCLKETE 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 780 NFEQEIGS-NMSSQLT--SDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKESLTARVDDISD 856
Cdd:TIGR01612 1628 SIEKKISSfSIDSQDTelKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKE 1707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 857 NERRHKLEnanaqLTSLLTRMESTRKQLATAI--SELQDYETKEKALQIN--IDNVLEQQRDLEKQQADFQLQYDKITAK 932
Cdd:TIGR01612 1708 IAIANKEE-----IESIKELIEPTIENLISSFntNDLEGIDPNEKLEEYNteIGDIYEEFIELYNIIAGCLETVSKEPIT 1782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 933 EDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKPRELEKklleCVNELK-KYENVNKKALDQYMTASSQKEELTKRMAEQ 1011
Cdd:TIGR01612 1783 YDEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEAKEFDR----IINHFKkKLDHVNDKFTKEYSKINEGFDDISKSIENV 1858
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 392896701 1012 KKSEDsiEELLKVLENRKYEA----IDLTFKQVKKNFEQVFKQLV 1052
Cdd:TIGR01612 1859 KNSTD--ENLLFDILNKTKDAyagiIGKKYYSYKDEAEKIFINIS 1901
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
692-1047 |
3.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 692 KELAELQKSLAEAEKMVRERTQEAEKIRNRmqQHENQIGDFHRKHRELTEAKNAisqqfymvTSTKEPKKDQLLGIKNHL 771
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKA--AEAKKKADEAKKAEEAKKADEA--------KKAEEAKKADEAKKAEEK 1545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 772 R--ELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKvdEMTKQLAtvSRRRMDLMHRKNAIENLLTKKLYKTKESLTA 849
Cdd:PTZ00121 1546 KkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA--EEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 850 RVDDISDNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDlEKQQADFQLQYDKI 929
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEE 1700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 930 TAKEDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKPRELEKKllecvnelKKYENVNKKALDQYMTASSQKEELTKRMA 1009
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK--------KKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
330 340 350
....*....|....*....|....*....|....*...
gi 392896701 1010 EQKKSEDSIEELLKVLENRKYEAIDLTFKQVKKNFEQV 1047
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
686-1071 |
3.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 686 QKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQigdfhrkhRELTEAKNAisQQFYMVTSTKEPKKDQLL 765
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDA--------RKAEEARKA--EDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 766 GIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSR--RRMDLMHR---KNAIENLLTKKL 840
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEeeRKAEEARKaedAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 841 YKTKESLTARVDDISDNERRHKLEnaNAQLTSLLTRMESTRKQLATAISELQDYETKEKAlqinidnvLEQQRDLEKQQA 920
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFE--EARMAHFARRQAAIKAEEARKADELKKAEEKKKA--------DEAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 921 DFQLQYDKITAKEDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKPRELEKKllecvNELKKYENVNKKALDQYMTASSQ 1000
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA-----DEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896701 1001 KEELTKRMAEQKKSED----SIEELLKVLENRKYEAIDLTFKQVKKNFEQVFKQlvphgrGKMQMRAREQRDDEE 1071
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA------DEAKKKAEEAKKADE 1448
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
702-1031 |
3.79e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 702 AEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENF 781
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 782 EQEIGSNMSSQLTSDEEQTVKKLRKKV------DEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKESLTARVDDIS 855
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAeeakkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 856 DNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDY----ETKEKALQINIDNVLEQQRDlEKQQADFQLQYDKITA 931
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 932 KEDEVKQKREDSlKKMRLLGALPTDTFSKWQNVKPRELEKKLLEcvnELKKYEnvNKKALDQYMTASSQKEELTKRMAEQ 1011
Cdd:PTZ00121 1471 KADEAKKKAEEA-KKADEAKKKAEEAKKKADEAKKAAEAKKKAD---EAKKAE--EAKKADEAKKAEEAKKADEAKKAEE 1544
|
330 340
....*....|....*....|...
gi 392896701 1012 KKSEDSI---EELLKVLENRKYE 1031
Cdd:PTZ00121 1545 KKKADELkkaEELKKAEEKKKAE 1567
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
705-980 |
3.91e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 705 EKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTstkepkkdQLLGIKNHLRELLAQKENFEQE 784
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET--------ELCAEAEEMRARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 785 IGSNMSSQLTSDEEQTV------KKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTK-------------KLYKTKE 845
Cdd:pfam01576 76 ILHELESRLEEEEERSQqlqnekKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKleedillledqnsKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 846 SLTARVDDISDN--ERRHKLENanaqLTSLLTRMESTrkqlataISELQDYETKEKALQINIDNVleqQRDLEKQQADFQ 923
Cdd:pfam01576 156 LLEERISEFTSNlaEEEEKAKS----LSKLKNKHEAM-------ISDLEERLKKEEKGRQELEKA---KRKLEGESTDLQ 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896701 924 LQYDKITAKEDEVK---QKREDSLKKmrLLGALPTDTFSKWQNVKP-RELEKKLLECVNEL 980
Cdd:pfam01576 222 EQIAELQAQIAELRaqlAKKEEELQA--ALARLEEETAQKNNALKKiRELEAQISELQEDL 280
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1082-1149 |
4.26e-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: 39.89 E-value: 4.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896701 1082 ISVLVSFVSDDGDSETREMTQlSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMI 1149
Cdd:cd03277 107 IELLVKFREGEQLQELDPHHQ-SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDML 173
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1098-1157 |
4.47e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 40.08 E-value: 4.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1098 REMTQLSGGQKSLVALAIIFSiqkcDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQ 1157
Cdd:cd03237 111 REVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1098-1178 |
4.53e-03 |
|
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: 39.90 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1098 REMTQLSGGQKSLVALAIIFSIQK--CDPAPFYLFDEIDAALDAQHR-KSVADMIQSLSDQA--QFVTTTFRPELLATAE 1172
Cdd:cd03240 111 DMRGRCSGGEKVLASLIIRLALAEtfGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKnfQLIVITHDEELVDAAD 190
|
....*.
gi 392896701 1173 KFYGVR 1178
Cdd:cd03240 191 HIYRVE 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1102-1155 |
4.80e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 41.04 E-value: 4.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 392896701 1102 QLSGGQKSLVALAIIFSiqkCDPApFYLFDEIDAALDAQHRKSVADMIQSLSDQ 1155
Cdd:COG1123 142 QLSGGQRQRVAIAMALA---LDPD-LLIADEPTTALDVTTQAEILDLLRELQRE 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1047-1162 |
5.26e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 40.47 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 1047 VFKQ--LVPH-------GRG-KMQMRAREQRDD--EEGINSVELyEGIsvlvsfvsddgdsETREMTQLSGGQKSLVALA 1114
Cdd:PRK11432 83 VFQSyaLFPHmslgenvGYGlKMLGVPKEERKQrvKEALELVDL-AGF-------------EDRYVDQISGGQQQRVALA 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 392896701 1115 IIFSIQkcdpAPFYLFDEIDAALDAQHRKSVADMIQSLsdQAQFVTTT 1162
Cdd:PRK11432 149 RALILK----PKVLLFDEPLSNLDANLRRSMREKIREL--QQQFNITS 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1091-1161 |
5.39e-03 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain] Cd Length: 213 Bit Score: 39.81 E-value: 5.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896701 1091 DDGDSETREMTQLSGGQKSLVALAIIFSIQkcdpAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQ----FVTT 1161
Cdd:cd03259 119 GLEGLLNRYPHELSGGQQQRVALARALARE----PSLLLLDEPLSALDAKLREELREELKELQRELGittiYVTH 189
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-47 |
5.66e-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: 39.97 E-value: 5.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 392896701 3 IKEVRITGFRSYkDNTNVSgFSPRSNVVVGRNGSGKSNFFHAIQF 47
Cdd:cd03242 1 LKSLELRNFRNY-AELELE-FEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
678-893 |
6.19e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 678 RSKLELHTQK-DRFTKELAELQKSLAEaekmvrERTQEAEKIRNRMQQHENQIGDF-------HRKHRELTEAKNAISQQ 749
Cdd:PRK10929 207 RLRSELAKKRsQQLDAYLQALRNQLNS------QRQREAERALESTELLAEQSGDLpksivaqFKINRELSQALNQQAQR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 750 FYMVTSTKEPKKDQLLGIKNHLRELLAQkenfeqeigsnmsSQLTSDEEQTVKKLRKKVD---EMTK--QLAT-VSRRRM 823
Cdd:PRK10929 281 MDLIASQQRQAASQTLQVRQALNTLREQ-------------SQWLGVSNALGEALRAQVArlpEMPKpqQLDTeMAQLRV 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896701 824 DLMHRKNAIENLLTKKLYKTK--ESLTARVDDISDNERRHKLENANAQLTSL------LTRMESTRKQLATAISELQD 893
Cdd:PRK10929 348 QRLRYEDLLNKQPQLRQIRQAdgQPLTAEQNRILDAQLRTQRELLNSLLSGGdtlileLTKLKVANSQLEDALKEVNE 425
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
237-502 |
7.74e-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: 40.48 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 237 IKEKTKL-DEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLEslgrglrEDKETLQAEETKMVEEKMTLKLEIDSLNE 315
Cdd:pfam05483 273 LEEKTKLqDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE-------EDLQIATKTICQLTEEKEAQMEELNKAKA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 316 EN----TRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKL---LEEESRLKTDIRIDESRAKEILA-KQGQRSQFS 387
Cdd:pfam05483 346 AHsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKsseLEEMTKFKNNKEVELEELKKILAeDEKLLDEKK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 388 SVDDRDKFLRNEIRRISGLIadnkereETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAY 467
Cdd:pfam05483 426 QFEKIAEELKGKEQELIFLL-------QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
250 260 270
....*....|....*....|....*....|....*
gi 392896701 468 VAQQTAAREEKAIRDKIGNTEQDISAANDQLRRIV 502
Cdd:pfam05483 499 LENKELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-1034 |
7.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 675 DKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVT 754
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 755 STKE-------------PKKDQLLGIKNHLRELLAQKENFEQEIgSNMSSQLTSDEEQT---------VKKLRKKVDEMT 812
Cdd:PRK03918 273 KEIEeleekvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRL-SRLEEEINGIEERIkeleekeerLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 813 KQLATVSRRRM---DLMHRKNAIENLLTKKLYKTKESLTARVDDISdnERRHKLENANAQLTSLLTRMESTRKQLATAIS 889
Cdd:PRK03918 352 KRLEELEERHElyeEAKAKKEELERLKKRLTGLTPEKLEKELEELE--KAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 890 ELQDYE----------TKEKALQINIDNVLEQQRDL-EKQQADFQLQYDKITAKEDEVKQKREDSLKKMRLLGALPTDTF 958
Cdd:PRK03918 430 ELKKAKgkcpvcgrelTEEHRKELLEEYTAELKRIEkELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 959 SKWQNVKPRELEK------KLLECVNELKKYENVNKKALDQYMTASSQKEELTKRMaeqKKSEDSIEELLKVLENRKYEA 1032
Cdd:PRK03918 510 EKLKKYNLEELEKkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL---DELEEELAELLKELEELGFES 586
|
..
gi 392896701 1033 ID 1034
Cdd:PRK03918 587 VE 588
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
28-50 |
9.36e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 9.36e-03
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
27-424 |
9.77e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 27 SNVVVGRNGSGKSNFFHAIQFVL-SDEYAHLKEEQrlgLLHESTGPKVahaRVEITFDnsekrlmaFENSEVKIVRQVGK 105
Cdd:PHA02562 29 KTLITGKNGAGKSTMLEALTFALfGKPFRDIKKGQ---LINSINKKDL---LVELWFE--------YGEKEYYIKRGIKP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 106 KKDQYYIDNKMVPRA----------EVVNLMESAGFSRsnpyyIVKQGKIN-----ELATspdAYKLKLLREVAGTRVYD 170
Cdd:PHA02562 95 NVFEIYCNGKLLDESasskdfqkyfEQMLGMNYKSFKQ-----IVVLGTAGyvpfmQLSA---PARRKLVEDLLDISVLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 171 ERKeeslKILKE-TKMKTEKIQGL---LKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQ 246
Cdd:PHA02562 167 EMD----KLNKDkIRELNQQIQTLdmkIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 247 KVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLeslgrglredketlqAEETKMVEEKMTLKLEIDSLNEENTRERQGRQN 326
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF---------------QKVIKMYEKGGVCPTCTQQISEGPDRITKIKDK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896701 327 AeHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRidesrakeilakqGQRSQFSSVDDRDKFLRNEIRRISGL 406
Cdd:PHA02562 308 L-KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIS-------------TNKQSLITLVDKAKKVKAAIEELQAE 373
|
410
....*....|....*...
gi 392896701 407 IADNKEREETIQKELADV 424
Cdd:PHA02562 374 FVDNAEELAKLQDELDKI 391
|
|
| |
