|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1172 |
0e+00 |
|
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: 1130.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 2 QLSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFNGTKNRKPQQMAEVS 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 82 LSFNNTKNLLPT-EYSQVTITRRYYRTGDSEYLLNGVTCRLKDINDLFLDTGIGSDSYAIIELKMVDDILNDKDGSRREL 160
Cdd:TIGR02168 81 LVFDNSDGLLPGaDYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 161 FEEAAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSVHSQHEE 240
Cdd:TIGR02168 161 FEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 241 IQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKS 320
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 321 LTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINK 400
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 401 QLEIYAIQLSSLKQELEKTTSDTSAHSANLSefESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLT 480
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 481 QANRKLDSKQNEFNLTKSMVENLEGFPEAIKFLKKNASWGKD-TPLLSDILTCDEKFRLCIENYLESFMNYYVVENEAQA 559
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGiLGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 560 IQAVNLLSDSAKGKANFFVLTRFN------NYTSSQKNTFGDCVSALDIVEYDNKYKGLIQYILDGVYII----TGNQDI 629
Cdd:TIGR02168 559 KKAIAFLKQNELGRVTFLPLDSIKgteiqgNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddldNALELA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 630 IPEDPQSVFITQNGKLAKRKYSISGGSVGlFEGKRIGRAKNMEKLEADIKQITSDIENIRVVLDTKLKEFYLLKENTKKL 709
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLVRPGGVITGGSAK-TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 710 --EVEELRREINLVNNEYITLKTKQEQLASMLSDNSLRREDVLEKIAKIEEDININTPLAKEGKDELESLEERLNQLNDD 787
Cdd:TIGR02168 718 rkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 788 FSLQTTQLSNKSAVYNQENIGFHQQQNRVNSLEQEIGYKQTTFDQSKERIAKNLEELEIANGEIRQMVDSADVSEDELIS 867
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 868 FYKEKESIEQGVHEAEKDYYSTRVRIDEVEKEVKEIRRNREECDEILVTLQNRVTETKIGLSSIKERLNVEFNLNLDDIL 947
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 948 ANQNPDDvlPSEEELKEKVIKIKNSLDRLGPINPMAMEAYQEIKERHVFITTQKEDLAKSKESLMETINEIDTVAKATFL 1027
Cdd:TIGR02168 958 ALENKIE--DDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1028 DAFEKIRDNFIRVFRSLFtDEDSCDLKLVDPENPLDSAIDIMAKPKGKRPLTINQLSGGEKTLTAISLLFAIYLIKPAPF 1107
Cdd:TIGR02168 1036 DTFDQVNENFQRVFPKLF-GGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPF 1114
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110280676 1108 CIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTDIIYGITMVEQGVSRLVPVDL 1172
Cdd:TIGR02168 1115 CILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1178 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 766.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFNGTKNRKPQQMAEV 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 81 SLSFNNTKNLLPTEYSQVTITRRYYRTGDSEYLLNGVTCRLKDINDLFLDTGIGSDSYAIIELKMVDDILNDKDGSRREL 160
Cdd:COG1196 81 SLTFDNSDGTLPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 161 FEEAAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSVHSQHEE 240
Cdd:COG1196 161 IEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 241 IQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKS 320
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 321 LTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINK 400
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 401 QLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLT 480
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 481 QANRKLDSKQNEFNLTKSMVENLEGFPEAIKFLKKNASWGKDTPLLSDILTCDEKFRLCIENYLESFMNYYVVENEAQAI 560
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 561 QAVNLLSDSAKGKANFFVLTrfnnytssqkntfgdcvsaldiveydnkykgliqyildgvyiitgnqdiipedpqsvfit 640
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLD------------------------------------------------------------ 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 641 qngKLAKRKYSISGGSVGLFEGKRIGRAKNMEKLEADIKQITSDIENIRVVLDTKLKEFYLLKENTKKLEVEELRREInl 720
Cdd:COG1196 581 ---KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG-- 655
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 721 vnneyitlktkQEQLASMLSDNSLRREDVLEKIAKIEEDININtpLAKEGKDELESLEERLNQLnddfslqttqlsnksa 800
Cdd:COG1196 656 -----------GSAGGSLTGGSRRELLAALLEAEAELEELAER--LAEEELELEEALLAEEEEE---------------- 706
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 801 vynqenigfhqqqnrvnsleqeigykqttfDQSKERIAKNLEELEIANGEIRQmvdsadvsedelisfykekesieqgvh 880
Cdd:COG1196 707 ------------------------------RELAEAEEERLEEELEEEALEEQ--------------------------- 729
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 881 eaekdyystrvridevEKEVKEIRRNREECDEILvtlqnrvtetkiglssikerlnvefnlnldDILANQNPDDVLPSEE 960
Cdd:COG1196 730 ----------------LEAEREELLEELLEEEEL------------------------------LEEEALEELPEPPDLE 763
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 961 ELKEKVIKIKNSLDRLGPINPMAMEAYQEIKERHVFITTQKEDLAKSKESLMETINEIDTVAKATFLDAFEKIRDNFIRV 1040
Cdd:COG1196 764 ELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQEL 843
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1041 FRSLFtDEDSCDLKLVDPENPLDSAIDIMAKPKGKRPLTINQLSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDA 1120
Cdd:COG1196 844 FPRLF-GGGEAELLLTDPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDA 922
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 1121 NIDKFNNIIRQFAGESQFIIVTHNKRTMASTDIIYGITMVEQGVSRLVPVDLRSLNEA 1178
Cdd:COG1196 923 NVERFAELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEEL 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-1172 |
2.91e-127 |
|
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: 419.47 E-value: 2.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 5 KLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFNGtKNRKPQQMAEVSLSF 84
Cdd:TIGR02169 4 RIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNG-KNGQSGNEAYVTVTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 85 NNTKNLLPTEYsqvTITRRYYRTGD---SEYLLNGVTCRLKDINDLFLDTGIGSDSYAIIELKMVDDILNDKDGSRRELF 161
Cdd:TIGR02169 83 KNDDGKFPDEL---EVVRRLKVTDDgkySYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRKII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 162 EEAAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSVHSQHEEI 241
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 242 QALNKTLDEKTDLRTQYNSQINEKESDVE--RVKLEMVNKE--KLLADRQKTLNEHvnlIRTFESDKKIKNERLRFLNDK 317
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEeiEQLLEELNKKikDLGEEEQLRVKEK---IGELEAEIASLERSIAEKERE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 318 SKSLTDQIELDKQSndraafsLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQ 397
Cdd:TIGR02169 317 LEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 398 INKQL-----EIYAIQ--LSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEK 470
Cdd:TIGR02169 390 YREKLeklkrEINELKreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 471 EIEQIREQLTQANRKLDSKQNEFNLTKSMVENLE----GFPEAIKFLKKNAS--WGkdtpLLSDILTCDEKFRLCIENYL 544
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrGGRAVEEVLKASIQgvHG----TVAQLGSVGERYATAIEVAA 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 545 ESFMNYYVVENEAQAIQAVNLLSDSAKGKANFFVLTRFNNYTS--SQKNTFGDCVSALDIVEYDNKYKGLIQYILDGVYI 622
Cdd:TIGR02169 546 GNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRdlSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLV 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 623 ITGNQDIIPEDPQSVFITQNGKLAKRKYSISGGSVGLFEG---KRIGRAK------NMEKLEADIKQITSDIENIRVVLD 693
Cdd:TIGR02169 626 VEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGilfSRSEPAElqrlreRLEGLKRELSSLQSELRRIENRLD 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 694 TKLKEfylLKENTKKLEveELRREINLVNNEYITLKTKQEQLASMLSDNSLRREDVLEKIAKIEEDININTPLAKEGKDE 773
Cdd:TIGR02169 706 ELSQE---LSDASRKIG--EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 774 LESLEERLN-----QLNDDFSLQTTQLSNKSAVYNQENIGFHQQQNRVNSLEQEIGYKQTTFDQSKERIAKNLEELEIAN 848
Cdd:TIGR02169 781 LNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 849 GEIRQMvdsadvsEDELisfykekESIEQGVHEAEKDYYSTRVRIDEVEKEVKEIRRNREECDEILVTLQNRVTETKIGL 928
Cdd:TIGR02169 861 GKKEEL-------EEEL-------EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 929 SSIKERLNvefnlNLDDILANQNPD-DVLPSEEELKEKVIKIKNSLDRLGPINPMAMEAYQEIKERHVFITTQKEDLAKS 1007
Cdd:TIGR02169 927 EALEEELS-----EIEDPKGEDEEIpEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1008 KESLMETINEIDTVAKATFLDAFEKIRDNFIRVFRSLftDEDSCDLKLVDPENPLDSAIDIMAKPKGKRPLTINQLSGGE 1087
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL--SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGE 1079
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1088 KTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTDIIYGITMVEQGVSRL 1167
Cdd:TIGR02169 1080 KSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQV 1159
|
....*
gi 110280676 1168 VPVDL 1172
Cdd:TIGR02169 1160 FGLKL 1164
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1165 |
9.69e-98 |
|
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: 337.71 E-value: 9.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 3 LSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFngTKNRKPQQMAEVSL 82
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 83 SFNNTKNLLPTEYSQVTITRRYYRTGDSEYLLNGVTCRLKDINDLFLDTGIGSDSYAIIELKMVDDILNDKDGSRRELFE 162
Cdd:pfam02463 80 TFDNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 163 EAAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSVHSQHEEIQ 242
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 243 ALNKTLDEKTDLRTQYNSQINEKESD-VERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSL 321
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEkLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 322 TDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQ 401
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 402 LEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETlqAEDERIQQQVINLEKEIEQIREQLTQ 481
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE--ELEKQELKLLKDELELKKSEDLLKET 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 482 ANRKLDSKQNEFNLTKSMVENLEGFPEAIKFLKKNASWGKDTPLLSDILTCDEKFRLcienylesfmnYYVVENEAQAIQ 561
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL-----------GVAVENYKVAIS 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 562 AVNLLSDSAKGKANFFVLTRFNNYTSSqkNTFGDCVSALDIVEYDNKYKGLIQYILDGVYIITGNQDIIPEDPQSVFITQ 641
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTEL--PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 642 NGKLAKRKYSIsggsvGLFEGKRIGRAKNMEKLEADIKQITSDIENIRVVLDTKLKEFYLLKENTKKLEVEELRREINLV 721
Cdd:pfam02463 625 VEGILKDTELT-----KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 722 NNEYITLKTKQEQLASMLSDNSLRREDVLEKIAKIEEDININTPLAKEGKDELESLEERLNQLNDDFSLQTTQLSNKSAV 801
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 802 YNQENIGFHQQQNRVNSLEQEIGYKQTTFDQSKERIAKNLEELEIANGEIRQMVDSADVSEDELISFYKEKESIE----- 876
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEelerl 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 877 --------QGVHEAEKDYYST--RVRIDEVEKEVKEIRRNREECDEILVTLQNRVTETKIGLSSIKERLNVEFNLNLDDI 946
Cdd:pfam02463 860 eeeitkeeLLQELLLKEEELEeqKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 947 LANQNPDDVLPSE---EELKEKVIKIKNSLDRLGPINPMAMEAYQEIKERHVFITTQKEDLAKSKESLMETINEIDTVAK 1023
Cdd:pfam02463 940 LLLEEADEKEKEEnnkEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1024 ATFLDAFEKIRDNFIRVFRSLFTDeDSCDLKLVDPENPLDSAIDIMAKPKGKRPLTINQLSGGEKTLTAISLLFAIYLIK 1103
Cdd:pfam02463 1020 KEFLELFVSINKGWNKVFFYLELG-GSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYK 1098
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110280676 1104 PAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTDIIYGITMVEQGVS 1165
Cdd:pfam02463 1099 PAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVS 1160
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1073-1166 |
7.01e-51 |
|
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: 178.04 E-value: 7.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1073 KGKRPLTINQLSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTD 1152
Cdd:cd03278 104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
90
....*....|....
gi 110280676 1153 IIYGITMVEQGVSR 1166
Cdd:cd03278 184 RLYGVTMQESGVSK 197
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-98 |
1.58e-48 |
|
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: 171.11 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 3 LSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFNGTKNRKPQQMAEVSL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90
....*....|....*.
gi 110280676 83 SFNNTKNllptEYSQV 98
Cdd:cd03278 81 TFDNSDG----RYSII 92
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1069-1172 |
2.13e-19 |
|
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: 88.78 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1069 MAKPKGKRPLTINQLSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGES-QFIIVTHnKRT 1147
Cdd:cd03275 142 SKNPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNfQFIVISL-KEE 220
|
90 100
....*....|....*....|....*..
gi 110280676 1148 MAS-TDIIYGITM-VEQGVSRLVPVDL 1172
Cdd:cd03275 221 FFSkADALVGVYRdQECNSSKVLTLDL 247
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1080-1166 |
4.89e-19 |
|
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: 85.82 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1080 INQ-LSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNII-RQFAGESQFIIVTHNKRTMASTDIIYGI 1157
Cdd:cd03239 91 VEQiLSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIkEMAKHTSQFIVITLKKEMFENADKLIGV 170
|
....*....
gi 110280676 1158 TMVeQGVSR 1166
Cdd:cd03239 171 LFV-HGVST 178
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1069-1158 |
6.19e-18 |
|
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: 84.62 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1069 MAKPKGKRPLTINQLSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTM 1148
Cdd:cd03272 145 LTNMKQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELL 224
|
90
....*....|
gi 110280676 1149 ASTDIIYGIT 1158
Cdd:cd03272 225 EVADKFYGVK 234
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1078-1165 |
1.26e-17 |
|
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: 81.25 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1078 LTINQLSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNII-RQFAGESQFIIVTHNKRTMASTDIIYG 1156
Cdd:cd03227 73 FTRLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLIH 152
|
....*....
gi 110280676 1157 ITMVEQGVS 1165
Cdd:cd03227 153 IKKVITGVY 161
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-128 |
1.32e-17 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 83.89 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVVI-NFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIF-NGTKNRKPqqmA 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYkRGQAGITK---A 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 110280676 79 EVSLSFNNT-KNLLPTEYS---QVTITRRYYRTGDSEYLLNGVTCRLKDINDLF 128
Cdd:cd03273 78 SVTIVFDNSdKSQSPIGFEnypEITVTRQIVLGGTNKYLINGHRAQQQRVQDLF 131
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-133 |
1.44e-16 |
|
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: 80.69 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 3 LSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEqKTRALRSDKMENVIFNGTKNRKPQQMAEVSL 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGE-KSSHLRSKNLKDLIYRARVGKPDSNSAYVTA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 110280676 83 SFNNTKNLLPTeysqvtiTRRYYRTGDSEYLLNGVTCRLKDINDLFLDTGI 133
Cdd:cd03275 80 VYEDDDGEEKT-------FRRIITGGSSSYRINGKVVSLKEYNEELEKINI 123
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-94 |
2.94e-15 |
|
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: 75.04 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 3 LSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDkmeNVIFNGTKNRKPQQMAEVSL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGS---LLFLAGGGVKAGINSASVEI 77
|
90
....*....|..
gi 110280676 83 SFNNTKNLLPTE 94
Cdd:cd03239 78 TFDKSYFLVLQG 89
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
524-622 |
1.61e-14 |
|
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: 70.75 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 524 PLLSDILTCDEKFRLCIENYLESFMNYYVVENEAQAIQAVNLLSDSAKGKANFFVLTRFN-NYTSSQKNTFGDCVSALDI 602
Cdd:pfam06470 6 GRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKpRPRRPGADLKGGAGPLLDL 85
|
90 100
....*....|....*....|
gi 110280676 603 VEYDNKYKGLIQYILDGVYI 622
Cdd:pfam06470 86 VEYDDEYRKALRYLLGNTLV 105
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-84 |
2.73e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 73.12 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 2 QLSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRalRSDKMENVIFNGTKNrkpqqmAEVS 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGSEE------ASVE 72
|
...
gi 110280676 82 LSF 84
Cdd:COG0419 73 LEF 75
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-130 |
3.81e-14 |
|
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: 72.64 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 3 LSKLEIKGFKSFGDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVL-GEQKTRALRSDKMENVIFNGTKNrkpqqmAEVS 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGEVR------AQVK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 110280676 82 LSF-NNTKNllpteysQVTITRRYyrtgdsEYLLNGVTCRLKDINDLFLD 130
Cdd:cd03240 75 LAFeNANGK-------KYTITRSL------AILENVIFCHQGESNWPLLD 111
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1079-1166 |
1.19e-13 |
|
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: 72.33 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1079 TINQLSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTDIIYGiT 1158
Cdd:cd03273 163 SLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFR-T 241
|
....*...
gi 110280676 1159 MVEQGVSR 1166
Cdd:cd03273 242 RFVDGTST 249
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-59 |
4.46e-13 |
|
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: 71.96 E-value: 4.46e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 110280676 1 MQLSKLEIKGFKSFGDkVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSD 59
Cdd:COG3593 1 MKLEKIKIKNFRSIKD-LSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE 58
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-208 |
7.94e-13 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 68.29 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGFKSFGDkVVINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFNGTKNRKPQQMAEVSLSFN 85
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 86 NTKNLlpteySQVTITRRYYRTGDSEYLLNGVTCRLKDINDL--FLDTGIGSDSYAIielkmvdDILNDKDGSRRELFEE 163
Cdd:pfam13476 80 NNDGR-----YTYAIERSRELSKKKGKTKKKEILEILEIDELqqFISELLKSDKIIL-------PLLVFLGQEREEEFER 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110280676 164 AAGISKFKMRKKQtLKKLEETDKDLERVEDLLfEINKNLKSLEKQ 208
Cdd:pfam13476 148 KEKKERLEELEKA-LEEKEDEKKLLEKLLQLK-EKKKELEELKEE 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-511 |
1.39e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVViNFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFNGTKNRKpqqmAEV 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV-EFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTE----IEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 81 SLSFNNTKnllpteysqVTITRRYYRTGDSEYLLNGVTCRL---KDINDlFLDTGIGSDSY--AI-IELKMVDDILNDkD 154
Cdd:PRK03918 76 KFEKNGRK---------YRIVRSFNRGESYLKYLDGSEVLEegdSSVRE-WVERLIPYHVFlnAIyIRQGEIDAILES-D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 155 GSRRELFEEAAGISKFKMRKKQTLKKLEETDKDLERVEDLLF---EINKNLKSLEKqaKQTEKYHEIKEdyknASIDLAK 231
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEK--ELEEVLREINE----ISSELPE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 232 VSvhSQHEEIQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNE-- 309
Cdd:PRK03918 219 LR--EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyi 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 310 RLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEevgtassaFK 389
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE--------AK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 390 LKQEQVYQINKQLEIYAIQ-----LSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDT-KNAE------------- 450
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEklekeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElKKAKgkcpvcgreltee 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 451 -----LETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLdSKQNEFNLTKSMVENLEGFPEAIK 511
Cdd:PRK03918 449 hrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKELAEQLKELEEKLK 513
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
524-622 |
3.50e-12 |
|
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: 64.56 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 524 PLLSDILTCDEKFRLCIENYLESFMNYYVVENEAQAIQAVNLLSDSAKGKANFFVLTR-------FNNYTSSQKNTFGDC 596
Cdd:smart00968 5 GRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKikprspaGSKLREALLPEPGFV 84
|
90 100
....*....|....*....|....*.
gi 110280676 597 VSALDIVEYDNKYKGLIQYILDGVYI 622
Cdd:smart00968 85 GPAIDLVEYDPELRPALEYLLGNTLV 110
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-86 |
4.87e-12 |
|
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: 66.55 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 3 LSKLEIKGFKSFGDKVVIN-FDEGITGIVGPNGCGKSNVVDAIRWVLGeQKTRALRSDKMENVIFNGtKNRKPQQMAEVS 81
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGpFHKSFSAIVGPNGSGKSNVIDSMLFVFG-FRASKMRQKKLSDLIHNS-AGHPNLDSCSVE 80
|
....*
gi 110280676 82 LSFNN 86
Cdd:cd03274 81 VHFQE 85
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
5-160 |
1.29e-11 |
|
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: 66.13 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 5 KLEIKGFKSFGDKVVI-NFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRaLRSDKMENVIFNGTknrKPQQM-AEVSL 82
Cdd:cd03272 3 QVIIQGFKSYKDQTVIePFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTH-LREEQRQALLHEGS---GPSVMsAYVEI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110280676 83 SFNNTKNLLPTEYSQVTItRRYYRTGDSEYLLNGVTCRLKDINDLFLDTGIG-SDSYAIIELKMVDDILNDKDGSRREL 160
Cdd:cd03272 79 IFDNSDNRFPIDKEEVRL-RRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSrSNPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1066-1142 |
1.73e-11 |
|
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: 65.01 E-value: 1.73e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110280676 1066 IDIMAKPKGKRpltINQLSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVT 1142
Cdd:cd03274 114 IAQMPKKSWKN---ISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVIS 187
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-514 |
2.31e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVvINFDEGITGIVGPNGCGKSNVVDAIRWVLGEQKtralRSDKMENVIFNGTKNrkpqqmAEV 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSE-IEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMIKKGKNN------LEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 81 SLSFNntknllpTEYSQVTITRRYYRTG-----DSEYLLNG--VTCRLKDINDLFLDT--GIGSDSY---AIIELKMVDD 148
Cdd:PRK01156 70 ELEFR-------IGGHVYQIRRSIERRGkgsrrEAYIKKDGsiIAEGFDDTTKYIEKNilGISKDVFlnsIFVGQGEMDS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 149 ILNDKDGSRRELFEEAAGISKFK---MRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKE-DYKN 224
Cdd:PRK01156 143 LISGDPAQRKKILDEILEINSLErnyDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLkEIER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 225 ASIDLAKVSVHSQH--EEIQALNKTLDEKtdlrTQYNSQINEKESDVERVkLEMVNKEKLLADRQKTL------------ 290
Cdd:PRK01156 223 LSIEYNNAMDDYNNlkSALNELSSLEDMK----NRYESEIKTAESDLSME-LEKNNYYKELEERHMKIindpvyknrnyi 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 291 NEHVNLIRTFESDKKI----------KNERLRFLNDKSKSLTDQIELDKQSNDRAAfSLDSLTKEKESAEKIFEEISLKV 360
Cdd:PRK01156 298 NDYFKYKNDIENKKQIlsnidaeinkYHAIIKKLSVLQKDYNDYIKKKSRYDDLNN-QILELEGYEMDYNSYLKSIESLK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 361 EKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKTTS--DTSAHSANLSEFESKAN 438
Cdd:PRK01156 377 KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREnlDELSRNMEMLNGQSVCP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 439 EVKRTLDTKNAE--LETLQAEDERIQQQVINLEKEIEQIREQLTQ--------ANRKLDSKQNEFNLTKSMVENLEGFPE 508
Cdd:PRK01156 457 VCGTTLGEEKSNhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDlkkrkeylESEEINKSINEYNKIESARADLEDIKI 536
|
....*.
gi 110280676 509 AIKFLK 514
Cdd:PRK01156 537 KINELK 542
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-854 |
2.40e-10 |
|
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: 64.99 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVVINF--DEGITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSDKMENVIFngtknRKPQQMA 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFtaLGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLY-----AAPSEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 79 EVSLSFnNTKNLLPTEYSQVTITRRYYRTGDSEYLLNGVTCRLKDIndlfldtgigsdsyAIIELKMVDDILNDKDGSRR 158
Cdd:TIGR00618 76 FAELEF-SLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRI--------------LAAKKSETEEVIHDLLKLDY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 159 ELFEEAAGISKFKM---------RKKQTLKKLEETDKdlerVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDL 229
Cdd:TIGR00618 141 KTFTRVVLLPQGEFaqflkakskEKKELLMNLFPLDQ----YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 230 AKVSVHSQHEEIQALNKTLDEKTDLRTQYNSQINEKESDVERVKL---------EMVNKEKLLADRQKTLN--------- 291
Cdd:TIGR00618 217 YHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLlkqlrarieELRAQEAVLEETQERINrarkaapla 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 292 EHVNLIRTFESDKKIKNERLRF-LNDKSKSLTDQIELDKQSND--RAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYE 368
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSkMRSRAKLLMKRAAHVKQQSSieEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 369 E-------QKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEiyaiqLSSLKQELEKTTSDTSAHSANLSEFESKANEVK 441
Cdd:TIGR00618 377 LtqhihtlQQQKTTLTQKLQSLCKELDILQREQATIDTRTSA-----FRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 442 RTLDTKNAEL-ETLQAEDERIQQqvinlEKEIEQIREQLTQ-----ANRKLDSKQNEFNLTKSMVEnlegfPEAIKFLKK 515
Cdd:TIGR00618 452 QCEKLEKIHLqESAQSLKEREQQ-----LQTKEQIHLQETRkkavvLARLLELQEEPCPLCGSCIH-----PNPARQDID 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 516 NAswGKDTPLLSDILTCDEKFRLCIENylesfmnyyvVENEAQAI--QAVNLLSDSAKGKANFFVLT-RFNNYTSSQKNT 592
Cdd:TIGR00618 522 NP--GPLTRRMQRGEQTYAQLETSEED----------VYHQLTSErkQRASLKEQMQEIQQSFSILTqCDNRSKEDIPNL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 593 FGDCVSALDIVEYDNKYK----GLIQYILDGVYIITGNQDIIPEDPQSVFITQNGKLAKRKY---------SISGGSVGL 659
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEdmlaCEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALqltltqervREHALSIRV 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 660 FEGKRIGRAKNMEK-LEADIKQITSDIENIRVVlDTKLKEfyllkENTKkleVEELRREINLVNNEYITLKTKQEQLASM 738
Cdd:TIGR00618 670 LPKELLASRQLALQkMQSEKEQLTYWKEMLAQC-QTLLRE-----LETH---IEEYDREFNEIENASSSLGSDLAAREDA 740
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 739 L--SDNSLRRE--DVLEKIAKIEEDININTPLAKEGKDELESLEERLNQLNDDFSLQTTQLSNKSAVYNQE--------N 806
Cdd:TIGR00618 741 LnqSLKELMHQarTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdedilN 820
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 110280676 807 IGFHQQQNRVNSLEQEI---GYKQTTFDQSKERIAKNLEELEIANGEIRQM 854
Cdd:TIGR00618 821 LQCETLVQEEEQFLSRLeekSATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-84 |
8.63e-10 |
|
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: 59.98 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVVINF----DEGITGIVGPNGCGKSNVVDAIRWVL-GeqKTRALRSDKMENVIFNGTKNRkpq 75
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALyG--KTPRYGRQENLRSVFAPGEDT--- 75
|
....*....
gi 110280676 76 qmAEVSLSF 84
Cdd:cd03279 76 --AEVSFTF 82
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
151-504 |
1.95e-09 |
|
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: 61.96 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 151 NDKDGSRRELFEEAAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKyhEIKEDYKNASIDLA 230
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS--EISDLNNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 231 KvSVHSQHEEIQalNKTLDEKTDLrTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNER 310
Cdd:TIGR04523 310 K-ELKSELKNQE--KKLEEIQNQI-SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 311 LRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKL 390
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 391 KQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEK 470
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
330 340 350
....*....|....*....|....*....|....*.
gi 110280676 471 EIEQIREQLTQANRK--LDSKQNEFNLTKSMVENLE 504
Cdd:TIGR04523 546 ELNKDDFELKKENLEkeIDEKNKEIEELKQTQKSLK 581
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-49 |
3.71e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 59.24 E-value: 3.71e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 110280676 1 MQLSKLEIKGFKSFGDkVVINFD--EGITGIVGPNGCGKSNVVDAIRWVLG 49
Cdd:COG3950 1 MRIKSLTIENFRGFED-LEIDFDnpPRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-522 |
1.33e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 171 KMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEikEDYKNASIDLAKVSVHSQHEEIQALNKTLDE 250
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 251 KTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNE--HVNLIRTFESDKKIKNERLRFLNDKSKSLTDQIELD 328
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 329 KQSNDRAAFSLDSLTKEKESAEKIF-----------------EEISLKVEKLKQEYEEQKEKNKLLQEEVGTASsafKLK 391
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKkkeaeekkkaeelkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK---KIA 1760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 392 QEQVYQINKQLEIYAIQLSSLKQEL-----------EKTTSDTSAHSANLSEFESKANEVkrtldtKNAELETLQAEDER 460
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELdeedekrrmevDKKIKDIFDNFANIIEGGKEGNLV------INDSKEMEDSAIKE 1834
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110280676 461 I---QQQVINLEKEIEQIREQLTQANRKLDSKQNEFNLTKsmvENLEGFPEAIKFLKKNASWGKD 522
Cdd:PTZ00121 1835 VadsKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK---DLKEDDEEEIEEADEIEKIDKD 1896
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-90 |
1.44e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 2 QLSKLEIKGFKSFGDkVVINFDeGITGIVGPNGCGKSNVVDAIRWvLGE------QKTRALRSDkMENVIFNGTKNRKPQ 75
Cdd:COG4637 1 MITRIRIKNFKSLRD-LELPLG-PLTVLIGANGSGKSNLLDALRF-LSDaargglQDALARRGG-LEELLWRGPRTITEP 76
|
90
....*....|....*
gi 110280676 76 QMAEVSLSFNNTKNL 90
Cdd:COG4637 77 IRLELEFAEEDERDL 91
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-59 |
2.18e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 54.67 E-value: 2.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 5 KLEIKGFKSFGDKVVINFDEG-ITGIVGPNGCGKSNVVDAIRWVLGEQKTRALRSD 59
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
178-492 |
2.97e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 178 LKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSVHSQHEEIQALNKTLDEKTDLRTQ 257
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 258 YNSQINEKESDVERVKLEMVNKEKL-----LADRQKTLNEHVNLIRTFESD-KKIKNERLRFLNDKSKSLTDQIELDKQ- 330
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVl 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 331 SNDRAAFSLDSLTKEKESAEKIFEEISL-KVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQE---QVYQINKQLEIYA 406
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 407 IQLSSLKQEL-EKTTSDTSAHSANLSEFESKANE------VKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQL 479
Cdd:PRK03918 570 EELAELLKELeELGFESVEELEERLKELEPFYNEylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
330
....*....|...
gi 110280676 480 TQANRKLDSKQNE 492
Cdd:PRK03918 650 EELEKKYSEEEYE 662
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
339-1171 |
3.11e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 339 LDSL-TKEKESAEKIFEEIsLKVEKLKQEYEEQKEKNKLLQEEVGT---ASSAFKLKQEQVYQINKQLEIYAIQLSSLKQ 414
Cdd:PRK01156 140 MDSLiSGDPAQRKKILDEI-LEINSLERNYDKLKDVIDMLRAEISNidyLEEKLKSSNLELENIKKQIADDEKSHSITLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 415 ELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFN 494
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 495 LTKSMVENLEGFPEAIKFLKknaswgkdtpllSDILTCDEKFRLCIEnyLESFMNYYvvENEAQAIQAVNLLSDSAKGKA 574
Cdd:PRK01156 299 DYFKYKNDIENKKQILSNID------------AEINKYHAIIKKLSV--LQKDYNDY--IKKKSRYDDLNNQILELEGYE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 575 NFFVlTRFNNYTSSQKNtfgdcvsaldIVEYDNKYKGLIQYILDgvyiITGNQDIIPEDPQSVFITQNGKLAKRKYSISG 654
Cdd:PRK01156 363 MDYN-SYLKSIESLKKK----------IEEYSKNIERMSAFISE----ILKIQEIDPDAIKKELNEINVKLQDISSKVSS 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 655 --GSVGLFEGKRIGRAKNMEKLEADIK----QITSDIENIRvvldtKLKEFYLLKENTKKLEVEELRREINLVNNEYITL 728
Cdd:PRK01156 428 lnQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSN-----HIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDL 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 729 KTKQEQLASMLSDNSLRREDVLEKIAKIEEDININTPLAKEGKDELESLEERLNQLN-DDFSLQTTQLSNKSAVynQENI 807
Cdd:PRK01156 503 KKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNALAV--ISLI 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 808 GFHQQQNRVNSLEQEIgykqttfdqskERIAKNLEELEIANGEIRQMVDSADVSEDELISFYKEKEsieqgvheaeKDYY 887
Cdd:PRK01156 581 DIETNRSRSNEIKKQL-----------NDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKY----------NEIQ 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 888 STRVRIDEVEKEVKEIRRNREECDEIlvtlQNRVTETKIGLSSIKERLNvEFNLNLDDILANQnpddvlpSEEELKEKVI 967
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLK-KSRKALDDAKANR-------ARLESTIEIL 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 968 KIKNSldrlgpinpmameayqEIKERhvfITTQKEDLaKSKESLMETINEIDTVAKATFLDAFEK-IRDNFIRVFRSLFT 1046
Cdd:PRK01156 708 RTRIN----------------ELSDR---INDINETL-ESMKKIKKAIGDLKRLREAFDKSGVPAmIRKSASQAMTSLTR 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1047 DE-DSCDLKLVDPENPLDSAIDIMakpKGKRPLTINQLSGGEKTLTAISLLFAI--YLIKPAPFCIFDEVDAPLDDANID 1123
Cdd:PRK01156 768 KYlFEFNLDFDDIDVDQDFNITVS---RGGMVEGIDSLSGGEKTAVAFALRVAVaqFLNNDKSLLIMDEPTAFLDEDRRT 844
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 110280676 1124 KFNNII----RQFAGESQFIIVTHNKRTMASTDIIYGITMVeQGVSRLVPVD 1171
Cdd:PRK01156 845 NLKDIIeyslKDSSDIPQVIMISHHRELLSVADVAYEVKKS-SGSSKVIPLR 895
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-497 |
4.43e-08 |
|
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: 57.75 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 2 QLSKLEIKGFKSFG----DKVVINFDEGITGIVGPNGCGKSNVVDAIRWVLgeqkTRALRSDKMENVIFNGTK-NRKPQQ 76
Cdd:TIGR00606 2 KFLKMSILGVRSFGiedkDKQIIDFFSPLTILVGPNGAGKTTIIECLKYIC----TGDFPPGTKGNTFVHDPKvAQETDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 77 MAEVSLSFNNTKNLLPTEYSQVTITRRYYRTGDSEylLNGVTCRLKDINDLFLDTGIGSDSYAIIE-LKMVDDILND--- 152
Cdd:TIGR00606 78 RAQIRLQFRDVNGEECAVVRSMVCTQKTKKTEFKT--LEGVITRYKHGEKVSLSSKCAEIDREMIShLGVSKAVLNNvif 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 153 -----------KDGSRRELFEEAAGISKF-----KMRK-----KQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQ 211
Cdd:TIGR00606 156 chqedsnwplsEGKALKQKFDEIFSATRYikaleTLRQvrqtqGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLES 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 212 TEKYHEIKEDY------KNASIDLAKVSVHSQHEEIQALNKTLDEKTDLRTQY-----------NSQINEKESDVERvkl 274
Cdd:TIGR00606 236 SREIVKSYENEldplknRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELelkmekvfqgtDEQLNDLYHNHQR--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 275 EMVNKEKLLADRQKTL---NEHVNLIRTFESDKKIKNERLRFLNDKSKSLTDQIELDKQSNdRAAFSLDSLTKEKESAEK 351
Cdd:TIGR00606 313 TVREKERELVDCQRELeklNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSL-ATRLELDGFERGPFSERQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 352 IFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLS 431
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110280676 432 EFESKANEVKRTLD-----TKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFNLTK 497
Cdd:TIGR00606 472 RILELDQELRKAERelskaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
259-504 |
5.65e-08 |
|
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: 57.34 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 259 NSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKI--------------KNERLRFLNDKSKSLTDQ 324
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIleqqikdlndklkkNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 325 IELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKL-------KQEQVYQ 397
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLlekeklnIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 398 INKQLEIYAIQLSSLKQELEKTTSDTSahsaNLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIRE 477
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLES----QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270
....*....|....*....|....*....|....
gi 110280676 478 QL-------TQANRKLDSKQNEFNLTKSMVENLE 504
Cdd:TIGR04523 268 QLsekqkelEQNNKKIKELEKQLNQLKSEISDLN 301
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-491 |
7.37e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDkVVINFDEGITGIVGPNGCGKSNVVDAIRWVLgeQKTRALrSDKMENVIFNGTKNrkpqqmAEV 80
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADLRLEDGVTVIHGVNGSGKSSLLEACFFAL--YGSKAL-DDTLDDVITIGAEE------AEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 81 SLSF--------------------NNTKNLLPT---EYSQVTITRRYYRT---GDSEYLLNGVTCRLKDINDLFLDTGig 134
Cdd:PRK02224 71 ELWFehaggeyhierrvrlsgdraTTAKCVLETpegTIDGARDVREEVTEllrMDAEAFVNCAYVRQGEVNKLINATP-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 135 SDSYAiielkMVDDILNDkdgSRRELFEEAAGISKFKMRKKQTLKK--LEETDKDLERVEDLlfEINKNLKSLEKQAKQT 212
Cdd:PRK02224 149 SDRQD-----MIDDLLQL---GKLEEYRERASDARLGVERVLSDQRgsLDQLKAQIEEKEEK--DLHERLNGLESELAEL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 213 ----EKYHEiKEDYKNASIDLAKvSVHSQHEEIQALNKTLDEK-TDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQ 287
Cdd:PRK02224 219 deeiERYEE-QREQARETRDEAD-EVLEEHEERREELETLEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 288 KTLNEhvnliRTFES-DKKIKNERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKE----KESAEKIFE---EISLK 359
Cdd:PRK02224 297 DLLAE-----AGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddlEERAEELREeaaELESE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 360 VEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANE 439
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 440 VK--------------RTLDTKNAELETLQAEDERIQQQVINLEKEIEQIrEQLTQANRKLDSKQN 491
Cdd:PRK02224 452 GKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEE 516
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-128 |
9.34e-08 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 55.55 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 3 LSKLEIKGFKSFgDKVVINFDEGITGIVGPNGCGKSNVVDAIrWVLGeqKTRALRSDKMENVIfngtknRKPQQMAEVSL 82
Cdd:COG1195 2 LKRLSLTNFRNY-ESLELEFSPGINVLVGPNGQGKTNLLEAI-YLLA--TGRSFRTARDAELI------RFGADGFRVRA 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 110280676 83 SFNNtknllptEYSQVTITRRYYRTGDSEYLLNGVTC-RLKDINDLF 128
Cdd:COG1195 72 EVER-------DGREVRLGLGLSRGGKKRVRINGKPVrRLSDLAGLL 111
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1075-1144 |
1.69e-07 |
|
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: 51.86 E-value: 1.69e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110280676 1075 KRPLTINQLSGGEKTLTAISLLfaiyLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGE-SQFIIVTHN 1144
Cdd:cd00267 73 RRIGYVPQLSGGQRQRVALARA----LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHD 139
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
338-504 |
2.04e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 338 SLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQvyqINKQLEIYAIQLSSLKQElE 417
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELGERARALYRS-G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 418 KTTSDTSA--HSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFNL 495
Cdd:COG3883 100 GSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
....*....
gi 110280676 496 TKSMVENLE 504
Cdd:COG3883 180 QEALLAQLS 188
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
178-492 |
2.37e-07 |
|
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: 55.11 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 178 LKKLEETDKDLERVEDLLFEINKNLKSLEKQAK-QTEKYHEIKEDYKNASIDLAKVSVHSQHEeiQALNKTLDEKTDLRT 256
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKlQDENLKELIEKKDHLTKELEDIKMSLQRS--MSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 257 QYNSQINEKEsdveRVKLEMVNKEKllADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTdqIELDKQSNDraa 336
Cdd:pfam05483 324 KTICQLTEEK----EAQMEELNKAK--AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIIT--MELQKKSSE--- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 337 fsLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQE----------QVYQINKQLEIYA 406
Cdd:pfam05483 393 --LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihdleiQLTAIKTSEEHYL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 407 IQLSSLKQELEK---TTSDTSAHSANLS----EFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQL 479
Cdd:pfam05483 471 KEVEDLKTELEKeklKNIELTAHCDKLLlenkELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
330
....*....|...
gi 110280676 480 TQANRKLDSKQNE 492
Cdd:pfam05483 551 ESVREEFIQKGDE 563
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
174-492 |
2.73e-07 |
|
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: 55.12 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 174 KKQTLKKLEETDKDL-------ER-VEDLLFEINK-----NLKSLEKQAKQTEKYHEikeDYKNASIDLAKVSVHSQHEE 240
Cdd:pfam15921 487 KKMTLESSERTVSDLtaslqekERaIEATNAEITKlrsrvDLKLQELQHLKNEGDHL---RNVQTECEALKLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 241 IQALNKTLDEKTDLRTQYNSQINEKEsdVERVKLEM-VNKEKLLADRQKTLNEHVNL-IRTFE---SD---KKIK----- 307
Cdd:pfam15921 564 IEILRQQIENMTQLVGQHGRTAGAMQ--VEKAQLEKeINDRRLELQEFKILKDKKDAkIRELEarvSDlelEKVKlvnag 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 308 NERLRFLNDkSKSLTDQIeLDKQSNDRAafSLDSLTKEKESAEKIF----EEISLKVEKLKQEYE----EQKEKNKLLQE 379
Cdd:pfam15921 642 SERLRAVKD-IKQERDQL-LNEVKTSRN--ELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKsaqsELEQTRNTLKS 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 380 EVGTASSAFKLKQEQVYQIN-KQLEIYAIQlsSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKN----AELETL 454
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITaKRGQIDALQ--SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKnkmaGELEVL 795
|
330 340 350
....*....|....*....|....*....|....*...
gi 110280676 455 QAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNE 492
Cdd:pfam15921 796 RSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
178-479 |
8.51e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 178 LKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKeDYKNASIdlakvsVHSQHEEIQALNKTLDEKtdlrtq 257
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEF-SLKAEVL------IQKFGRSLKAKKRFSLLK------ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 258 ynsqineKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKiknERLRFLNDKSKSLTDQIEldkqsndraaF 337
Cdd:COG5022 866 -------KETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELES---EIIELKKSLSSDLIENLE----------F 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 338 SLDSLTKEKesaeKIFEEISLKVEKLKqEYEEQKEKNKLLQEEvgtasSAFKLKQEQVYQINKQLEIYAIQLSSLKQELE 417
Cdd:COG5022 926 KTELIARLK----KLLNNIDLEEGPSI-EYVKLPELNKLHEVE-----SKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110280676 418 KTTSDTSAHSANLSEFESKANEVKRtLDTKNAELETLQAEDE----------RIQQQVINLEKEIEQIREQL 479
Cdd:COG5022 996 NFKKELAELSKQYGALQESTKQLKE-LPVEVAELQSASKIISsestelsilkPLQKLKGLLLLENNQLQARY 1066
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-503 |
8.93e-07 |
|
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: 53.58 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 161 FEEAAGISKFKMRKKQTL----------KKLEETDKDLERVEDLLFEINKNLKSLEKQAKQT------EKYHEIKEDYKN 224
Cdd:pfam15921 196 FEEASGKKIYEHDSMSTMhfrslgsaisKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqQHQDRIEQLISE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 225 ASIDLAKV-----SVHSQHEEIQALNKTLDEKT-DLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIR 298
Cdd:pfam15921 276 HEVEITGLtekasSARSQANSIQSQLEIIQEQArNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 299 TFESDKKikNERLRFlNDKSKSLTDQIE-----LDKQSNDraafsldsLTKEKESAEKIFEEI---SLKVEKLKQEYEEQ 370
Cdd:pfam15921 356 SELTEAR--TERDQF-SQESGNLDDQLQklladLHKREKE--------LSLEKEQNKRLWDRDtgnSITIDHLRRELDDR 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 371 KEKNKLLQEEVGTASSAFKLKQEQ----VYQINKQLEIYA---IQLSSLKQELEKTTSDTSAHSANL-------SEFESK 436
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSsltAQLESTKEMLRKVVEELTAKKMTLessertvSDLTAS 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 437 ANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANR---KLDSKQNEFNLTKSMVENL 503
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENM 574
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
278-492 |
1.35e-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: 52.07 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 278 NKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTDQI-ELDKQsndraafsLDSLTKEKESAEKIFEEI 356
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIrALEQE--------LAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 357 SLKVEKLKQEYEEQkekNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESK 436
Cdd:COG4942 96 RAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 437 ANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNE 492
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-483 |
3.02e-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: 50.92 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 229 LAKVSVHSQHEEIQALNKTLDektdlrtQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKN 308
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 309 ERLRFLNDKSKSLtdQIELDKQSND-----RAAFSLDSLTKEKE--SAEKiFEEISLKVEKLKQEYEEQKEKNKLLQEEv 381
Cdd:COG4942 83 AELAELEKEIAEL--RAELEAQKEElaellRALYRLGRQPPLALllSPED-FLDAVRRLQYLKYLAPARREQAEELRAD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 382 gtassafklkQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAhsaNLSEFESKANEVKRTLDTKNAELETLQAEDERI 461
Cdd:COG4942 159 ----------LAELAALRAELEAERAELEALLAELEEERAALEA---LKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260
....*....|....*....|..
gi 110280676 462 QQQVINLEKEIEQIREQLTQAN 483
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAAG 247
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-73 |
4.80e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 50.04 E-value: 4.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110280676 3 LSKLEIKGFKSFGDKVVINFDEG------ITGIVGPNGCGKSNVVDAIRWVlgeqKTRALRSDKMENVIFNGTKNRK 73
Cdd:COG1106 2 LISFSIENFRSFKDELTLSMVASglrllrVNLIYGANASGKSNLLEALYFL----RNLVLNSSQPGDKLVEPFLLDS 74
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
169-421 |
5.23e-06 |
|
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: 50.88 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 169 KFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKnasidlakvsvhsqhEEIQALNKTL 248
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI---------------EELHQENKAL 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 249 DEKTdlrTQYNSQINEKESDVERVKLEmvnkeklLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTD----- 323
Cdd:pfam05483 621 KKKG---SAENKQLNAYEIKVNKLELE-------LASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADeavkl 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 324 QIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTassafkLKQEQVyQINKQLE 403
Cdd:pfam05483 691 QKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSN------IKAELL-SLKKQLE 763
|
250
....*....|....*...
gi 110280676 404 IYAIQLSSLKQELEKTTS 421
Cdd:pfam05483 764 IEKEEKEKLKMEAKENTA 781
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-492 |
6.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 344 KEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQ--EQVYQINKQLEIYAIQLSSLKQELEKTTS 421
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110280676 422 ---DTSAHSANLSEFESKANEVKRTLDTKN-AELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNE 492
Cdd:COG4717 161 leeELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1077-1166 |
6.02e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.37 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1077 PLTINQLSGGEKTLTAISLLFAIY--LIKPAPFCIFDEVDAPLDDANID-KFNNIIRQFAGES--QFIIVTHNKRTMAST 1151
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAetFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKnfQLIVITHDEELVDAA 189
|
90
....*....|....*
gi 110280676 1152 DIIYGITMVEQGVSR 1166
Cdd:cd03240 190 DHIYRVEKDGRQKSR 204
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-504 |
6.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVvINFDEGITGIVGPNGCGKSNVVDAIRWVLGEqktralRSDKMENVIFNGTKnRKPQqmaev 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRT-IEFSPGLNVIYGPNEAGKSTLLAFIRAMLLE------RLEKEADELFKPQG-RKPE----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 81 slsfnntknLLPTEYSQVTITRRYYRTGDSEYllNGVTCRLKDINDlfldtgigsdsyaiiELKMVDDILNDKDGSRREL 160
Cdd:COG4717 68 ---------LNLKELKELEEELKEAEEKEEEY--AELQEELEELEE---------------ELEELEAELEELREELEKL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 161 fEEAAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSVHSQHEE 240
Cdd:COG4717 122 -EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 241 IQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMVNKEKL---------------------LADRQKTLNEHVN---- 295
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallallgLGGSLLSLILTIAgvlf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 296 ---------LIRTFESDKKIKNERLRFLNDKSKSLTDQIELDKQSNDR---AAFSLDSLTKEKESAEKIFEEISlKVEKL 363
Cdd:COG4717 281 lvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 364 KQEYEEQ---KEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEiyaiQLSSLKQELEKTTSDTSAHSA--NLSEFESKAN 438
Cdd:COG4717 360 EEELQLEeleQEIAALLAEAGVEDEEELRAALEQAEEYQELKE----ELEELEEQLEELLGELEELLEalDEEELEEELE 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 439 EVKRTLDTKNAELETLQAEDERIQQQVINLEK--EIEQIREQLTQANRKLDSKQNEFNLTKSMVENLE 504
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-504 |
7.18e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 142 ELKMVDDILNDKDGSRRELFEE----AAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKyhE 217
Cdd:TIGR04523 55 ELKNLDKNLNKDEEKINNSNNKikilEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEK--Q 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 218 IKEDYKNasidlakvsvhsqheeiqaLNKTLDEKTDLRTQYNSqINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLI 297
Cdd:TIGR04523 133 KKENKKN-------------------IDKFLTEIKKKEKELEK-LNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 298 RTFESDKKIKNERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLL 377
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 378 QEEVGTASSAFKLKQEQVYQINKQLEIYAIQ------------LSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLD 445
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwnkelkseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 110280676 446 TKNAELETLQAEDERIQQQVINLEKEIEQIREQLTqanrKLDSKQNEFNLTKSMVENLE 504
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK----NLESQINDLESKIQNQEKLN 407
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
157-482 |
7.67e-06 |
|
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: 50.11 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 157 RRELFEEAAGISKFKMRKKQTlkKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVsVHS 236
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSS--ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL-LQA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 237 QHEEIQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMV----NKEKLLADRQKTLNEHVNLIRtfesdkKIKNERLR 312
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltaHCDKLLLENKELTQEASDMTL------ELKKHQED 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 313 FLNDKSKS--LTDQIELDKQSNdraafsldslTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKL 390
Cdd:pfam05483 522 IINCKKQEerMLKQIENLEEKE----------MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 391 KQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETL------QAEDERIQQQ 464
Cdd:pfam05483 592 LENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyqkEIEDKKISEE 671
|
330
....*....|....*...
gi 110280676 465 viNLEKEIEQIREQLTQA 482
Cdd:pfam05483 672 --KLLEEVEKAKAIADEA 687
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
173-415 |
8.98e-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: 49.38 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 173 RKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKyheikedyknasidlakvsvhsqheEIQALNKTLDEkt 252
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-------------------------RIAALARRIRA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 253 dlrtqYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIrtfesDKKIKNERLRFL---NDKSKSLTDQIELDK 329
Cdd:COG4942 74 -----LEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL-----YRLGRQPPLALLlspEDFLDAVRRLQYLKY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 330 QSNDRAAfSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVgtassafKLKQEQVYQINKQLEIYAIQL 409
Cdd:COG4942 144 LAPARRE-QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-------AERQKLLARLEKELAELAAEL 215
|
....*.
gi 110280676 410 SSLKQE 415
Cdd:COG4942 216 AELQQE 221
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
421-494 |
9.60e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 9.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110280676 421 SDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFN 494
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1028-1177 |
1.03e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 49.16 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1028 DAFEKIRDN------FIRVFRSLFTDEDSCDLKLVDPENpldsaidimakpkgKRPLTINQLSGGekTLTAISLLFAIYL 1101
Cdd:COG4637 212 ERFERILEAlrdafpGFEDIEVEPDEDGRVLLEFREKGL--------------DRPFPARELSDG--TLRFLALLAALLS 275
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 1102 IKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTDI--IYGITMVEQGVSRLVPVDLRSLNE 1177
Cdd:COG4637 276 PRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDALEPeeVLVLEREDDGETRIRRLSDLELPE 353
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-68 |
1.05e-05 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 49.00 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 1 MQLSKLEIKGFKSFgDKVVINFDEGITGIVGPNGCGKSNVVDAIrWVLGeqKTRALRSDKMENVIFNG 68
Cdd:PRK00064 1 MYLTRLSLTDFRNY-EELDLELSPGVNVLVGENGQGKTNLLEAI-YLLA--PGRSHRTARDKELIRFG 64
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
174-478 |
1.12e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 49.63 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 174 KKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAK-QTEKYHE--IKEDYKNASIDLAKVSVHSQHEEIQALNKTLDE 250
Cdd:NF033838 120 KKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKdQKEEDRRnyPTNTYKTLELEIAESDVEVKKAELELVKEEAKE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 251 KTDLRTqynsqINEKESDVERVKLEMVNKEKLLADRQKTlNEHVNLIRTFESDKKIKNERLRFLNDKSKS------LTDQ 324
Cdd:NF033838 200 PRDEEK-----IKQAKAKVESKKAEATRLEKIKTDREKA-EEEAKRRADAKLKEAVEKNVATSEQDKPKRrakrgvLGEP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 325 IELDKQSNDraAFSLDSLTKEKE------SAEKIFEEISLKVEKLKQEYEEQKEKNKllqeevgtassafklkqeQVYQI 398
Cdd:NF033838 274 ATPDKKEND--AKSSDSSVGEETlpspslKPEKKVAEAEKKVEEAKKKAKDQKEEDR------------------RNYPT 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 399 N--KQLEiyaIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAE---LETLQAEDERIQQQVINLEKEIE 473
Cdd:NF033838 334 NtyKTLE---LEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEatrLEKIKTDRKKAEEEAKRKAAEED 410
|
....*
gi 110280676 474 QIREQ 478
Cdd:NF033838 411 KVKEK 415
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
326-487 |
1.21e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 326 ELDKQSnDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQI--NKQLE 403
Cdd:COG1579 14 ELDSEL-DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 404 IYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEderIQQQVINLEKEIEQIREQLTQAN 483
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
|
....
gi 110280676 484 RKLD 487
Cdd:COG1579 170 AKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
354-1177 |
1.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 354 EEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQL-EIYAIQLSSLKQELEKTTSDTSAHSANLSE 432
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 433 FESKANEVKRTLDTKNAELETLQAE----DERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFNLTKSMVENLEGFPE 508
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 509 AI-KFLKKNASWgKDTPL-----LSDILTCDEKFRLCIENYLESFMNYYVV--ENEAQAIQAVNLLSDsaKGKANFFvlt 580
Cdd:COG4913 444 ALrDALAEALGL-DEAELpfvgeLIEVRPEEERWRGAIERVLGGFALTLLVppEHYAAALRWVNRLHL--RGRLVYE--- 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 581 RFNNYTSSQKNTFGDCVSALDIVEY-DNKYKGLIQYILDGVYiitgnqDII----PED----PQSvfITQNGkLAKRKYS 651
Cdd:COG4913 518 RVRTGLPDPERPRLDPDSLAGKLDFkPHPFRAWLEAELGRRF------DYVcvdsPEElrrhPRA--ITRAG-QVKGNGT 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 652 IsggsvglfegkrigRAKNmekleaDIKQITSDienirvvldtklkeFYLLKENTKKL-----EVEELRREINLVNNEYI 726
Cdd:COG4913 589 R--------------HEKD------DRRRIRSR--------------YVLGFDNRAKLaaleaELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 727 TLKTKQEQLAsmlsdnslRREDVLEKIAKIEEDInINTPLAKEgkdELESLEERLNQL---NDDFSLQTTQLSnksavyn 803
Cdd:COG4913 635 ALEAELDALQ--------ERREALQRLAEYSWDE-IDVASAER---EIAELEAELERLdasSDDLAALEEQLE------- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 804 qenigfhQQQNRVNSLEQEIGYKQTTFDQSKERIAKNLEELEIANGEIRQMVDSADVSEDELISFYKEKESIEQGVHEAE 883
Cdd:COG4913 696 -------ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 884 KDYYstrvriDEVEKEVKEIRRNREECDEILVTLQNR----VTETKIGLSSIKERLNVEFNLNLDDI----------LAN 949
Cdd:COG4913 769 ENLE------ERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLPEYLALLDRLEEDGLpeyeerfkelLNE 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 950 QNPDDVLPSEEELKEKVIKIKnslDRLGPINpmamEAYQEIK---ERHVFIT---TQKEDLAKSKESLMETINEIDTvAK 1023
Cdd:COG4913 843 NSIEFVADLLSKLRRAIREIK---ERIDPLN----DSLKRIPfgpGRYLRLEarpRPDPEVREFRQELRAVTSGASL-FD 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1024 ATFLDAFEKIRDNFIRVFRSlftDEDSCDL----KLVDPENPLDSAIDIMAKPKGKRPLT---INQLSGGEK-TLTAISL 1095
Cdd:COG4913 915 EELSEARFAALKRLIERLRS---EEEESDRrwraRVLDVRNHLEFDAEEIDREDGEEVETyssSGGKSGGEKqKLAYFIL 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1096 LFAI-YLikpapFCIFDEVD---AP--LDDAnidkFNNIIRQFAGES---------QFIIVTHNKRTMASTDIIYGITMV 1160
Cdd:COG4913 992 AAALaYQ-----LGLEGRGRpsfRTvvLDEA----FSKMDEEFARRAlrlfkelglQLLIATPLDKIQAIEPYVGSVLVV 1062
|
890 900
....*....|....*....|
gi 110280676 1161 ---EQGVSRLVPVDLRSLNE 1177
Cdd:COG4913 1063 hkdDGRRSRVRELTIEELRE 1082
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
179-504 |
2.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 179 KKLEETDKDLERVEDLLFEINKNLKSLEKQaKQTEKYHEIKEDYKN---------ASIDLAKVSVHSQHEEIQALNKTLD 249
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQ-KEQDWNKELKSELKNqekkleeiqNQISQNNKIISQLNEQISQLKKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 250 EKTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTDQIELDK 329
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 330 QSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQ-------EYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQL 402
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 403 EIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTL---------DTKNAELETLQAE-----------DERIQ 462
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTqkslkkkqeekQELID 592
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110280676 463 Q---QVINLEKEIEQIREQLTQANRKLDSKQNEFNLTKSMVENLE 504
Cdd:TIGR04523 593 QkekEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
304-516 |
2.79e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 304 KKIKNERLRFLNDKSKSLTdQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGT 383
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGI-LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 384 ASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQ 463
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110280676 464 QVINLEKEIEQIREQltQANRKLDSKQNEFNLTKSMVENLEGFPEAIKFLKKN 516
Cdd:COG4372 165 ELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
159-510 |
4.22e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 159 ELFEEAAGISKFKMRKKQTLKKLEETDKDLervEDLLFEINKNLKSLEKQAKQTEKYHEIkedyknasidlAKVSVHSQH 238
Cdd:TIGR00606 671 QLTDENQSCCPVCQRVFQTEAELQEFISDL---QSKLRLAPDKLKSTESELKKKEKRRDE-----------MLGLAPGRQ 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 239 EEIQALNKTLDEKTDLRTQYNSQINEKESDVER--VKLEMVNKEKLLAdrqKTLNEHVNLIRTFESDKKIKNERLRFLND 316
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqeTLLGTIMPEEESA---KVCLTDVTIMERFQMELKDVERKIAQQAA 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 317 KSKSltdqIELDKqsndraafSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQE---EVGTASSAFKLKQE 393
Cdd:TIGR00606 814 KLQG----SDLDR--------TVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQ 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 394 QVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVkrtLDTKNAELETLQAEDERIQQQVINLEKEIE 473
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNIHGYMK 958
|
330 340 350
....*....|....*....|....*....|....*...
gi 110280676 474 QIREQLTQA-NRKLDSKQNEFNLTKSMVENLEGFPEAI 510
Cdd:TIGR00606 959 DIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKI 996
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
239-490 |
4.40e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 239 EEIQALNKTLDEKTDLRTQYNSQI----NEKESDVERVKlEMVNKEKLLADRQKTLNEHVnlirtfesdKKIKNERLRfL 314
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELkelaEKRDELNAQVK-ELREEAQELREKRDELNEKV---------KELKEERDE-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 315 NDKSKSLTDQIELDKQSND---RAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEevgtASSAFKLK 391
Cdd:COG1340 84 NEKLNELREELDELRKELAelnKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEK----AKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 392 qEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKE 471
Cdd:COG1340 160 -EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|....*....
gi 110280676 472 IEQIREQLTQANRKLDSKQ 490
Cdd:COG1340 239 LRELRKELKKLRKKQRALK 257
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
174-482 |
4.40e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 174 KKQTLKKLEETDKDLERVEDLLFEINKNLKSLE-----------KQAKQTEKYHE-----------------IKEDYKNA 225
Cdd:TIGR00606 572 KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEqnknhinneleSKEEQLSSYEDklfdvcgsqdeesdlerLKEEIEKS 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 226 SIDLA----KVSVHSQH-EEIQALNKTLDEKTDLRTQYNSQINEKESDVERVKL----EMVNKEKLLADRQKTLNEHVNL 296
Cdd:TIGR00606 652 SKQRAmlagATAVYSQFiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 297 IRTFESDKKIKNERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLkvekLKQEYEEQKEKNKL 376
Cdd:TIGR00606 732 APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI----MERFQMELKDVERK 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 377 LQEEVGTASSAFKLKQEQvyQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKrtldTKNAELETLQA 456
Cdd:TIGR00606 808 IAQQAAKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK----SEKLQIGTNLQ 881
|
330 340
....*....|....*....|....*.
gi 110280676 457 EDERIQQQVINLEKEIEQIREQLTQA 482
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQSLIREIKDA 907
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-492 |
6.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 171 KMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSvhsqHEEIQALNKTLDE 250
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA----EEKAEAAEKKKEE 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 251 KtdlrtqynsqinEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNErlrfLNDKSKSLTDQIELDKQ 330
Cdd:PTZ00121 1376 A------------KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE----AKKKAEEKKKADEAKKK 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 331 SND-RAAFSLDSLTKEKESAEKIFE--EISLKVEKLKQEYEEQK---EKNKLLQEEVGTASSAFKLKQEQvyqiNKQLEI 404
Cdd:PTZ00121 1440 AEEaKKADEAKKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKkadEAKKKAEEAKKKADEAKKAAEAK----KKADEA 1515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 405 YAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAElETLQAEDERIQQQVINLEKEIEQIREQLTQANR 484
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
....*...
gi 110280676 485 KLDSKQNE 492
Cdd:PTZ00121 1595 EEVMKLYE 1602
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
182-466 |
8.82e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 182 EETDKDLERVEDLLFEINKnLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSVH---------SQHEEIQALNKTLDEKT 252
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQA-IAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGyksdetliaSRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 253 D-LRTQYNSQINEKESDVERVKLEMVNKE-----------KLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKS 320
Cdd:pfam12128 293 RtLDDQWKEKRDELNGELSAADAAVAKDRselealedqhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 321 LTDQIE-----LDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKL----LQEEVGTASSAFKLK 391
Cdd:pfam12128 373 VTAKYNrrrskIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLefneEEYRLKSRLGELKLR 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 392 QEQVY---QINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVI 466
Cdd:pfam12128 453 LNQATatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
710-923 |
1.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 710 EVEELRREINLVNNEYITLKTKQEQLASMLSDNSLRREDVLEKIAKIEEDININTPLAKEGKDELESLEERLNQLNDDFS 789
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 790 LQTTQLSnKSAVYNQENIGFHQQQ-NRVNSLEQEIGYKQTTFDQSKERIAKNLEELEIANGEIRQMVDSADVSEDELIsf 868
Cdd:COG4942 108 ELLRALY-RLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE-- 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110280676 869 yKEKESIEQGVHEAEKDYYSTRVRIDEVEKEVKEIRRNREECDEILVTLQNRVTE 923
Cdd:COG4942 185 -EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-88 |
1.22e-04 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 44.74 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGF-KSFG-----DKVVINFDEG-ITGIVGPNGCGKSNVVDAIrwvlgeqkTRALRSDKMEnVIFNGTK--NRKPQQ 76
Cdd:cd03219 1 LEVRGLtKRFGglvalDDVSFSVRPGeIHGLIGPNGAGKTTLFNLI--------SGFLRPTSGS-VLFDGEDitGLPPHE 71
|
90
....*....|....
gi 110280676 77 MAE--VSLSFNNTK 88
Cdd:cd03219 72 IARlgIGRTFQIPR 85
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
175-1052 |
1.30e-04 |
|
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: 46.58 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 175 KQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASidlakvsvhsqheeiQALNKTLDEKTDL 254
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLD---------------QKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 255 RTQYNSQINEKESDVErvKLEMVNKEKLLADRQKTLNEHV-NLIRTFESDKKIKNERLRFLNDKSKSLTDQIELDKQSND 333
Cdd:TIGR01612 1138 KKKSENYIDEIKAQIN--DLEDVADKAISNDDPEEIEKKIeNIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGI 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 334 RAAF--SLDSLTKEKESAEKIFEEISLK-VEKLKQEYEEQKEKNKLLQEEVGTASSafklkqeqvyqINKQLEIYAIQLS 410
Cdd:TIGR01612 1216 NLSYgkNLGKLFLEKIDEEKKKSEHMIKaMEAYIEDLDEIKEKSPEIENEMGIEMD-----------IKAEMETFNISHD 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 411 SLK------QELEKTTSDTSAHSANLSE---FESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEK-----EIEQIR 476
Cdd:TIGR01612 1285 DDKdhhiisKKHDENISDIREKSLKIIEdfsEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilklnKIKKII 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 477 EQLTQANRKLDSKQNEFNLTKSMVENLegfpeaIKFLKKNASWGKDTPLLSDILTcDEKFRLCIENYLESfMNYYVVE-- 554
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDKSEKL------IKKIKDDINLEECKSKIESTLD-DKDIDECIKKIKEL-KNHILSEes 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 555 -------NEAQAIQAVNLLSDS---AKGKANFFVLTRFNNYTSSQKNTFGDcvsaldIVEYDNKYKGLIQYILDGVYIIT 624
Cdd:TIGR01612 1437 nidtyfkNADENNENVLLLFKNiemADNKSQHILKIKKDNATNDHDFNINE------LKEHIDKSKGCKDEADKNAKAIE 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 625 GNQDIIPEDPQSVFITQNgklakrKYSisggsvglfegkRIGRAKNMEKLEADIKQITSDIENI--RVVLDTKLKEFYLL 702
Cdd:TIGR01612 1511 KNKELFEQYKKDVTELLN------KYS------------ALAIKNKFAKTKKDSEIIIKEIKDAhkKFILEAEKSEQKIK 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 703 KENTKKLEVEELRREINLVNNEYITLKTKQEQLasmlsdnslrrEDVLEKIAKIEEDINintplakEGKDELESLEERLN 782
Cdd:TIGR01612 1573 EIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENF-----------ENKFLKISDIKKKIN-------DCLKETESIEKKIS 1634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 783 QLNDDfsLQTTQLSnksavynqenigfhQQQNRVNSLEqeigykqtTFDQSKERIAKNLEEleiangeirqmvdsadvSE 862
Cdd:TIGR01612 1635 SFSID--SQDTELK--------------ENGDNLNSLQ--------EFLESLKDQKKNIED-----------------KK 1673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 863 DELISFYKEKESIEQGVHEAEKDYystrvRIDEVEKevkeirrnreeCDEILVTLQNRVTETKIGLSSIKERLNVEFNLN 942
Cdd:TIGR01612 1674 KELDELDSEIEKIEIDVDQHKKNY-----EIGIIEK-----------IKEIAIANKEEIESIKELIEPTIENLISSFNTN 1737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 943 -LDDILANQNPDDVLPSEEELKEKVIKIKNSLdrLGPINPMAMEA--YQEIKERHvfITTQKE-----DLAKSKESLMET 1014
Cdd:TIGR01612 1738 dLEGIDPNEKLEEYNTEIGDIYEEFIELYNII--AGCLETVSKEPitYDEIKNTR--INAQNEflkiiEIEKKSKSYLDD 1813
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 110280676 1015 I--NEIDTV----------AKATFLDAFEKIRDNFIRVFRSLFTDEDSCD 1052
Cdd:TIGR01612 1814 IeaKEFDRIinhfkkkldhVNDKFTKEYSKINEGFDDISKSIENVKNSTD 1863
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
672-1149 |
1.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 672 EKLEADIKQITSDIENIRVVLDTKLKefyLLKENTKKLEVEELRREINLVNNEYITLKTKQEQLASMLSDNSLRREDVLE 751
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEK---LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 752 KIAKIEEDININTPLAKEgkdELESLEERLNQLNDDFSLQTTQLSnksavynqenigfhQQQNRVNSLEQEIGY--KQTT 829
Cdd:COG4717 175 LQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELE--------------EAQEELEELEEELEQleNELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 830 FDQSKERIAKNLEELEIANG--EIRQMVDSADVSEDEL---------------ISFYKEKESIEQGVHEAEKDYYSTRVR 892
Cdd:COG4717 238 AAALEERLKEARLLLLIAAAllALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 893 IDEVEKEVKEIRRNREECDEILVTLQNRVTETKIGLSSI----KERLNVEFNLNLDDILANQNPDDV---------LPSE 959
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAeeleEELQLEELEQEIAALLAEAGVEDEeelraaleqAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 960 EELKEKVIKIKNSLDRLGP--INPMAMEAYQEIKERHVFITTQKEDLAKSKESLMETINEIDT----------------- 1020
Cdd:COG4717 398 QELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAeleqleedgelaellqe 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1021 -------------------VAKATFLDAFEKIRDNF--------IRVFRSLFTDEDScdlKLVDPENPldsaiDIMAKPK 1073
Cdd:COG4717 478 leelkaelrelaeewaalkLALELLEEAREEYREERlppvleraSEYFSRLTDGRYR---LIRIDEDL-----SLKVDTE 549
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110280676 1074 GKRPLTINQLSGGEKTLTAISLLFAIYLI---KPAPFcIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMA 1149
Cdd:COG4717 550 DGRTRPVEELSRGTREQLYLALRLALAELlagEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVE 627
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-504 |
1.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 123 DINDLFLDTGIGSDSYAIIELKmVDDILNDKDGSRRELFEEAAGISKFKM---RKKQTLKKLEETDKDL-ERVEDLLFEI 198
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEAR-REELEDRDEELRDRLEECRVAAQAHNEeaeSLREDADDLEERAEELrEEAAELESEL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 199 NKNLKSLEKQAKQTEKYHE----IKEDYKNASIDLAKVSVHSQ--HEEIQALNKTLDE-KTDLRTQYNSqINEKESDVER 271
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEeieeLRERFGDAPVDLGNAEDFLEelREERDELREREAElEATLRTARER-VEEAEALLEA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 272 VKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTDQIELDKQSnDRAAFSLDSLTKEKESAEK 351
Cdd:PRK02224 452 GKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRI-ERLEERREDLEELIAERRE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 352 IFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQ------ELEKTTSDTSA 425
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIER 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 426 HSANLSEFESKANEVKRTLDTKNAELETLQAE--DERI---QQQVINLEKEIEQIREQLTQANRKLDSKQNEFNLTKSMV 500
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEfdEARIeeaREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
....
gi 110280676 501 ENLE 504
Cdd:PRK02224 691 EELE 694
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-48 |
1.94e-04 |
|
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: 45.28 E-value: 1.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110280676 1 MQLSKLEIKGFKSFgDKVVINFDEGITGIVGPNGCGKSNVVDAIRWVL 48
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEIDLDEDLTVLIGKNNSGKSSILEALDIFL 47
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
406-493 |
2.13e-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: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 406 AIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRK 485
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
....*...
gi 110280676 486 LDSKQNEF 493
Cdd:COG4942 99 LEAQKEEL 106
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
157-488 |
2.23e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 157 RRELFEEAAGISKFKMRKKqtlKKLEETDKDLERVEDLLFEINKNLKSLEkqakqtekyheikEDYKNASIDLAKVSVHS 236
Cdd:PRK04863 281 RRVHLEEALELRRELYTSR---RQLAAEQYRLVEMARELAELNEAESDLE-------------QDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 237 QH--------EEIQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNE-------HVNLIRTFE 301
Cdd:PRK04863 345 RQqekieryqADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVqqtraiqYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 302 SDKK--------IKN--ERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEIS-------------- 357
Cdd:PRK04863 425 RAKQlcglpdltADNaeDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawdvarellrr 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 358 ---------------LKVEKLKQEYEEQKEKNKLLQEevgtassaFKLKQEQVYQINKQLEIYAIQL------------- 409
Cdd:PRK04863 505 lreqrhlaeqlqqlrMRLSELEQRLRQQQRAERLLAE--------FCKRLGKNLDDEDELEQLQEELearleslsesvse 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 410 -----SSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINlEKEIEQIREQLTQANR 484
Cdd:PRK04863 577 arerrMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLER-ERELTVERDELAARKQ 655
|
....
gi 110280676 485 KLDS 488
Cdd:PRK04863 656 ALDE 659
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
239-439 |
2.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 239 EEIQALNKTLDEKtdlrtqyNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLN--D 316
Cdd:COG3883 37 AELDALQAELEEL-------NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 317 KSKSLTD---QIELDKQSNDRAAFSLDSLTKEKESAEKifeeislKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQE 393
Cdd:COG3883 110 GSESFSDfldRLSALSKIADADADLLEELKADKAELEA-------KKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110280676 394 QVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANE 439
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1068-1143 |
2.82e-04 |
|
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: 42.44 E-value: 2.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 1068 IMAKPKGKRPLTINQLSGGEKTLtaisLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGEsqFIIVTH 1143
Cdd:cd03221 56 IVTWGSTVKIGYFEQLSGGEKMR----LALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGT--VILVSH 125
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
160-503 |
3.49e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 160 LFEEAAGISKFKMRKKQtlKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQT--------EKYHEIKEDY--------- 222
Cdd:pfam06160 69 LFEAEELNDKYRFKKAK--KALDEIEELLDDIEEDIKQILEELDELLESEEKNreeveelkDKYRELRKTLlanrfsygp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 223 ---------KNASIDL--------------AKVSVHSQHEEIQALNKTLDE----KTDLRTQYNSQINE-----KESDVE 270
Cdd:pfam06160 147 aidelekqlAEIEEEFsqfeeltesgdyleAREVLEKLEEETDALEELMEDipplYEELKTELPDQLEElkegyREMEEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 271 RVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKikNERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKEKESAE 350
Cdd:pfam06160 227 GYALEHLNVDKEIQQLEEQLEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 351 KIFEEISLKVEKLKQEY-----------------EEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLK 413
Cdd:pfam06160 305 EQNKELKEELERVQQSYtlnenelervrglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFK 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 414 QELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNaeL----ETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSK 489
Cdd:pfam06160 385 ESLQSLRKDELEAREKLDEFKLELREIKRLVEKSN--LpglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEA 462
|
410
....*....|....
gi 110280676 490 QNEFNLTKSMVENL 503
Cdd:pfam06160 463 QDDVDTLYEKTEEL 476
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
408-484 |
4.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110280676 408 QLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANR 484
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
160-518 |
4.59e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 160 LFEEAAGISKFKMRKKQtlKKLEETDKDLERVEDLLFEINKNLKSL-EKQAKQTEKYHEIKEDYKNASIDLAKVSvHSQH 238
Cdd:PRK04778 88 LFEAEELNDKFRFRKAK--HEINEIESLLDLIEEDIEQILEELQELlESEEKNREEVEQLKDLYRELRKSLLANR-FSFG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 239 EEIQALNKTLDEKTDLRTQYN------------SQINEKESDVERVKLEMVNKEKLLADRQKTLN--------------- 291
Cdd:PRK04778 165 PALDELEKQLENLEEEFSQFVeltesgdyvearEILDQLEEELAALEQIMEEIPELLKELQTELPdqlqelkagyrelve 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 292 -----EHVNLIRTFESdkkIKNERlrflnDKSKSLTDQIELD--KQSNDRAAFSLDSL--TKEKESAEKIFEEIslKVEK 362
Cdd:PRK04778 245 egyhlDHLDIEKEIQD---LKEQI-----DENLALLEELDLDeaEEKNEEIQERIDQLydILEREVKARKYVEK--NSDT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 363 LKQEYEEQKEKNKLLQEEVGTASSAFKLKQ---EQVYQINKQLEiyaiqlsSLKQELEKTTSDTSAHSANLSEFESKANE 439
Cdd:PRK04778 315 LPDFLEHAKEQNKELKEEIDRVKQSYTLNEselESVRQLEKQLE-------SLEKQYDEITERIAEQEIAYSELQEELEE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 440 VKRTLdtknaelETLQAEDERIQQQVINLEKEiEQireqltQANRKLDSKQNEFNLTKSMVE--NLEGFPEAIKFLKKNA 517
Cdd:PRK04778 388 ILKQL-------EEIEKEQEKLSEMLQGLRKD-EL------EAREKLERYRNKLHEIKRYLEksNLPGLPEDYLEMFFEV 453
|
.
gi 110280676 518 S 518
Cdd:PRK04778 454 S 454
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
247-502 |
4.97e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 247 TLDEKTDLRTQYNSQINEK---ESDVERVKLEMVNKEKLLADRQ---KTLNEHVNLIRTFESDKKIKNERLRFLNDKSKS 320
Cdd:pfam17380 245 LAEDVTTMTPEYTVRYNGQtmtENEFLNQLLHIVQHQKAVSERQqqeKFEKMEQERLRQEKEEKAREVERRRKLEEAEKA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 321 ltDQIELDKQS-----NDRAAFS----LDSLTKE--KESAEKIF-EEISLKVEKLKqEYE----EQKEKNKLLQEEVGTA 384
Cdd:pfam17380 325 --RQAEMDRQAaiyaeQERMAMErereLERIRQEerKRELERIRqEEIAMEISRMR-ELErlqmERQQKNERVRQELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 385 SSAFKLKQEQVYQINKQLeiyaIQLSSLKQELEkttsdtsahsanlsefESKANEVKRTLDTKNAELETLQAEDERIQQQ 464
Cdd:pfam17380 402 RKVKILEEERQRKIQQQK----VEMEQIRAEQE----------------EARQREVRRLEEERAREMERVRLEEQERQQQ 461
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 110280676 465 VINL-EKEIEQIREQLT----QANRKLDSKQNEFNLTKSMVEN 502
Cdd:pfam17380 462 VERLrQQEEERKRKKLElekeKRDRKRAEEQRRKILEKELEER 504
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
263-494 |
5.01e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 263 NEKESDVerVKLEMVNKEKLLAdrQKTLNEHVNLIRTFESDKKIK--NERLRFLNDKSKSLtdQIELDKQSNDRAAF--- 337
Cdd:COG3206 131 PVKGSNV--IEISYTSPDPELA--AAVANALAEAYLEQNLELRREeaRKALEFLEEQLPEL--RKELEEAEAALEEFrqk 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 338 -SLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAF-KLKQEQVYQINKQleiyaiQLSSLKQE 415
Cdd:COG3206 205 nGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpELLQSPVIQQLRA------QLAELEAE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 416 L-EKTTSDTSAHS------ANLSEFESK-ANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIRE---QLTQANR 484
Cdd:COG3206 279 LaELSARYTPNHPdvialrAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEleaELRRLER 358
|
250
....*....|
gi 110280676 485 KLDSKQNEFN 494
Cdd:COG3206 359 EVEVARELYE 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
335-907 |
5.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 335 AAFSLDSLTKE-KESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGtassAFKLKQEQVYQINKQLEIYAIQLSSLK 413
Cdd:COG4717 40 LAFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 414 QELEKTtsdtsAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQqvinLEKEIEQIREQLTQANRKLDSKQNEF 493
Cdd:COG4717 116 EELEKL-----EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 494 NLtkSMVENLEGFPEAIKFLKKNASwgkdtPLLSDILTCDEKFRLcIENYLESFMNYYVVENEAQAIQAVNLLsdsakgk 573
Cdd:COG4717 187 SL--ATEEELQDLAEELEELQQRLA-----ELEEELEEAQEELEE-LEEELEQLENELEAAALEERLKEARLL------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 574 anFFVLTrfnnytssqkntfgdcvSALDIVEYDNKYKGLIQYILDGVYIITGnqdiipedpqsVFITQNGKLAKRKysis 653
Cdd:COG4717 252 --LLIAA-----------------ALLALLGLGGSLLSLILTIAGVLFLVLG-----------LLALLFLLLAREK---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 654 ggSVGLFEGKRIGRAKNMEKLE-ADIKQITSDIENIRVVLDTKLKEFYLLKENTKKL--EVEELRREINLVNNEyitlkt 730
Cdd:COG4717 298 --ASLGKEAEELQALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELlrEAEELEEELQLEELE------ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 731 kqEQLASMLSDNSLRREDVLEKIAKIEEdinintplakegkdELESLEERLNQLNDDFSLQTTQLSNKSAVYNQENIgfh 810
Cdd:COG4717 370 --QEIAALLAEAGVEDEEELRAALEQAE--------------EYQELKEELEELEEQLEELLGELEELLEALDEEEL--- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 811 qqQNRVNSLEQEIgykqttfDQSKERIAKNLEELEIANGEIRQMVDSADVSEDELisfykEKESIEQGVHEAEKDYYSTR 890
Cdd:COG4717 431 --EEELEELEEEL-------EELEEELEELREELAELEAELEQLEEDGELAELLQ-----ELEELKAELRELAEEWAALK 496
|
570
....*....|....*..
gi 110280676 891 VRIDEVEKEVKEIRRNR 907
Cdd:COG4717 497 LALELLEEAREEYREER 513
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
708-975 |
5.58e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 708 KLEVEELRREINLVNNEYITLKTKQEQLASMLSD-----NSLRRE--DVLEKIAKIEEDININTPLAKEGKDELESLEER 780
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrDELNAQvkELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 781 LNQLNDDFslqtTQLSNKSAVYNQENIGFHQQQNRVNSLEQEIGYKQTTFDQSKE------RIAKNLEELEIANGEIRQM 854
Cdd:COG1340 87 LNELREEL----DELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElvekikELEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 855 VDSadvsEDELISFYKEKESIEQGVHEAEKDYYSTRVRIDEVEKEVKEIRRNREECDEILVTLQNRVTETKIGLSSIKER 934
Cdd:COG1340 163 KEL----RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 110280676 935 LNvEFNLNLDDILANQNPDDVLPSEEELKEKVIKIKNSLDR 975
Cdd:COG1340 239 LR-ELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
983-1143 |
5.60e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.06 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 983 AMEAYQEIKERHVFITTQKEDLAKSKESLMETINEIDTVAKATFLDAFEKIRdnfiRVFRSLFTDEDscDLKlVDPENPL 1062
Cdd:COG3950 98 LKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVR----EALNKLLPDFK--DIR-IDRDPGR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1063 DSAIDimakpKGKRPLTINQLSGGEKTLTAI--SLLFAIYLIKPAPFC--------IFDEVDAPLddaNID---KFNNII 1129
Cdd:COG3950 171 LVILD-----KNGEELPLNQLSDGERSLLALvgDLARRLAELNPALENplegegivLIDEIDLHL---HPKwqrRILPDL 242
|
170
....*....|....
gi 110280676 1130 RQFAGESQFIIVTH 1143
Cdd:COG3950 243 RKIFPNIQFIVTTH 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
434-492 |
5.70e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 5.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 110280676 434 ESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNE 492
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE 73
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
359-497 |
8.14e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.29 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 359 KVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQE-QVYQinKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKA 437
Cdd:pfam12795 4 ELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRaAAYQ--KALDDAPAELRELRQELAALQAKAEAAPKEILASLSLE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 438 nEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFNLTK 497
Cdd:pfam12795 82 -ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPA 140
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-46 |
8.38e-04 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 42.67 E-value: 8.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 110280676 3 LSKLEIKGFKSFgDKVVINFDEGITGIVGPNGCGKSNVVDAIRW 46
Cdd:cd03242 1 LKSLELRNFRNY-AELELEFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
875-1144 |
1.11e-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: 42.38 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 875 IEQGVHEAEKDYYSTRVRIDEVEKEVKEIRRNREECDEILVTLQNRVTETKIGLSSIKERLNVEFNLNLDDilanqnpdD 954
Cdd:pfam13304 34 DERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDS--------E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 955 VLPSEEELKEKVIKIKNSLDRLGPINPMAMEAYQEIKERHVFITTQKEDLAKSKESLMETINEIDTVAKATFLDAFEKIR 1034
Cdd:pfam13304 106 EREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1035 DNFIRVFRSL---FTDEDSCDLKLVDPENPLDSAIDIMAKPKGKRPLTINQLSGGEKTLTAISLLFAIYLIKPAPFCIfD 1111
Cdd:pfam13304 186 QRLVRGLKLAdlnLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPKGGLLLI-D 264
|
250 260 270
....*....|....*....|....*....|....
gi 110280676 1112 EVDAPLDDANIDKFNNIIRQFAGE-SQFIIVTHN 1144
Cdd:pfam13304 265 EPESGLHPKLLRRLLELLKELSRNgAQLILTTHS 298
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1083-1152 |
1.12e-03 |
|
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: 41.43 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110280676 1083 LSGGEKTLTAISLLFAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGES---QFIIVT-HNKRTMASTD 1152
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQpgrQFIFITpQDISGLASSD 183
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-184 |
1.16e-03 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 42.46 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1 MQLSKLEIKGFKSFGDKVViNFDEGITGIVGPNGCGKSNVVDAIRWVLGEQktraLRSDKMENVIFNGtkNRKPQQMAEV 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTL-AFPPGVTAVVGENAAGKTNLLEAIYLALTGE----LPNGRLADLVRFG--EGEAWVHAEV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 81 SLSFNNTKnllpteySQVTITRryyrtGDSEYLLNGVTCRLKDINDLFLDTGIGSDSyaiIELkmvddILNDKDGSRREL 160
Cdd:PRK14079 74 ETGGGLSR-------LEVGLGP-----GRRELKLDGVRVSLRELARLPGAVLIRPED---LEL-----VLGPPEGRRAYL 133
|
170 180
....*....|....*....|....
gi 110280676 161 feeAAGISKFKMRKKQTLKKLEET 184
Cdd:PRK14079 134 ---DRLLSRLSARYAALLSAYERA 154
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
169-515 |
1.18e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 169 KFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQ-AKQTEKYHEIKEDYKNASIDLAKVSVHSQHEEIQ--ALN 245
Cdd:pfam05557 24 EHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKReAEAEEALREQAELNRLKKKYLEALNKKLNEKESQlaDAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 246 KTLDEKTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFE---SDKKIKNERLRFLNDKSKSLT 322
Cdd:pfam05557 104 EVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEkqqSSLAEAEQRIKELEFEIQSQE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 323 DQIELDKQSNDRAAfSLDSLTKEKESAE---KIFEEISLKVEKLKQE--------YEEQKEKNKLLQEEVGTASSAFKLK 391
Cdd:pfam05557 184 QDSEIVKNSKSELA-RIPELEKELERLRehnKHLNENIENKLLLKEEvedlkrklEREEKYREEAATLELEKEKLEQELQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 392 QEQVYQINKQLEIYA--------IQLSS----LKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDE 459
Cdd:pfam05557 263 SWVKLAQDTGLNLRSpedlsrriEQLQQreivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVR 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 460 RIQQQVINLEKEIEQIREQltqanrkLDSKQNEFNLTKSMVENLEGFPEAIKFLKK 515
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAI-------LESYDKELTMSNYSPQLLERIEEAEDMTQK 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
301-498 |
1.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 301 ESDKKIKNERLRFLNDKSKSLTDQI-ELDKQsndraafsLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQE 379
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELdALQAE--------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 380 EVGT-ASSAFKL---------------------KQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKA 437
Cdd:COG3883 87 ELGErARALYRSggsvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110280676 438 NEVKRTLDTKNAELETLQAedeRIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFNLTKS 498
Cdd:COG3883 167 EAAKAELEAQQAEQEALLA---QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
705-936 |
1.28e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 705 NTKKLEVEELRREINLVNNEYITLKTKQEQLASMLSDNSLRRE--DVLEK-IAKIEEDININTPLAKEGKDELESLEERL 781
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREelETLEAeIEDLRETIAETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 782 NQLNDDfslqttqlsNKSAVYNQEnigfhqqqnrVNSLEQE-IGYKQTTFDQSKERIAKNLEE----LEIANGEIRQMVD 856
Cdd:PRK02224 289 EELEEE---------RDDLLAEAG----------LDDADAEaVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 857 SADVSEDELISFYKEKESIEQGVHEAEKDYYSTRVRIDEVEKEVKEIRRN--------------REECDEILVTLQNRVT 922
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgnaedfLEELREERDELREREA 429
|
250
....*....|....
gi 110280676 923 ETKIGLSSIKERLN 936
Cdd:PRK02224 430 ELEATLRTARERVE 443
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
182-493 |
1.32e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 182 EETDKDLERVEDLLFEINKNLKsLEKQAKQTEKYHEIKedyKNASIDLAKVSVHSQH-EEIQALNKTLDEKTDLRTQYns 260
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSE-AEDMLACEQHALLRK---LQPEQDLQDVRLHLQQcSQELALKLTALHALQLTLTQ-- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 261 qinekESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKI---KNERLRFLNDKSKSLTDQIEldKQSNDRAAF 337
Cdd:TIGR00618 658 -----ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFN--EIENASSSL 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 338 SLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQiNKQLEIYAIQLSSLKQEL- 416
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF-NRLREEDTHLLKTLEAEIg 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 417 EKTTSDTSAHSANLSEFESKANEVKRTLDTKNA---ELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKlDSKQNEF 493
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGI-NQIKIQF 888
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-38 |
1.65e-03 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain] Cd Length: 173 Bit Score: 40.46 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKG-FKSFGDKVV---INFD--EG-ITGIVGPNGCGKS 38
Cdd:cd03230 1 IEVRNlSKRYGKKTAlddISLTveKGeIYGLLGPNGAGKT 40
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1079-1155 |
1.82e-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: 40.44 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110280676 1079 TI--NQLSGGEKTLTAIsllfAIYLIKPAPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTDIIY 1155
Cdd:cd03228 91 TIreNILSGGQRQRIAI----ARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1079-1144 |
1.96e-03 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 40.10 E-value: 1.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 1079 TINQLSGGEKTLTAIslLFAIYLikPAPFCIFDEVDAPLDDANIDKFNNIIRQFA--GESqFIIVTHN 1144
Cdd:cd03216 79 MVYQLSVGERQMVEI--ARALAR--NARLLILDEPTAALTPAEVERLFKVIRRLRaqGVA-VIFISHR 141
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1033-1163 |
2.03e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 42.13 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1033 IRDNfIRVFRSLFTDEDSCD-LKLVDpenpLDSaiDIMAKPKG-KRPLTIN--QLSGGEKTltaiSLLFAIYLIKPAPFC 1108
Cdd:COG2274 565 IREN-ITLGDPDATDEEIIEaARLAG----LHD--FIEALPMGyDTVVGEGgsNLSGGQRQ----RLAIARALLRNPRIL 633
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 110280676 1109 IFDEVDAPLDDANIDKFNNIIRQFAGESQFIIVTHNKRTMASTDIIYgitMVEQG 1163
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII---VLDKG 685
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
692-871 |
2.30e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 692 LDTKLKEFYLLKENTKKlEVEELRREINLVNNEYITLKTKQEQLASMLSDNSLRREDVLEKIAKIEEDI-NINTPlaKEG 770
Cdd:COG1579 15 LDSELDRLEHRLKELPA-ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNN--KEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 771 KD---ELESLEERLNQLNDDFSLQTTQLSNKSAVYNQEnigfhqqQNRVNSLEQEIGYKQTTFDQSKERIAKNLEELEia 847
Cdd:COG1579 92 EAlqkEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELE-- 162
|
170 180
....*....|....*....|....
gi 110280676 848 nGEIRQMVDSADvseDELISFYKE 871
Cdd:COG1579 163 -AEREELAAKIP---PELLALYER 182
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-44 |
2.32e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.92 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|....*....
gi 110280676 12 KSFGDKVV-----INFDEG-ITGIVGPNGCGKSNVVDAI 44
Cdd:cd00267 7 FRYGGRTAldnvsLTLKAGeIVALVGPNGSGKSTLLRAI 45
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-38 |
2.53e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 41.25 E-value: 2.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGF-KSFGDKVV---INFD--EG-ITGIVGPNGCGKS 38
Cdd:COG4152 2 LELKGLtKRFGDKTAvddVSFTvpKGeIFGLLGPNGAGKT 41
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-38 |
2.53e-03 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 40.82 E-value: 2.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGF-KSFGDKVV---INFD--EG-ITGIVGPNGCGKS 38
Cdd:COG1131 1 IEVRGLtKRYGDKTAldgVSLTvePGeIFGLLGPNGAGKT 40
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
271-494 |
2.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 271 RVKLEmvNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTDQIELDkqsndRAAFSLDSLTKEKESAE 350
Cdd:COG4913 609 RAKLA--ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 351 K---IFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSafklkqeqvyqinkqleiyaiQLSSLKQELEkttsdtsAHS 427
Cdd:COG4913 682 AssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEK---------------------ELEQAEEELD-------ELQ 733
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 428 ANLSEFESKANEVKRT-LDTKNAELetlqAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFN 494
Cdd:COG4913 734 DRLEAAEDLARLELRAlLEERFAAA----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
240-492 |
2.58e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 240 EIQALNKTLDEKTDLRTQynsQINEKESDVERvkLEMVNKEKLlADRQKTLNEHVNLIRTFESDKKIKNERLrflndksk 319
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQ---QIKTYNKNIEE--QRKKNGENI-ARKQNKYDELVEEAKTIKAEIEELTDEL-------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 320 sltdqIELDKQSNDRAAfsldSLTKEKESAEKIFEEISL--KVEKLKQEYEEQKEKNKLLQEEVGTASSAfklkQEQVYQ 397
Cdd:PHA02562 244 -----LNLVMDIEDPSA----ALNKLNTAAAKIKSKIEQfqKVIKMYEKGGVCPTCTQQISEGPDRITKI----KDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 398 INKQLEiyaiQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIRE 477
Cdd:PHA02562 311 LQHSLE----KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
|
250
....*....|....*
gi 110280676 478 QLTQANRKLDSKQNE 492
Cdd:PHA02562 387 ELDKIVKTKSELVKE 401
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-202 |
2.70e-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: 41.22 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 26 ITGIVGPNGCGKSNVVDAIRWVLGEQKtralrsdkmeNVIFNGTKNRKPQQMAEVSLSFNNTKNLLPTEY--SQVTITRR 103
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDA----------LVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFeiSEFLEDGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 104 YYRTGdSEYLLNGVTCRLKDINDLFLDTGIGSDSYAIIELKMVDDILNDKDGSRRELFEEAAGISKFKMRKKQTLKKLEE 183
Cdd:pfam13304 71 RYRYG-LDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIIS 149
|
170
....*....|....*....
gi 110280676 184 TDKDLERVEDLLFEINKNL 202
Cdd:pfam13304 150 PLSFLLLLDEGLLLEDWAV 168
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
189-505 |
2.73e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 189 ERVEDLLFEINKNLKSLEKQAKQTEKYHEiKEDYKNASIDLAKVSVHSQHEEIQALNKTLDE-KTDLRTQYNSQ---INE 264
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWD-RDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQmaaIQG 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 265 KESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTK 344
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 345 EKESAEKIfEEISLKVEKLKQEYEEQKEKNKLLQEEV----------GTASSAFKLKQEQV-YQIN------KQLEIYAI 407
Cdd:pfam15921 536 LKNEGDHL-RNVQTECEALKLQMAEKDKVIEILRQQIenmtqlvgqhGRTAGAMQVEKAQLeKEINdrrlelQEFKILKD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 408 QLSSLKQELEKTTSDTSAHSANL----SEFESKANEVKRTLD-------TKNAELETLQAEDERIQQQVINLEKEIEQIR 476
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDqllnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
330 340
....*....|....*....|....*....
gi 110280676 477 EQLTQanrKLDSKQNEFNLTKSMVENLEG 505
Cdd:pfam15921 695 NKLKM---QLKSAQSELEQTRNTLKSMEG 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
174-375 |
2.91e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 174 KKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTE----KYHEIKEDYKNASIDLAKV----------SVHSQHE 239
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkKLAELEKKLDELEEELAELlkeleelgfeSVEELEE 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 240 EIQALNKTLDEKTDLRTQyNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEHVNLIRTFE---SDKKIKNERLRFLND 316
Cdd:PRK03918 593 RLKELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkySEEEYEELREEYLEL 671
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110280676 317 KS--KSLTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISlKVEKLKQEYEEQKEKNK 375
Cdd:PRK03918 672 SRelAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVK 731
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
347-482 |
3.02e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 347 ESAEKIFEEISLKVEKLKQEYE----EQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQ----LSSLKQELE- 417
Cdd:pfam07111 470 PPAPPVDADLSLELEQLREERNrldaELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRaqesLASVGQQLEv 549
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 418 --KTTSDTSAHSANLSEFESKANEV-KRTLDTKNAELETlqaedeRIQQQVINLEKEIEQIREQLTQA 482
Cdd:pfam07111 550 arQGQQESTEEAASLRQELTQQQEIyGQALQEKVAEVET------RLREQLSDTKRRLNEARREQAKA 611
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
179-494 |
3.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 179 KKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKY---HEIKEDYKNASIDLAkvsvhSQHEEIQALNKTLDektdlr 255
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLAEYSWDEIDVA-----SAEREIAELEAELE------ 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 256 tqynsQINEKESDVERVklemvnkEKLLADRQKTLNEHVNLIRTFESDKKIKNERLRFLNDKSKSLTDQIE-LDKQSNDR 334
Cdd:COG4913 679 -----RLDASSDDLAAL-------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 335 AAFSLDSLtKEKESAEKIFEEISlkvEKLKQEYEEQKEKNKLLQEEVGTASSAFKlkqeQVYQINKQ--------LEIYA 406
Cdd:COG4913 747 LRALLEER-FAAALGDAVERELR---ENLEERIDALRARLNRAEEELERAMRAFN----REWPAETAdldadlesLPEYL 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 407 IQLSSLKQElekttsdtsahsaNLSEFESKANEVKRTldTKNAELETLQAEderiqqqvinLEKEIEQIREQLTQANRKL 486
Cdd:COG4913 819 ALLDRLEED-------------GLPEYEERFKELLNE--NSIEFVADLLSK----------LRRAIREIKERIDPLNDSL 873
|
....*...
gi 110280676 487 dsKQNEFN 494
Cdd:COG4913 874 --KRIPFG 879
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-38 |
3.54e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 3.54e-03
10 20 30
....*....|....*....|....*....|...
gi 110280676 12 KSFGDKVVI---NFD---EGITGIVGPNGCGKS 38
Cdd:PRK11819 332 KSFGDRLLIddlSFSlppGGIVGIIGPNGAGKS 364
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
255-503 |
3.58e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 255 RTQYNSQINEKESDVERV--KLEMVNKEK--LLADRQKTLNEHVNLIRTFESDKKIKNERlrflNDKSKSLTDQIELDKQ 330
Cdd:pfam15905 89 RGEQDKRLQALEEELEKVeaKLNAAVREKtsLSASVASLEKQLLELTRVNELLKAKFSED----GTQKKMSSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 331 SNDRAAfsldsltKEKESAEKIfEEISLKVEKLKQEYEEQKEKNKLLQEEVgtaSSAFKLKQEQVYQINKQLEiYAIQLS 410
Cdd:pfam15905 165 RNKLEA-------KMKEVMAKQ-EGMEGKLQVTQKNLEHSKGKVAQLEEKL---VSTEKEKIEEKSETEKLLE-YITELS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 411 SLKQELEKTTSDTSAHSANLSEFESKANEVKRTLDTKNAELETLQAE-DERIQQQVINLEKEIEQIREQLTQANRKLDSK 489
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDlNEKCKLLESEKEELLREYEEKEQTLNAELEEL 312
|
250
....*....|....
gi 110280676 490 QNEFNLTKSMVENL 503
Cdd:pfam15905 313 KEKLTLEEQEHQKL 326
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-482 |
3.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 162 EEAAGISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNAsidlAKVSVHSQHEEI 241
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA----AEKKKEEAKKKA 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 242 QALNKTLDEKTDLRtQYNSQINEKESDVERVKLEMVNKEKllADRQKTLNEHVnliRTFESDKKIKNERLRF--LNDKSK 319
Cdd:PTZ00121 1381 DAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKK--ADEAKKKAEEK---KKADEAKKKAEEAKKAdeAKKKAE 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 320 SLTDQIELDKQSND-RAAFSLDSLTKEKESAE---KIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQv 395
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEaKKADEAKKKAEEAKKADeakKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA- 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 396 yqiNKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEfESKANEVKRTLDTKNAElETLQAEDERIQQQVINLEKEIEQI 475
Cdd:PTZ00121 1534 ---KKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMK 1608
|
....*..
gi 110280676 476 REQLTQA 482
Cdd:PTZ00121 1609 AEEAKKA 1615
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-482 |
3.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 303 DKKIKNERLRFLNDKSKSLTDQIELDKQSNDRAAF--SLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQK-EKNKLLQE 379
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELraELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 380 EVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKAN----EVKRTLDTKNAELETLQ 455
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELE 425
|
170 180
....*....|....*....|....*..
gi 110280676 456 AEDERIQQQVINLEKEIEQIREQLTQA 482
Cdd:COG4913 426 AEIASLERRKSNIPARLLALRDALAEA 452
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-38 |
4.26e-03 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 40.41 E-value: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGFK-SFGDKVV---INFD--EG-ITGIVGPNGCGKS 38
Cdd:COG1120 2 LEAENLSvGYGGRPVlddVSLSlpPGeVTALLGPNGSGKS 41
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1080-1144 |
4.51e-03 |
|
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: 39.76 E-value: 4.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 1080 INQLSGGEKTLTAISllfAIYLIKPaPFCIFDEVDAPLDDANIDKFNNIIRQFAGESQ-FIIVTHN 1144
Cdd:cd03225 132 PFTLSGGQKQRVAIA---GVLAMDP-DILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHD 193
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
349-504 |
4.62e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 349 AEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSA 428
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110280676 429 NLSEFESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQANRKLDSKQNEFNLTKSMVENLE 504
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
3-54 |
4.76e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.42 E-value: 4.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 110280676 3 LSKLEIKGFKSFgDKVVINFDE-GITGIVGPNGCGKSNVVDAIRWVL-GEQKTR 54
Cdd:pfam13555 1 LTRLQLINWGTF-DGHTIPIDPrGNTLLTGPSGSGKSTLLDAIQTLLvPAKRAR 53
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
240-484 |
4.89e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 240 EIQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMvnkEKLLADRQKTLNEHVNLIRTFESDKKIKNErlrfLNDKSK 319
Cdd:pfam00038 55 EIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKY---EDELNLRTSAENDLVGLRKDLDEATLARVD----LEAKIE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 320 SLTDQIELDKQSND------RAAFSLDSLTKEKESAEKIfeEISLKVEKLKQEYEEQKEKNKL------------LQEEV 381
Cdd:pfam00038 128 SLKEELAFLKKNHEeevrelQAQVSDTQVNVEMDAARKL--DLTSALAEIRAQYEEIAAKNREeaeewyqskleeLQQAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 382 GTASSAFKLKQEQVYQINKQLEIYAIQLSSLKQElekttsdtsahsanlsefeskanevKRTLDTKNAELE-TLQAEDER 460
Cdd:pfam00038 206 ARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ-------------------------KASLERQLAETEeRYELQLAD 260
|
250 260
....*....|....*....|....
gi 110280676 461 IQQQVINLEKEIEQIREQLTQANR 484
Cdd:pfam00038 261 YQELISELEAELQETRQEMARQLR 284
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-38 |
4.92e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 41.07 E-value: 4.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGF-KSFGDKVVI---NFD---EGITGIVGPNGCGKS 38
Cdd:TIGR03719 323 IEAENLtKAFGDKLLIddlSFKlppGGIVGVIGPNGAGKS 362
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
142-486 |
5.25e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 142 ELKMVDDILNDKDGSRRELFEEAAGISKFKMRKKQTLKKLEETdkdLERVEDLLFEINKNLKSLEKQAkqTEKYHEIKEd 221
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLEGES--TDLQEQIAE- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 222 yKNASIDLAKVSVHSQHEEIQALNKTLDEKTDLRTQ-------YNSQINEKESDVERVKLEMVNKEKLLAD--------- 285
Cdd:pfam01576 227 -LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNalkkireLEAQISELQEDLESERAARNKAEKQRRDlgeelealk 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 286 ----------------RQKTLNEHVNLIRTFESDKKIKNERLRFLNDKS----KSLTDQIELDKQSNDraafsldSLTKE 345
Cdd:pfam01576 306 teledtldttaaqqelRSKREQEVTELKKALEEETRSHEAQLQEMRQKHtqalEELTEQLEQAKRNKA-------NLEKA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 346 KESAEKIFEEISLKVEKL---KQEYEEQKEK-NKLLQEEVGTASSAFKLKQEQVYQINK---QLEIYAIQLSSLKQELEK 418
Cdd:pfam01576 379 KQALESENAELQAELRTLqqaKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKNIK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 419 TTSDTSAHSANLSEFESKANE-----------VKRTLDTKNAELETLQAEDER----------IQQQVINLEKEIEQIR- 476
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEetrqklnlstrLRQLEDERNSLQEQLEEEEEAkrnverqlstLQAQLSDMKKKLEEDAg 538
|
410
....*....|..
gi 110280676 477 --EQLTQANRKL 486
Cdd:pfam01576 539 tlEALEEGKKRL 550
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
309-489 |
5.41e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.78 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 309 ERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKEKESAEKIFEEISLKVEKLKQEYEEQKEKNKL----LQE-EVGT 383
Cdd:pfam05701 35 ERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELaklrVEEmEQGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 384 ASSAFKLKQEQVYQINKQLEIYAIQLSSLKQELEKT-------TSDTSAHSANLSEFESKANEVKRTLDTKNAELET--- 453
Cdd:pfam05701 115 ADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLrkeyaslVSERDIAIKRAEEAVSASKEIEKTVEELTIELIAtke 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110280676 454 ---------LQAEDERI------QQQVINLEKEIEQIREQLTQANRKLDSK 489
Cdd:pfam05701 195 slesahaahLEAEEHRIgaalarEQDKLNWEKELKQAEEELQRLNQQLLSA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
392-504 |
5.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 392 QEQVYQINKQLEIYAIQLSSLKQELEKTTSDTSAHSANLSEFESKANEVKrtldtKNAELETLQAEDERIQQQVINLEKE 471
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110
....*....|....*....|....*....|...
gi 110280676 472 IEQIREQLTQANRKLDSKQNEFNLTKSMVENLE 504
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
667-1045 |
6.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 667 RAKNMEKLEADIKQITSDIENIRvvldtklKEFYLLKENTKKL-EVEELRREINLVNNEYITLKTKQEQLASMLSDNSLR 745
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVKELkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 746 REDVLEKIAKIEED---ININTPLAKEGKDELESLEERLNQLNDDFSLQTT--QLSNKSAVYNQENI-----GFHQQQNR 815
Cdd:PRK03918 323 INGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLekeleELEKAKEE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 816 VNSLEQEIGYKQTTFDQSKERIAKNLEELEIANGEIRqmVDSADVSED---ELISFYKEK-ESIEQGVHEAEKDYYSTRV 891
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP--VCGRELTEEhrkELLEEYTAElKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 892 RIDEVEKEVK---EIRRNREECDEI---------------------LVTLQNRVTETKIGLSSIKERLNVEFNL------ 941
Cdd:PRK03918 481 ELRELEKVLKkesELIKLKELAEQLkeleeklkkynleelekkaeeYEKLKEKLIKLKGEIKSLKKELEKLEELkkklae 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 942 -------------NLDDILANQNPDDVLPSEEELKE------KVIKIKNSLDRLgpinpmaMEAYQEIKERHVFITTQKE 1002
Cdd:PRK03918 561 lekkldeleeelaELLKELEELGFESVEELEERLKElepfynEYLELKDAEKEL-------EREEKELKKLEEELDKAFE 633
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 110280676 1003 DLAKSKESLMETINEIDTVAKATFLDAFEKIRDNFIRVFRSLF 1045
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-38 |
6.88e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 39.68 E-value: 6.88e-03
10 20 30
....*....|....*....|....*....|....*....
gi 110280676 7 EIKG-FKSFGDKVVIN-----FDEG-ITGIVGPNGCGKS 38
Cdd:COG4604 3 EIKNvSKRYGGKVVLDdvsltIPKGgITALIGPNGAGKS 41
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
158-380 |
7.22e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 158 RELFEEAAGI--SKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEKYHEIKEDYKNASIDLAKVSvH 235
Cdd:PRK05771 63 RSYLPKLNPLreEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLL-G 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 236 SQHEEIQA--LNKTLDEKTDLRTQYNSQINEKEsDVERVKLEMVNKEKLLADRQKTLNEHvNLIRTFESDKKIKNERLRF 313
Cdd:PRK05771 142 FKYVSVFVgtVPEDKLEELKLESDVENVEYIST-DKGYVYVVVVVLKELSDEVEEELKKL-GFERLELEEEGTPSELIRE 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110280676 314 LNDKSKSLTDQIEldkqsndraafsldSLTKE-KESAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEE 380
Cdd:PRK05771 220 IKEELEEIEKERE--------------SLLEElKELAKKYLEELLALYEYLEIELERAEALSKFLKTD 273
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-38 |
7.22e-03 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain] Cd Length: 235 Bit Score: 39.41 E-value: 7.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGF-KSFGDKVV---INFD--EG-ITGIVGPNGCGKS 38
Cdd:cd03261 1 IELRGLtKSFGGRTVlkgVDLDvrRGeILAIIGPSGSGKS 40
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
167-326 |
7.34e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 167 ISKFKMRKKQTLKKLEETDKDLERVEDLLFEINKNLKSLEKQAKQTEkyHEIKEDYKNASIDLAKVSVHSQHEEIQALNK 246
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE--LEIEEVEARIKKYEEQLGNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 247 TLDEKTDLRTQYNSQINEKESDVERVKLEMVNKEKLLADRQKTLNEhvnLIRTFESDKKIKNERLRFLNDKSKSLTDQIE 326
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
342-481 |
7.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 342 LTKEKESAEKIFEEISLKVEKLKQEYE-EQKEKNKllqeevgtassafKLKQEQVYQINKQLEIYAIQLSSLKQElektt 420
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALlEAKEEIH-------------KLRNEFEKELRERRNELQKLEKRLLQK----- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110280676 421 sdtsahsanlsefESKANEVKRTLDTKNAELETLQAEDERIQQQVINLEKEIEQIREQLTQ 481
Cdd:PRK12704 95 -------------EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-38 |
7.91e-03 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain] Cd Length: 211 Bit Score: 39.10 E-value: 7.91e-03
10 20 30
....*....|....*....|....*....|....*....
gi 110280676 6 LEIKGF-KSFGDKVVIN-----FDEGITGIVGPNGCGKS 38
Cdd:cd03264 1 LQLENLtKRYGKKRALDgvsltLGPGMYGLLGPNGAGKT 39
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1083-1146 |
7.94e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 39.05 E-value: 7.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110280676 1083 LSGGEKTLTAIsllFAIYLIKPApFCIFDEVDAPLDDANIDKFNNIIRQFAGESQ-FIIVTHNKR 1146
Cdd:cd03217 105 FSGGEKKRNEI---LQLLLLEPD-LAILDEPDSGLDIDALRLVAEVINKLREEGKsVLIITHYQR 165
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1044-1143 |
9.21e-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: 38.78 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 1044 LFTD--EDSCDLKLVDPENPLDSAIDIMAK-----PKGKRPLTinqLSGGEKTLTAIsllfAIYLIKPAPFCIFDEVDAP 1116
Cdd:cd03226 84 LFTDsvREELLLGLKELDAGNEQAETVLKDldlyaLKERHPLS---LSGGQKQRLAI----AAALLSGKDLLIFDEPTSG 156
|
90 100
....*....|....*....|....*...
gi 110280676 1117 LDDANIDKFNNIIRQFAGESQFIIV-TH 1143
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIViTH 184
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
157-415 |
9.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 157 RRELFEEAAGISKF-KMRK--KQTLKKLEETDKDLE----RVEDLLFEINKNLKSLEKQAKQT-----EKYHEIKEDYKN 224
Cdd:PHA02562 152 RRKLVEDLLDISVLsEMDKlnKDKIRELNQQIQTLDmkidHIQQQIKTYNKNIEEQRKKNGENiarkqNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 225 ASIDLAKVSvhsqhEEIQALNKTLDEKTDLRTQYNSQINEKESDVERVKLEMvnkeklladrqKTLNEHvNLIRTFESDK 304
Cdd:PHA02562 232 IKAEIEELT-----DELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVI-----------KMYEKG-GVCPTCTQQI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110280676 305 KIKNERLRFLNDKSKSLTDQIELDKQSNDRAAFSLDSLTKekesAEKIFEEISLKVEKLKQEYEEQKEKNKLLQEEVGTA 384
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE----QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|.
gi 110280676 385 SSAFKLKQEQVYQINKQLEIYAIQLSSLKQE 415
Cdd:PHA02562 371 QAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
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| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-38 |
9.86e-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: 39.04 E-value: 9.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110280676 6 LEIKGF-KSFGDKVVIN-----FDEG-ITGIVGPNGCGKS 38
Cdd:cd03259 1 LELKGLsKTYGSVRALDdlsltVEPGeFLALLGPSGCGKT 40
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