|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
592-1081 |
5.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 592 ASQRISQLEQDLASMREfrgLLKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTALLSRSRQLTEKLTV 671
Cdd:COG1196 293 LLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 672 KSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDLA 751
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 752 MKDELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTTLEVL 831
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 832 RERSLQCEnlkDTVENLTAKLASTIADNQEQDLEKTRQY--SQKLGLLTEQ--LQSLTLFLQTKLKEKTEQETLLLSTAC 907
Cdd:COG1196 530 IGVEAAYE---AALEAALAAALQNIVVEDDEVAAAAIEYlkAAKAGRATFLplDKIRARAALAAALARGAIGAAVDLVAS 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 908 PPTQEHPL--PNDRTFLGSILTAVADEEPESTPVPLLGSDKSAfTRVASMVSLQPAETpgmEESLAEMSIMTTELQSLCS 985
Cdd:COG1196 607 DLREADARyyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV-TLEGEGGSAGGSLT---GGSRRELLAALLEAEAELE 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 986 LLQESKEEAIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGEL 1065
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
490
....*....|....*.
gi 73623035 1066 ISLREEVTHLTRSLRR 1081
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
663-902 |
8.06e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 663 RQLTEKLTVKSQQAL--------QERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDS 734
Cdd:COG1196 216 RELKEELKELEAELLllklreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 735 QLKELQSQHTHCAQDLAMKDELLcqltQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQenqvah 814
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 815 lELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKE 894
Cdd:COG1196 366 -ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
....*...
gi 73623035 895 KTEQETLL 902
Cdd:COG1196 445 EEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
548-1190 |
7.33e-10 |
|
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: 63.54 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 548 DLLKKLRAKLQSLKaereearhreemalRGKDAAEIVLEAfcahaSQRISQLEQDLASMRefrglLKDAQTQLVGLHAKQ 627
Cdd:TIGR02168 193 DILNELERQLKSLE--------------RQAEKAERYKEL-----KAELRELELALLVLR-----LEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 628 EELVQQTVSLTSTLQQdwrsmqLDyTTWTALLSRSRQLTEKLTVKsQQALQErdvAIEEKQEVSRVLEQVSAQLEECKGQ 707
Cdd:TIGR02168 249 KEAEEELEELTAELQE------LE-EKLEELRLEVSELEEEIEEL-QKELYA---LANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 708 TEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDLAMKDELLCQLTQSNEEQAAQWQKEEMALkhmqAELQQ 787
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV----AQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 788 QQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTTleVLRERSLQCENLKDTVENLTAKLASTIA--DNQEQDLE 865
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEalEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 866 KTRQYSQKLGLLTEQLQSLTLFLQTKLKEK------------------------------TEQETLLLSTACPP------ 909
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLegfsegvkallknqsglsgilgvlselisvDEGYEAAIEAALGGrlqavv 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 910 ---------TQEHPLPND---RTFLgsILTAVADEEPESTPVPLLGSDKSAFTRVASMVSLQPAETPGMEESLAEMSIMT 977
Cdd:TIGR02168 552 venlnaakkAIAFLKQNElgrVTFL--PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 978 TELQSLCSLLQESKEEAIRTL-------------------------QRKICELQARLQAQEEQHQEVQKAkeadIEKLNQ 1032
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLdgdlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKA----LAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1033 ALCLRYKNEKELQEVIQQQNEKILEQidkSGELISLREEVTHLTRSLRRAETETKVLQEALAGQLDSNCQPMATNWIQEK 1112
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISAL---RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1113 VW---------LSQEVDKLRVMFLEMKNEKEKLMIKFQSHRNILEENLRRSDKELEKLDDIVQHIYKTLLSIPEVVRGCK 1183
Cdd:TIGR02168 783 EIeeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
....*..
gi 73623035 1184 ELQGLLE 1190
Cdd:TIGR02168 863 ELEELIE 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
593-903 |
1.32e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 593 SQRISQLEQDLASMREfrgLLKDAQTQLVGLHAKQEELVQQTvsltSTLQQDWRSMQLDYTTWTALLSRSRQLTEKLTVK 672
Cdd:TIGR02168 676 RREIEELEEKIEELEE---KIAELEKALAELRKELEELEEEL----EQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 673 SQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELEnsrlATDLRAQLQILanmDSQLKELQSQHTHCAQDLAM 752
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ----IEQLKEELKAL---REALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 753 KDELLcqltQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEfadqenqVAHLELGQVECQLKTTLEVLR 832
Cdd:TIGR02168 822 LRERL----ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73623035 833 ERSLQCENLKDTVENLTAKlastiADNQEQDLEKTRqysQKLGLLTEQLQSLTLFLQTKLKEKTEQETLLL 903
Cdd:TIGR02168 891 LLRSELEELSEELRELESK-----RSELRRELEELR---EKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
607-1098 |
1.57e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 607 REFRGLLKDAQTQLVGLH-----AKQEELVQQTVSLTSTLQQdwrsmqldyttwtalLSRSRQLTEKLTVKSQQALQERD 681
Cdd:COG1196 216 RELKEELKELEAELLLLKlreleAELEELEAELEELEAELEE---------------LEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 682 VAIEEKQEVSRVLEQVSAQLE-----------ECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDL 750
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEqdiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 751 AMKDELLCQLTQSNEEQAAQW---QKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTT 827
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELeelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 828 LEVLRERSLQCENLKDTVENLTAKLAST------IADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEK------ 895
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELleeaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALllaglr 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 896 -------------TEQETLLLSTACPPTQEHPLPNDRTFLGSILTAVADEEPESTPVPLLGSDKSAFTRVASMVSLQPAE 962
Cdd:COG1196 521 glagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 963 TPGMEESLAEMSIMTTELQSLcSLLQESKEEAIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEK 1042
Cdd:COG1196 601 VDLVASDLREADARYYVLGDT-LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 73623035 1043 ELQEVIQQQNEKILEQIDKSGELISLREEVTHLTRSLRRAETETKVLQEALAGQLD 1098
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
587-1172 |
4.55e-09 |
|
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: 61.14 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 587 AFCAHASQRISQLEQDLASMREFRGLLKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTALLsrsRQLT 666
Cdd:TIGR00618 156 QFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKEL---KHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 667 EKL--TVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELEN---------SRLATDLRAQLQILANMDSQ 735
Cdd:TIGR00618 233 EALqqTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 736 LKELQSQHTHCAQDLAMKDELLCQ----LTQSNEEQAAQWQKEEMALKHMQA----ELQQQQAVLAKEVRDLKETLEFAD 807
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQqssiEEQRRLLQTLHSQEIHIRDAHEVAtsirEISCQQHTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 808 QENQVAHLELGQV-ECQLKTTLEVLRERSLQC--------ENLKDTVENLTAKLASTIADNQEQDLEKTRQYSQKLGLLT 878
Cdd:TIGR00618 393 QKLQSLCKELDILqREQATIDTRTSAFRDLQGqlahakkqQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 879 EQLQSLTLFLQTKLKEKTEQETLLLStacppTQEHPLPNDRTFLGSILTAVADEEPESTPVPLLG---SDKSAFTRVASM 955
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLE-----LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqTYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 956 VSLQPAETPGMEESLAEMSIMTTELQSLCSLLQESKEEaIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALc 1035
Cdd:TIGR00618 548 YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED-IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1036 lryKNEKELQEVIQQQNEKILEQIDKSGELISL-REEVTHLTRSLRRAETETKVLQEALAGQLDSNCQPMaTNWIQEkvw 1114
Cdd:TIGR00618 626 ---DLQDVRLHLQQCSQELALKLTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMQSEKEQL-TYWKEM--- 698
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 73623035 1115 LSQEVDKLRvmflemknEKEKLMIKFQSHRNILEENLRRSDKELEKLDDIVQHIYKTL 1172
Cdd:TIGR00618 699 LAQCQTLLR--------ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL 748
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
606-1159 |
6.61e-09 |
|
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: 60.52 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 606 MREFRGLLKDAQTQLVG---LHAKQEELVQQTVSltsTLQQDWRSMQLDYTTWTALLSRSRQLTEKLTVKSQQALQERDV 682
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNEsneLHEKQKFYLRQSVI---DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 683 AIEEKQEVSR------------------VLEQVSAQL---EECKGQT--EQLELENSRLATDLRAQLQILANMDSQLKEL 739
Cdd:pfam15921 157 AKCLKEDMLEdsntqieqlrkmmlshegVLQEIRSILvdfEEASGKKiyEHDSMSTMHFRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 740 -------QSQHTHCAQDLAMKDELLCQLTQSNEEQ-AAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETlefADQENQ 811
Cdd:pfam15921 237 kgrifpvEDQLEALKSESQNKIELLLQQHQDRIEQlISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 812 VAHLELGQVECQLKTTLEVLRERSLQCEnlkDTVENLTAKLASTIADNQEQDLEKTrQYSQKLGLLTEQLQSLTLFLQTK 891
Cdd:pfam15921 314 MYMRQLSDLESTVSQLRSELREAKRMYE---DKIEELEKQLVLANSELTEARTERD-QFSQESGNLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 892 LKE---KTEQETLLLS--TACPPTQEHPLP--NDRTF----LGSILTAVADE---EPESTPVPLLGSDKSaFTRVASMVS 957
Cdd:pfam15921 390 EKElslEKEQNKRLWDrdTGNSITIDHLRRelDDRNMevqrLEALLKAMKSEcqgQMERQMAAIQGKNES-LEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 958 LQPAETPGMEESLAEMSIMTTELQS-------LCSLLQEsKEEAIRTLQRKICELQAR--LQAQEEQHQEVQKAKEADIE 1028
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESsertvsdLTASLQE-KERAIEATNAEITKLRSRvdLKLQELQHLKNEGDHLRNVQ 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1029 KLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGELI-SLREEVTHLTRSL--RRAE-TETKVLQEALAGQLdSNCQPM 1104
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQLEKEIndRRLElQEFKILKDKKDAKI-RELEAR 626
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73623035 1105 ATNWIQEKVWL-SQEVDKLRVMfLEMKNEKEKLMIKFQSHRN----------ILEENLRRSDKELE 1159
Cdd:pfam15921 627 VSDLELEKVKLvNAGSERLRAV-KDIKQERDQLLNEVKTSRNelnslsedyeVLKRNFRNKSEEME 691
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
639-1094 |
2.47e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 639 STLQQDWRSMQLDyttwtALLSRSRQL---TEKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELEN 715
Cdd:COG4717 37 STLLAFIRAMLLE-----RLEKEADELfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 716 SRLATDLRA--QLQILANMDSQLKELQSQhthcaqdLAMKDELLCQLtqsnEEQAAQWQKEEMALKHMQAELQQQQAVLA 793
Cdd:COG4717 112 EELREELEKleKLLQLLPLYQELEALEAE-------LAELPERLEEL----EERLEELRELEEELEELEAELAELQEELE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 794 KEVRDLKETLEFADQENQVAHLELGQVECQLKTTLEVLRERslqCENLKDTVENLTAKLAStiadnqEQDLEKTRQYSQK 873
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE---LEELEEELEQLENELEA------AALEERLKEARLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 874 LGLLTEQLQSLTLFLQTKLKEKTEQETLLLSTACPPTQEHPLPNDRTFLGSILTAVADEEPEStpvpllGSDKSAFTRVA 953
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE------ELEEEELEELL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 954 SMVSLQPAETPgmeeslaemsimtTELQSLCSLLQEskeeaIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQ- 1032
Cdd:COG4717 326 AALGLPPDLSP-------------EELLELLDRIEE-----LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEl 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73623035 1033 -ALCLRYKNEKELQEVIQQQNEKILEQIDKSGELI------SLREEVTHLTRSLRRAETETKVLQEALA 1094
Cdd:COG4717 388 rAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeeELEEELEELEEELEELEEELEELREELA 456
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
672-1149 |
1.02e-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: 56.27 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 672 KSQQALQERDVAIEEKQ-EVSRVLEQVSAQ----------LEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQ 740
Cdd:pfam05483 223 KIQHLEEEYKKEINDKEkQVSLLLIQITEKenkmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 741 -------SQHTHCAQDLAMKDELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVA 813
Cdd:pfam05483 303 mslqrsmSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKII 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 814 HLELGQVECQLKTTLEVLRERSLQCENLKdtvenltaklasTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLK 893
Cdd:pfam05483 383 TMELQKKSSELEEMTKFKNNKEVELEELK------------KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 894 EKTEQETLLlsTACPPTQEHPLPNdrtfLGSILTAVADEEPESTPVpllgsdksafTRVASMVSLQPaetpgmEESLAEM 973
Cdd:pfam05483 451 EIHDLEIQL--TAIKTSEEHYLKE----VEDLKTELEKEKLKNIEL----------TAHCDKLLLEN------KELTQEA 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 974 SIMTTELQSLCSLLQESKEEAIRTLqRKICELQarlQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNE 1053
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERML-KQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1054 KILEQIDKSGELISLREEVTHLTRSLRRAETETKVLQEalagqlDSNCQPMATNWIQEKV-WLSQEVDKLRVMFLEMKNE 1132
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK------KGSAENKQLNAYEIKVnKLELELASAKQKFEEIIDN 658
|
490
....*....|....*...
gi 73623035 1133 KEK-LMIKFQSHRNILEE 1149
Cdd:pfam05483 659 YQKeIEDKKISEEKLLEE 676
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
988-1193 |
1.61e-06 |
|
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: 52.75 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 988 QESKEEAIRTLQRKICELQARLQAQEEQHQEVQK---AKEADIEKLNQALCLRYKNEKELQEVIQQQNEKI---LEQIDK 1061
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEeleSLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIAS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1062 -SGELISLREEVTHLTRSLRRAETETKVLQEALAgqldsncqpmatnwiqekvwlSQEVDKLRVMFLEMKNEKEKLmikf 1140
Cdd:TIGR02168 398 lNNEIERLEARLERLEDRRERLQQEIEELLKKLE---------------------EAELKELQAELEELEEELEEL---- 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 73623035 1141 QSHRNILEENLRRSDKELEKLDDIVQHIYKTLLSIPEVVRGCKELQGLLEFLS 1193
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
671-899 |
2.63e-06 |
|
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: 51.99 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 671 VKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQL-----------ELENSRLATDLRAQLQILANMDSQLKEL 739
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqallkekrEYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 740 Q---SQHTHCAQDLAMK-DELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVAHL 815
Cdd:TIGR02169 250 EeelEKLTEEISELEKRlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 816 ELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQD------LEKTRQYSQKLGLLTEQLQSLTLFLQ 889
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaetRDELKDYREKLEKLKREINELKRELD 409
|
250
....*....|
gi 73623035 890 TKLKEKTEQE 899
Cdd:TIGR02169 410 RLQEELQRLS 419
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
594-1163 |
2.86e-06 |
|
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: 51.76 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 594 QRISQLEQDLASMREFRGLLKDAQTQLVGLH----AKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTALLSRSRQLTEKL 669
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQeerqETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 670 TVKSQQALQERdvaieekqevsrvLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQhthCAQD 749
Cdd:pfam12128 328 EDQHGAFLDAD-------------IETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ---NNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 750 LAMKDEllcQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVaHLELGQVECQLKTTLE 829
Cdd:pfam12128 392 IAGIKD---KLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKL-RLNQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 830 VLRERslqCENLKDTVENLTAKL---------ASTIADNQEQDLEKTRQYSQKLGLLTEQLQ--------SLTLFLQTKL 892
Cdd:pfam12128 468 NFDER---IERAREEQEAANAEVerlqselrqARKRRDQASEALRQASRRLEERQSALDELElqlfpqagTLLHFLRKEA 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 893 KEKTEQETLLLSTAC-------PPTQEHPLPNDRTFLGSILTAVADEEPESTPV------------PLLGSDKSAFTRVA 953
Cdd:pfam12128 545 PDWEQSIGKVISPELlhrtdldPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASeeelrerldkaeEALQSAREKQAAAE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 954 SMVSLQPAEtpgMEESLAEMSI--------------MTTELQSLCSLLQESKEEAIRTLQRKICELQARLQAQEEQHQ-- 1017
Cdd:pfam12128 625 EQLVQANGE---LEKASREETFartalknarldlrrLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQaw 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1018 --------------------EVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGELIS-LREEVTHLT 1076
Cdd:pfam12128 702 leeqkeqkreartekqaywqVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAkLKREIRTLE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1077 RSLRRAET-ETKVLQEAlagqldsncQPMATNWIQEKVWLSQEVDKLRVMFLEMKNEKEKLMIKFQSHRNILEENLRRSD 1155
Cdd:pfam12128 782 RKIERIAVrRQEVLRYF---------DWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASE 852
|
....*...
gi 73623035 1156 KELEKLDD 1163
Cdd:pfam12128 853 KQQVRLSE 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
657-853 |
3.01e-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: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 657 ALLSRSRQLTEKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEEckgQTEQLELENSRLATDLRAQLQILANM---- 732
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 733 -----DSQLKELQSQHThcAQDLAMKDELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFAD 807
Cdd:COG4942 114 yrlgrQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 73623035 808 QENQVAHLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLA 853
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
587-898 |
5.52e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 587 AFCAHASQRISQLEQDLasmrEFRGLLKDAQTQLVGLHAKQEELVQQTVSLT---STLQQDWRSMqldyTTWTALLSRSR 663
Cdd:COG3096 272 DYMRHANERRELSERAL----ELRRELFGARRQLAEEQYRLVEMARELEELSareSDLEQDYQAA----SDHLNLVQTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 664 QLTEKLtVKSQQALQERDVAIEEKQEVsrvLEQVSAQLEECKGQTEQLELENSRLATDLrAQLQilanmdsqlKELQSQH 743
Cdd:COG3096 344 RQQEKI-ERYQEDLEELTERLEEQEEV---VEEAAEQLAEAEARLEAAEEEVDSLKSQL-ADYQ---------QALDVQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 744 T-----HCAQDLAMKDELLCQLTQSNEEQAAQWqkeemalkhmQAELQQQQAVLAKEVRDLKETLEFADQ-ENQVAH-LE 816
Cdd:COG3096 410 TraiqyQQAVQALEKARALCGLPDLTPENAEDY----------LAAFRAKEQQATEEVLELEQKLSVADAaRRQFEKaYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 817 L-----GQVECQ--LKTTLEVLRE-RSLQceNLKDTVENLTAKLA--STIADNQEQDLEKTRQYSQKLGL---LTEQLQS 883
Cdd:COG3096 480 LvckiaGEVERSqaWQTARELLRRyRSQQ--ALAQRLQQLRAQLAelEQRLRQQQNAERLLEEFCQRIGQqldAAEELEE 557
|
330
....*....|....*
gi 73623035 884 LTLFLQTKLKEKTEQ 898
Cdd:COG3096 558 LLAELEAQLEELEEQ 572
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
598-819 |
1.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 598 QLEQDLASMREFRGLLKDAQTQLVGLhAKQEELVQQTVSLTSTLQQDWRS-MQLDY-----TTWTALLSRS--RQLTEKL 669
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA-REQIELLEPIRELAERYAAARERlAELEYlraalRLWFAQRRLEllEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 670 TVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQT-EQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQ 748
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73623035 749 DLAmkdellcqltqsneEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKEtlEFADQENQVAHLELGQ 819
Cdd:COG4913 381 EFA--------------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRR--ELRELEAEIASLERRK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
693-897 |
1.83e-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: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 693 VLE--QVSAQLEECKGQTEQLElENSRLATDLRAQLQILAnmdsQLKELQSQHTHCAQDLAMKDELLCQLTQSNEEQAAQ 770
Cdd:COG4913 217 MLEepDTFEAADALVEHFDDLE-RAHEALEDAREQIELLE----PIRELAERYAAARERLAELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 771 -WQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEfadqENQVAHLELG-----QVECQLKTTLEVLRERSLQCENLKDT 844
Cdd:COG4913 292 lLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQIRGNGgdrleQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 73623035 845 VENLTAKLASTIAD---NQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEKTE 897
Cdd:COG4913 368 LAALGLPLPASAEEfaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
658-882 |
2.20e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 658 LLSRSRQLTEKLTVKSQQALQERDVAIEEKQEvsrVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLK 737
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEK---ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 738 ELQSQHTHCAQDLAMKDELLCQLTQS--------------NEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETL 803
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73623035 804 EFADQENQvahlelgqvecQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQdLEKTRQYSQKLGLLTEQLQ 882
Cdd:COG4942 167 AELEAERA-----------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-LAELQQEAEELEALIARLE 233
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
658-884 |
2.44e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 658 LLSRSRQLTEKltvkSQQALQERDVAieekQEVSRVLEQVSAQLEECKgqteqlelensRLATDLRAQLQILANMDSQLK 737
Cdd:PRK10929 111 ILQVSSQLLEK----SRQAQQEQDRA----REISDSLSQLPQQQTEAR-----------RQLNEIERRLQTLGTPNTPLA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 738 ELQ--SQHTHCAQDLAMKDEL-LCQLTQSNEEQaaqwqkeemaLKHMQAEL-QQQQAVLAKEVRDLKETLEFADQ---EN 810
Cdd:PRK10929 172 QAQltALQAESAALKALVDELeLAQLSANNRQE----------LARLRSELaKKRSQQLDAYLQALRNQLNSQRQreaER 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73623035 811 QVAHLEL-----GQVECQLKTTLEVLRERSlqcenlkdTVENLTAKLASTIADNQEQDLEKTRQYSQKLGLLTEQLQSL 884
Cdd:PRK10929 242 ALESTELlaeqsGDLPKSIVAQFKINRELS--------QALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQWL 312
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
816-1062 |
3.06e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 816 ELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIA--DNQEQDLEKTRQysqKLGLLTEQLQSLtlflQTKLK 893
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARriRALEQELAALEA---ELAELEKEIAEL----RAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 894 EKTEQetlllstacpptqehplpndrtfLGSILTAVADEEPESTPVPLLGSDksAFTRVASMVSLQPAETPGMEESLAEM 973
Cdd:COG4942 101 AQKEE-----------------------LAELLRALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 974 SIMTTELQSLCSLLQESKEEaIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNE 1053
Cdd:COG4942 156 RADLAELAALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*....
gi 73623035 1054 KILEQIDKS 1062
Cdd:COG4942 235 EAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
548-796 |
3.28e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 548 DLLKKLRAKLQSLKAEREEARHREEMALRGKDAAEIVLEAfcahASQRISQLEQDLasmREFRGLLKDAQTQLVGLHAKQ 627
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRI---RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 628 EELVQQTVSLTSTLQQDWRSMQLdyttwtallsRSRQLTEKLTVKSQQALQerdvaieekqeVSRVLEQVSAQLEECKGQ 707
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYR----------LGRQPPLALLLSPEDFLD-----------AVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 708 TEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDLAMKDELLCQLTQ---SNEEQAAQWQKEEMALKHMQAE 784
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKelaELAAELAELQQEAEELEALIAR 231
|
250
....*....|..
gi 73623035 785 LQQQQAVLAKEV 796
Cdd:COG4942 232 LEAEAAAAAERT 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
549-1139 |
4.18e-05 |
|
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: 48.04 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 549 LLKKLRAKLQSLKAEREEARHREEMALRGKDAAEIVLEAfcAHASQRISQLEQDLASMREFRGLLKDAQTQLVGLHAKQE 628
Cdd:TIGR00618 261 LLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 629 ELVQQTVSLTSTLQQDWRSMQL--DYTTWTALLSRSRQLTEKLTVKSQQalqerdvaIEEKQEVSRVLEQVSAQLEECKG 706
Cdd:TIGR00618 339 SIEEQRRLLQTLHSQEIHIRDAheVATSIREISCQQHTLTQHIHTLQQQ--------KTTLTQKLQSLCKELDILQREQA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 707 QTEQLELENSRLATDL-RAQLQILANMdsQLKELQSQHTHC-AQDLAMKDELLCQLTQSNEEQAAQWQKEEMALK----- 779
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLaHAKKQQELQQ--RYAELCAAAITCtAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLqetrk 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 780 -----HMQAELQQQQAVLAKEVRDLKETLEFADQ-----------ENQVAHLE--LGQVECQLKTTLEVLRERSLQCENL 841
Cdd:TIGR00618 489 kavvlARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrrmqrgEQTYAQLEtsEEDVYHQLTSERKQRASLKEQMQEI 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 842 KDTVENLTAKL--ASTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEKT------------EQETLLLSTAC 907
Cdd:TIGR00618 569 QQSFSILTQCDnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqdvrlhlqqcSQELALKLTAL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 908 PPTQEHpLPNDRTFLGSILTAVADEEpestpvpLLGSDKSAFTRVASMVSLQPAETPGMEESLAEMSIMTTELQSLCSLL 987
Cdd:TIGR00618 649 HALQLT-LTQERVREHALSIRVLPKE-------LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 988 QE---SKEEAIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGE 1064
Cdd:TIGR00618 721 NEienASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL 800
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73623035 1065 LISLREEVthlTRSLRRAETETKVLQEALAGQLDSncqpmATNWIQEKVWLSQEVDKLRVMFLEMKNEKEKLMIK 1139
Cdd:TIGR00618 801 LKTLEAEI---GQEIPSDEDILNLQCETLVQEEEQ-----FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE 867
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
646-943 |
5.54e-05 |
|
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: 47.76 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 646 RSMQLDYTTWTALLSRSRQLTEKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLAtdlraq 725
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK------ 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 726 lQILANMDSQLKELQSQHTHCAQDLAMKDELLCQLtqsnEEQAAQWQKEEMALKHMQA-----ELQQQQAVLAKEVRDLK 800
Cdd:TIGR02169 737 -ERLEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 801 ETLEFADQENQVAHLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTiadnqEQDLEKT----RQYSQKLGL 876
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-----EEELEELeaalRDLESRLGD 886
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73623035 877 LTEQLQSLTLFL------QTKLKEKTEQETLLLStacppTQEHPLPNDRTFLGSILTAVADEEPESTPVPLLG 943
Cdd:TIGR02169 887 LKKERDELEAQLrelerkIEELEAQIEKKRKRLS-----ELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
613-1164 |
9.07e-05 |
|
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: 46.89 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 613 LKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTALLSRSRQLTEKLTVKSQQALQERDVAIEEKQEVSR 692
Cdd:pfam02463 266 KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 693 VLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDLAMKDELLCQLTQSNEEQAAQWQ 772
Cdd:pfam02463 346 ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 773 KEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQvahLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKL 852
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE---LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 853 astIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEKTEQETL--LLSTACPPTQEHPLPNDRTFLGSILTA-V 929
Cdd:pfam02463 503 ---SKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAviVEVSATADEVEERQKLVRALTELPLGArK 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 930 ADEEPESTPVPLLGSDKSAFTRVASMVSLQPAETPGMEESLAEMSIMTTELQSLCSLLQESKEEAIRTLQRKICELQARL 1009
Cdd:pfam02463 580 LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLA 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1010 qaqEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGELISLREEVTHL-----TRSLRRAET 1084
Cdd:pfam02463 660 ---EKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELladrvQEAQDKINE 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1085 ETKVLQ----------EALAGQLDSNCQPMATNWIQEKVWLSQEVDKLRVMFLEMKNEKEKLMIK----FQSHRNILEEN 1150
Cdd:pfam02463 737 ELKLLKqkideeeeeeEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEelraLEEELKEEAEL 816
|
570
....*....|....
gi 73623035 1151 LRRSDKELEKLDDI 1164
Cdd:pfam02463 817 LEEEQLLIEQEEKI 830
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
585-832 |
1.29e-04 |
|
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: 46.60 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 585 LEAFCAHASQRISQLEQDLASMREFRGLLKDAQTQLVG-LHAKQEELVQQTVSLT----STLQQDWRSMQLDYTTWTALL 659
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEArIEELEEDLHKLEEALNdleaRLSHSRIPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 660 SRSRQLTEKLTVKSQQALQERDVAIEEKQEVSRvleqvsaQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKEL 739
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 740 QSQHTHCAQDLAMKDELLCQLTQSNEEQAAQWQKeemaLKHMQAELQQQQAVLAKEVRDLkETLEFADQENQVAHLELGQ 819
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEK----KRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLED 955
|
250
....*....|...
gi 73623035 820 VECQLKTTLEVLR 832
Cdd:TIGR02169 956 VQAELQRVEEEIR 968
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
597-826 |
1.97e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 597 SQLEQDLASMREFRGLLKDAQTQLVGLHAKQEelvqqtvslTSTLQQDWRSMQldytTWTALLSRSRQLTEKLTVKSQQA 676
Cdd:PRK10246 257 QEASRRQQALQQALAAEEKAQPQLAALSLAQP---------ARQLRPHWERIQ----EQSAALAHTRQQIEEVNTRLQST 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 677 LQER----DVAIEEKQEVSRVLEQVSAQLEEckgqTEQLELENSRLAtDLRAQLQILANMDSQLKELQSQHTHCAQDLAM 752
Cdd:PRK10246 324 MALRarirHHAAKQSAELQAQQQSLNTWLAE----HDRFRQWNNELA-GWRAQFSQQTSDREQLRQWQQQLTHAEQKLNA 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73623035 753 KDELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKT 826
Cdd:PRK10246 399 LPAITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKE 472
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
714-1161 |
2.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 714 ENSRLATDLRAQLqilANMDSQLKELQSQHTHCAQDLAMKDELLCQLTQsnEEQAAqwqKEEMALkhMQAELQQQQAvLA 793
Cdd:PRK04863 283 VHLEEALELRREL---YTSRRQLAAEQYRLVEMARELAELNEAESDLEQ--DYQAA---SDHLNL--VQTALRQQEK-IE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 794 KEVRDLKETLEFADQENQVahlelgqvecqlkttLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQ-DLEKTR--QY 870
Cdd:PRK04863 352 RYQADLEELEERLEEQNEV---------------VEEADEQQEENEARAEAAEEEVDELKSQLADYQQAlDVQQTRaiQY 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 871 SQKLGLLTE-----QLQSLTL-----FLQTkLKEKTEQETLLLSTAcpptqEHPLpndrtflgsiltAVADEEpestpvp 940
Cdd:PRK04863 417 QQAVQALERakqlcGLPDLTAdnaedWLEE-FQAKEQEATEELLSL-----EQKL------------SVAQAA------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 941 llgsdKSAFTRVASMVSlqpAETPGMEESLAEMSimtteLQSLCSLLQESKEEAIRTLQrkiceLQARLQAQEEQHQEVQ 1020
Cdd:PRK04863 472 -----HSQFEQAYQLVR---KIAGEVSRSEAWDV-----ARELLRRLREQRHLAEQLQQ-----LRMRLSELEQRLRQQQ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1021 KAKEAdIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGELISLREEVTH-------LTRSLRRAETETKVLQEAL 1093
Cdd:PRK04863 534 RAERL-LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQqleqlqaRIQRLAARAPAWLAAQDAL 612
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73623035 1094 AgQLDSNCqpmatnwiQEKVWLSQEVDKLRVMFLEmkNEKEklmikFQSHRNILEENLRRSDKELEKL 1161
Cdd:PRK04863 613 A-RLREQS--------GEEFEDSQDVTEYMQQLLE--RERE-----LTVERDELAARKQALDEEIERL 664
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
783-1096 |
2.26e-04 |
|
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: 45.43 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 783 AELQQQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQ 862
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 863 DLEKTrqysqklgLLTEQLQSLTLFLQTKLKEKTEQETLLLSTAcpptqehplpNDRTFLGSILTAVADEepestpvplL 942
Cdd:TIGR02168 760 EAEIE--------ELEERLEEAEEELAEAEAEIEELEAQIEQLK----------EELKALREALDELRAE---------L 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 943 GSDKSAFTRVASmvslqpaetpGMEESLAEMSIMTTELQSLCSLLqESKEEAIRTLQRKICELQARLQAQEEQHQEVQKA 1022
Cdd:TIGR02168 813 TLLNEEAANLRE----------RLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73623035 1023 KEADIEKLNQAlclryknEKELQEVIQQQNEKILEQIDKSGELISLREEVTHLTRSLRRAETETKVLQEALAGQ 1096
Cdd:TIGR02168 882 RASLEEALALL-------RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
674-884 |
2.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 674 QQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLElensrlatDLRAQLQILANMDSQLKELQSQHTHCAQdlamK 753
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ--------ERREALQRLAEYSWDEIDVASAEREIAE----L 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 754 DELLCQLTQSNEEqaaqwqkeemaLkhmqAELQQQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTTLEVLRE 833
Cdd:COG4913 674 EAELERLDASSDD-----------L----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 73623035 834 RSLQCEnlKDTVENLTAKLASTIADNQEQDLEktRQYSQKLGLLTEQLQSL 884
Cdd:COG4913 739 AEDLAR--LELRALLEERFAAALGDAVERELR--ENLEERIDALRARLNRA 785
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
967-1192 |
2.96e-04 |
|
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: 45.05 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 967 EESLAEMSIMTTELQSLCSLLQESKEEAIRtLQRKICELQARLQAQEEQHQEVQKAKEADIEKLN--QALCLRYKNE--- 1041
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEELRLEVSELEEEIEelQKELYALANEisr 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1042 KELQEVIQQQNEKILEQIDKSGELISLREE--VTHLTRSLRRAETETKVLQ---EALAGQLDS--NCQPMATNWIQEkvw 1114
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELEskLDELAEELAELEEKLEELKeelESLEAELEEleAELEELESRLEE--- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1115 LSQEVDKLRVMFLEMKNEKEKLMIKFQ---SHRNILEENLRRSDKELEKLDDIVQHIYKTLLS--IPEVVRGCKELQGLL 1189
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIErleARLERLEDRRERLQQEIEELLKKLEEAELKELQaeLEELEEELEELQEEL 456
|
...
gi 73623035 1190 EFL 1192
Cdd:TIGR02168 457 ERL 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
978-1192 |
4.04e-04 |
|
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: 44.67 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 978 TELQSLCSLLQEsKEEAIRTLQRKICELQARL------------QAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQ 1045
Cdd:TIGR02169 758 SELKELEARIEE-LEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1046 EvIQQQNEKILEQIDksgeliSLREEVTHLTRSLRRAETETKVLQEALAgQLDSncqpmatnwiqEKVWLSQEVDKLRVM 1125
Cdd:TIGR02169 837 E-LQEQRIDLKEQIK------SIEKEIENLNGKKEELEEELEELEAALR-DLES-----------RLGDLKKERDELEAQ 897
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73623035 1126 FLEMKNEKEKLMIKFQSHRNILE------ENLRRSDKELEKLDDIVQHIYKTLLSIPEVVRGCKELQGLLEFL 1192
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSelkaklEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
594-1094 |
4.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 594 QRISQLEQDLASMREFRGLLKDAQTQLVGLHAKQEELVQQtvslTSTLQQDWRSMqldyttwtallsrsrqltekltvks 673
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKL------------------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 674 QQALQERDvAIEEKQEVSRVLEQVSAQLEEckgqteqlelensrlatdLRAQLQILANMDSQLKELQSQHTHCAQDLamk 753
Cdd:COG4717 122 EKLLQLLP-LYQELEALEAELAELPERLEE------------------LEERLEELRELEEELEELEAELAELQEEL--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 754 DELLCQLTQSNEEQAAQWQKEemalkhmQAELQQQQAVLAKEVRDLKETLEfaDQENQVAHLELGQVECQLKTTLEVLRe 833
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEE-------LEELQQRLAELEEELEEAQEELE--ELEEELEQLENELEAAALEERLKEAR- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 834 rslqcenlkdtvenLTAKLASTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEKTEQETLLLSTACPPTQEh 913
Cdd:COG4717 250 --------------LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 914 plpndrtflgSILTAVADEEPESTPVPLLGSDKSAFTRVASMVSLQPAETpGMEESLAEMSIMT--TELQSLCSLLQESK 991
Cdd:COG4717 315 ----------ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEEleQEIAALLAEAGVED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 992 EEAIrtlqRKICELQARLQAQEEQHQEVQKAKEADIEKLNQAlcLRYKNEKELQEVIQQQNEKILEqidKSGELISLREE 1071
Cdd:COG4717 384 EEEL----RAALEQAEEYQELKEELEELEEQLEELLGELEEL--LEALDEEELEEELEELEEELEE---LEEELEELREE 454
|
490 500
....*....|....*....|...
gi 73623035 1072 VTHLTRSLRRAETETKvLQEALA 1094
Cdd:COG4717 455 LAELEAELEQLEEDGE-LAELLQ 476
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
599-1136 |
6.51e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 599 LEQDLASMREFRGLLKDAQTQLVGLhaKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTALLSRSRQLTEKLTVKSQQALQ 678
Cdd:COG5022 798 KLQPLLSLLGSRKEYRSYLACIIKL--QKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQ 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 679 ERDVA----IEEKQEVSRV--LEQVSAQLE----ECKGQTEQLELENSRLATDLRAQLQ-ILANMDS---------QLKE 738
Cdd:COG5022 876 RVELAerqlQELKIDVKSIssLKLVNLELEseiiELKKSLSSDLIENLEFKTELIARLKkLLNNIDLeegpsieyvKLPE 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 739 LQSQHTHCAQ----------DLAMKDELLCQLTQSNEE-------------QAAQWQKEEMALKHMQ---AELQQQQAVL 792
Cdd:COG5022 956 LNKLHEVESKlketseeyedLLKKSTILVREGNKANSElknfkkelaelskQYGALQESTKQLKELPvevAELQSASKII 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 793 AKEVRDLKETLEFADQENQVAhLELGQVECQLKtTLEVLRERSL----QCENLKDTvENLTAKLASTIADNQEQDLEKTR 868
Cdd:COG5022 1036 SSESTELSILKPLQKLKGLLL-LENNQLQARYK-ALKLRRENSLlddkQLYQLEST-ENLLKTINVKDLEVTNRNLVKPA 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 869 QYSQ-------KLGLLTEQLQSLTLFLQT--KLKEKTEQETLLLSTACPPTQEHPLPNDRTFLG---SILTAVA--DEEP 934
Cdd:COG5022 1113 NVLQfivaqmiKLNLLQEISKFLSQLVNTlePVFQKLSVLQLELDGLFWEANLEALPSPPPFAAlseKRLYQSAlyDEKS 1192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 935 ESTPVPLlgsdKSAFTRVASMVSLQPAETP---GMEESLAEMSIMTTELQSLCSLLQESKEEA------IRTLQRKICEL 1005
Cdd:COG5022 1193 KLSSSEV----NDLKNELIALFSKIFSGWPrgdKLKKLISEGWVPTEYSTSLKGFNNLNKKFDtpasmsNEKLLSLLNSI 1268
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1006 QARLQAQEEQ--------HQEVQ-----------------KAKEADIEKLNQALCLRYKNEKELQEViQQQNEKILE--- 1057
Cdd:COG5022 1269 DNLLSSYKLEeevlpatiNSLLQyinvglfnalrtkasslRWKSATEVNYNSEELDDWCREFEISDV-DEELEELIQavk 1347
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1058 --QIDKSG-----ELISLREEVTHLTRS-----LRRAETETKVLQEALAGqldsncqpMATNWIQEKVWLSQEV-DKLRV 1124
Cdd:COG5022 1348 vlQLLKDDlnkldELLDACYSLNPAEIQnlksrYDPADKENNLPKEILKK--------IEALLIKQELQLSLEGkDETEV 1419
|
650
....*....|..
gi 73623035 1125 MFLEMKNEKEKL 1136
Cdd:COG5022 1420 HLSEIFSEEKSL 1431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
694-902 |
6.74e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 694 LEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDLAMKDEllcQLTQSNEEQAAqwqk 773
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 774 eemalkhMQAELQQQQAVLAKEVRDL-----KETLEF---ADQENQVAHLE--LGQVECQLKTTLEVLRERSLQCENLKD 843
Cdd:COG4942 95 -------LRAELEAQKEELAELLRALyrlgrQPPLALllsPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 73623035 844 TVENLTAKLASTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLfLQTKLKEKTEQETLL 902
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE-LAAELAELQQEAEEL 225
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
967-1166 |
1.28e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 967 EESLAEMSIMTTELQSLCSLLQESKEEAIRTLQRKICELQARLQAQEEQhQEVQKAKEADIEKLNQALCLRYKNEKELQE 1046
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1047 VIQQQNEKILEQIDKSGELISLREEVTHLTRSLRRAETETKVLQEALAGQLDSncqpmATNWIQEKVWLSQEVDKLRVMF 1126
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-----LAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 73623035 1127 LEMKNEKEKLMIKFQSHRNILEENLRRSDKELEKLDDIVQ 1166
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
632-1093 |
1.70e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 632 QQTVSLTSTLQQDWRSMQLDYTTwtaLLSRSRQLTEKLTVKsQQALQERDVAIEEKQEVsrvLEQVSAQLEECKGQTE-- 709
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISE---LKKQNNQLKDNIEKK-QQEINEKTTEISNTQTQ---LNQLKDEQNKIKKQLSek 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 710 QLELE-NSRLATDLRAQLQilaNMDSQLKELQSQHthcAQDL--AMKDELlcqltQSNEEQAAQWQKEemalkhmQAELQ 786
Cdd:TIGR04523 273 QKELEqNNKKIKELEKQLN---QLKSEISDLNNQK---EQDWnkELKSEL-----KNQEKKLEEIQNQ-------ISQNN 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 787 QQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQDLEK 866
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 867 TRQYSQKLGLLTEQ--LQSLTLFLQTKLKEKTEQETLL--LSTACPPTQEHPLPNDRTFLGSILTAVADEEpestpvpll 942
Cdd:TIGR04523 415 KKLQQEKELLEKEIerLKETIIKNNSEIKDLTNQDSVKelIIKNLDNTRESLETQLKVLSRSINKIKQNLE--------- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 943 gSDKSAFTRVASMVSLQPAETPGMEESLAEM----SIMTTELQSLCSLLQEsKEEAIRTLQRKICELQARLQAQ--EEQH 1016
Cdd:TIGR04523 486 -QKQKELKSKEKELKKLNEEKKELEEKVKDLtkkiSSLKEKIEKLESEKKE-KESKISDLEDELNKDDFELKKEnlEKEI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1017 QEVQKakeaDIEKLNQALCLRYKNEKELQEVIQQQNEKILE---QIDKSGELIS-LREEVTHLTRSLRRAETETKVLQEA 1092
Cdd:TIGR04523 564 DEKNK----EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlikEIEEKEKKISsLEKELEKAKKENEKLSSIIKNIKSK 639
|
.
gi 73623035 1093 L 1093
Cdd:TIGR04523 640 K 640
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
967-1193 |
1.76e-03 |
|
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: 42.75 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 967 EESLAEMSIMTTELQSLCSLLQESKEEAIR--TLQRKICE-----LQARLQAQEEQHQEVQK---AKEADIEKLNQALCL 1036
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREyegyeLLKEKEALERQKEAIERqlaSLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1037 RYKNEKELQEVIQQQNEKILEQidKSGELISLREEVTHLT---RSLRRAETETKVLQEALAGQLdsncqpmaTNWIQEKV 1113
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEaeiASLERSIAEKERELEDAEERL--------AKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1114 WLSQEVDKLRVMFLEMKNEKEKLMIKFQSHRNILEENLRRS---DKEL----EKLDDIVQHIYKTLLSIPEVVRGCKELQ 1186
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevDKEFaetrDELKDYREKLEKLKREINELKRELDRLQ 412
|
....*..
gi 73623035 1187 GLLEFLS 1193
Cdd:TIGR02169 413 EELQRLS 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
941-1160 |
2.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 941 LLGSDKSAFTRVASMVSLQPAETPGMEESLAEMSIMTTELQSLCSLLQESK-------------EEAIRTLQRKICELQA 1007
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEkeleslegskrklEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1008 RLQAQEEQHQEVQKAKEAD------IEKLNQALCLRYKNEKELQEVIQQQN---EKILEQIDKSGELISLREEVTHLTRS 1078
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAeeyiklSEFYEEYLDELREIEKRLSRLEEEINgieERIKELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1079 LRRAETETKVLQEALA--GQLDSncqpmatnwiQEKVWLSQEVDKLRVMFLEMKNEKEKLMIKFqshRNILEE--NLRRS 1154
Cdd:PRK03918 354 LEELEERHELYEEAKAkkEELER----------LKKRLTGLTPEKLEKELEELEKAKEEIEEEI---SKITARigELKKE 420
|
....*.
gi 73623035 1155 DKELEK 1160
Cdd:PRK03918 421 IKELKK 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
613-873 |
2.98e-03 |
|
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: 41.98 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 613 LKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQldyttwtALLSRSRQLTEKLTVKSQqalqERDVAIEEK-QEVS 691
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIKDLGE----EEQLRVKEKiGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 692 RVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCA---QDLAMKDELLCQLTQSNEEQA 768
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTeeyAELKEELEDLRAELEEVDKEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 769 AQW-------QKEEMALKHMQAELQQQQAVLAKEVRDLKEtlEFADQENQVAHLELGQVEcqLKTTLEVLRER-SLQCEN 840
Cdd:TIGR02169 381 AETrdelkdyREKLEKLKREINELKRELDRLQEELQRLSE--ELADLNAAIAGIEAKINE--LEEEKEDKALEiKKQEWK 456
|
250 260 270
....*....|....*....|....*....|....*....
gi 73623035 841 LKDTVENLTA------KLASTIADNQEQDLEKTRQYSQK 873
Cdd:TIGR02169 457 LEQLAADLSKyeqelyDLKEEYDRVEKELSKLQRELAEA 495
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
988-1086 |
3.24e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 988 QESKEEAIRTLQRKICELQA-RLQAQEEQHQEVQ------KAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQID 1060
Cdd:COG0542 406 IDSKPEELDELERRLEQLEIeKEALKKEQDEASFerlaelRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|....*.
gi 73623035 1061 KSGELISLREEVTHLTRSLRRAETET 1086
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLLREE 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
659-865 |
3.99e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 659 LSRSRQLTEKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKE 738
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 739 -----------LQSQHThcaQDLAMKDELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFAD 807
Cdd:COG3883 98 sggsvsyldvlLGSESF---SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 73623035 808 QENQVAHLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQDLE 865
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
989-1099 |
4.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 989 ESKEEAIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGELISL 1068
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110
....*....|....*....|....*....|.
gi 73623035 1069 REEVTHLTRSLRRAETETKVLQEALAGQLDS 1099
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
991-1166 |
5.17e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 991 KEEAIRTLQRKICELQARL-----QAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKiLEQIDKSGEL 1065
Cdd:pfam02463 181 ETENLAELIIDLEELKLQElklkeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE-QEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1066 ISLREEVTHLTRSLRRAETETKVLQEALAGQLDSNCQPMATNWIQEKV-----------------WLSQEVDKLRVMFLE 1128
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrkvddeeklkesekekkKAEKELKKEKEEIEE 339
|
170 180 190
....*....|....*....|....*....|....*...
gi 73623035 1129 MKNEKEKLMIKFQSHRNILEENLRRSDKELEKLDDIVQ 1166
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
681-904 |
5.43e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 681 DVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLATDLRAqlqilanMDSQLKELQSQHTHCAQDLamkdELLCQL 760
Cdd:pfam10174 264 LLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLA-------LQTKLETLTNQNSDCKQHI----EVLKES 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 761 TQSNEEQAAQWQKEEMAL---------------KHMQaELQQQQAVLAKEVRDLKETLEFADQENQVAHLelgqvecQLK 825
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALrlrleekesflnkktKQLQ-DLTEEKSTLAGEIRDLKDMLDVKERKINVLQK-------KIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 826 TTLEVLRERSLQCENLKDTVENLT----------AKLASTIADN-------QEQDLEKTRQYSQKLGLLTEQLQSLTLFL 888
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQtdssntdtalTTLEEALSEKeriierlKEQREREDRERLEELESLKKENKDLKEKV 484
|
250
....*....|....*.
gi 73623035 889 QTKLKEKTEQETLLLS 904
Cdd:pfam10174 485 SALQPELTEKESSLID 500
|
|
| DUF4527 |
pfam15030 |
Protein of unknown function (DUF4527); This family of proteins is functionally uncharacterized. ... |
987-1098 |
5.54e-03 |
|
Protein of unknown function (DUF4527); This family of proteins is functionally uncharacterized. This family of proteins is found in vertebrates.
Pssm-ID: 464456 Cd Length: 277 Bit Score: 40.18 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 987 LQESKEEA--------IRTLQRKICELQARLQAQEEQHQEVQKAkeadiekLNQALCLRYKNEKELQEVIQQQNEKILEQ 1058
Cdd:pfam15030 2 LQDTEAEApeedlrlrVRQLHHQVLTLQCQLRDQASAHRELQAS-------RDEAGRLRDQLQGKLEELQKKQHEANLAV 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 73623035 1059 IDKSGELISL----REE---VTHLTRSLRRAETETKVLQEALAGQLD 1098
Cdd:pfam15030 75 TPLKAKLASLvqkcRERnhlITHLLQELHRHGAENHLLSETAQSMVD 121
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
988-1166 |
5.99e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 988 QESKEEAIRTLQRKICELQARLQAQEEQHQEVQKakeaDIEKLNQALclrykneKELQEVIQQQNEKILEqidksgelis 1067
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRI-------AALARRIRALEQELAA---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 1068 LREEVTHLTRSLRRAETETKVLQEALAGQLDSNCQPMATNWIqeKVWLSQE----VDKLRVMFLEMKNEKEKLMIKFQSH 1143
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL--ALLLSPEdfldAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180
....*....|....*....|...
gi 73623035 1144 RNILEENLRRSDKELEKLDDIVQ 1166
Cdd:COG4942 159 LAELAALRAELEAERAELEALLA 181
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
597-742 |
6.25e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 597 SQLEQDLASMREFRGLLKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQLDyttwtALLSRSRQLTEKLTVKSQ-- 674
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSAry 286
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73623035 675 -------QALQERDVAIEE--KQEVSRVLEQVSAQLEECKGQTEQLElenSRLAtDLRAQLQILANMDSQLKELQSQ 742
Cdd:COG3206 287 tpnhpdvIALRAQIAALRAqlQQEAQRILASLEAELEALQAREASLQ---AQLA-QLEARLAELPELEAELRRLERE 359
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
667-899 |
7.13e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 667 EKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHC 746
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 747 AQDLAMK-DELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVR---DLKETLEFADQENQVAHLELGQVEC 822
Cdd:pfam02463 256 SKQEIEKeEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrkvDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73623035 823 QLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEKTEQE 899
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
453-873 |
7.45e-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: 40.72 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 453 RDWKSQLAVPHPETQDSSTQTDTSHSGITNKLQ-------HLKESH----EMGQALQQARNVMQSWVLISKELISLLHLS 521
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceklekiHLQESAqslkEREQQLQTKEQIHLQETRKKAVVLARLLEL 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 522 LLHLEEDKTTVS------QESRRAETLVCCCFDLLKKLRAKLQSLKAEREEARHREEMALRGKDAAEIVLEAFCAHASQR 595
Cdd:TIGR00618 500 QEEPCPLCGSCIhpnparQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 596 ---------ISQLEQDLASMREFRGLLKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTAL---LSRSR 663
Cdd:TIGR00618 580 nrskedipnLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALqltLTQER 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 664 QLTEKLTVKSQQALQERDVAIEEKQEVSRVlEQVSAQLEeckgqteqlELENSRLAtdLRAQLQILANMDSQLKELQSQH 743
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLALQKMQSEK-EQLTYWKE---------MLAQCQTL--LRELETHIEEYDREFNEIENAS 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 744 THCAQDLAMKDELLCQLTQSNEEQaAQWQKEEMALKHMQAELQQQQAV-LAKEVRDLKETLEFADQENQVAHLELGQVEC 822
Cdd:TIGR00618 728 SSLGSDLAAREDALNQSLKELMHQ-ARTVLKARTEAHFNNNEEVTAALqTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 73623035 823 QLKTTL-EVLRERSLQCENLKDTVENLTAKLAS------TIADNQEQDLEKTRQYSQK 873
Cdd:TIGR00618 807 EIGQEIpSDEDILNLQCETLVQEEEQFLSRLEEksatlgEITHQLLKYEECSKQLAQL 864
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
968-1061 |
7.57e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 968 ESLAEMSIMTTELQSLcsllQESKEEAIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQAL-CLRYKNEKELQE 1046
Cdd:pfam03938 12 EESPEGKAAQAQLEKK----FKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELqQLQQKAQQELQK 87
|
90
....*....|....*
gi 73623035 1047 VIQQQNEKILEQIDK 1061
Cdd:pfam03938 88 KQQELLQPIQDKINK 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-804 |
9.18e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 495 QALQQARNVMQSWVLISKELISLLHLSLLHLEEDKTTVSQESRRAETLVCCCFDLLKKLRAKLQSLKAEREEARHREEMA 574
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 575 LRGKDAAEIVLEAfcahASQRISQLEQDLASMR-EFRGLLKDAQTQLVGLHAKQEELVQQTVSLTsTLQQDWRSMQLDYT 653
Cdd:TIGR02168 781 EAEIEELEAQIEQ----LKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIE 855
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73623035 654 TWTALLSRSRQLTEKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEEckgqteqLELENSRLatdlraqlqilanmD 733
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE-------LESKRSEL--------------R 914
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250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73623035 734 SQLKELQSQHTHCAQDLAmkdELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLE 804
Cdd:TIGR02168 915 RELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
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