|
Name |
Accession |
Description |
Interval |
E-value |
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-1020 |
6.67e-65 |
|
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: 238.33 E-value: 6.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 1 MRPIQLIMTAFGPYKQKEVIDFDDLGehRIFAISGNTGAGKTTIFDAICYVLYGEASGEERSDTSmLRSQFADDNVYTSV 80
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALG--PIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRS-LNSLYAAPSEAAFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 81 ELTFQLKGKRYEIKRQLGHKKQGNKTITGHAVELYEVIDEEKIPAVdrfHVTDVNKKVEDLIGLSKHQFSQIVMLPQGEF 160
Cdd:TIGR00618 78 ELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAA---KKSETEEVIHDLLKLDYKTFTRVVLLPQGEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 161 RKLLTSETENKEEILRRIFKTDRYklmRELLDQKRKQWKDVLQEKQKERELYfrnvfklpirdgSLLETLVEQEHVNTHQ 240
Cdd:TIGR00618 155 AQFLKAKSKEKKELLMNLFPLDQY---TQLALMEFAKKKSLHGKAELLTLRS------------QLLTLCTPCMPDTYHE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 241 VVEALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFHAAKSVNEKFIDLQQKNEKYNTLQENRTVIEMKETSFKRAEQA 320
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 321 KRLLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMS------------NFELAQEKYEAVKNKEP-----ERENAKKLVQ 383
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqqssieeqrrllQTLHSQEIHIRDAHEVAtsireISCQQHTLTQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 384 RLEELQPIIASLAEKqlnLQNAEIQLGKLK-ESMQNLDRQLEEHTNQKQLMAGELQ---QLERALEQYVDKVEELTNMRE 459
Cdd:TIGR00618 380 HIHTLQQQKTTLTQK---LQSLCKELDILQrEQATIDTRTSAFRDLQGQLAHAKKQqelQQRYAELCAAAITCTAQCEKL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 460 DAKVLKQAYDVWQEKQKFEQEKETafIKMQETVRAYENMERrwlseqagilaLHLHDGEFCPVCGSTNHPKKATEQSDai 539
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQ--IHLQETRKKAVVLAR-----------LLELQEEPCPLCGSCIHPNPARQDID-- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 540 dekELNDLRDKKNIAEKLHVQVEEKWNFYHHQYEQVIEEVKKRGYQSEELAETYSALVQKGKQLATEVN-TLKASEETRK 618
Cdd:TIGR00618 522 ---NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPnLQNITVRLQD 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 619 QIAVKIKSVEEKVDALQKQKRDVETEQH---------RIEMDCMQLRTSYEHDKKNIPENLQTVQAWKVQFDQAMH---- 685
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDlqdvrlhlqQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELlasr 678
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 686 ELKLMEDEWKKVQEAY---------------QHWQNENIRIQAEQEGASNQFESAKSKKEETFTRFMKELEQSGFT---- 746
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYwkemlaqcqtllrelETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvlka 758
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 747 DQITYKEAKLSDAEMDMLQKEIQSYYSSLEVLAKQIEELQGELKDKEymdiTALGEHIKDLEINLDIIKEK-RQRAQNAV 825
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLE----AEIGQEIPSDEDILNLQCETlVQEEEQFL 834
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 826 TYISDLHENIRRIDEQIHEEEKAFQ----------ELVDLYEVMKGDNESRISFERYILIEYLEQIVQIANERLRKLSNG 895
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKYEECSKqlaqltqeqaKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEG 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 896 QFYLKRSERVEKRNRQSGLGLDVYDAYTGQTRDVKTLSGGEKFNASLCLALGMADVIQAyEGGISIETMFIDEGFGSLDE 975
Cdd:TIGR00618 915 RFHGRYADSHVNARKYQGLALLVADAYTGSVRPSATLSGGETFLASLSLALALADLLST-SGGTVLDSLFIDEGFGSLDE 993
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 822508355 976 ESLTKAVDALIDLQKSGRFIGVISHVQELKNAMPAVLEVTKQKDG 1020
Cdd:TIGR00618 994 DSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKTNAG 1038
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-170 |
9.20e-36 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 135.09 E-value: 9.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 1 MRPIQLIMTAFGPYKQKEVIDFDDLGEHRIFAISGNTGAGKTTIFDAICYVLYGEASGEERSDtsMLRSQFADDNVYTSV 80
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFTGLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQE--NLRSVFAPGEDTAEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 81 ELTFQLKGKRYEIKRQlghkkqgnktitghavelyevideekipavdrfhvtdvnkkvedlIGLSKHQFSQIVMLPQGEF 160
Cdd:cd03279 79 SFTFQLGGKKYRVERS---------------------------------------------RGLDYDQFTRIVLLPQGEF 113
|
170
....*....|
gi 822508355 161 RKLLTSETEN 170
Cdd:cd03279 114 DRFLARPVST 123
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
926-1020 |
1.91e-33 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 128.54 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 926 TRDVKTLSGGEKFNASLCLALGMADVIQAyEGGISIETMFIDEGFGSLDEESLTKAVDALIDLQKSGRFIGVISHVQELK 1005
Cdd:cd03279 118 ARPVSTLSGGETFLASLSLALALSEVLQN-RGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELK 196
|
90
....*....|....*
gi 822508355 1006 NAMPAVLEVTKQKDG 1020
Cdd:cd03279 197 ERIPQRLEVIKTPGG 211
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
30-1016 |
2.71e-32 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 136.08 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 30 IFAISGNTGAGKTTIFDAICYVLYGEASGEERSDTS----MLRsqfadDNVYTSVELTFQLKGKRYE-IKRQLGHKKQGN 104
Cdd:PRK10246 32 LFAITGPTGAGKTTLLDAICLALYHETPRLNNVSQSqndlMTR-----DTAECLAEVEFEVKGEAYRaFWSQNRARNQPD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 105 KTITGHAVELYEVIDEeKIPAvDRfhVTDVNKKVEDLIGLSKHQFSQIVMLPQGEFRKLLTSETENKEEILRRIFKTDRY 184
Cdd:PRK10246 107 GNLQAPRVELARCADG-KILA-DK--VKDKLELTATLTGLDYGRFTRSMLLSQGQFAAFLNAKPKERAELLEELTGTEIY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 185 KLMRELLDQKRKQWKDVLQEKQKErelyfrnvfklpirdGSLLETLVEQEhvnthqvVEALEQETAAYKAEVEQLQVEQD 264
Cdd:PRK10246 183 GQISAMVFEQHKSARTELEKLQAQ---------------ASGVALLTPEQ-------VQSLTASLQVLTDEEKQLLTAQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 265 VQTKQL----------KDAETRFHAAKSVNEKFIDLQQKNEKYNTLQENRTVIEMKEtsfKRAEQAKRLLPFEQWHEE-- 332
Cdd:PRK10246 241 QQQQSLnwltrldelqQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWE---RIQEQSAALAHTRQQIEEvn 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 333 -------------------AMQNEQKAESLLKQIIAKKENI-MSNFELAQEKYEAVKNKEpERENAKKLVQRLEELQPII 392
Cdd:PRK10246 318 trlqstmalrarirhhaakQSAELQAQQQSLNTWLAEHDRFrQWNNELAGWRAQFSQQTS-DREQLRQWQQQLTHAEQKL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 393 ASLAEKQLNLQNAEIQLGKLKESMQNLDRQ----LEEHTNQKQLMAGELQQLERALEQYVDKVEE-LTNMREDAKVLKQA 467
Cdd:PRK10246 397 NALPAITLTLTADEVAAALAQHAEQRPLRQrlvaLHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAaLNEMRQRYKEKTQQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 468 Y-DVwqeKQKFEQEketAFIKMQETVRAyenmerrwlseqagilalHLHDGEFCPVCGSTNHPkkATEQSDAIdekELND 546
Cdd:PRK10246 477 LaDV---KTICEQE---ARIKDLEAQRA------------------QLQAGQPCPLCGSTSHP--AVEAYQAL---EPGV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 547 LRDKKNIAEKLHVQVEEKWNFYHHQYEQVIEEVKKRGYQSEELAETYSALVQKGKQLATEVNT-----------LKASEE 615
Cdd:PRK10246 528 NQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNItlqpqddiqpwLDAQEE 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 616 TRKQI---------AVKIKSVEEKVDALQKQkrdVETEQHRIEMDCMQLRTSYEHDKKNIP---ENLQTVQAWKVQFDQ- 682
Cdd:PRK10246 608 HERQLrllsqrhelQGQIAAHNQQIIQYQQQ---IEQRQQQLLTALAGYALTLPQEDEEASwlaTRQQEAQSWQQRQNEl 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 683 -----------AMHELKLMEDEWKKVQE--AYQHWQ---NENIRIQAEQEGASNQFESAKSKKEETFTRFMKELEQSGFT 746
Cdd:PRK10246 685 talqnriqqltPLLETLPQSDDLPHSEEtvALDNWRqvhEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFD 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 747 DQITYKEAKLSDAEMDMLQKEIQSYYSSLE---VLAKQIEElqgelkdkeymditALGEHIKDLEINLDIIKEKRQRAQN 823
Cdd:PRK10246 765 DQQAFLAALLDEETLTQLEQLKQNLENQRQqaqTLVTQTAQ--------------ALAQHQQHRPDGLDLTVTVEQIQQE 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 824 AVTYISDLHENIRR---IDEQIHEEEKAFQELVDLYEVMkgDNESRIS-----------------FERYILIEYLEQIVQ 883
Cdd:PRK10246 831 LAQLAQQLRENTTRqgeIRQQLKQDADNRQQQQALMQQI--AQATQQVedwgylnsligskegdkFRKFAQGLTLDNLVW 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 884 IANERLRKLsNGQFYLKR--SERVEkrnrqsglgLDVYDAYTGQT-RDVKTLSGGEKFNASLCLALGMADVIQAyegGIS 960
Cdd:PRK10246 909 LANQQLTRL-HGRYLLQRkaSEALE---------LEVVDTWQADAvRDTRTLSGGESFLVSLALALALSDLVSH---KTR 975
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*.
gi 822508355 961 IETMFIDEGFGSLDEESLTKAVDALIDLQKSGRFIGVISHVQELKNAMPAVLEVTK 1016
Cdd:PRK10246 976 IDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKK 1031
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-230 |
5.59e-28 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 112.41 E-value: 5.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 2 RPIQLIMTAFGPYKQKEVIDFDDlgehRIFAISGNTGAGKTTIFDAICYVLYGEASGEERsdtsmLRSQFA-DDNVYTSV 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDD----GLNLIVGPNGAGKSTILEAIRYALYGKARSRSK-----LRSDLInVGSEEASV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 81 ELTFQLKGKRYEIKRqlghkkqgnktitghavelyevideekipavdrfhvtdvnkkvedliglskhqfsqivmlPQGEF 160
Cdd:COG0419 72 ELEFEHGGKRYRIER------------------------------------------------------------RQGEF 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822508355 161 RKLLTSETENKEEILRRIFKTDRYKLMRELLDQKRKQWKDVLQEK---QKERELYFRNVFKL-PIRDGSLLETL 230
Cdd:COG0419 92 AEFLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELaelQKLKQEILAQLSGLdPIETLSGGERL 165
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-208 |
7.48e-16 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 76.77 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 6 LIMTAFGPYKQKEvIDFDdlgeHRIFAISGNTGAGKTTIFDAICYVLYGEASGEERSD-TSMLRSQFA---DDNVYTSVE 81
Cdd:pfam13476 1 LTIENFRSFRDQT-IDFS----KGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSgGGFVKGDIRiglEGKGKAYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 82 LTFQLKGKR--YEIKRQLGHKKQGNKTITGHAVELyevideekipavdrFHVTDVNKKVEDLIGLSKHQFSQIVMLPQGE 159
Cdd:pfam13476 76 ITFENNDGRytYAIERSRELSKKKGKTKKKEILEI--------------LEIDELQQFISELLKSDKIILPLLVFLGQER 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822508355 160 FRKLLTSETENKEEILRRIFKTDRYKLMRELLDQKRKQWKDVLQEKQKE 208
Cdd:pfam13476 142 EEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
927-1022 |
2.12e-15 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 76.11 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 927 RDVKTLSGGEKFNASLCLALGMADVIqayegGISIETMFIDEGFGSLDEESLTKAVDALIDLQKS--GRFIGVISHVQEL 1004
Cdd:cd03240 111 DMRGRCSGGEKVLASLIIRLALAETF-----GSNCGILALDEPTTNLDEENIEESLAEIIEERKSqkNFQLIVITHDEEL 185
|
90
....*....|....*...
gi 822508355 1005 KNAMPAVLEVTKQKDGCS 1022
Cdd:cd03240 186 VDAADHIYRVEKDGRQKS 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11-852 |
3.63e-14 |
|
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: 77.40 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 11 FGPYKQKEVIDFDdlgeHRIFAISGNTGAGKTTIFDAICYVLyGEASgeersdTSMLRSQFADDNV-----------YTS 79
Cdd:TIGR02168 10 FKSFADPTTINFD----KGITGIVGPNGCGKSNIVDAIRWVL-GEQS------AKALRGGKMEDVIfngsetrkplsLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 80 VELTF-----QLKGKRYE---IKRQLGHKKQGNKTITGHAVELYEVIdeekipavDRFHVTDVNKKVEDLIGLSKhqFSQ 151
Cdd:TIGR02168 79 VELVFdnsdgLLPGADYSeisITRRLYRDGESEYFINGQPCRLKDIQ--------DLFLDTGLGKRSYSIIEQGK--ISE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 152 IVMLPQGEFRKLL------TSETENKEEILRRIFKTDR-----YKLMREL------LDQKRKQWKDVLQEKQKERELyfr 214
Cdd:TIGR02168 149 IIEAKPEERRAIFeeaagiSKYKERRKETERKLERTREnldrlEDILNELerqlksLERQAEKAERYKELKAELREL--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 215 nvfklpirDGSLLETLVEQEHVNthqvVEALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFHaakSVNEKFIDLQQKN 294
Cdd:TIGR02168 226 --------ELALLVLRLEELREE----LEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---ELEEEIEELQKEL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 295 EKYNTLQENRTV-IEMKETSFKRAEQAKRLLPFEQWHEEAMQNEQKAEslLKQIIAKKENIMSNFELAQEKYEAVKNKEP 373
Cdd:TIGR02168 291 YALANEISRLEQqKQILRERLANLERQLEELEAQLEELESKLDELAEE--LAELEEKLEELKEELESLEAELEELEAELE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 374 ERENAKKLVQR-LEELQPIIASLaEKQLNLQNAEI-----QLGKLKESMQNLDRQLEEH-----TNQKQLMAGELQQLER 442
Cdd:TIGR02168 369 ELESRLEELEEqLETLRSKVAQL-ELQIASLNNEIerleaRLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 443 ALE----QYVDKVEELTNMREDAKVLKQAYDVWQEKQKFEQEKETAFIKMQETVRAYENMERRWLSEQAGI--------- 509
Cdd:TIGR02168 448 ELEelqeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlse 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 510 ---------LALHLHDGE-----------------------------FCPVCGST-NHPKKATEQSDAIDEKELNDLRDK 550
Cdd:TIGR02168 528 lisvdegyeAAIEAALGGrlqavvvenlnaakkaiaflkqnelgrvtFLPLDSIKgTEIQGNDREILKNIEGFLGVAKDL 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 551 KNIAEKLHVQVE----------------EKWNFYHHQYEQVIEE---VKKRGYQSEELAETYSALVQKGKQLATEVNTLK 611
Cdd:TIGR02168 608 VKFDPKLRKALSyllggvlvvddldnalELAKKLRPGYRIVTLDgdlVRPGGVITGGSAKTNSSILERRREIEELEEKIE 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 612 ASEETRKQIAVKIKSVEEKVDALQKQKRDVETEQHRIEMDCMQLRTSYEHDKKNIPENLQTVQAWKVQFDQAMHELKLME 691
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 692 DEWKKVQEAYQHWQNENIRIQAEQEGASNQFESAKSKKEETFTRFmKELEQSGFTDQITYKEAKlsdAEMDMLQKEIQSY 771
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLE---RRIAATERRLEDL 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 772 YSSLEVLAKQIEELQGELKDKEymdiTALGEHIKDLEINLDIIKEKRQRAQNAVTYISDLHENIRRIDEQIHEEEKAFQE 851
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
.
gi 822508355 852 L 852
Cdd:TIGR02168 920 L 920
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
6-97 |
1.35e-12 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 67.63 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 6 LIMTAFGPYKQKEVIDFDDLgehrIFAISGNTGAGKTTIFDAICYVLYGEASGEERS---DTSMLRSQfaddNVYTSVEL 82
Cdd:cd03240 4 LSIRNIRSFHERSEIEFFSP----LTLIVGQNGAGKTTIIEALKYALTGELPPNSKGgahDPKLIREG----EVRAQVKL 75
|
90
....*....|....*.
gi 822508355 83 TFQL-KGKRYEIKRQL 97
Cdd:cd03240 76 AFENaNGKKYTITRSL 91
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
33-1016 |
4.22e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 70.32 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 33 ISGNTGAGKTTIFDAICYVLYGEASGEERSDtsMLRSqfadDNVYTSVELTFQLKGKRYEIKRQLGHKKQGNKTitghav 112
Cdd:PRK01156 28 ITGKNGAGKSSIVDAIRFALFTDKRTEKIED--MIKK----GKNNLEVELEFRIGGHVYQIRRSIERRGKGSRR------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 113 ELYEVIDEEKIPAvdrfHVTDVNKKVE-DLIGLSKHQFSQIVMLPQGEFRKLLTSETENKEEILRRIFKTDR----YKLM 187
Cdd:PRK01156 96 EAYIKKDGSIIAE----GFDDTTKYIEkNILGISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEILEINSlernYDKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 188 RELLDQKRKQWKDV--LQEKQKERELYFRNVFKlPIRDGSLLETLVEQEHVNTHQVVEALEQETAAYKAEVEQLQVEQDV 265
Cdd:PRK01156 172 KDVIDMLRAEISNIdyLEEKLKSSNLELENIKK-QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 266 QTKQLKDAETRFHAAKSVNEKFIDLQQKNEKYNTLQENRTViemketsfkraeqAKRLLPFEQWheeamqneqkaeSLLK 345
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVY-------------KNRNYINDYF------------KYKN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 346 QIIAKKEnIMSNFELAQEKYEAVKNK----EPERENAKKLVQRLEELQPIIASLAEKQLNLQNAeiqlgklKESMQNLDR 421
Cdd:PRK01156 306 DIENKKQ-ILSNIDAEINKYHAIIKKlsvlQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY-------LKSIESLKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 422 QLEEHTNQKQLMAGELQqleraleqyvdkvEELTNMREDAKVLKQAYDvwqEKQKFEQEKETAFIKMQETVRAYENMERR 501
Cdd:PRK01156 378 KIEEYSKNIERMSAFIS-------------EILKIQEIDPDAIKKELN---EINVKLQDISSKVSSLNQRIRALRENLDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 502 wLSEQAGILALHlhdgEFCPVCGStnhpkkateqsdaidekelnDLRDKKniaeklhvqveekwnfyhhqyeqvieevkk 581
Cdd:PRK01156 442 -LSRNMEMLNGQ----SVCPVCGT--------------------TLGEEK------------------------------ 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 582 rgyqSEELAETYSalvqkgkqlatevNTLKASEETRKQIAVKIKSVEEKVDALQKQKRDVETEQHRIEMDCMQLRTSYEH 661
Cdd:PRK01156 467 ----SNHIINHYN-------------EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARA 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 662 DKKNIPENLQTVQAWKVQFDQAMHELKLMEDEwkKVQEAYQHWQNENIRIQA-EQEGASNQFESAKSKKEETFTRfMKEL 740
Cdd:PRK01156 530 DLEDIKIKINELKDKHDKYEEIKNRYKSLKLE--DLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESR-LQEI 606
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 741 EqSGFTDQITYKEAKLSdaEMDMLQKEIQSYYSSLEVLAKQIEELQGElkdkeymditalgehIKDLEINLDIIKEKRQR 820
Cdd:PRK01156 607 E-IGFPDDKSYIDKSIR--EIENEANNLNNKYNEIQENKILIEKLRGK---------------IDNYKKQIAEIDSIIPD 668
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 821 AQNAVTYISDLHENIRRIDEQIHEEEKAFQELVDLYEVMKGDNES---RISfERYILIEYLEQIVQIAN--ERLRKL--S 893
Cdd:PRK01156 669 LKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINElsdRIN-DINETLESMKKIKKAIGdlKRLREAfdK 747
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 894 NGQFYLKR---SERVEKRNRQ--SGLGLDVYDAYTGQ-----------TRDVKTLSGGEKFNASLCLALGMADVIQAyeg 957
Cdd:PRK01156 748 SGVPAMIRksaSQAMTSLTRKylFEFNLDFDDIDVDQdfnitvsrggmVEGIDSLSGGEKTAVAFALRVAVAQFLNN--- 824
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822508355 958 giSIETMFIDEGFGSLDEESLTKAVDAL-IDLQKSGRF--IGVISHVQELKNAMPAVLEVTK 1016
Cdd:PRK01156 825 --DKSLLIMDEPTAFLDEDRRTNLKDIIeYSLKDSSDIpqVIMISHHRELLSVADVAYEVKK 884
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
927-985 |
7.13e-11 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 59.56 E-value: 7.13e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822508355 927 RDVKTLSGGEK-FNASLCLALGMADVIQAYEG-GISIETMFIDEGFGSLDEESLTKAVDAL 985
Cdd:pfam13558 28 RRSGGLSGGEKqLLAYLPLAAALAAQYGSAEGrPPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-883 |
1.82e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 167 ETENKEEILRRIFKTDRYKLMRELLDQKRKQWKDVLQEKQKERELYFRNVFKLPIRDGSLLETLVEQEHVNTHQVVEALE 246
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 247 QETA--AYKAEVEQLQVEQDVQTKQLKDAETRFHAAKSVNEKFIDLQQKNEKYNTLQENRTVIEMK-----ETSFKRAEQ 319
Cdd:PTZ00121 1289 KKKAdeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAaadeaEAAEEKAEA 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 320 AKrlLPFEQWHEEAMQNEQKAESLLKQIIAKKENimsnfELAQEKYEAVKNKEPERENAKKLVQRLEELQPiiASLAEKQ 399
Cdd:PTZ00121 1369 AE--KKKEEAKKKADAAKKKAEEKKKADEAKKKA-----EEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKK 1439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 400 LNLQNAEIQLGKLKES---MQNLDRQLEEhtNQKQLMAGELQQLERALEQYVDKVEELTNMREDAKVLKQAYDVWQEKQK 476
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEakkAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 477 FEQEKETAFIKMQETVRAYENMERRWLSEQAGIL--ALHLHDGEfcpvcgstnhPKKATEQSDAIDEKELNDLRDKKNIA 554
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKAE----------EKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 555 EKLHVQVEEKWNFYHHQYEQVIEEVKKrgyqsEELAETYSALVQKGKQLATEVNTLKASEETRKQIAVKIKSVEEKVDAL 634
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 635 QKQ-KRDVETEQHRIEmdcmQLRTSYEHDKKnipenlqtvqawkvqfdqAMHELKLMEDEWKKVQEAYQHWQNENIR--- 710
Cdd:PTZ00121 1663 AAEeAKKAEEDKKKAE----EAKKAEEDEKK------------------AAEALKKEAEEAKKAEELKKKEAEEKKKaee 1720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 711 IQAEQEGASNQFESAKSKKEEtftrfmkeleqsgftDQITYKEAKLSDAEMDMLQKEIQSYYSSLEVLAKQIEE-LQGEL 789
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEE---------------DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEEL 1785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 790 KDKEYMDITALGEHIKDLEINLDIIKEKRQRAQNAV-----TYISDLHENIRRIDEQIhEEEKAFQELVDLYEVMKGDN- 863
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIndskeMEDSAIKEVADSKNMQL-EEADAFEKHKFNKNNENGEDg 1864
|
730 740
....*....|....*....|..
gi 822508355 864 --ESRISFERYILIEYLEQIVQ 883
Cdd:PTZ00121 1865 nkEADFNKEKDLKEDDEEEIEE 1886
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
403-1005 |
3.16e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 403 QNAEIQLGKLKESMQNLdRQLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAKVLKQAYDVWQEKQKFEQE-- 480
Cdd:COG4717 64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEla 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 481 -KETAFIKMQETVRAYENMER--RWLSEQAGILALHLHDGEfcpvcgstNHPKKATEQSDAIDEKELNDLRDKKNIAEKL 557
Cdd:COG4717 143 eLPERLEELEERLEELRELEEelEELEAELAELQEELEELL--------EQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 558 HVQVEEKWNFYHHQYEQvIEEVKKRGYQSEELAETYSALVQKGKQLATEVNTLKASEETRKQIAVKIKSVEEKVDALQKQ 637
Cdd:COG4717 215 LEEAQEELEELEEELEQ-LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 638 KRDVETEQHRIEmdcmqlrtsyEHDKKNIPENLQTvQAWKVQFDQAMHELKLMEDEWKKVQEAYQHWQ---------NEN 708
Cdd:COG4717 294 AREKASLGKEAE----------ELQALPALEELEE-EELEELLAALGLPPDLSPEELLELLDRIEELQellreaeelEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 709 IRIQAEQEGASNQFESAKSKKEETFTRFMKELEQ-SGFTDQITYKEAKLSDAEMDMLQkeiQSYYSSLEVLAKQIEELQG 787
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyQELKEELEELEEQLEELLGELEE---LLEALDEEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 788 ELKDKEyMDITALGEHIKDLEINLDIIKEKRQraqnavtyISDLHENIRRIDEQIHEEEKAFQELVDLYEVMkgdNESRI 867
Cdd:COG4717 440 ELEELE-EELEELREELAELEAELEQLEEDGE--------LAELLQELEELKAELRELAEEWAALKLALELL---EEARE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 868 SFERyiliEYLEQIVQIANERLRKLSNGQFylkrservEKRNRQSGLGLDVYDAyTGQTRDVKTLSGGEKFNASLCLALG 947
Cdd:COG4717 508 EYRE----ERLPPVLERASEYFSRLTDGRY--------RLIRIDEDLSLKVDTE-DGRTRPVEELSRGTREQLYLALRLA 574
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 822508355 948 MADVIQAYeggisIETMFIDEGFGSLDEESLTKAVDALIDLQKSGRFIGVISHVQELK 1005
Cdd:COG4717 575 LAELLAGE-----PLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVE 627
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-1015 |
1.51e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 33 ISGNTGAGKTTIFDAICYVLYGeasGEERSDTSMLRSQFADDNVY-TSVELTFQLKGKRYEIKRQLghkKQGNKTITGHa 111
Cdd:PRK03918 28 IIGQNGSGKSSILEAILVGLYW---GHGSKPKGLKKDDFTRIGGSgTEIELKFEKNGRKYRIVRSF---NRGESYLKYL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 112 vELYEVIdEEKIPAVDRFhvtdvnkkVEDLIGLskHQFSQIVMLPQGEFRKLLTSEtENKEEILRRIFKTDRYklmrell 191
Cdd:PRK03918 101 -DGSEVL-EEGDSSVREW--------VERLIPY--HVFLNAIYIRQGEIDAILESD-ESREKVVRQILGLDDY------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 192 DQKRKQWKDVLQEKQKERElyfrnvfklpirdgsLLETLVEQEHvNTHQVVEALEQETAAYKAEVEQLQVEQDVQTKQLK 271
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIE---------------RLEKFIKRTE-NIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 272 DAETRFHAAKSVNEKFIDLQQKNEKyntlqenrtviemKETSFKRAEQAKRLLpfeqwhEEAMQNEQKAESLLKQIIAKK 351
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELES-------------LEGSKRKLEEKIREL------EERIEELKKEIEELEEKVKEL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 352 ENIMsnfELAQEKYEAVKNKEPERENAKKLVQRLEELQPIIASLAEKQLNLQNAEIQLGKLKESMQNLDRQLEehtnqkq 431
Cdd:PRK03918 286 KELK---EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 432 lmagELQQLERALEQYVDKVEELTNMREDAKVLKQAyDVWQEKQKFEQEKETAFIKMQETVRAYENMERRWLSEQAGILA 511
Cdd:PRK03918 356 ----ELEERHELYEEAKAKKEELERLKKRLTGLTPE-KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 512 LHLHDGEfCPVCGstnhpkkateqsdaideKELNDlRDKKNIAEKlhvqveekwnfYHHQYEQVIEEVKKRGYQSEELae 591
Cdd:PRK03918 431 LKKAKGK-CPVCG-----------------RELTE-EHRKELLEE-----------YTAELKRIEKELKEIEEKERKL-- 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 592 tysalvqkgKQLATEVNTLKASEET---RKQIAVKIKSVEEKVDALQKQKRDVETEQHRiemDCMQLRTSYEHDKKNIPE 668
Cdd:PRK03918 479 ---------RKELRELEKVLKKESElikLKELAEQLKELEEKLKKYNLEELEKKAEEYE---KLKEKLIKLKGEIKSLKK 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 669 NLQTVQAWKvqfdqamHELKLMEDEWKKVQEayqhwQNENIRIQAEQEGASNQFESAKSKKE-ETFTRFMKELEQSGFTD 747
Cdd:PRK03918 547 ELEKLEELK-------KKLAELEKKLDELEE-----ELAELLKELEELGFESVEELEERLKElEPFYNEYLELKDAEKEL 614
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 748 QITYKEAKLSDAEMDMLQKEIQSYYSSLEVLAKQIEELQGELKDKEYMDI----TALGEHIKDLEINLDIIKEKRQraqn 823
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreeyLELSRELAGLRAELEELEKRRE---- 690
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 824 avtyisDLHENIRRIDEQIHEEEKAFQELVDLYEVMKGDNESRISFERY--ILIEY-LEQIVQIANERLRKLSNGqfylK 900
Cdd:PRK03918 691 ------EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYkaLLKERaLSKVGEIASEIFEELTEG----K 760
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 901 RSERVEKRNRQSglgLDVYDAYTGQTRDVKTLSGGEKFNASLCLALGMAdviqAYEGGiSIETMFIDEGFGSLDEESLTK 980
Cdd:PRK03918 761 YSGVRVKAEENK---VKLFVVYQGKERPLTFLSGGERIALGLAFRLALS----LYLAG-NIPLLILDEPTPFLDEERRRK 832
|
970 980 990
....*....|....*....|....*....|....*
gi 822508355 981 AVDALIDLQKSGRFIGVISHVQELKNAMPAVLEVT 1015
Cdd:PRK03918 833 LVDIMERYLRKIPQVIIVSHDEELKDAADYVIRVS 867
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
858-1001 |
1.21e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 56.17 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 858 VMKGDNESRISFE------RYILI----EYLEQIVQIANER---LRKLSNGQFYLKRSERVEKRNRQSGLGLDVYDAYTG 924
Cdd:COG0419 62 INVGSEEASVELEfehggkRYRIErrqgEFAEFLEAKPSERkeaLKRLLGLEIYEELKERLKELEEALESALEELAELQK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 925 QTR----------DVKTLSGGEKfnaslcLALGMADVIQayeggisietMFIDegFGSLDEESLTKAVDALIDLQksgrf 994
Cdd:COG0419 142 LKQeilaqlsgldPIETLSGGER------LRLALADLLS----------LILD--FGSLDEERLERLLDALEELA----- 198
|
....*..
gi 822508355 995 igVISHV 1001
Cdd:COG0419 199 --IITHV 203
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-482 |
6.08e-08 |
|
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: 57.00 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 32 AISGNTGAGKTTIFDAICYVLYGEASGEERSDT-SML--RSQFADDNVYTSVELTFQLKGKR----YEIKRQLGHKKQGN 104
Cdd:TIGR02169 27 VISGPNGSGKSNIGDAILFALGLSSSKAMRAERlSDLisNGKNGQSGNEAYVTVTFKNDDGKfpdeLEVVRRLKVTDDGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 105 KT---ITGHAVELYEVIDEekipaVDRFHVT----------DVNKkvedliglskhqfsqIVMLPQGEFRKLL-----TS 166
Cdd:TIGR02169 107 YSyyyLNGQRVRLSEIHDF-----LAAAGIYpegynvvlqgDVTD---------------FISMSPVERRKIIdeiagVA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 167 ETENKEEILRRIFKTDRYKLMR--ELLDQKRKQwkdvLQEKQKERElyfrnvfkLPIRDGSLLETLVEQEHVNTHQVVEA 244
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERldLIIDEKRQQ----LERLRRERE--------KAERYQALLKEKREYEGYELLKEKEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 245 LEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFHAA----KSVNEKFIDLQQknEKYNTLQENRTVIEMKETSFKRAEQA 320
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIeqllEELNKKIKDLGE--EEQLRVKEKIGELEAEIASLERSIAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 321 KrllpfEQWHEEAMQNEQKAESLLKQIIAKKENIMSNFELAQEKYEAVKNKEPERENA-KKLVQRLEELQPIIASLAEKQ 399
Cdd:TIGR02169 313 K-----ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEElEDLRAELEEVDKEFAETRDEL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 400 LNLQNAeiqLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAkvlkqAYDVWQEKQKFEQ 479
Cdd:TIGR02169 388 KDYREK---LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-----ALEIKKQEWKLEQ 459
|
...
gi 822508355 480 EKE 482
Cdd:TIGR02169 460 LAA 462
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-1016 |
7.75e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 1 MRPIQLIMTAFGPYKQKEViDFDDlgehRIFAISGNTGAGKTTIFDAICYVLYGEASGEERSDTSMLRSqfADDnvyTSV 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADADL-RLED----GVTVIHGVNGSGKSSLLEACFFALYGSKALDDTLDDVITIG--AEE---AEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 81 ELTFQLKGKRYEIKRQLghKKQGNKTITGHAV-ELYEVIDEEkipavdrfhVTDVNKKVEDLIGLSKHQFSQIVMLPQGE 159
Cdd:PRK02224 71 ELWFEHAGGEYHIERRV--RLSGDRATTAKCVlETPEGTIDG---------ARDVREEVTELLRMDAEAFVNCAYVRQGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 160 FRKLLTSETENKEEILRRIFKTDRYKLMRELLDQKRKQWKDVLQEKqkerelyfRNVFklpirdGSLLETLVEQEHVNTH 239
Cdd:PRK02224 140 VNKLINATPSDRQDMIDDLLQLGKLEEYRERASDARLGVERVLSDQ--------RGSL------DQLKAQIEEKEEKDLH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 240 QVVEALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFHAAKSVNEKFIDLQQKNEKyntLQENRTVIEMKETSFKRA-- 317
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED---LRETIAETEREREELAEEvr 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 318 EQAKRLLPFEQWHEEAMQN-----------EQKAESLLKQIIAKKENIMsnfELAQEKYEAVKNKEPERENAKKLVQRLE 386
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEaglddadaeavEARREELEDRDEELRDRLE---ECRVAAQAHNEEAESLREDADDLEERAE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 387 ELQPIIASLAEKqlnLQNAEIQLGKLKESMQNLDRQLEEhtnqkqlMAGELQQLERALEQYVDKVEELTNMREDAKvlkq 466
Cdd:PRK02224 360 ELREEAAELESE---LEEAREAVEDRREEIEELEEEIEE-------LRERFGDAPVDLGNAEDFLEELREERDELR---- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 467 aydvwqekqkfEQEKETafikmQETVRAYENMERRwlseqagilALHLHDGEFCPVCGstnHPKKATEQSDAIDEKelnd 546
Cdd:PRK02224 426 -----------EREAEL-----EATLRTARERVEE---------AEALLEAGKCPECG---QPVEGSPHVETIEED---- 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 547 lRDKKniaEKLHVQVEEkwnfyhhqYEQVIEEVKKRGYQSEELAETysalvqkGKQLATEVNTLKASEETRKQIAVKIKS 626
Cdd:PRK02224 474 -RERV---EELEAELED--------LEEEVEEVEERLERAEDLVEA-------EDRIERLEERREDLEELIAERRETIEE 534
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 627 VEEKVDALQKQKRDVETEQHRIEMDCMQLRTSYEHDKknipENLQTVQAWKVQFDQAMHELKLMEDEWKKVQEAYQHWQN 706
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR----EEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIER 610
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 707 ENIRIQAEQEGASNQFESAKSKKEETftrfmKELeqsgftdqitykEAKLSDAEMDMLQKEIQSYYSSLEVLAKQIEELQ 786
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERK-----REL------------EAEFDEARIEEAREDKERAEEYLEQVEEKLDELR 673
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 787 gELKDKEYMDITALGEHIKDLEinldIIKEKRQRAQNAVTYISDLHENIRrideqiheeekafqELVDLYEVMKGDNESR 866
Cdd:PRK02224 674 -EERDDLQAEIGAVENELEELE----ELRERREALENRVEALEALYDEAE--------------ELESMYGDLRAELRQR 734
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 867 isferyilieyleqivqiaN-ERLRKLSNGQFYLkrserVEKRNRQSGLGLD------VYDAyTGQTRDVKTLSGGEK-- 937
Cdd:PRK02224 735 -------------------NvETLERMLNETFDL-----VYQNDAYSHIELDgeyeltVYQK-DGEPLEPEQLSGGERal 789
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 938 FNASL-C-----LALGMadviqayEGGISIETMFIDEGFGSLDEESLTKAVDALIDLQKSG-RFIGVISHVQELKNAMPA 1010
Cdd:PRK02224 790 FNLSLrCaiyrlLAEGI-------EGDAPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHDDELVGAADD 862
|
....*.
gi 822508355 1011 VLEVTK 1016
Cdd:PRK02224 863 LVRVEK 868
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
5-881 |
2.60e-07 |
|
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: 54.98 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 5 QLIMTAFGPYKQKEVIDFDdlgeHRIFAISGNTGAGKTTIFDAICYVLYGEASGEERSD--TSMLRSQFADDNVYTSVEL 82
Cdd:pfam02463 4 RIEIEGFKSYAKTVILPFS----PGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSErlSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 83 TFQLKGKR-------YEIKRQLGHKKQGNKTITGHAVELYEVIDEEKIPAVDRFHVTDVNK-KVEDLIGLSKHQFSQI-- 152
Cdd:pfam02463 80 TFDNEDHElpidkeeVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQgGKIEIIAMMKPERRLEie 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 153 -VMLPQGEFRKL------LTSETENKEEILRRI--FKTDRYKLMRELLDQKRKQWKDVLQEKQKERELY---------FR 214
Cdd:pfam02463 160 eEAAGSRLKRKKkealkkLIEETENLAELIIDLeeLKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldylklneeRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 215 NVFKLPIRDGSLLETLVEQEHVNTHQVVEALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFHAAKSVNEKFIDLQQKN 294
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 295 EKYNTLQE---NRTVIEMKETSFKRAEQAKRLLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMSNFELAQEKYEAVKNK 371
Cdd:pfam02463 320 EKEKKKAEkelKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 372 EPERENAKKLVQRLEELQPIIASLAEKQLNLQNAEIQLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQYVDKV 451
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 452 EELTNMREDAKVLKQAYDVWQEKQKFEQEKETAFIKMQETVRAYENMERRWLSEQAGILALHLHDGEFcpVCGSTNHPKK 531
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST--AVIVEVSATA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 532 ATEQSDAIDEKELNDLR---------------DKKNIAEKLHVQVEEKWNFYHHQYEQVIEEV------KKRGYQSEELA 590
Cdd:pfam02463 558 DEVEERQKLVRALTELPlgarklrllipklklPLKSIAVLEIDPILNLAQLDKATLEADEDDKrakvveGILKDTELTKL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 591 ETYSALVQKGKQLATEVNTLKASEETRKQIAVKIKSVEEKVDALQKQKRDVETE----QHRIEMDCMQLRTSYEHDKKNI 666
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKeeilRRQLEIKKKEQREKEELKKLKL 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 667 PENLQTVQAWKVQFDQAMHELKLMEDEWKKVQEAYQHWQNENIRIQAEQEGASNQFESA--------KSKKEETFTRFMK 738
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELaeerekteKLKVEEEKEEKLK 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 739 ELEqsgFTDQITYKEAKLSDAEMDMLQKEIQS----YYSSLEVLAKQIEELQGELKDKEYMDITALGEHIKDLEINLDII 814
Cdd:pfam02463 798 AQE---EELRALEEELKEEAELLEEEQLLIEQeekiKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822508355 815 KEKRQRAQNAVTYISDLHENIRRIDEQIHEEEKAFQELVDLYEVmkgdNESRISFERYILIEYLEQI 881
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE----IEERIKEEAEILLKYEEEP 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
222-490 |
3.71e-07 |
|
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: 54.29 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 222 RDGSLLETLVEQEHVNthQVVEALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFHAA-KSVNEKFIDLQQKNEKYNTL 300
Cdd:TIGR02168 668 TNSSILERRREIEELE--EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 301 QE--NRTVIEMKETSFKRAEQAKRLLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMSNFELAQEKYEAVK----NKEPE 374
Cdd:TIGR02168 746 EEriAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 375 RENAKKLVQRLE-ELQPIIASLAEKQLNLQNAEIQLGKLKESMQNLDRQLEEHTNQKqlmAGELQQLERALEQYVDKVEE 453
Cdd:TIGR02168 826 LESLERRIAATErRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEE 902
|
250 260 270
....*....|....*....|....*....|....*...
gi 822508355 454 LTNMREDAKVLKQAYDVWQEKQ-KFEQEKETAFIKMQE 490
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLaQLELRLEGLEVRIDN 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
415-844 |
3.93e-07 |
|
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: 54.29 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 415 SMQNLDRQLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAkvlkqaydvwqekQKFEQEKETAFIKMQETVRA 494
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-------------RKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 495 YENMERRWLSEQAGILAlhlhdgefcpvcgstnhpkkatEQSDAIDEKELndLRDKKNIAEKLHVQVEEKWNFYHHQYEQ 574
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSK----------------------ELTELEAEIEE--LEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 575 VIEEVKKRGYQSEELAETYSALVQKGKQLATEVNTLkaseetRKQIAVKIKSVEEKVDALQKQKRDVETEQHRIEmdcmQ 654
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESL------ERRIAATERRLEDLEEQIEELSEDIESLAAEIE----E 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 655 LRTSyehdkknIPENLQTVQAWKVQFDQAMHELKLMEDEWKKVQEAYQHWQNENIRIQAEQEGASNQFESAkskkeetft 734
Cdd:TIGR02168 864 LEEL-------IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL--------- 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 735 rfmkELEQSGFTDQITYKEAKLSDAEMDMLQKEIQSYysslEVLAKQIEELQGELKDKEyMDITALGehikdlEINLDII 814
Cdd:TIGR02168 928 ----ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE----NKIEDDEEEARRRLKRLE-NKIKELG------PVNLAAI 992
|
410 420 430
....*....|....*....|....*....|...
gi 822508355 815 ---KEKRQRAQNAVTYISDLHENIRRIDEQIHE 844
Cdd:TIGR02168 993 eeyEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-88 |
9.49e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.67 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 5 QLIMTAFGPYKQKEVIDFddlGEHRIFAISGNTGAGKTTIFDAICYVLYGEASGEERSDTSMLRSQFAddnvYTSVELTF 84
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTF---GEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVA----AVSAELIF 73
|
....
gi 822508355 85 QLKG 88
Cdd:cd03227 74 TRLQ 77
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
311-768 |
1.67e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 311 ETSFKRAEQAKRLLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMSN--FELAQEKYEAVKNKEPERENAKKLVQRLEEL 388
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltFLLEESRDKANQLEEKTKLQDENLKELIEKK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 389 QPIIASLAEKQLNLQNAEIQLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAKVLKQay 468
Cdd:pfam05483 292 DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 469 dvwQEKQKFEQEKETAFIKMQETVRAYENMERRWLSEQAGILALHLHDGEFCPVCGSTNHPKKATEQSDAIDEKELNDLR 548
Cdd:pfam05483 370 ---QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 549 DKKNIAEKLHVQV---EEKWNFYHHQYEQVIEEVKKRGYQSEELAETYSALVQKGKQLATEVNTLKASEETRKQIAVKIK 625
Cdd:pfam05483 447 AREKEIHDLEIQLtaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 626 SVEEK----VDALQKQKRDVETE---------QHRIEMDCmQLRTSYEHDKKNIPENLQTVQAWKVQFDQAMHELKLMED 692
Cdd:pfam05483 527 KQEERmlkqIENLEEKEMNLRDElesvreefiQKGDEVKC-KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 693 EWKKVQEAYQHWQNENIRIQAEQEGASN----------QFESAKSKKEETFTRFMKELEQSGFTDQITYKE---AKLSDA 759
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAyeikvnklelELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEvekAKAIAD 685
|
....*....
gi 822508355 760 EMDMLQKEI 768
Cdd:pfam05483 686 EAVKLQKEI 694
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-512 |
2.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 243 EALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFHAAKSvnekfiDLQQKNEKYNTLQENRTVIEMKETsfkRAEQAKR 322
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRL------ELEELELELEEAQAEEYELLAELA---RLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 323 LLpfeqwHEEAMQNEQKAESLLKQIIakkenimsnfELAQEKYEAVKNKEPERENAKKLVQRLEELQpiiASLAEKQLNL 402
Cdd:COG1196 306 RL-----EERRRELEERLEELEEELA----------ELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 403 QNAEIQLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAKvlkqaydvwQEKQKFEQEKE 482
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---------EALAELEEEEE 438
|
250 260 270
....*....|....*....|....*....|
gi 822508355 483 TAFIKMQETVRAYENMERRWLSEQAGILAL 512
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
929-1023 |
3.60e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.12 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 929 VKTLSGGEKFNASLCLALGMADVIqayeggiSIETMFIDEGFGSLDEESLTKAVDALIDLQKSGRFIGVISHVQELKNAM 1008
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLK-------PRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELA 147
|
90
....*....|....*
gi 822508355 1009 PAVLEVTKQKDGCSQ 1023
Cdd:cd03227 148 DKLIHIKKVITGVYK 162
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
541-853 |
3.72e-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: 51.21 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 541 EKELNDLRDKKNIAEKLHVQVEEKWNFYHHQYEQVIEEVKKrgyQSEELAETYSALVQKGKQLATEVNTLKAS-EETRKQ 619
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELRE---ELEELQEELKEAEEELEELTAELQELEEKlEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 620 IAvkikSVEEKVDALQKQKRDVETEQHRIEMDCMQLRTSYEHDKKNIPENLQTVQAWKVQFDQAMHELKLMEDEWKKVQE 699
Cdd:TIGR02168 276 VS----ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 700 AYQHWQNENIRIQAEQEGASNQFEsAKSKKEETFTRFMKELEQSG--FTDQITYKEAKLSDAE--MDMLQKEIQSYYSSL 775
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLE-ELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEdrRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 776 EvlAKQIEELQGELKDKEYMdITALGEHIKDLEINLDIIKEKRQRAQNAVT-YISDLHENIRRID--EQIHEEEKAFQEL 852
Cdd:TIGR02168 431 E--EAELKELQAELEELEEE-LEELQEELERLEEALEELREELEEAEQALDaAERELAQLQARLDslERLQENLEGFSEG 507
|
.
gi 822508355 853 V 853
Cdd:TIGR02168 508 V 508
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
5-96 |
5.98e-06 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 47.69 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 5 QLIMTAFGPYKQKEVIDfddlGEHRIFAISGNTGAGKTTIFDAICYVLYGEASGEERSDTSMLRSQFADDNVYT-SVELT 83
Cdd:cd03239 3 QITLKNFKSYRDETVVG----GSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSaSVEIT 78
|
90
....*....|...
gi 822508355 84 FQlkgKRYEIKRQ 96
Cdd:cd03239 79 FD---KSYFLVLQ 88
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
331-826 |
2.10e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 331 EEAMQNEQKAESLLKQI-----IAKKENIMSNFELAQEKYEAVKNKEPERENAKKLVQRLEELqpiiaslaEKQLNLQNA 405
Cdd:pfam15921 285 EKASSARSQANSIQSQLeiiqeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL--------EKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 406 EI-----QLGKLKESMQNLDRQLEE-----HTNQKQLMAGELQ----------------QLERALEqyvDKVEELTNMRE 459
Cdd:pfam15921 357 ELteartERDQFSQESGNLDDQLQKlladlHKREKELSLEKEQnkrlwdrdtgnsitidHLRRELD---DRNMEVQRLEA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 460 DAKVLKQAYDVWQEKQKFE-QEKETAFIKMQETVRAYEN---MERRWLSE-QAGILALHLHDGEFCPVCGSTNHPKKATE 534
Cdd:pfam15921 434 LLKAMKSECQGQMERQMAAiQGKNESLEKVSSLTAQLEStkeMLRKVVEElTAKKMTLESSERTVSDLTASLQEKERAIE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 535 QSDAIDEK-------ELNDLRDKKNIAEKL-HVQVE-EKWNFYHHQYEQVIEEVKKRGYQSEEL----AETYSALVQKGK 601
Cdd:pfam15921 514 ATNAEITKlrsrvdlKLQELQHLKNEGDHLrNVQTEcEALKLQMAEKDKVIEILRQQIENMTQLvgqhGRTAGAMQVEKA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 602 QLATEVNTlkaseetRKQIAVKIKSVEEKVDAlqkQKRDVETEQHRIEMDCMQLRTSYEhdkknipENLQTVQAWKVQFD 681
Cdd:pfam15921 594 QLEKEIND-------RRLELQEFKILKDKKDA---KIRELEARVSDLELEKVKLVNAGS-------ERLRAVKDIKQERD 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 682 QAMHELKLMEDEWKKVQEAYQ----HWQNENIRIQAEQEGASNQFESAKSKKEETfTRFMKELEQS---------GFTDQ 748
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQT-RNTLKSMEGSdghamkvamGMQKQ 735
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822508355 749 ITYKEaklsdAEMDMLQKEIQSYYSSLEVLAKQIEELQGElKDKEYMDITALGEHIKDLEINLDIIKEKRQRAQNAVT 826
Cdd:pfam15921 736 ITAKR-----GQIDALQSKIQFLEEAMTNANKEKHFLKEE-KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVA 807
|
|
| DNA_S_dndD |
TIGR03185 |
DNA sulfur modification protein DndD; This model describes the DndB protein encoded by an ... |
5-481 |
3.11e-05 |
|
DNA sulfur modification protein DndD; This model describes the DndB protein encoded by an operon associated with a sulfur-containing modification to DNA. The operon is sporadically distributed in bacteria, much like some restriction enzyme operons. DndD is described as a putative ATPase. The small number of examples known so far include species from among the Firmicutes, Actinomycetes, Proteobacteria, and Cyanobacteria. [DNA metabolism, Restriction/modification]
Pssm-ID: 274475 [Multi-domain] Cd Length: 650 Bit Score: 48.14 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 5 QLIMTAFGPYKQKEVIDFDDLGEHRIFAISGNTGAGKTTIFDAICYVLYG-EASGEERSD-------TSMLRSQFADDNV 76
Cdd:TIGR03185 5 QLTLENFGPYRGRQTFDLSPSSPKPIILIGGLNGAGKTTLLDAIQLALYGkRALCSGRGNksyeqylRGLINRQAGKTNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 77 yTSVELTFQLkgkryeikrqlghkkqgnktITGHAVELYEVIDEEKIPAVDRFHVTDVNKKVEDLIGLSKHQFSQIV-ML 155
Cdd:TIGR03185 85 -ASITLTFSV--------------------VEGGKRHEYTLVRSWHINNKDVKEKLTVYKDDEEDDSLNDIWDEFINeLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 156 P---------QGEFRKLLTSETENKEEILRRIFKTdrykLMRELLDQKRKQWKDVLQEKQKErelyfrnvfKLPIRDGSL 226
Cdd:TIGR03185 144 PleladlfffDGEKIEALANPDRLASLLKEAIEVL----LGLDLIDRLAGDLTNVLRRRKKS---------ELPSSILSE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 227 LETLvEQEHVNTHQVVEALEQETAAYKAEVEQLQ-----VEQDVQTKQLKDAETRFHAAKSVNEKFIDLQQKNEKYNTLQ 301
Cdd:TIGR03185 211 IEAL-EAELKEQSEKYEDLAQEIAHLRNELEEAQrslesLEKKFRSEGGDLFEEREQLERQLKEIEAARKANRAQLRELA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 302 E-------NRTVIEMKETSFKRAEQAKR-------LLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMSNFELAQEKYEA 367
Cdd:TIGR03185 290 AdplplllIPNLLDSTKAQLQKEEQSQQnqltqeeLEERDKELLESLPKLALPAEHVKEIAAELAEIDKPATTDSEIPHR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 368 VKNKEPER-ENAKKLVQRleELQPIIASLAEKQLNLQNAEIQLGKL------KESMQNLDRQLEEHTNqkqlmagELQQL 440
Cdd:TIGR03185 370 LSGSELTQlEVLIQQVKR--ELQDAKSQLLKELRELEEELAEVDKKistipsEEQIAQLLEELGEAQN-------ELFRS 440
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 822508355 441 ERALEQYVDKVEELTNMREDAKVLKQAYdVWQEKQKFEQEK 481
Cdd:TIGR03185 441 EAEIEELLRQLETLKEAIEALRKTLDEK-TKQKINAFELER 480
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
33-453 |
3.71e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 33 ISGNTGAGKTTIFDAICYVLYGeasgeeRSDTSMLRSQFADDNVY--TSVELTFQLKGKRYEIKRqlghkkqgnktitGH 110
Cdd:PHA02562 32 ITGKNGAGKSTMLEALTFALFG------KPFRDIKKGQLINSINKkdLLVELWFEYGEKEYYIKR-------------GI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 111 AVELYEVI-DEEKIP--AVDRfhvtDVNKKVEDLIGLSKHQFSQIVMLPQGEFRKLLTSETENkeeilrrifktdRYKLM 187
Cdd:PHA02562 93 KPNVFEIYcNGKLLDesASSK----DFQKYFEQMLGMNYKSFKQIVVLGTAGYVPFMQLSAPA------------RRKLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 188 RELLDQKRKQWKDVLQeKQKERELYFRnvfklpIRDGSLLETLVEQEhVNTHQvvEALEQETAAYKAEVEQLqveQDVQT 267
Cdd:PHA02562 157 EDLLDISVLSEMDKLN-KDKIRELNQQ------IQTLDMKIDHIQQQ-IKTYN--KNIEEQRKKNGENIARK---QNKYD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 268 KQLKDAETRFHAAKSVNEKFIDLQQKNEKY----NTLQENRTVIEMKETSFKRAEQAkrllpFEQWHE--EAMQNEQKAE 341
Cdd:PHA02562 224 ELVEEAKTIKAEIEELTDELLNLVMDIEDPsaalNKLNTAAAKIKSKIEQFQKVIKM-----YEKGGVcpTCTQQISEGP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 342 SLLKQIIAKKENIMSNFELAQEKYEAVKNKEPErenAKKLVQRLEELQpiiASLAEKQLNLQNAEIQLGKLKESMQNLDr 421
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAIDELEEIMDE---FNEQSKKLLELK---NKISTNKQSLITLVDKAKKVKAAIEELQ- 371
|
410 420 430
....*....|....*....|....*....|..
gi 822508355 422 qlEEHTNQKQLMAGELQQLERALEQYVDKVEE 453
Cdd:PHA02562 372 --AEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
33-466 |
4.25e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 33 ISGNTGAGKTTIFDAICYVLYGEASGEERSDTSMLRSQFADD-NVYTSVELTFQ-LKGKRYEIKRQL----GHKKQGNKT 106
Cdd:TIGR00606 33 LVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQEtDVRAQIRLQFRdVNGEECAVVRSMvctqKTKKTEFKT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 107 ITGHAVELYeviDEEKIPAVDRfhVTDVNKKVEDLIGLSKHQFSQIVMLPQGEFRKLLTSETENKEEiLRRIFKTDRYKL 186
Cdd:TIGR00606 113 LEGVITRYK---HGEKVSLSSK--CAEIDREMISHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQK-FDEIFSATRYIK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 187 MRELLDQKRKQWKDVLQEKQKERELYFRNVFKLP-IRDGSlleTLVEQEHVNTHQVVEALEQETAAYKAEVEQLQ----- 260
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACeIRDQI---TSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlsk 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 261 -VEQDVQTKQLKDAETRFHAAKSVNEKFID--LQQKNEKYNTLQENRTViEMKETSFKRAEQAKRLLPFEQWHEEAMQ-- 335
Cdd:TIGR00606 264 iMKLDNEIKALKSRKKQMEKDNSELELKMEkvFQGTDEQLNDLYHNHQR-TVREKERELVDCQRELEKLNKERRLLNQek 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 336 ----NEQ-----KAESLLKQIIAKKENIMSN-FELAQEKYEAVKNKEPERENAKKLVQRLEELQPIIAS--LAEKQLNLQ 403
Cdd:TIGR00606 343 tellVEQgrlqlQADRHQEHIRARDSLIQSLaTRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAqlCADLQSKER 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 404 NAEIQLGKLKESMQNLDR-------QLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAKVLKQ 466
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRtielkkeILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK 492
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
16-60 |
1.96e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 40.28 E-value: 1.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 822508355 16 QKEVIDFDDLGehrIFAISGNTGAGKTTIFDAICYVLYG-------EASGEE 60
Cdd:pfam13555 13 DGHTIPIDPRG---NTLLTGPSGSGKSTLLDAIQTLLVPakrarfnKAANAG 61
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-484 |
2.15e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 243 EALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRfhaaksvnekfidLQQKNEKYNTLQENRTVIEMKETSFKRAEQAKR 322
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERR-------------IAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 323 LlpfeqwhEEAMQNEQKAESLLKQIIAKKENIMSNFELAQEKYEAVKNKEPERENAKKLVQRLEELQPIIASLAEKQLNL 402
Cdd:COG4942 97 A-------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 403 QNAEIQLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQyvdkveELTNMREDAKVLKQAYDVWQEKQKFEQEKE 482
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA------ELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 822508355 483 TA 484
Cdd:COG4942 244 PA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
268-649 |
2.53e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 268 KQLKDAETRFHAAKSVNEKFIDLQQKnekyntLQENRTVIEMKETSFKRAEQAKRLLPFEQWHEEAMQNEQKAESLLKQI 347
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEE------LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 348 IAKKENIMSNFELAQEKYEAVKNKEPERENAKKLVQRL---------EELQPIIASLAEKQLNLQNAEIQLGKLKESMQN 418
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslateEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 419 LDRQLEEHTNQKQLmAGELQQLERALEQYV----------------DKVEELTNMREDAKVLKQAYDVWQEKQKFEQEKE 482
Cdd:COG4717 225 LEEELEQLENELEA-AALEERLKEARLLLLiaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 483 TAFIKMQETVRAYENMERRWLSEQAGILALHLHDGEFCPVCGSTNHPKKATEQSDAIDEKELNDLRDK-KNIAEKLHVQV 561
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 562 EEKWNFYHHQYEQVIEEVKKRGYQSEELAETYSALVQkgkqlATEVNTLKASEETRKQIAVKIKSVEEKVDALQKQKRDV 641
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEE-----LLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
....*...
gi 822508355 642 ETEQHRIE 649
Cdd:COG4717 459 EAELEQLE 466
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
227-467 |
2.60e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 227 LETLVEQEHVNTHQVVEALEQETAAYKAEVEQLQ--VEQDVQTKQLKDAETRfhaAKSVNEKFIDLQQKnekyntLQENR 304
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEaaLEEFRQKNGLVDLSEE---AKLLLQQLSELESQ------LAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 305 TVIEMKETSFKRAEQAKRLLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMSNFelaQEKYEAVKNKEPERENAKKLVQr 384
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARY---TPNHPDVIALRAQIAALRAQLQ- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 385 lEELQPIIASLaekQLNLQNAEIQLGKLKESMQNLDRQLEEhTNQKQLmagELQQLERALEQYVDKVEELTNMREDAKVL 464
Cdd:COG3206 309 -QEAQRILASL---EAELEALQAREASLQAQLAQLEARLAE-LPELEA---ELRRLEREVEVARELYESLLQRLEEARLA 380
|
...
gi 822508355 465 KQA 467
Cdd:COG3206 381 EAL 383
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
164-496 |
3.52e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 164 LTSETENKEEILRRIFKTDRYKLMRelLDQKRKQWKDV---LQEKQKERELYFRNVFKLPIRDGSLLETL----VEQEHV 236
Cdd:pfam15921 466 LTAQLESTKEMLRKVVEELTAKKMT--LESSERTVSDLtasLQEKERAIEATNAEITKLRSRVDLKLQELqhlkNEGDHL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 237 NTHQV-VEALEQETAAYKAEVEQLQvEQDVQTKQLKDAETRFHAA---------KSVNEKFIDLQQ-------KNEKYNT 299
Cdd:pfam15921 544 RNVQTeCEALKLQMAEKDKVIEILR-QQIENMTQLVGQHGRTAGAmqvekaqleKEINDRRLELQEfkilkdkKDAKIRE 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 300 LQENRTVIEMKETSFKRA--EQAKRLLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMSNFELAQEKYEAVKNK------ 371
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAgsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlkmqlk 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 372 --EPERENAKKLVQRLE-------------------------ELQPIIASLAEKqlnLQNAEIQLGKLKESMQNLDRQLE 424
Cdd:pfam15921 703 saQSELEQTRNTLKSMEgsdghamkvamgmqkqitakrgqidALQSKIQFLEEA---MTNANKEKHFLKEEKNKLSQELS 779
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822508355 425 EHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAKV-LKQAYDVWQekqkfEQEKETAFIKMQETVRAYE 496
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLqFAECQDIIQ-----RQEQESVRLKLQHTLDVKE 847
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
573-852 |
3.99e-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: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 573 EQVIEEVKK---RGYQSEELAETYSALV-QKGKQLATE-VNTLKASEETRKQIAVKIKSVEEKVDALQKQKRDVETEQHR 647
Cdd:TIGR02169 190 DLIIDEKRQqleRLRREREKAERYQALLkEKREYEGYElLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 648 IEMDCMQLRTsyEHDKKNIPENLQ---TVQAWKVQFDQAMHELKLMEDEWKKVQEAYQHWQNENIRIQAEQEGASNQFES 724
Cdd:TIGR02169 270 IEQLLEELNK--KIKDLGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 725 AKSKKEETFTRFMK----------ELEQSGFTDQITYKEAKLSDAEMDMLQKEIQSYYSSLEVLAKQIEELQGELKDKEy 794
Cdd:TIGR02169 348 ERKRRDKLTEEYAElkeeledlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN- 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822508355 795 MDITALGEHIKDLEINLDI----IKEKRQRAQNAVTYISDLHENIRRIDEQIHEEEKAFQEL 852
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDkaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
225-469 |
5.28e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 225 SLLETLVEQEHVNTHQVVEALEQETAAYKAEvEQLQVEQDVQTKQLK---DAETRFHAAKSVN---EKFID--LQQKNEK 296
Cdd:COG3206 94 PVLERVVDKLNLDEDPLGEEASREAAIERLR-KNLTVEPVKGSNVIEisyTSPDPELAAAVANalaEAYLEqnLELRREE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 297 YNT--------LQENRTVIEMKETSFKRAEQAKRLLPFEQWHEEAMQNEQKAESLLKQIIAKKENIMSNFELAQEKYEAV 368
Cdd:COG3206 173 ARKalefleeqLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 369 KNKEPERENAKKLVQRLEELQPIIASLAEKQLNLQNAEIQLGKLKESMQNLDRQLEEHT--------NQKQLMAGELQQL 440
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAqrilasleAELEALQAREASL 332
|
250 260 270
....*....|....*....|....*....|....*.
gi 822508355 441 ERALEQYVDKVE-------ELTNMREDAKVLKQAYD 469
Cdd:COG3206 333 QAQLAQLEARLAelpeleaELRRLEREVEVARELYE 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
585-868 |
5.55e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 585 QSEELAETYSALVQKGKQLATEVNTLKASEETRKQiavKIKSVEEKVDALQKQKRDVETEQHRIEMDCMQLRTSYEHDKK 664
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 665 NIPENLQTVQAWKVQFDQAMHELKLMEDEWKKVQEAYQHWQNENIRIQAEQEGASNQFESAKSKKEETFTRFMKEL-EQS 743
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALrAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 744 GFTDQITYKEAKLSDA--EMDMLQKEIQSYYSSLEVLAKQIEELQGELKDKEYMDITALGEHIKDLEINLDIIKEKRQRA 821
Cdd:COG1196 397 ELAAQLEELEEAEEALleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 822508355 822 QNAVTYISDLHENIRRIDEQIHEEEKAFQELVDLYEVMKGDNESRIS 868
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
610-988 |
5.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 610 LKASEETRKQIAVKIKSVEEKVDALQKQKRDVETEQHRIemdcmQLRTSYEHDKKNIPENLQTVQAWKVQ---FDQAMHE 686
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAL-----QRLAEYSWDEIDVASAEREIAELEAElerLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 687 LKLMEDEWKKVQEAYQHWQNENIRIQAEQEGASNQFESAKSKKEETFTRFmKELEQSGFTDQITYKEAKLSDAEMDM--- 763
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRALLEERFAAALGDAver 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 764 -----LQKEIQSYYSSLEVLAKQIEELQGELKDKEYMDITALGEHIKDLE---------INLDII----KEKRQRAQNAV 825
Cdd:COG4913 766 elrenLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPeylalldrlEEDGLPeyeeRFKELLNENSI 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 826 TYISDLHENIRRideqihEEEKAFQELVDLYEVMKgdnesRISF--ERYILIEYLEQIVQIANE---RLRKLSNG----- 895
Cdd:COG4913 846 EFVADLLSKLRR------AIREIKERIDPLNDSLK-----RIPFgpGRYLRLEARPRPDPEVREfrqELRAVTSGaslfd 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 896 -----QFYLK--------RSERVEKRNRQSGLGLDV-----YDAY-----TGQT----RDVKTLSGGEKFN-------AS 941
Cdd:COG4913 915 eelseARFAAlkrlierlRSEEEESDRRWRARVLDVrnhleFDAEeidreDGEEvetySSSGGKSGGEKQKlayfilaAA 994
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 822508355 942 LCLALGMADviqayEGGISIETMFIDEGFGSLDEESLTKAVDALIDL 988
Cdd:COG4913 995 LAYQLGLEG-----RGRPSFRTVVLDEAFSKMDEEFARRALRLFKEL 1036
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-52 |
9.74e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 42.28 E-value: 9.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 822508355 1 MRPIQLIMTAFGPYKQKEVI-DFDDLgehriF-AISGNTGAGKTTIFDAICYVL 52
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQ-----FnAITGLNGSGKSNILDAICFVL 49
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
226-466 |
2.57e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 226 LLETLVEQEhvnthQVVEALEQETAAYKAEVEQLQVEQDVQTKQLKDAETRFhaaksvnekfiDLQQKnekyNTLQENRT 305
Cdd:PRK04863 360 LEERLEEQN-----EVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAL-----------DVQQT----RAIQYQQA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 306 ViemketsfKRAEQAKRLLP--------FEQWHEEAMQNEQKAESL---LKQIIAKKENIMSNFELAqekYEAVKN--KE 372
Cdd:PRK04863 420 V--------QALERAKQLCGlpdltadnAEDWLEEFQAKEQEATEEllsLEQKLSVAQAAHSQFEQA---YQLVRKiaGE 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 373 PERENA----KKLVQRLEELQPIIASLAEKQLNLQNAEiQLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQYV 448
Cdd:PRK04863 489 VSRSEAwdvaRELLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
250
....*....|....*....
gi 822508355 449 DKV-EELTNMREDAKVLKQ 466
Cdd:PRK04863 568 ESLsESVSEARERRMALRQ 586
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-484 |
3.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 336 NEQKAESLLKQIIAKKENImsnfELAQEKYEAVKNKEPERENAKKLVQRLEELQPI----------IASLAEKQLNLQNA 405
Cdd:COG4913 608 NRAKLAALEAELAELEEEL----AEAEERLEALEAELDALQERREALQRLAEYSWDeidvasaereIAELEAELERLDAS 683
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822508355 406 EIQLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMREDAKVLKQAYDVWQEKQKFEQEKETA 484
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
18-402 |
3.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 18 EVIDFDDlgehRIFAISGNTGAGKTTIFDAICYVLY-----------GEASGEERS-------------DTSMLRSQFA- 72
Cdd:COG4913 18 HTIDFDG----RGTLLTGDNGSGKSTLLDAIQTLLVpakrprfnkaaNDAGKSDRTllsyvrgkygserDEAGTRPVYLr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 73 DDNVYTSVELTFQLKGKR--------YEIKrqlghkkqGNKTITGHAVELYeVIDEEKI------PAVDRFHVTDVnKKV 138
Cdd:COG4913 94 PGDTWSAIAATFANDGSGqtvtlaqvFWLK--------GDASSLGDVKRFF-VIADGPLdledfeEFAHGFDIRAL-KAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 139 EDLIGLSKH-QFSQIvmlpQGEFRKLLTSETEN---------------------KEEIL--RRIFKT--------DRYKL 186
Cdd:COG4913 164 LKKQGVEFFdSFSAY----LARLRRRLGIGSEKalrllhktqsfkpigdlddfvREYMLeePDTFEAadalvehfDDLER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 187 MRELLDQKRKQwKDVLQEKQKERELYfrnvfklpirdGSLLETLVEQEHVNTHQVVEALEQETAAYKAEVEQLQVEQDVQ 266
Cdd:COG4913 240 AHEALEDAREQ-IELLEPIRELAERY-----------AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 267 TKQLKDAETRFHAAKsvnEKFIDLQQK--NEKYNTLQENRTVIEMKETsfKRAEQAKRLLPFEQW----HEEAMQNEQKA 340
Cdd:COG4913 308 EAELERLEARLDALR---EELDELEAQirGNGGDRLEQLEREIERLER--ELEERERRRARLEALlaalGLPLPASAEEF 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822508355 341 ESLLKQIIAKKENIMSNFELAQEKYEAVKNKEperenaKKLVQRLEELQPIIASLAEKQLNL 402
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAAL------RDLRRELRELEAEIASLERRKSNI 438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-483 |
4.24e-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: 41.21 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 242 VEALEQETAAYKAEVEQLqvEQDVQTKQLKDAETRFHAAK---SVNEKFIdlQQKNEKYNTLQENRTVIEMKETSFKRAE 318
Cdd:TIGR02169 746 LSSLEQEIENVKSELKEL--EARIEELEEDLHKLEEALNDleaRLSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKL 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 319 QakRLLPFEQWHEEAMQNEQKAESLLKqiiAKKENIMSNFELAQEKYEAVKNKEPERENA-KKLVQRLEELQPIIASLAE 397
Cdd:TIGR02169 822 N--RLTLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKKEELEEELEELEAAlRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 398 KqlnLQNAEIQLGKLKESMQNLDRQLEEHTNQKQLMAGELQQLERALEQYVDKVEELTNMRedakvlkqayDVWQEKQKF 477
Cdd:TIGR02169 897 Q---LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE----------DVQAELQRV 963
|
....*.
gi 822508355 478 EQEKET 483
Cdd:TIGR02169 964 EEEIRA 969
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
540-860 |
4.83e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 540 DEKELNDLRDKKNIAEKLHVQVEEKWNFYHHQY---EQVIEEVKKRGYQSEELAETYSALVQKGKQLATEVNTLKAseet 616
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK---- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 617 rkqiavKIKSVEEKVDALQKQKRDVETEQHRIEMDCMQLRTSYEHDKKNIPENLQTVQAWKVQFDQAMHELKLMEDEWKK 696
Cdd:TIGR04523 226 ------QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 697 V-QEAYQHWQNE---NIRIQAEQ----EGASNQFESAKSKKEETFTRFMKELEQSGFTDQITYKEAKLSDAEMDMLQKEI 768
Cdd:TIGR04523 300 LnNQKEQDWNKElksELKNQEKKleeiQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 769 QSYYSSLEVLAKQIEELQGELKDKEYMDiTALGEHIKDLEINLDIIKEKRQRAQNAvtyISDLHENIRRIDEQIHEEEKA 848
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLN-QQKDEQIKKLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELI 455
|
330
....*....|..
gi 822508355 849 FQELVDLYEVMK 860
Cdd:TIGR04523 456 IKNLDNTRESLE 467
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
5-96 |
5.23e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.37 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822508355 5 QLIMTAFGPYKQKEVIDFDDlgehRIFAISGNTGAGKTTIFDAICYVLyGEAS-----GEERSDTSMLRSQFADDNVYTS 79
Cdd:cd03278 3 KLELKGFKSFADKTTIPFPP----GLTAIVGPNGSGKSNIIDAIRWVL-GEQSakslrGEKMSDVIFAGSETRKPANFAE 77
|
90
....*....|....*..
gi 822508355 80 VELTFQLKGKRYEIKRQ 96
Cdd:cd03278 78 VTLTFDNSDGRYSIISQ 94
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
932-1004 |
6.11e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.38 E-value: 6.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822508355 932 LSGGEKFNASLCLALGMADVIqayeggisietMFIDEGFGSLDEESLTKAVDALIDLQKSGRFIGVISHVQEL 1004
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDL-----------LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPEL 142
|
|
| |
