|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1-1047 |
0e+00 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 1671.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKGEWKVDFTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSTVSQSQNDLMTRDTAECL 80
Cdd:PRK10246 1 MKILSLRLKNLNSLKGEWKIDFTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLNNVSQSQNDLMTRDTAECL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 81 AEVEFEVKGESYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLEMTASLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:PRK10246 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQAPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 161 FLNAKPKERAELLEELTGTEIYGQISALVFEKHKTARTDLEKLQAQASGVSLLAPEQQHSLNESLQALTDEEKQLLARQQ 240
Cdd:PRK10246 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 241 LHQQHLHWLTRQNELQAEMNRRQQALRVSQEEQENAQPQLAALNLAHPARQLRPHWERIEEQTAAAGRTRQQIQEVNARL 320
Cdd:PRK10246 241 QQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 321 QSVLHLRSRIRHSAQQQSAELRATMQTLTGWLTEHERFRLWSSELAGWRALFAQQSSDKVQLLKWQQQCASDIRKRDALP 400
Cdd:PRK10246 321 QSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 401 PNPLTLTPEEATAALAQHTQQQPLRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQFMDV 480
Cdd:PRK10246 401 AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 481 KTICEQEARIKDLESQRALLQSGQPCPLCGSTSHPAIASYQALEPGVNQARRDALEKEVKTLAEEGAALRGQLETLTQQL 560
Cdd:PRK10246 481 KTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 561 HRDESEVQALVKEEQALTQEWQTLCDALNVTLHPQDDISPWLTARQDYEQQLYQLSQRHMLQAQIAAHTGQVTQFQQQID 640
Cdd:PRK10246 561 QRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 641 QRQTTLLSELRRYGLSLPADGEEASWLNARADDAQTWQQRQTELGELQTRIAQLTPLLETLPETDILPESDERVALDNWR 720
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 721 QVHDDCVSLQSQWQTLQQQEAQEMQRVAQAQAHFDAALKASVFDDRAAFLAALLDDETIARLEQHRQALENQLQQAQALA 800
Cdd:PRK10246 721 QVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLV 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 801 AQANQALAEHQQHPPEGLDLTLTPEHIQQAVAQLTGQLRDNTTRQGEIRQQLKQDANNRQQQQSLMLEIENASQQVEDWG 880
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVEDWG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 881 YLNALIGSKEGDKFRKFAQGLTLDNLVWLANNQLTRLHGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGESFLVSL 960
Cdd:PRK10246 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVWLANQQLTRLHGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGESFLVSL 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNATGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
Cdd:PRK10246 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
|
....*..
gi 501083054 1041 DKMFAVE 1047
Cdd:PRK10246 1041 DSAFAVK 1047
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-1039 |
0e+00 |
|
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: 775.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKGEWKVDFTAEPfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSTVSQSQNDLMTRDTAECL 80
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALG----PIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 81 AEVEFEVKGESYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLEMTASLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:TIGR00618 77 AELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 161 FLNAKPKERAELLEELTGTEIYGQISALVFEKHKTARTDLEKLQAQASGVSLLAPEQQHSLNESLQALTDEEKQLLARQQ 240
Cdd:TIGR00618 157 FLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 241 LHQQHLHWLTRQNELQAEMNRRQQALRVSQEEQENAQPQLAALNLAHPARQLRPHWERIEEQTAAAGRTRQQIQEVNARL 320
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 321 QSVLHLRSRIRH---SAQQQSAELRATMQTLTGWLTEHERFRLWSSELAGWRALFAQQSSDKVQLLKWQQQCASDIRKRD 397
Cdd:TIGR00618 317 QSKMRSRAKLLMkraAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 398 ALPPNPLTLTPEEATAAlAQHTQQQPLRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQF 477
Cdd:TIGR00618 397 SLCKELDILQREQATID-TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 478 MDVKTICEQEARIKDLESQRALLQSGQPCPLCGSTSHPAIASYQALEPGVNQARRDALEKEVKTLAEEGAALRGQLETLT 557
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 558 QQLHRDESEVQALVKEEQALTQEWQTLCDALNVTLHPQDDISPWLTARQDYEQQLYQLSQRHMLQAQIAAHTGQVTQFQQ 637
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 638 QIDQRQTTLLSELRRYGLSLPADGEEASWLNARADDAQTWQQRQTELGELQTRIAQLTPLLETLPETDILPESDERVALD 717
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 718 NWRQVHDDCVSLQSQWQTLQQQEAQEMQRVAQAQAHFDAALKASVFDDRAAFLAALLDDETIARLEQHRQALENQLQQAQ 797
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 798 ALAAQANQALAEHQQHPPEGLD-LTLTPEHIQQAVAQLTGQLRDNTTRQGEIRQQLKQDANNRQQQQSLMLEIENASQQV 876
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDiLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 877 EDWGYLNALIGSKEGDKFRKFAQGLTLDNLVWLANNQLTRLHGRYLLQRKAS--EALELEVVDTWQADAVRDTRTLSGGE 954
Cdd:TIGR00618 876 DKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNArkYQGLALLVADAYTGSVRPSATLSGGE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 955 SFLVSLALA--LALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNATGKTIGVISHVEAMKERIPVQIKVKKI 1032
Cdd:TIGR00618 956 TFLASLSLAlaLADLLSTSGGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKT 1035
|
....*..
gi 501083054 1033 NGLGYSK 1039
Cdd:TIGR00618 1036 NAGSHVM 1042
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-205 |
3.21e-30 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 118.96 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 2 KILSLRLKNLNSLKGEWKVDFTAepfasnGLFAITGPTGAGKTTLLDAICLALYHETprlSTVSQSQNDLMTRDTAECLA 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDD------GLNLIVGPNGAGKSTILEAIRYALYGKA---RSRSKLRSDLINVGSEEASV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 82 EVEFEVKGESYRAFWsqnrarnqpdgnlqvprvelarcadgkiladkvkdklemtasltgldygrftrsmllSQGQFAAF 161
Cdd:COG0419 72 ELEFEHGGKRYRIER---------------------------------------------------------RQGEFAEF 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501083054 162 LNAKPKERAELLEELTGTEIYGQISALVFEKHKTARTDLEKLQA 205
Cdd:COG0419 95 LEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAE 138
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-162 |
2.35e-27 |
|
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: 110.82 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKGEWKVDFTaePFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLstvSQSQNDLMTRDTAECL 80
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFT--GLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRY---GRQENLRSVFAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 81 AEV--EFEVKGESYRAFwsqnRARnqpdgnlqvprvelarcadgkiladkvkdklemtasltGLDYGRFTRSMLLSQGQF 158
Cdd:cd03279 76 AEVsfTFQLGGKKYRVE----RSR--------------------------------------GLDYDQFTRIVLLPQGEF 113
|
....
gi 501083054 159 AAFL 162
Cdd:cd03279 114 DRFL 117
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
945-1031 |
1.13e-23 |
|
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: 100.04 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 945 RDTRTLSGGESFLVSLALAL--ALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNATGKTIGVISHVEAMKER 1022
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALalSEVLQNRGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKER 198
|
....*....
gi 501083054 1023 IPVQIKVKK 1031
Cdd:cd03279 199 IPQRLEVIK 207
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-206 |
5.98e-21 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 91.79 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 6 LRLKNLNSLKgEWKVDFtaepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPRLSTVSQSQN-----DLMTRDTAECL 80
Cdd:pfam13476 1 LTIENFRSFR-DQTIDF------SKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFvkgdiRIGLEGKGKAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 81 AEVEFEVKGE--SYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLEmtasltgldygRFTRSMLLSQGQF 158
Cdd:pfam13476 74 VEITFENNDGryTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKI-----------ILPLLVFLGQERE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501083054 159 AAFLNAKPKERAELLEELTGTEIYGQISALVFEKHKTARTDLEKLQAQ 206
Cdd:pfam13476 143 EEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-617 |
1.73e-13 |
|
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: 75.09 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 154 SQGQFAAFLNAKPKERAELLEELTGTEIYGQISALVFEKHKTARTDLEKLQAQASGV--SLLAPEQQHSLNESLQALTDE 231
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELerQLKSLERQAEKAERYKELKAE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 232 EKQLlarqqlhqQHLHWLTRQNELQAEMNRRQQALRVSQEEQENAQPQLAALNlahparqlrphwERIEEQTAAAGRTRQ 311
Cdd:TIGR02168 222 LREL--------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE------------EKLEELRLEVSELEE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 312 QIQEVNARLQSVLHLRSRIRHSAQQQSAELratmqtltgwlteherfrlwsselagwRALFAQQSSDKVQLLKWQQqcas 391
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERL---------------------------ANLERQLEELEAQLEELES---- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 392 dirKRDALppnpltltpEEATAALAQhtQQQPLRQRLASLHGQIAPKQKRREQLQTAIQNSQQEL-ARRSAALEGKRQKY 470
Cdd:TIGR02168 331 ---KLDEL---------AEELAELEE--KLEELKEELESLEAELEELEAELEELESRLEELEEQLeTLRSKVAQLELQIA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 471 KEKNQqfmdvktICEQEARIKDLESQRALLQSGQPcplcgstshPAIASYQALEPGVNQARRDALEKEVKTLAEEGAALR 550
Cdd:TIGR02168 397 SLNNE-------IERLEARLERLEDRRERLQQEIE---------ELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501083054 551 GQLETLTQQLHRDESEVQALVKEEQALTQEWQTLCDALNVTLHPQDDISPWLTARQDYEQQLYQLSQ 617
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-556 |
5.31e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 70.32 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKgewkvdfTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPrlstvSQSQNDLMTRDTAECL 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHD-------DSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKR-----TEKIEDMIKKGKNNLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 81 AEVEFEVKGESYRAFWSQNRARNQPDGNLQVPRvelarcaDGKILADKVKDKLE-MTASLTGLDYGRFTRSMLLSQGQFA 159
Cdd:PRK01156 69 VELEFRIGGHVYQIRRSIERRGKGSRREAYIKK-------DGSIIAEGFDDTTKyIEKNILGISKDVFLNSIFVGQGEMD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 160 AFLNAKPKERAELLEELTgteiygQISALVfEKHKTARTDLEKLQAQASGVSLLAPEQQHSLNEslqaLTDEEKQLlarQ 239
Cdd:PRK01156 142 SLISGDPAQRKKILDEIL------EINSLE-RNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQI---A 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 240 QLHQQHLHWLTRQNELQAEMNRRQQALRVSQEEQENAQPQLAALNlahparqlrphweRIEEQTAAAGRTRQQIQEVNAR 319
Cdd:PRK01156 208 DDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN-------------RYESEIKTAESDLSMELEKNNY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 320 LQSVLHLRSRIRHSA--------------QQQSAELRATMQTLTGWLTEHERFRLWSSELagwralfaqqSSDKVQLLKW 385
Cdd:PRK01156 275 YKELEERHMKIINDPvyknrnyindyfkyKNDIENKKQILSNIDAEINKYHAIIKKLSVL----------QKDYNDYIKK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 386 QqqcasdiRKRDALppNPLTLTPEEataalaQHTQQQPLRQRLASLHGQIAPKQKRREQLQTAIqnsQQELARRSAALEG 465
Cdd:PRK01156 345 K-------SRYDDL--NNQILELEG------YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI---SEILKIQEIDPDA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 466 KRQKYKEKNQQFMDVKT-ICEQEARIKDLESQR-------ALLQSGQPCPLCGST-----SHPAIASYQALEPGVNQaRR 532
Cdd:PRK01156 407 IKKELNEINVKLQDISSkVSSLNQRIRALRENLdelsrnmEMLNGQSVCPVCGTTlgeekSNHIINHYNEKKSRLEE-KI 485
|
570 580
....*....|....*....|....
gi 501083054 533 DALEKEVKTLAEEGAALRGQLETL 556
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKEYL 509
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-284 |
1.17e-11 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 68.50 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 6 LRLKNLNSLKGEW-KVDFTAepFASNglfAITGPTGAGKTTLLDAICLALYHETPRLSTVSQSQNDLMTRDtaeCLAEVE 84
Cdd:PHA02562 7 IRYKNILSVGNQPiEIQLDK--VKKT---LITGKNGAGKSTMLEALTFALFGKPFRDIKKGQLINSINKKD---LLVELW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 85 FEVKGESYRAFwsqnRArnqpdgnlQVPRVELARCaDGKILADK--VKDKLEMTASLTGLDYGRFTRSMLLSQGQFAAFL 162
Cdd:PHA02562 79 FEYGEKEYYIK----RG--------IKPNVFEIYC-NGKLLDESasSKDFQKYFEQMLGMNYKSFKQIVVLGTAGYVPFM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 163 NAKPKERAELLEELTGTEIYGQISALVFEKHKTARTDLEKLQAQASGVSllapEQ---QHSLNESLQALTDEEkqlLARQ 239
Cdd:PHA02562 146 QLSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQ----QQiktYNKNIEEQRKKNGEN---IARK 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 501083054 240 QLHQQHLhwLTRQNELQAEMNRRQQALRVSQEEQENAQPQLAALN 284
Cdd:PHA02562 219 QNKYDEL--VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLN 261
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
425-1017 |
6.86e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 425 RQRLASLHGQIAPKQKRREQLQTAIQNSQQELARrsaaLEGKRQKYKEKNQQFMDVKTICEQEARIKDLESQRALLQSgq 504
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEE----LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE-- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 505 pcplcgstshpAIASYQALepgvnQARRDALEKEVKTLAEEGAALRGQLETLT-QQLHRDESEVQALVKEEQALTQEWQT 583
Cdd:COG4717 154 -----------RLEELREL-----EEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 584 LCDALNVTLHPQDDISPWLTARQDyEQQLYQLSQRHMLQAQIAAHTGQVTQFQQQIDQRQTTLLSELRRYGLSLPADGEE 663
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 664 ASWLNARADDAQTWQQRQTELGELQTRIAQLTPLLETLPETDILPESDErvaLDNWRQVHDDcvslqsqwqtlqQQEAQE 743
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR---IEELQELLRE------------AEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 744 MQRVAQAQAHFDAALKASVFDDRAAFLAALLDDETIARLEQHRQALENQLQQAQALAAQANQALAEHQqhppegldLTLT 823
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--------LEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 824 PEHIQQAVAQLTGQLRDNTTRQGEIRQQLKQDANNRQQQQsLMLEIENASQQ----VEDWGYLNalIGSKEGDKFRKFAQ 899
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEEDGELAE-LLQELEELKAElrelAEEWAALK--LALELLEEAREEYR 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 900 GLTLDNLVWLANNQLTRL-HGRYLLQRkASEALELEVVDtwQADAVRDTRTLSGGE----------SFLVslalalalsd 968
Cdd:COG4717 511 EERLPPVLERASEYFSRLtDGRYRLIR-IDEDLSLKVDT--EDGRTRPVEELSRGTreqlylalrlALAE---------- 577
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 501083054 969 lvSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNATGKTIGVISHVE 1017
Cdd:COG4717 578 --LLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEE 624
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-790 |
9.69e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 154 SQGQFAAFLNAKPKERAELLEELTG-----------------------------TEIYGQISAL-----VFEKHKTARTD 199
Cdd:COG1196 142 GQGMIDRIIEAKPEERRAIIEEAAGiskykerkeeaerkleateenlerledilGELERQLEPLerqaeKAERYRELKEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 200 LEKLQAQASGVSL-LAPEQQHSLNESLQALTDEEKQLLARQQLHQQHLHWL-TRQNELQAEMNRRQQALRVSQEEQENAQ 277
Cdd:COG1196 222 LKELEAELLLLKLrELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEAQAEEYELLAELARLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 278 PQLAALNLAhpARQLRPHWERIEEQTAAAGRTRQQIQEVNARLQSVLHLRSRIRHSAQQQSAELRATMQTLTGwlTEHER 357
Cdd:COG1196 302 QDIARLEER--RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--ELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 358 FRLWSSELAGWRALFAQQSSDKVQLLKWQQQCASDIRKRDALppnpltltpEEATAALAQHTQQqpLRQRLASLHGQIAP 437
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL---------EEELEELEEALAE--LEEEEEEEEEALEE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 438 KQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQFMDVKticEQEARIKDLESQRALLQSGqpcplcgstshPAI 517
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA---ARLLLLLEAEADYEGFLEG-----------VKA 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 518 ASYQALEPGVNQARRDALEKEVKTLAEEGAALRGQLETLTQQLHRDESEVQALVKEEQALTQEWQTLcDALNVTLHPQDD 597
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL-DKIRARAALAAA 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 598 ISPW--LTARQDYEQQLYQLSQRHMLQAQIAAHTGQVTQFQQQIDQRQTTLLSELRRyglsLPADGEEASWLNARADdaq 675
Cdd:COG1196 592 LARGaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE----VTLEGEGGSAGGSLTG--- 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 676 twQQRQTELGELQTRIAQLTPLLETLPETDILPESDERVALDNWRQVHDdcvsLQSQWQTLQQQEAQEMQRVAQAQAHFD 755
Cdd:COG1196 665 --GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE----AEEERLEEELEEEALEEQLEAEREELL 738
|
650 660 670
....*....|....*....|....*....|....*
gi 501083054 756 AALKASVFDDRAAFLAALLDDETIARLEQHRQALE 790
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-569 |
4.47e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKgewKVDFTAEPfasnGLFAITGPTGAGKTTLLDAICLALYHETprlsTVSQSQNDLMTRDTAECL 80
Cdd:PRK02224 1 MRFDRVRLENFKCYA---DADLRLED----GVTVIHGVNGSGKSSLLEACFFALYGSK----ALDDTLDDVITIGAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 81 AEVEFEVKGESYRAfwsQNRARNQPDgnlqvpRVELARC--ADGKILADKVKDKLEMTASLTGLDYGRFTRSMLLSQGQF 158
Cdd:PRK02224 70 IELWFEHAGGEYHI---ERRVRLSGD------RATTAKCvlETPEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 159 AAFLNAKPKERAELLEELTgteiygQISAL--VFEKHKTARTDLEKLQAQASGvsllapeqqhslneslqALTDEEKQLl 236
Cdd:PRK02224 141 NKLINATPSDRQDMIDDLL------QLGKLeeYRERASDARLGVERVLSDQRG-----------------SLDQLKAQI- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 237 arQQLHQQHLHwlTRQNELQAEMNRRQQALRVSQEEQENAQPQLAALNlahparqlrphwERIEEQTaaagRTRQQIQEV 316
Cdd:PRK02224 197 --EEKEEKDLH--ERLNGLESELAELDEEIERYEEQREQARETRDEAD------------EVLEEHE----ERREELETL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 317 NA---RLQSVLHLRSRIRHSAQQQSAELRATMQTLtgwlteherfrlwSSELAGWRALFAQQSSDKVQLLKWQQQCASDI 393
Cdd:PRK02224 257 EAeieDLRETIAETEREREELAEEVRDLRERLEEL-------------EEERDDLLAEAGLDDADAEAVEARREELEDRD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 394 RK-RDALppnpltltPEEATAALAQHTQQQPLRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKE 472
Cdd:PRK02224 324 EElRDRL--------EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 473 KNQQFMDVKT----------------------ICEQEARIK----DLESQRALLQSGQpCPLCGstshpaiasyQALEPG 526
Cdd:PRK02224 396 LRERFGDAPVdlgnaedfleelreerdelrerEAELEATLRtareRVEEAEALLEAGK-CPECG----------QPVEGS 464
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 501083054 527 VNQARRDALEKEVKTLAEEGAALRGQLETLTQQLHRDESEVQA 569
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-580 |
6.04e-09 |
|
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: 60.47 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 3 ILSLRLKNLNSLKGEWKVDFtaepfaSNGLFAITGPTGAGKTTLLDAICLALYHET------PRLST-VSQSQNDlmtRD 75
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPF------SKGFTVISGPNGSGKSNIGDAILFALGLSSskamraERLSDlISNGKNG---QS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 76 TAECLAEVEFevkgesyrafwsQNRARNQPDgNLQVPRvELARCADGKILADKVKDK------LEMTASLTGLDYGRFTR 149
Cdd:TIGR02169 73 GNEAYVTVTF------------KNDDGKFPD-ELEVVR-RLKVTDDGKYSYYYLNGQrvrlseIHDFLAAAGIYPEGYNV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 150 SMllsQGQFAAFLNAKPKERAELLEELTGTEIYGqisalvfEKHKTARTDLEKLQAQASGVSLLAPEqqhsLNESLQALT 229
Cdd:TIGR02169 139 VL---QGDVTDFISMSPVERRKIIDEIAGVAEFD-------RKKEKALEELEEVEENIERLDLIIDE----KRQQLERLR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 230 DEEKQLLarqqlhqqhlhwltRQNELQAEMNRRQQALRVSQEEQENAQpqlaalnlahpARQLRPHWERIEEQTAAAGRT 309
Cdd:TIGR02169 205 REREKAE--------------RYQALLKEKREYEGYELLKEKEALERQ-----------KEAIERQLASLEEELEKLTEE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 310 RQQI-QEVNARLQSVLHLRSRIRHSAQQQSAELRATMQTLTGWLTEHERfrlwsselagwralfaQQSSDKVQLLKWQQQ 388
Cdd:TIGR02169 260 ISELeKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER----------------SIAEKERELEDAEER 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 389 CASDIRKRDAlppnpltltpeeataalaqhtqqqpLRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQ 468
Cdd:TIGR02169 324 LAKLEAEIDK-------------------------LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 469 KYKEKNQQFMDVKTICEQEARIKD--LESQRALLQSGQPCPLCGSTSHPAIASyqaLEPGVNQ--ARRDALEKEVKTLAE 544
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINelKRELDRLQEELQRLSEELADLNAAIAG---IEAKINEleEEKEDKALEIKKQEW 455
|
570 580 590
....*....|....*....|....*....|....*.
gi 501083054 545 EGAALRGQLETLTQQLHRDESEVQALVKEEQALTQE 580
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-126 |
3.38e-08 |
|
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: 54.92 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 3 ILSLRLKNLNSLKGEWKVDFTaepfasNGLFAITGPTGAGKTTLLDAICLALYHETPRLSTVSQSQNDlMTRDTAEcLAE 82
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFF------SPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPK-LIREGEV-RAQ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 501083054 83 VEFE---VKGESYRAFWSQNRARN-----QPDGNLQVPRvELARCADG-KILA 126
Cdd:cd03240 73 VKLAfenANGKKYTITRSLAILENvifchQGESNWPLLD-MRGRCSGGeKVLA 124
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-559 |
7.97e-07 |
|
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: 53.53 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 197 RTDLEKLQAQASGVSLLAPEQQHSLNESLQALTDEEKQLLARQQLHQQHLHWLTRQNELQAEMNRRQQALrvsQEEQENA 276
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL---EQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 277 QPQLAALNLAHPARQLRPHWERIEEQTAAAGRTRQQIQEVNARLQSVLHLRSRIRHSAQQQSAELRAtmQTLTGWLTEHE 356
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--LTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 357 RfrlwSSELAGWRALFAQQSSDKvqllkwQQQCASDIRKRDalppnpLTLTPEEATAALAQhtqqqpLRQRLASLHG--- 433
Cdd:TIGR02169 835 I----QELQEQRIDLKEQIKSIE------KEIENLNGKKEE------LEEELEELEAALRD------LESRLGDLKKerd 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 434 ----QIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQFMDVKTICEQEARIKDLESQRALLQsgqpcplc 509
Cdd:TIGR02169 893 eleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE-------- 964
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 510 gstshpaiASYQALEPgVN----------QARRDALEKEVKTLAEEGAALRGQLETLTQQ 559
Cdd:TIGR02169 965 --------EEIRALEP-VNmlaiqeyeevLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
424-877 |
1.91e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 424 LRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQFMdvkticEQEARIKDLESQRALLQSG 503
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY------ELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 504 QpcplcgSTSHPAIASYQALEpGVNQARRDALEKEVKTLAEEGAALRGQLETLTQQLHRDESEVQALVKEEQALTQEWQT 583
Cdd:COG1196 311 R------RELEERLEELEEEL-AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 584 LCDALnvtLHPQDDISPWLTARQDYEQQLYQLSQR--HMLQAQIAAHTGQVTQFQQQIDQRQTTLLSELRRYGLSLPADG 661
Cdd:COG1196 384 LAEEL---LEALRAAAELAAQLEELEEAEEALLERleRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 662 EEASWLNARADDAQTWQQRQTELGELQTRIAQLTPLLETLPETDILPESDERVALDNWRQVHDDCVSLQSQWQTLQQQEA 741
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 742 Q------------EMQRVAQAQAHFDAALKASvfddRAAFLAALLDDETIARLEQHRQALENQLQQAQALAAQANQALAE 809
Cdd:COG1196 541 EaalaaalqnivvEDDEVAAAAIEYLKAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501083054 810 HQQHPPEGLDLTLTPEHIQQAVAQLTGQLRDNTTRQGEIRQQLKQDANNRQQQQSLMLEIENASQQVE 877
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
424-588 |
3.17e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 424 LRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQFMDVKTICEQEARIKDLESQRALLQSg 503
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 504 qpcplcgstshpaiASYQALEpgvNQARRDALEKEVKTLAEEGAALRGQLETLTQQLhrdESEVQALVKEEQALTQEWQT 583
Cdd:COG1579 108 --------------LEDEILE---LMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
|
....*
gi 501083054 584 LCDAL 588
Cdd:COG1579 168 LAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-694 |
4.03e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 169 RAELLEELTGTEIYGQISALVFEKHKTARTDLEKLQAQASGVSLLAPEQQHSLNESLQALTDEEKQLLARQQLHQQHLHW 248
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 249 LTRQNELQAEMNRRQQALRVSQEEQENAQpQLAALNLAHPARQLRPHWERIEEQTAAAGRTRQQIQEVNARLQSVLHLRS 328
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 329 RIRHSAQQQSAELRATMQTLTGWLTEHERFRLWSSELAGWRALFAQQSSDKVQLLKWQQQCASDIRKRDALPPNPLtLTP 408
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAG 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 409 EEATAALAQHTQQQPLRQRLASLHGQIApkQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQFMDVKTICEQEA 488
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIV--VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 489 RIKDLESQRALLQSGQpcplcGSTSHPAIASYQALEPGVNQARRDALEKEVKTLAEEGAALRGQLETLTQQLHRDESEVQ 568
Cdd:COG1196 603 LVASDLREADARYYVL-----GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 569 ALVKEEQALTQEWQTLcdalnvtlhpqddispwlTARQDYEQQLYQLSQRHMLQAQIAAHTGQVTQFQQQIDQRQTTLLS 648
Cdd:COG1196 678 EAELEELAERLAEEEL------------------ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 501083054 649 ELRRYGLSLPADGEEASwlnARADDAQTWQQRqteLGELQTRIAQL 694
Cdd:COG1196 740 ELLEEEELLEEEALEEL---PEPPDLEELERE---LERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
411-627 |
1.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 411 ATAALAQHTQQQPLRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQfmdvktICEQEARI 490
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE------LAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 491 KDLESQRALLQ----------------------SGQPCPLCGSTSHPAIASYQALEPGVNQARRDALEKEVKTLaEEGAA 548
Cdd:COG4942 86 AELEKEIAELRaeleaqkeelaellralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501083054 549 LRGQLETLTQQLHRDESEVQALVKEEQALTQEWQTLCDALNVTLhpqDDISPWLTARQDYEQQLYQLSQRhmLQAQIAA 627
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIAR--LEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
529-955 |
1.94e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 529 QARRDALEKEVKTLAEEGAALRGQLETLTQQLHRDESEVQALVKEEQALTQEWQTLCDALNVTlhpQDDISPWLTARQDY 608
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 609 EQQLYQLSQRH-MLQAQIAAHTGQVTQFQQQIDQRQTTLLSELRRYglsLPADGEEASWLNARADDAQTWQQRQTELGEL 687
Cdd:COG1196 322 EEELAELEEELeELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 688 QTRIAQLTPLLETLPETDILPESDERVALDNWRQVHDDCVSLQSQWQTLQQQEAQEMQRVAQAQAHfDAALKASVFDDRA 767
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL-LAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 768 AFLAALLDDETIARLEQHRQALENQLQQAQALAAQANQALAEHQQHPPEGLDLTLTPEHIQQAVAQLTGQL----RDNTT 843
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnivVEDDE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 844 RQGEIRQQLKQDANNR------QQQQSLMLEIENASQQVEDWGYLNALIGSKEGDKFRKFAQGLTLDNLVWLANNQLTRL 917
Cdd:COG1196 558 VAAAAIEYLKAAKAGRatflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
410 420 430
....*....|....*....|....*....|....*...
gi 501083054 918 HGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGES 955
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-50 |
2.03e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.97 E-value: 2.03e-05
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-54 |
3.76e-05 |
|
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: 45.04 E-value: 3.76e-05
10 20
....*....|....*....|....*....
gi 501083054 26 PFASNGLFAITGPTGAGKTTLLDAICLAL 54
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIGLAL 45
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-55 |
6.08e-05 |
|
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: 44.54 E-value: 6.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 501083054 1 MKILSLRLKNLNSLKGewkVDFTAEPfasNGLFAITGPTGAGKTTLLDAICLALY 55
Cdd:cd00267 2 IENLSFRYGGRTALDN---VSLTLKA---GEIVALVGPNGSGKSTLLRAIAGLLK 50
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
931-1002 |
6.56e-05 |
|
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: 42.61 E-value: 6.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501083054 931 LELEVV--DTWQADAVRDTRTLSGGE-----SFLVSLALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDA 1002
Cdd:pfam13558 12 FEVEVRdeDGSEVETYRRSGGLSGGEkqllaYLPLAAALAAQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
143-558 |
1.12e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 143 DYGRFTRSMLLSQGQFAAFLNAKPKERAELLEELTG--TEIYGQISALVFEKHKTARTdLEKLQAQASGVSLLapEQQHS 220
Cdd:PRK04863 255 DRDLFKHLITESTNYVAADYMRHANERRVHLEEALElrRELYTSRRQLAAEQYRLVEM-ARELAELNEAESDL--EQDYQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 221 -----LNESLQALTDEEKQLLARQQLHQQHLHwLTRQNELQAEMNRRQQALRVSQEEQENAQPQLAAlnlahparQLRPH 295
Cdd:PRK04863 332 aasdhLNLVQTALRQQEKIERYQADLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKS--------QLADY 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 296 WERIEEQTAAAGRTRQQIQEVnARLQSVLHLRSRIRHSAQQQSAELRATMQTLTGWLTEHERfRLWSSELAgwralfAQQ 375
Cdd:PRK04863 403 QQALDVQQTRAIQYQQAVQAL-ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQ-KLSVAQAA------HSQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 376 SSDKVQLLkwqQQCASDIRKRDALppnpltltpEEATAALAQHTQQQPLRQRLASLHGQIAPKQKRREQLQTAIQ----- 450
Cdd:PRK04863 475 FEQAYQLV---RKIAGEVSRSEAW---------DVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERllaef 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 451 ------------NSQQELARRSAALEGKRQKYKEKNQQFMDVKTICEQ-EARIKDLESQRALLQSGQP-----CPLCGST 512
Cdd:PRK04863 543 ckrlgknlddedELEQLQEELEARLESLSESVSEARERRMALRQQLEQlQARIQRLAARAPAWLAAQDalarlREQSGEE 622
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501083054 513 shpaIASYQALEpgvnQARRDALEKEVKT------LAEEGAALRGQLETLTQ 558
Cdd:PRK04863 623 ----FEDSQDVT----EYMQQLLERERELtverdeLAARKQALDEEIERLSQ 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-476 |
1.99e-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: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 251 RQNELQAEMNRRQQALRVSQEEQENAQPQLAALNlahparqlrphwERIEEQTAAAGRTRQQIQEVNARLQSvlhlrsri 330
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALE------------RRIAALARRIRALEQELAALEAELAE-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 331 rhsAQQQSAELRATMQTLTGWLTEHERFRLWSSELAGWRALFAQQS-SDKVQLLKWQQQCASDIRKRdalppnplTLTPE 409
Cdd:COG4942 88 ---LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQ--------AEELR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501083054 410 EATAALAQhtQQQPLRQRLASLHGQIAPKQKRREQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQ 476
Cdd:COG4942 157 ADLAELAA--LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-343 |
2.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 167 KERAELLEELTGTeiygqisalvFEKHKTARTDLEKLQAQASGVSL--------LAPEQQHSLNESLQALTDEEKQLLAR 238
Cdd:COG4913 248 REQIELLEPIREL----------AERYAAARERLAELEYLRAALRLwfaqrrleLLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 239 QQLHQQHLHWLTRQ---------NELQAEMNRRQQALRVSQEEQENAQPQLAALNLAHP----------------ARQLR 293
Cdd:COG4913 318 LDALREELDELEAQirgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPasaeefaalraeaaalLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501083054 294 PHWERIEEQTAAAGRT----RQQIQEVNARLQSVLHLRSRIRHSAQQQSAELRA 343
Cdd:COG4913 398 EELEALEEALAEAEAAlrdlRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-570 |
3.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKgEWKVDFTaepfasNGLFAITGPTGAGKTTLLDAICLALYHETPrlSTVSQSQNDLMTRD-TAEC 79
Cdd:PRK03918 1 MKIEELKIKNFRSHK-SSVVEFD------DGINLIIGQNGSGKSSILEAILVGLYWGHG--SKPKGLKKDDFTRIgGSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 80 LAEVEFEVKGESYRAFWSQNRArnqpdgnlqvprVELARCADG-KILADKVKDKLEMTASLtgLDYGRFTRSMLLSQGQF 158
Cdd:PRK03918 72 EIELKFEKNGRKYRIVRSFNRG------------ESYLKYLDGsEVLEEGDSSVREWVERL--IPYHVFLNAIYIRQGEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 159 AAFLNAKpKERAELLEELTGTEIYGQI---SALVFEKHKTARTDLEKLQAQASGVSLLAPEQQHSLNESLQALTDEEKQL 235
Cdd:PRK03918 138 DAILESD-ESREKVVRQILGLDDYENAyknLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 236 larqqlhqqhlhwltrqNELQAEMnrrqQALRVSQEEQENAQPQLAALNLAhpARQLRPHWERIEEQTaaaGRTRQQIQE 315
Cdd:PRK03918 217 -----------------PELREEL----EKLEKEVKELEELKEEIEELEKE--LESLEGSKRKLEEKI---RELEERIEE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 316 VNARLQSvlhLRSRIRHSAQ-QQSAE----LRATMQTLTGWLTEHE-RFRLWSSELAGWRALFaQQSSDKVQLLKWQQQC 389
Cdd:PRK03918 271 LKKEIEE---LEEKVKELKElKEKAEeyikLSEFYEEYLDELREIEkRLSRLEEEINGIEERI-KELEEKEERLEELKKK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 390 ASDIRKR-DALPPNPLTLtpEEATAALAqhtQQQPLRQRLASLhgqiaPKQKRREQLqtaiqnsqQELARRSAALEGKRQ 468
Cdd:PRK03918 347 LKELEKRlEELEERHELY--EEAKAKKE---ELERLKKRLTGL-----TPEKLEKEL--------EELEKAKEEIEEEIS 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 469 KYKEKnqqfmdvktICEQEARIKDLESQRALLQSGQP-CPLCG---STSHPA--IASYqalepgvnQARRDALEKEVKTL 542
Cdd:PRK03918 409 KITAR---------IGELKKEIKELKKAIEELKKAKGkCPVCGrelTEEHRKelLEEY--------TAELKRIEKELKEI 471
|
570 580
....*....|....*....|....*...
gi 501083054 543 AEEGAALRGQLETLTQQLHRdESEVQAL 570
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKK-ESELIKL 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-695 |
3.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 169 RAELLEEltgTEIYGQISALV--FEKHKTARTDLEKLQAQasgVSLLAPEQQHslNESLQALT------DEEKQLLARQQ 240
Cdd:COG4913 214 REYMLEE---PDTFEAADALVehFDDLERAHEALEDAREQ---IELLEPIREL--AERYAAARerlaelEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 241 LHQQHLHWLTRQNELQAEMNRRQQALRVSQEEQENAQPQLAALNLA---HPARQLrphwERIEEQTAAAGRTRQQIQEVN 317
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgNGGDRL----EQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 318 ARLQSVLH---------------LRSRIRHSAQQQSAELRATMQTLTGWLTEHERFRlwsSELAGWRALFAQQSSDKVQL 382
Cdd:COG4913 362 ARLEALLAalglplpasaeefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLR---RELRELEAEIASLERRKSNI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 383 LKWQQQCASDIR-----KRDALPP----------------------NPLTLT---PEEATAALAQHTQQQPLRQRLaslH 432
Cdd:COG4913 439 PARLLALRDALAealglDEAELPFvgelievrpeeerwrgaiervlGGFALTllvPPEHYAAALRWVNRLHLRGRL---V 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 433 GQIAPKQKRREQLQTAIQNSqqeLARRSAALEGKRQKY--KEKNQQFMDVKtiCEQEARIKDleSQRALLQSGQpcplcg 510
Cdd:COG4913 516 YERVRTGLPDPERPRLDPDS---LAGKLDFKPHPFRAWleAELGRRFDYVC--VDSPEELRR--HPRAITRAGQ------ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 511 sTSHP----------AIASYQALepGV-NQARRDALEKEVKTLAEEGAALRGQLETLTQQLHR----------------D 563
Cdd:COG4913 583 -VKGNgtrhekddrrRIRSRYVL--GFdNRAKLAALEAELAELEEELAEAEERLEALEAELDAlqerrealqrlaeyswD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 564 ESEVQALVKEEQALTQEWQTLCDALNVTLHPQDDISPWLTARQDYEQQLYQLSQRH-MLQAQIAAHTGQVTQfqqqidqr 642
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIgRLEKELEQAEEELDE-------- 731
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 501083054 643 qttllSELRRYGLSLPADGEEASWLNARADDAQTWQQRQTELGELQTRIAQLT 695
Cdd:COG4913 732 -----LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-54 |
5.64e-04 |
|
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: 41.91 E-value: 5.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 501083054 3 ILSLRLKNLNSLKGEWKVDFtaepfaSNGLFAITGPTGAGKTTLLDAICLAL 54
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGG------SNSFNAIVGPNGSGKSNIVDAICFVL 46
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
844-1016 |
6.27e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 844 RQGEIRQQLKQDANNRQQQqslmleienasqqvedwgyLNALIGSKEGDKFRKfaqglTLDNLVWLANNQLTRLHGRYLL 923
Cdd:COG0419 87 RQGEFAEFLEAKPSERKEA-------------------LKRLLGLEIYEELKE-----RLKELEEALESALEELAELQKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 924 QRKASEALElevvdtwqadAVRDTRTLSGGESFLVSLalalalsdlvshkTRIDSLFLDegFGTLDSETLDTALDALDAL 1003
Cdd:COG0419 143 KQEILAQLS----------GLDPIETLSGGERLRLAL-------------ADLLSLILD--FGSLDEERLERLLDALEEL 197
|
170
....*....|...
gi 501083054 1004 natgktiGVISHV 1016
Cdd:COG0419 198 -------AIITHV 203
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
409-579 |
7.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 409 EEATAALAQHTQQQplrqRLASLHGQIAPKQKRREQLQTAIQNSQQELAR---RSAALEGKRQKYKEKNQQFMDVKTICE 485
Cdd:COG3206 192 EEAEAALEEFRQKN----GLVDLSEEAKLLLQQLSELESQLAEARAELAEaeaRLAALRAQLGSGPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 486 QEARIKDLESQRALLQSGqpcplcGSTSHPAIASYQALEPGVNQARRDALEKEVKTLAEEGAALRGQLETLTQQLHRDES 565
Cdd:COG3206 268 LRAQLAELEAELAELSAR------YTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
170
....*....|....
gi 501083054 566 EVQALVKEEQALTQ 579
Cdd:COG3206 342 RLAELPELEAELRR 355
|
|
| UreG |
cd05540 |
urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is ... |
35-80 |
8.67e-04 |
|
urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is an enzyme which catalyzes the decomposition of urea to form ammonia and carbon dioxide. Bacterial urease is a trimer of three subunits which are encoded by genes ureA, ureB, and ureC. Up to four accessory proteins (ureD, ureE, ureF, and ureG) are required for urease catalytical function. UreG may play an important role in nickel incorporation of the urease metallocenter. UreG is a member of the Fer4_NifH superfamily which contains an ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349776 Cd Length: 191 Bit Score: 41.48 E-value: 8.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 501083054 35 ITGPTGAGKTTLLDAICLALyHETPRLSTVSqsqNDLMTRDTAECL 80
Cdd:cd05540 5 IGGPVGSGKTALVEALCRAL-RDKYSIAVVT---NDIYTKEDAEFL 46
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
190-341 |
1.58e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 190 FEKHKTARTDLEKLQAQASGvsllAPEQQHSLNESLQALTDEEKQLlARQQLHQQHLhwltrqNELQAEMNRRQQALRVS 269
Cdd:PRK11281 72 LDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKDDNDEE-TRETLSTLSL------RQLESRLAQTLDQLQNA 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501083054 270 QEEQENAQPQLAALnlahparQLRPhwERIEEQTAAAgrtRQQIQEVNARLQSVLHLRSRIRHSAQQQ-SAEL 341
Cdd:PRK11281 141 QNDLAEYNSQLVSL-------QTQP--ERAQAALYAN---SQRLQQIRNLLKGGKVGGKALRPSQRVLlQAEQ 201
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-60 |
2.24e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 2.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKGEwKVDFtaepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPR 60
Cdd:COG3593 1 MKLEKIKIKNFRSIKDL-SIEL------SDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-62 |
2.63e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 40.23 E-value: 2.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501083054 4 LSLRLKNLN-SLKGEWK---------VDFTAEPfasNGLFAITGPTGAGKTTLLDAicLALYHETPRLS 62
Cdd:cd03213 2 VTLSFRNLTvTVKSSPSksgkqllknVSGKAKP---GELTAIMGPSGAGKSTLLNA--LAGRRTGLGVS 65
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-114 |
4.06e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 40.26 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 3 ILSLRLKNlNSLKGEWKVDFtaepfaSNGLFAITGPTGAGKTTLLDAICLALyhetprlstVSQSQNDLMTRDTAECLAE 82
Cdd:cd03241 1 LLELSIKN-FALIEELELDF------EEGLTVLTGETGAGKSILLDALSLLL---------GGRASADLIRSGAEKAVVE 64
|
90 100 110
....*....|....*....|....*....|..
gi 501083054 83 VEFEVKGESyRAFWSQNRARNQPDGNLQVPRV 114
Cdd:cd03241 65 GVFDISDEE-EAKALLLELGIEDDDDLIIRRE 95
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
420-584 |
6.69e-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: 40.39 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 420 QQQPLRQRLASLHGQIapkqkrrEQLQTAIQNSQQELARRSAALEGKRQKYKEKNQQFMDVK-TICEQEARIKDLESQRA 498
Cdd:TIGR04523 378 ENQSYKQEIKNLESQI-------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKeTIIKNNSEIKDLTNQDS 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 499 LLQSgqpcplcgstshpaiaSYQALEpgvnqARRDALEKEVKTLAEEGAALRGQLETLTQQLHRDESEVQALVKEEQALT 578
Cdd:TIGR04523 451 VKEL----------------IIKNLD-----NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
....*.
gi 501083054 579 QEWQTL 584
Cdd:TIGR04523 510 EKVKDL 515
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
25-82 |
7.79e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 38.89 E-value: 7.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 25 EPFASNGLFAIT--GPTGAGKTTLLDAICLALyHETPRLSTVSqsqNDLMTRDTAECLAE 82
Cdd:COG0378 6 ALFAEKGVLAVNlmGSPGSGKTTLLEKTIRAL-KDRLRIAVIE---GDIYTTEDAERLRA 61
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-50 |
8.33e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 39.89 E-value: 8.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 501083054 1 MKILSLRLKNLNSLKgEWKVDFtaepfaSNGLFAITGPTGAGKTTLLDAI 50
Cdd:pfam13175 1 MKIKSIIIKNFRCLK-DTEIDL------DEDLTVLIGKNNSGKSSILEAL 43
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
949-1039 |
9.95e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083054 949 TLSGGESFLVSLALALALSDLVShkTRIDSLFLDEGFGTLDSETLDTAL-DALDALNA-TGKTIGVISHVEAMKERIPVQ 1026
Cdd:cd03240 115 RCSGGEKVLASLIIRLALAETFG--SNCGILALDEPTTNLDEENIEESLaEIIEERKSqKNFQLIVITHDEELVDAADHI 192
|
90
....*....|...
gi 501083054 1027 IKVKKiNGLGYSK 1039
Cdd:cd03240 193 YRVEK-DGRQKSR 204
|
|
|