|
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: 1563.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKGEWKIDFTREPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:PRK10246 1 MKILSLRLKNLNSLKGEWKIDFTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLNNVSQSQNDLMTRDTAECL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 81 AEVEFEVKDEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:PRK10246 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQAPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQ 240
Cdd:PRK10246 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEQAQPQLAALSLAQPARNLRPHWERIAEHSTALAHTRQQIEEVNTRL 320
Cdd:PRK10246 241 QQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 321 QSTMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALA 400
Cdd:PRK10246 321 QSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 401 AITLTLTADEVASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQQLADV 480
Cdd:PRK10246 401 AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 481 KTICEQEARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQARLLTLEKEVKKLGEEGATLRGQLDALTKQL 560
Cdd:PRK10246 481 KTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 561 QRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
Cdd:PRK10246 561 QRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 641 QRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRMQQLTPILETLPQSDELPHSEETVALENWR 720
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 721 QVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLV 800
Cdd:PRK10246 721 QVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLV 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 801 TQTAETLTQHQQHRPGGLSLTVTVEQIQQELAQTHQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQVEDWG 880
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVEDWG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKASEALEVEVVDTWQADAVRDTRTLSGGESFLVSL 960
Cdd:PRK10246 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVWLANQQLTRLHGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGESFLVSL 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
Cdd:PRK10246 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
|
....*..
gi 446621497 1041 ESAFAVK 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: 985.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKGEWKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALG----PIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 81 AEVEFEVKDEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:TIGR00618 77 AELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQ 240
Cdd:TIGR00618 157 FLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEQAQPQLAALSLAQPARNLRPHWERIAEHSTALAHTRQQIEEVNTRL 320
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 321 QSTMALRASIRHH---AAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLN 397
Cdd:TIGR00618 317 QSKMRSRAKLLMKraaHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 398 ALAAITLTLTAdEVASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQQL 477
Cdd:TIGR00618 397 SLCKELDILQR-EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 478 ADVKTICEQEARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQARLLTLEKEVKKLGEEGATLRGQLDALT 557
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 558 KQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQ 637
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 638 QIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRMQQLTPILETLPQSDELPHSEETVALE 717
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 718 NWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQ 797
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 798 TLVTQTAETLTQHQQHRP-GGLSLTVTVEQIQQELAQTHQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQV 876
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPsDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 877 EDWGYLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKAS--EALEVEVVDTWQADAVRDTRTLSGGE 954
Cdd:TIGR00618 876 DKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNArkYQGLALLVADAYTGSVRPSATLSGGE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 955 SFLVSLALA--LALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKI 1032
Cdd:TIGR00618 956 TFLASLSLAlaLADLLSTSGGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKT 1035
|
....*..
gi 446621497 1033 NGLGYSK 1039
Cdd:TIGR00618 1036 NAGSHVM 1042
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-205 |
2.00e-30 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 119.34 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 2 KILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRlsnVSQSQNDLMTRDTAECLA 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDD------GLNLIVGPNGAGKSTILEAIRYALYGKARS---RSKLRSDLINVGSEEASV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 82 EVEFEVKDEAYRAFWsqnrarnqpdgnlqvprvelarcadgkiladkvkdkleltatltgldygrftrsmllSQGQFAAF 161
Cdd:COG0419 72 ELEFEHGGKRYRIER---------------------------------------------------------RQGEFAEF 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446621497 162 LNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQA 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 |
1.10e-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: 111.98 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKGEWKIDFTrePFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlmtRDTAECL 80
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFT--GLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSV---FAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 81 AEV--EFEVKDEAYRAFwsqnRARnqpdgnlqvprvelarcadgkiladkvkdkleltatltGLDYGRFTRSMLLSQGQF 158
Cdd:cd03279 76 AEVsfTFQLGGKKYRVE----RSR--------------------------------------GLDYDQFTRIVLLPQGEF 113
|
....
gi 446621497 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 |
9.89e-24 |
|
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: 100.42 E-value: 9.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 945 RDTRTLSGGESFLVSLALAL--ALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKER 1022
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALalSEVLQNRGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKER 198
|
....*....
gi 446621497 1023 IPVQIKVKK 1031
Cdd:cd03279 199 IPQRLEVIK 207
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-206 |
1.42e-22 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 96.41 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 6 LRLKNLNSLKgEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQN-----DLMTRDTAECL 80
Cdd:pfam13476 1 LTIENFRSFR-DQTIDF------SKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFvkgdiRIGLEGKGKAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 81 AEVEFEVKDEA--YRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLEltatltgldygRFTRSMLLSQGQF 158
Cdd:pfam13476 74 VEITFENNDGRytYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKI-----------ILPLLVFLGQERE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446621497 159 AAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQ 206
Cdd:pfam13476 143 EEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-717 |
3.28e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 154 SQGQFAAFLNAKPKERAELLEELTG-----------------------------TEIYGQIS-----AMVFEQHKSARTE 199
Cdd:COG1196 142 GQGMIDRIIEAKPEERRAIIEEAAGiskykerkeeaerkleateenlerledilGELERQLEplerqAEKAERYRELKEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 200 LEKLQAQASGVAL-LTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWL-TRLDELQQEASRRQQALQQALAEEEQAQ 277
Cdd:COG1196 222 LKELEAELLLLKLrELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEAQAEEYELLAELARLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 278 PQLAAL-----SLAQPARNLRphwERIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQQSLNAWL 352
Cdd:COG1196 302 QDIARLeerrrELEERLEELE---EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 353 QEHDRFRQwnNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALAAITLTLTADEVASAQAQHAEQRpLRQRLVALH 432
Cdd:COG1196 379 EELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-AAEEEAELE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 433 GQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQQLADVKTICEQEARIKTLEAQRAQLQAGQPCPLCGST 512
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 513 SHPAVEAY--QALEPGV--NQARLLTLEKEVKKLGEEGATL--------RGQLDALTKQLQRDE--NEAQSLRQDEQALT 578
Cdd:COG1196 536 YEAALEAAlaAALQNIVveDDEVAAAAIEYLKAAKAGRATFlpldkiraRAALAAALARGAIGAavDLVASDLREADARY 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 579 QQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLP 658
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 446621497 659 QEDEEESWLATRQQEAQSWQQRQNELTALQNRMQQLTPILETLPQSDELPHSEETVALE 717
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-578 |
7.34e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 69.55 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKgEWKIDFTrepfasNGLFAITGPTGAGKTTLLDAICLALYHETPrlsnvSQSQNDLMTRDTAECL 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHD-DSEIEFD------TGINIITGKNGAGKSSIVDAIRFALFTDKR-----TEKIEDMIKKGKNNLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 81 AEVEFEVKDEAYRAFWSQNRARNQPDGNLQVPRvelarcaDGKILADKVKDKLE-LTATLTGLDYGRFTRSMLLSQGQFA 159
Cdd:PRK01156 69 VELEFRIGGHVYQIRRSIERRGKGSRREAYIKK-------DGSIIAEGFDDTTKyIEKNILGISKDVFLNSIFVGQGEMD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 160 AFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTEL-------EKLQAQASGVALLTpEQVQSLTASLQVLTDEE 232
Cdd:PRK01156 142 SLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEIsnidyleEKLKSSNLELENIK-KQIADDEKSHSITLKEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 233 KQL---ITAQQQEQQSLN-WLTRLDELQQEASRRQQALQQA---LAEEEQAQPQLAAL---------SLAQPARN-LRPH 295
Cdd:PRK01156 221 ERLsieYNNAMDDYNNLKsALNELSSLEDMKNRYESEIKTAesdLSMELEKNNYYKELeerhmkiinDPVYKNRNyINDY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 296 WERIAEhstaLAHTRQQIEEVNTRLQSTmalrasirHHAAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQ 375
Cdd:PRK01156 301 FKYKND----IENKKQILSNIDAEINKY--------HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 376 TSDREHLRQWQQQLTHAEQKLNALAAITLT---LTADEVasaqaqhaeqrplrqrlvalhgqivpqQKRLAQLQVAIQNV 452
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKiqeIDPDAI---------------------------KKELNEINVKLQDI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 453 TLEQTQRNAALNKMRHRYKEkmqqladvkticeqeariktLEAQRAQLQAGQPCPLCGST-----SHPAVEAYQALEPGV 527
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDE--------------------LSRNMEMLNGQSVCPVCGTTlgeekSNHIINHYNEKKSRL 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 446621497 528 NQaRLLTLEKEVKKLGEEGATLRGQLDAL-TKQLQRDENEAQSLRQDEQALT 578
Cdd:PRK01156 482 EE-KIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLE 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
410-1017 |
7.76e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 410 EVASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNvtLEQTQRNAALNKMRHRYKEKMQQLadvkticeqEAR 489
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAEL---------PER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 490 IKTLEAQRAQLQAgqpcplcgstshpaveayqalepgvNQARLLTLEKEVKKLGEEGATLRGQLDALT-KQLQRDENEAQ 568
Cdd:COG4717 148 LEELEERLEELRE-------------------------LEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 569 SLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEhERQLRLLSQRHELQGQIAAHnQQIIQYQQQIEQRQQQLLT 648
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALLAL-LGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 649 ALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTAlqnrmQQLTPILETLPQSDELPHSEETVALENWRQVHEQCLA 728
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE-----EELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 729 LHSQQQTLQqqdvlaaqsLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLVTQTAETLT 808
Cdd:COG4717 356 AEELEEELQ---------LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 809 QHQqhrpgglsLTVTVEQIQQELAQTHQKLRENTTSQGEIRQQLKQ---DADNRQQQQTLMQQIAQMTQQVEDWGYLNsl 885
Cdd:COG4717 427 EEE--------LEEELEELEEELEELEEELEELREELAELEAELEQleeDGELAELLQELEELKAELRELAEEWAALK-- 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 886 IGSKEGDKFRKFAQGLTLDNLVHLANQQLTRL-HGRYLLQRkASEALEVEVVDtwQADAVRDTRTLSGGE---------- 954
Cdd:COG4717 497 LALELLEEAREEYREERLPPVLERASEYFSRLtDGRYRLIR-IDEDLSLKVDT--EDGRTRPVEELSRGTreqlylalrl 573
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446621497 955 SFLVslalalalsdlvSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVE 1017
Cdd:COG4717 574 ALAE------------LLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEE 624
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-481 |
9.38e-12 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 68.89 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 6 LRLKNLNSLKGEWkIDFTREPFASNglfAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDtaeCLAEVEF 85
Cdd:PHA02562 7 IRYKNILSVGNQP-IEIQLDKVKKT---LITGKNGAGKSTMLEALTFALFGKPFRDIKKGQLINSINKKD---LLVELWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 86 EVKDEAYRAFwsqnRArnqpdgnlQVPRVELARCaDGKILADK--VKDKLELTATLTGLDYGRFTRSMLLSQGQFAAFLN 163
Cdd:PHA02562 80 EYGEKEYYIK----RG--------IKPNVFEIYC-NGKLLDESasSKDFQKYFEQMLGMNYKSFKQIVVLGTAGYVPFMQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 164 AKPKERAELLEELTGTEIYGQISAMVfeqhKSARTELEklqaqasgvalltpEQVQSLTASLqvltDEEKQLITAQQQEQ 243
Cdd:PHA02562 147 LSAPARRKLVEDLLDISVLSEMDKLN----KDKIRELN--------------QQIQTLDMKI----DHIQQQIKTYNKNI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 244 QSLNWLTrldelQQEASRRQQALQQALAEEEQAQPQLAALSlaqparnlrphwERIAEHStalahtrQQIEEVNTRLQst 323
Cdd:PHA02562 205 EEQRKKN-----GENIARKQNKYDELVEEAKTIKAEIEELT------------DELLNLV-------MDIEDPSAALN-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 324 malraSIRHHAAKQSAELQQQQqslnawlQEHDRFRQwNNELAGWRAQFSQQ----TSDREHLRQWQQQLTHAEQKLNAL 399
Cdd:PHA02562 259 -----KLNTAAAKIKSKIEQFQ-------KVIKMYEK-GGVCPTCTQQISEGpdriTKIKDKLKELQHSLEKLDTAIDEL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 400 AAItltltADEVASAQaqhAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQQLAD 479
Cdd:PHA02562 326 EEI-----MDEFNEQS---KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
..
gi 446621497 480 VK 481
Cdd:PHA02562 398 LV 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-617 |
1.23e-11 |
|
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: 69.32 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 154 SQGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVAlltpEQVQSLTAslQVLTDEEK 233
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELE----RQLKSLER--QAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 234 QLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEQAQPQLAALSlaqparnlrphwERIAEHSTALAHTRQQI 313
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE------------EKLEELRLEVSELEEEI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 314 EEVNTRLQSTMALRASIRHHAAKQSAelqqqqqslnawlqehdRFRQWNNELAGWRAQfsqqtsdrehLRQWQQQLTHAE 393
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRE-----------------RLANLERQLEELEAQ----------LEELESKLDELA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 394 QKLNALAAITLTLTAdEVASAQAQHAEQRPLRQrlvALHGQIVPQQKRLAQLQVAIQNVTLEQtqrnAALNKMRHRYKEK 473
Cdd:TIGR02168 337 EELAELEEKLEELKE-ELESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQI----ASLNNEIERLEAR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 474 MQQLADVKTICEQEARIKTLEAQRAQLQAgqpcplcgstshpaveayqalepgvNQARLLTLEKEVKKLGEEGATLRGQL 553
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKE-------------------------LQAELEELEEELEELQEELERLEEAL 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446621497 554 DALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQ 617
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-579 |
8.36e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKgewKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlsnVSQSQNDLMTRDTAECL 80
Cdd:PRK02224 1 MRFDRVRLENFKCYA---DADLRLED----GVTVIHGVNGSGKSSLLEACFFALYGSKA----LDDTLDDVITIGAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 81 AEVEFEVKDEAYRAfwsQNRARNQPDgnlqvpRVELARC--ADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQF 158
Cdd:PRK02224 70 IELWFEHAGGEYHI---ERRVRLSGD------RATTAKCvlETPEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 159 AAFLNAKPKERAELLEELTgteiygQISA--MVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTAslqvlTDEEKQLI 236
Cdd:PRK02224 141 NKLINATPSDRQDMIDDLL------QLGKleEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 237 TAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEQAQPQLAalSLAQPARNLRphwERIAEHSTALAHTRQQIEEV 316
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE--TLEAEIEDLR---ETIAETEREREELAEEVRDL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 317 NTRLQSTMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQwnnELAGWRAQFSQQTSDREHLRQWQQQL-THAEQK 395
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLeERAEEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 396 LNALAAItltltADEVASAQAQHAEQrplRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQ 475
Cdd:PRK02224 362 REEAAEL-----ESELEEAREAVEDR---REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 476 QLadvkticeQEARiKTLEAQRAQLQAGQpCPLCGstsHPAVEAYQALEPGVNQARLLTLEKEVKKLGEEGATLRGQLDA 555
Cdd:PRK02224 434 TL--------RTAR-ERVEEAEALLEAGK-CPECG---QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
570 580
....*....|....*....|....
gi 446621497 556 LtKQLQRDENEAQSLRQDEQALTQ 579
Cdd:PRK02224 501 A-EDLVEAEDRIERLEERREDLEE 523
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-89 |
2.56e-09 |
|
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: 58.39 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 3 ILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlMTRDTAEcLAE 82
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFS------PLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPK-LIREGEV-RAQ 72
|
....*..
gi 446621497 83 VEFEVKD 89
Cdd:cd03240 73 VKLAFEN 79
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
35-384 |
2.05e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 35 ITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL------AEVEFEVKDEAYR--AFWSQNRARNQPD 106
Cdd:COG4913 29 LTGDNGSGKSTLLDAIQTLLVPAKRPRFNKAANDAGKSDRTLLSYVrgkygsERDEAGTRPVYLRpgDTWSAIAATFAND 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 107 GNLQVprVELARCADGK-------------ILADKVKDKLELTATLTGLDYGRFTRSMLL-------SQGQFAA------ 160
Cdd:COG4913 109 GSGQT--VTLAQVFWLKgdasslgdvkrffVIADGPLDLEDFEEFAHGFDIRALKARLKKqgveffdSFSAYLArlrrrl 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 161 -------------FLNAKPKE------RAELLEEltgTEIYGQISAMV--FEQHKSARTELEKLQAQasgVALLTP---- 215
Cdd:COG4913 187 gigsekalrllhkTQSFKPIGdlddfvREYMLEE---PDTFEAADALVehFDDLERAHEALEDAREQ---IELLEPirel 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 216 -EQVQSLTASLQVLtDEEKQLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEQAQPQLAALSLAQPARNLRp 294
Cdd:COG4913 261 aERYAAARERLAEL-EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 295 hweRIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQW-NNELAGWRAQFS 373
Cdd:COG4913 339 ---RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAlEEALAEAEAALR 415
|
410
....*....|.
gi 446621497 374 QQTSDREHLRQ 384
Cdd:COG4913 416 DLRRELRELEA 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-505 |
1.16e-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: 56.23 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 3 ILSLRLKNLNSLKGEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETP---RLSNVSqsqnDLMTRDTAEC 79
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPF------SKGFTVISGPNGSGKSNIGDAILFALGLSSSkamRAERLS----DLISNGKNGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 80 LAevefevkDEAYRAFWSQNRARNQPDgNLQVPRvELARCADGKI----LADKVKDKLELTATLTGLDYGRFTRSMLLsQ 155
Cdd:TIGR02169 72 SG-------NEAYVTVTFKNDDGKFPD-ELEVVR-RLKVTDDGKYsyyyLNGQRVRLSEIHDFLAAAGIYPEGYNVVL-Q 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 156 GQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGV------------------ALLTPEQ 217
Cdd:TIGR02169 142 GDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKrqqlerlrrerekaeryqALLKEKR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 218 VQSLTASLQVLTDEEKQL--ITAQQQE-QQSLNWLT-RLDELQQEASRRQQALQQ------ALAEEEQAQPQ-------- 279
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKeaIERQLASlEEELEKLTeEISELEKRLEEIEQLLEElnkkikDLGEEEQLRVKekigelea 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 280 ---LAALSLAQPARNLRPHWERIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQqqqsLNAWLQEHD 356
Cdd:TIGR02169 302 eiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED----LRAELEEVD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 357 -RFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLnalaaitltltadevasaqaqHAEQRPLRQRLVALHGQI 435
Cdd:TIGR02169 378 kEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL---------------------SEELADLNAAIAGIEAKI 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446621497 436 VPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQQLADV-KTICEQEARIKTLEAQRAQLQAGQP 505
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVR 507
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
203-595 |
1.56e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.69 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 203 LQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEQAQPQLAA 282
Cdd:PRK11281 26 FARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 283 LS--LAQPAR------NLRPHWERIAEHSTALAHTRQQIEEVNTRL--QSTMALRA-SIRHHAAKQSAELQQQQQSLNA- 350
Cdd:PRK11281 106 LKddNDEETRetlstlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAqAALYANSQRLQQIRNLLKGGKVg 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 351 -WLQEHDRFRQWNNELAGWRAQFSQQ--------------TSDREHLRQWQQQLTHAEQKL-NALAAITLTLTADEVASA 414
Cdd:PRK11281 186 gKALRPSQRVLLQAEQALLNAQNDLQrkslegntqlqdllQKQRDYLTARIQRLEHQLQLLqEAINSKRLTLSEKTVQEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 415 Q----AQHAEQRPLRQRLVALHGQI----VPQQKRLAQL---QVAIQNV--TLEQTQRN---------AALNKMRHRYKE 472
Cdd:PRK11281 266 QsqdeAARIQANPLVAQELEINLQLsqrlLKATEKLNTLtqqNLRVKNWldRLTQSERNikeqisvlkGSLLLSRILYQQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 473 KM------------QQLADVK----TICEQEARIKTLEAQRAQLQAGQPcplcgstshpaveayQALEPGVNQArLLTLE 536
Cdd:PRK11281 346 QQalpsadlieglaDRIADLRleqfEINQQRDALFQPDAYIDKLEAGHK---------------SEVTDEVRDA-LLQLL 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446621497 537 KEVKKLgeegatlrgqLDALTKQLQRDENEAQSLRQDEqaltQQWQAVTASLNITLQPQ 595
Cdd:PRK11281 410 DERREL----------LDQLNKQLNNQLNLAINLQLNQ----QQLLSVSDSLQSTLTQQ 454
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-564 |
6.48e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKgEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlSNVSQSQNDLMTRD-TAEC 79
Cdd:PRK03918 1 MKIEELKIKNFRSHK-SSVVEFDD------GINLIIGQNGSGKSSILEAILVGLYWGHG--SKPKGLKKDDFTRIgGSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 80 LAEVEFEVKDEAYRAFWSQNRArnqpdgnlqvprVELARCADG-KILADKVKDKLELTATLtgLDYGRFTRSMLLSQGQF 158
Cdd:PRK03918 72 EIELKFEKNGRKYRIVRSFNRG------------ESYLKYLDGsEVLEEGDSSVREWVERL--IPYHVFLNAIYIRQGEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 159 AAFLNAKpKERAELLEELTGTEIYGQI---SAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQL 235
Cdd:PRK03918 138 DAILESD-ESREKVVRQILGLDDYENAyknLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 236 ItaqqqeqqslnwltRLDELQQEASRRQQALQQALAEEEQAQPQLaaLSLAQPARNLRphwERIAEHSTALAHTRQQIEE 315
Cdd:PRK03918 217 P--------------ELREELEKLEKEVKELEELKEEIEELEKEL--ESLEGSKRKLE---EKIRELEERIEELKKEIEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 316 VNTRLQSTMALRASirhhaAKQSAELQQQQQSLNAWLQE-HDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQ 394
Cdd:PRK03918 278 LEEKVKELKELKEK-----AEEYIKLSEFYEEYLDELREiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 395 KLNALaaitltltadevasaqaqhaEQRplrqrlVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNaaLNKMRHRYKEKM 474
Cdd:PRK03918 353 RLEEL--------------------EER------HELYEEAKAKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 475 QQLADVKT-ICEQEARIKTLEAQRAQLQ-AGQPCPLCG---STSHPA--VEAYqalepgvnQARLLTLEKEVKKLGEEGA 547
Cdd:PRK03918 405 EEISKITArIGELKKEIKELKKAIEELKkAKGKCPVCGrelTEEHRKelLEEY--------TAELKRIEKELKEIEEKER 476
|
570
....*....|....*..
gi 446621497 548 TLRGQLDALTKQLQRDE 564
Cdd:PRK03918 477 KLRKELRELEKVLKKES 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-431 |
1.20e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQL-ITAQQQEQQSLNWLTRLDELQQEASRRQQALQQA 269
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 270 LAEEEQAQPQLAALS-----LAQPARNLRphwERIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQ 344
Cdd:TIGR02168 823 RERLESLERRIAATErrledLEEQIEELS---EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 345 QQSLNAWLQEHDRFRQWNNELAGWRAQFsqqtsdREHLRQWQQQLTHAEQKLNALAAITL----TLTADEVASAQAQHAE 420
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQERLSEEYSLTLeeaeALENKIEDDEEEARRR 973
|
250
....*....|.
gi 446621497 421 QRPLRQRLVAL 431
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-841 |
4.62e-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: 50.83 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 160 AFLNAKPKERAELLEELTGT-EIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITA 238
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKlDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 239 QQQEQQSLNWLTRLDELQQEASRRQQALQQALaEEEQAQPQLAALSLAQparnlrphwERIAEHSTALAHTRQQIEEVNT 318
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEI-EELLKKLEEAELKELQ---------AELEELEEELEELQEELERLEE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 319 RLQSTMALRASIRHH---AAKQSAELQQQQQSLNAWLQEHDRFRQ-------WNNELAGWRAQFSQQTSDREhlrQWQQQ 388
Cdd:TIGR02168 462 ALEELREELEEAEQAldaAERELAQLQARLDSLERLQENLEGFSEgvkallkNQSGLSGILGVLSELISVDE---GYEAA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 389 LTHA-EQKLNALAAITLTlTADEVASAQAQHAEQR----PLR----QRLVALHGQIVPQQKRLaqLQVAIQNVTLEqTQR 459
Cdd:TIGR02168 539 IEAAlGGRLQAVVVENLN-AAKKAIAFLKQNELGRvtflPLDsikgTEIQGNDREILKNIEGF--LGVAKDLVKFD-PKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 460 NAALNKMRHRYK--EKMQQLADVKTICEQEARIKTLEAQRAQ---LQAGQPcplcGSTSHPAVEayqalepgvNQARLLT 534
Cdd:TIGR02168 615 RKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRpggVITGGS----AKTNSSILE---------RRREIEE 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 535 LEKEVKKLGEEGATLRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQddiqpwldaQDEHERQLRL 614
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---------EQLEERIAQL 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 615 LSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLltalagyaltlpQEDEEEswLATRQQEAQSWQQR----QNELTALQNR 690
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEI------------EELEAQ--IEQLKEELKALREAldelRAELTLLNEE 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 691 MQQLTPILETLPQSDELPHSEETVALENWRQVHEQCLAL-HSQQQTLQQQDVLAAQsLQKAQAQFDTALQAsvfddqqaf 769
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaAEIEELEELIEELESE-LEALLNERASLEEA--------- 888
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621497 770 LAALMDEQTLTQLEQlkQNLENQRRQAQTLVTQTAETLTQHQQHrpgglsltvtVEQIQQELAQTHQKLREN 841
Cdd:TIGR02168 889 LALLRSELEELSEEL--RELESKRSELRRELEELREKLAQLELR----------LEGLEVRIDNLQERLSEE 948
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-591 |
1.39e-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: 49.35 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 192 QHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDE---------------EKQLITAQQQEQQSLnwlTRLDELQ 256
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSElreakrmyedkieelEKQLVLANSELTEAR---TERDQFS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 257 QEASRRQQALQQALAEEEQAQPQLAaLSLAQPARnlrpHWERIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAK 336
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELS-LEKEQNKR----LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 337 QSAELQQQQQSLNAWLQEHDRFRqwnnelagwraqfSQQTSDREHLRQWQQQLTHAEQKLNA----LAAITLTLTADEVA 412
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLT-------------AQLESTKEMLRKVVEELTAKKMTLESsertVSDLTASLQEKERA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 413 sAQAQHAEQRPLRQRlVALHGQIVPQQK----RLAQLQVAIQNVTLEQTQRNAALNKMRhrykekmQQLADVKTICEQEA 488
Cdd:pfam15921 512 -IEATNAEITKLRSR-VDLKLQELQHLKnegdHLRNVQTECEALKLQMAEKDKVIEILR-------QQIENMTQLVGQHG 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 489 RIK-TLEAQRAQLQAGQpcplcgSTSHPAVEAYQALEPGVN------QARLLTLEKEVKKLGEEGAT-------LRGQLD 554
Cdd:pfam15921 583 RTAgAMQVEKAQLEKEI------NDRRLELQEFKILKDKKDakirelEARVSDLELEKVKLVNAGSErlravkdIKQERD 656
|
410 420 430
....*....|....*....|....*....|....*..
gi 446621497 555 ALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNIT 591
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT 693
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
931-1002 |
1.99e-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: 44.15 E-value: 1.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446621497 931 LEVEVVDTWQADAVRDTRTLSGGE-----SFLVSLALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDA 1002
Cdd:pfam13558 14 VEVRDEDGSEVETYRRSGGLSGGEkqllaYLPLAAALAAQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-65 |
2.35e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.97 E-value: 2.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446621497 26 PFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVS 65
Cdd:pfam13555 18 PIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRARFNKA 57
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-54 |
4.46e-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: 4.46e-05
10 20
....*....|....*....|....*....
gi 446621497 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 |
9.41e-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: 43.77 E-value: 9.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446621497 1 MKILSLRLKNLNSLKGewkIDFTrepFASNGLFAITGPTGAGKTTLLDAICLALY 55
Cdd:cd00267 2 IENLSFRYGGRTALDN---VSLT---LKAGEIVALVGPNGSGKSTLLRAIAGLLK 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-773 |
9.66e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 225 LQVLTDEEKQLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEQAQPQLAALSLAQPARNLRphwERIAEHST 304
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE---AELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 305 ALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQqslnawLQEHDRFRQWNNELAGWRAQFSQQtsdREHLRQ 384
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAEL---EEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 385 WQQQLTHAEQKLNALAAITLTLTADEVASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALN 464
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 465 KMRHRYKEKMQQLADVKTICEQEariktLEAQRAQLqagqpcplcgstshpaveayqalepGVNQARLLTLEKEVKKLGE 544
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEE-----LEELLAAL-------------------------GLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 545 EGATLRGQLDALTKQLQRDENEAQslrqdEQALTQQWQAvtaslnitlqpqDDIQPWLDAQDEHERQLRLLSQRHELQGQ 624
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQE-----IAALLAEAGV------------EDEEELRAALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 625 IAAHnqqiiqyqqqieqrqqqlltalAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRMQQLTPILETLPQS 704
Cdd:COG4717 411 LEEL----------------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446621497 705 DElphseetvaLENWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAAL 773
Cdd:COG4717 469 GE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEYFSRL 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
238-500 |
1.04e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 238 AQQQEQQSLNwlTRLDELQQEASRRQQALQQALAEEEQAQPQLAALSlaqparnlrphwERIAEHSTALAHTRQQIEEVN 317
Cdd:COG4942 17 AQADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALE------------RRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 318 TRLQSTmalrasirhhaAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQT-SDREHLRQWQQQLTHAEQKL 396
Cdd:COG4942 83 AELAEL-----------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 397 NALAAITLTLTADEVASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQQ 476
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|....
gi 446621497 477 LADVKTICEQEARIKTLEAQRAQL 500
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-502 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 289 ARNLRPHWERIAEHSTALAHTRQQIEevntRLQSTMALRASIRHhAAKQSAELQQQQQSLNAWLQEHdRFRQWNNELAGW 368
Cdd:COG4913 227 ADALVEHFDDLERAHEALEDAREQIE----LLEPIRELAERYAA-ARERLAELEYLRAALRLWFAQR-RLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 369 RAQFSQQtsdREHLRQWQQQLTHAEQKLNALaaitltltadEVASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVA 448
Cdd:COG4913 301 RAELARL---EAELERLEARLDALREELDEL----------EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446621497 449 IQNVTLEQTQRNAALNKMRHRYKEKMQQLADVKTICEQ-----EARIKTLEAQRAQLQA 502
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeaEAALRDLRRELRELEA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-446 |
2.74e-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: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 249 LTRLDELQQEASRRQQALQQALAEEEQAQPQLAALSLAQPARNLRPHWERiaehSTALAHTRQQIEEVNTRLQSTMALRA 328
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA----QRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 329 SIRHHAAKQSAELQQQQQSLNAwlQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHA----EQKLNALAAITL 404
Cdd:COG4913 313 RLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPlpasAEEFAALRAEAA 390
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446621497 405 TLTADEVASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQ 446
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
251-451 |
2.76e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 251 RLDELQQEASRRQQALQQALAEEEQAQPQLAALslaqpaRNLRPHWERIAEHSTA---LAHTRQQIEEVNTRLQstmALR 327
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDAL------QERREALQRLAEYSWDeidVASAEREIAELEAELE---RLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 328 ASirhhaakqSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQtsdREHLRQWQQQLTHAEQKLNALAAITLTLT 407
Cdd:COG4913 682 AS--------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446621497 408 ADEVASAQAQHAEQRPLRQRlvaLHGQIVPQQKRLAQLQVAIQN 451
Cdd:COG4913 751 LEERFAAALGDAVERELREN---LEERIDALRARLNRAEEELER 791
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
946-1016 |
8.27e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 8.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446621497 946 DTRTLSGGESFLVSLalalalsdlvshkTRIDSLFLDegFGTLDSETLDTALDALDALnasgktiGVISHV 1016
Cdd:COG0419 155 PIETLSGGERLRLAL-------------ADLLSLILD--FGSLDEERLERLLDALEEL-------AIITHV 203
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-54 |
1.07e-03 |
|
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: 41.14 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446621497 3 ILSLRLKNLNSLKGEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLAL 54
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGG------SNSFNAIVGPNGSGKSNIVDAICFVL 46
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
24-54 |
1.12e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 41.20 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|...
gi 446621497 24 REPFASNGLFAIT--GPTGAGKTTLLDAICLAL 54
Cdd:COG0378 5 RALFAEKGVLAVNlmGSPGSGKTTLLEKTIRAL 37
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-60 |
1.17e-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: 42.30 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKGEwKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPR 60
Cdd:COG3593 1 MKLEKIKIKNFRSIKDL-SIEL------SDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-624 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 364 ELAGWRAQFSQQTSDREHLRQWQQQLthaEQKLNALAAITLTLTAD-EVASAQAQHAEQRPLRQRLVALHGQIVPQQKRL 442
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDAL---QERREALQRLAEYSWDEiDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 443 AQLQVAIQnvtleqtqrnaALNKMRHRYKEKMQQLadvkticeqEARIKTLEAQRAQLQAGqpcpLCGSTSHPAVEAYQA 522
Cdd:COG4913 695 EELEAELE-----------ELEEELDELKGEIGRL---------EKELEQAEEELDELQDR----LEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 523 LEPGVNQARLLTLEKEVKKlgeegaTLRGQLDALTKQLQRDENEAQSLRQDeqaLTQQWQAVTASLNITLQPQDDIQPWL 602
Cdd:COG4913 751 LEERFAAALGDAVERELRE------NLEERIDALRARLNRAEEELERAMRA---FNREWPAETADLDADLESLPEYLALL 821
|
250 260
....*....|....*....|....*
gi 446621497 603 DAQDE---HERQLRLLSQRHELQGQ 624
Cdd:COG4913 822 DRLEEdglPEYEERFKELLNENSIE 846
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
318-593 |
1.40e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 318 TRLQSTMALRASIRHHAAKQSAELqqqqqsLNAWLQEhdrFRQWNNELagwRAQFSQQTSD--REHLRQWQQQLTHAEQK 395
Cdd:COG3206 130 EPVKGSNVIEISYTSPDPELAAAV------ANALAEA---YLEQNLEL---RREEARKALEflEEQLPELRKELEEAEAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 396 LNALAAitltltadevasaqaqhaeqrplRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQ 475
Cdd:COG3206 198 LEEFRQ-----------------------KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 476 QLADVK---TICEQEARIKTLEAQRAQLQAGqpcplcGSTSHPAVEAYQALEPGVNQARLLTLEKEVKKLGEEGATLRGQ 552
Cdd:COG3206 255 ALPELLqspVIQQLRAQLAELEAELAELSAR------YTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446621497 553 LDALTKQLQRDENEAQSLRQDEQ---ALTQQWQAVTASLNITLQ 593
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAelrRLEREVEVARELYESLLQ 372
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-90 |
1.44e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 41.80 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 3 ILSLRLKNlNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALyhetprlsnVSQSQNDLMTRDTAECLAE 82
Cdd:cd03241 1 LLELSIKN-FALIEELELDFEE------GLTVLTGETGAGKSILLDALSLLL---------GGRASADLIRSGAEKAVVE 64
|
....*...
gi 446621497 83 VEFEVKDE 90
Cdd:cd03241 65 GVFDISDE 72
|
|
| UreG |
cd05540 |
urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is ... |
35-80 |
1.89e-03 |
|
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: 40.71 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446621497 35 ITGPTGAGKTTLLDAICLALyHETPRLSNVSqsqNDLMTRDTAECL 80
Cdd:cd05540 5 IGGPVGSGKTALVEALCRAL-RDKYSIAVVT---NDIYTKEDAEFL 46
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-62 |
2.20e-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: 40.61 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446621497 4 LSLRLKNLNSLKGEWKIDFTRE-------PFASNGLFAITGPTGAGKTTLLDAicLALYHETPRLS 62
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKQllknvsgKAKPGELTAIMGPSGAGKSTLLNA--LAGRRTGLGVS 65
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
168-625 |
2.34e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 168 ERAELLEELTGT--EIYGQISAMVFEQHKSART--ELEKLQAQASgvalltpeqvqSLTASLQVLTDEEKQLITAQQQEQ 243
Cdd:COG3096 279 ERRELSERALELrrELFGARRQLAEEQYRLVEMarELEELSARES-----------DLEQDYQAASDHLNLVQTALRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 244 QSLNWLTRLDELQQEAsrRQQALQQALAEEEQAQPQlAALSLAQparnlrphwERIAEHSTALAHTRQQIEEVNTR-LQS 322
Cdd:COG3096 348 KIERYQEDLEELTERL--EEQEEVVEEAAEQLAEAE-ARLEAAE---------EEVDSLKSQLADYQQALDVQQTRaIQY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 323 TMALRASIRHHAAKQSAELQQQqqSLNAWLQEHdrfrqwnnelagwRAQFSQQTsdrEHLRQWQQQLT----HAEQKLNA 398
Cdd:COG3096 416 QQAVQALEKARALCGLPDLTPE--NAEDYLAAF-------------RAKEQQAT---EEVLELEQKLSvadaARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 399 LAAitLTLTADEVASAQAQHAEQRPLRQrlvalhgqiVPQQKRLAQLQVAIQnvtleqtqrnaalnkmrhrykekmQQLA 478
Cdd:COG3096 478 YEL--VCKIAGEVERSQAWQTARELLRR---------YRSQQALAQRLQQLR------------------------AQLA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 479 DVKTICEQEARIKTLEAQRAQLQAGQpcplcgSTSHPAVEAYQALEpgvnQARLLTLEKEVKKLGEEGATLRGQLDALTK 558
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQ------LDAAEELEELLAEL----EAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621497 559 QLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLdaqdEHERQL-----RLLSQRHELQGQI 625
Cdd:COG3096 593 RIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLL----EREREAtverdELAARKQALESQI 660
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-627 |
2.43e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 412 ASAQAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMRHRYKEKMQQLADV-KTICEQEARI 490
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 491 KTLEAQRAQLQA-------------GQPCPLCGSTSHPAVEAYQALE--PGVNQARlltlEKEVKKLGEEGATLRGQLDA 555
Cdd:COG4942 93 AELRAELEAQKEelaellralyrlgRQPPLALLLSPEDFLDAVRRLQylKYLAPAR----REQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621497 556 LTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAA 627
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-50 |
2.90e-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: 41.43 E-value: 2.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446621497 1 MKILSLRLKNLNSLKgEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAI 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 |
3.80e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 949 TLSGGESFLVSLALALALSDLVShkTRIDSLFLDEGFGTLDSETLDTAL-DALDALNA-SGKTIGVISHVEAMKERIPVQ 1026
Cdd:cd03240 115 RCSGGEKVLASLIIRLALAETFG--SNCGILALDEPTTNLDEENIEESLaEIIEERKSqKNFQLIVITHDEELVDAADHI 192
|
90
....*....|...
gi 446621497 1027 IKVKKiNGLGYSK 1039
Cdd:cd03240 193 YRVEK-DGRQKSR 204
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
232-467 |
6.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 232 EKQLITAQQQEQQSLNWL-TRLDELQQEASRRQQALQQALAEEEQAQPQLAALSLAQparnlrphweRIAEHSTALAHTR 310
Cdd:COG3206 163 EQNLELRREEARKALEFLeEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ----------QLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 311 QQIEEVNTRLQSTMALRASIRHHAAKQSAElqQQQQSLNAWLQEHDRfrqwnnELAGWRAQFSQQTSDrehLRQWQQQLT 390
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEA------ELAELSARYTPNHPD---VIALRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446621497 391 HAEQKLNALAAITLTLTADEVASAQAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNKMR 467
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREAS---LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-130 |
6.78e-03 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 39.18 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 27 FASNGLFAITGPTGAGKTTLLDAI-CLALYHETPR---LSNVSQSQNDLMTRDTA-----ECLAEvEFEVkdEAYRAFWS 97
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTTSgqiLFNGQPRKPDQFQKCVAyvrqdDILLP-GLTV--RETLTYTA 106
|
90 100 110
....*....|....*....|....*....|....*.
gi 446621497 98 QNRARN-QPDGNLQ--VPRVELARCADGKILADKVK 130
Cdd:cd03234 107 ILRLPRkSSDAIRKkrVEDVLLRDLALTRIGGNLVK 142
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-400 |
7.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 216 EQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWLTRLDELQ------QEASRRQQALQQALAEEEQAQPQLAALslaqpa 289
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAAL------ 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621497 290 rnlrphweriaehstalahtRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQWNN-----E 364
Cdd:COG4913 691 --------------------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraL 750
|
170 180 190
....*....|....*....|....*....|....*.
gi 446621497 365 LAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALA 400
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAE 786
|
|
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