|
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: 1577.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 1 MKILSLRLKNLNSLKGEWKIDFTREPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:PRK10246 1 MKILSLRLKNLNSLKGEWKIDFTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLNNVSQSQNDLMTRDTAECL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:PRK10246 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQAPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
Cdd:PRK10246 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSAALAHTRQQIEEVNTRL 320
Cdd:PRK10246 241 QQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 321 QSTMVLRASIRHHAANQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNTLA 400
Cdd:PRK10246 321 QSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 401 AITLTLTADEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNVALNEMRQRYKEKTQQLADV 480
Cdd:PRK10246 401 AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 481 KTICEQEARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLLALENEVKKLGEEGAALRGQLDALTKQL 560
Cdd:PRK10246 481 KTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 561 QRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
Cdd:PRK10246 561 QRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 641 QRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRIQQLTPILETLPQSDDLPHSEETVALDNWR 720
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 721 QVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLV 800
Cdd:PRK10246 721 QVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLV 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 801 TQTAETLAQHQQHRPDGLALTVTVEQIQQELAQTHQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQVEDWG 880
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVEDWG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKASEALEVEVVDTWQADAVRDTRTLSGGESFLVSL 960
Cdd:PRK10246 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVWLANQQLTRLHGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGESFLVSL 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
Cdd:PRK10246 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
|
....*..
gi 446621575 1041 ESTFAVK 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: 999.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 1 MKILSLRLKNLNSLKGEWKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALG----PIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:TIGR00618 77 AELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
Cdd:TIGR00618 157 FLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSAALAHTRQQIEEVNTRL 320
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 321 QSTMVLRASIRHHAAN---QSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLN 397
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAhvkQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 398 TLAAITLTLTAdEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNVALNEMRQRYKEKTQQL 477
Cdd:TIGR00618 397 SLCKELDILQR-EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 478 ADVKTICEQEARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLLALENEVKKLGEEGAALRGQLDALT 557
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 558 KQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQ 637
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 638 QIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRIQQLTPILETLPQSDDLPHSEETVALD 717
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 718 NWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQ 797
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 798 TLVTQTAETLAQHQQHRP-DGLALTVTVEQIQQELAQTHQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQV 876
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPsDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 877 EDWGYLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKAS--EALEVEVVDTWQADAVRDTRTLSGGE 954
Cdd:TIGR00618 876 DKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNArkYQGLALLVADAYTGSVRPSATLSGGE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 955 SFLVSLALA--LALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKI 1032
Cdd:TIGR00618 956 TFLASLSLAlaLADLLSTSGGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKT 1035
|
....*..
gi 446621575 1033 NGLGYSK 1039
Cdd:TIGR00618 1036 NAGSHVM 1042
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-205 |
9.00e-31 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 120.50 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 2 KILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRlsnVSQSQNDLMTRDTAECLA 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDD------GLNLIVGPNGAGKSTILEAIRYALYGKARS---RSKLRSDLINVGSEEASV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 82 EVEFEVKGEAYRAFWsqnrarnqpdgnlqvprvelarcadgkiladkvkdkleltatltgldygrftrsmllSQGQFAAF 161
Cdd:COG0419 72 ELEFEHGGKRYRIER---------------------------------------------------------RQGEFAEF 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446621575 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 |
3.86e-28 |
|
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: 113.13 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 1 MKILSLRLKNLNSLKGEWKIDFTrePFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlmtRDTAECL 80
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFT--GLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSV---FAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 81 AEV--EFEVKGEAYRAFwsqnRARnqpdgnlqvprvelarcadgkiladkvkdkleltatltGLDYGRFTRSMLLSQGQF 158
Cdd:cd03279 76 AEVsfTFQLGGKKYRVE----RSR--------------------------------------GLDYDQFTRIVLLPQGEF 113
|
....
gi 446621575 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 |
1.01e-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: 100.42 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 945 RDTRTLSGGESFLVSLALAL--ALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKER 1022
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALalSEVLQNRGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKER 198
|
....*....
gi 446621575 1023 IPVQIKVKK 1031
Cdd:cd03279 199 IPQRLEVIK 207
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-206 |
1.95e-22 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 96.03 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 6 LRLKNLNSLKgEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQN-----DLMTRDTAECL 80
Cdd:pfam13476 1 LTIENFRSFR-DQTIDF------SKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFvkgdiRIGLEGKGKAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 81 AEVEFEVKGEA--YRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLEltatltgldygRFTRSMLLSQGQF 158
Cdd:pfam13476 74 VEITFENNDGRytYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKI-----------ILPLLVFLGQERE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446621575 159 AAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQ 206
Cdd:pfam13476 143 EEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-578 |
2.30e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 71.47 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 1 MKILSLRLKNLNSLKgEWKIDFTrepfasNGLFAITGPTGAGKTTLLDAICLALYHETPrlsnvSQSQNDLMTRDTAECL 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHD-DSEIEFD------TGINIITGKNGAGKSSIVDAIRFALFTDKR-----TEKIEDMIKKGKNNLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRvelarcaDGKILADKVKDKLE-LTATLTGLDYGRFTRSMLLSQGQFA 159
Cdd:PRK01156 69 VELEFRIGGHVYQIRRSIERRGKGSRREAYIKK-------DGSIIAEGFDDTTKyIEKNILGISKDVFLNSIFVGQGEMD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 160 AFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTEL-------EKLQAQASGVALLTpEQVQSLTASLQVLTDEE 232
Cdd:PRK01156 142 SLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEIsnidyleEKLKSSNLELENIK-KQIADDEKSHSITLKEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 233 KQLLTAQQQEQQSLNW----LTRLDELQQEASRRQQALQQA---LAEEEKAQPQLAAL---------SLAQPARN-LRPH 295
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNlksaLNELSSLEDMKNRYESEIKTAesdLSMELEKNNYYKELeerhmkiinDPVYKNRNyINDY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 296 WERIAEhsaaLAHTRQQIEEVNTRLQSTmvlrasirHHAANQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQ 375
Cdd:PRK01156 301 FKYKND----IENKKQILSNIDAEINKY--------HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 376 TSDREHLRQWQQQLTHAEQKLNtlAAITLTLTADEV-ASALaqhaeqrplrqrlvalhgqivpqQKRLAQLMVTIQNVTL 454
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMS--AFISEILKIQEIdPDAI-----------------------KKELNEINVKLQDISS 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 455 EQTQRNVALNEMRQRYKEktqqladvkticeqeariktLEAQRAQLQAGQPCPLCGST-----SHPAVEAYQALEPGVNq 529
Cdd:PRK01156 424 KVSSLNQRIRALRENLDE--------------------LSRNMEMLNGQSVCPVCGTTlgeekSNHIINHYNEKKSRLE- 482
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 446621575 530 SRLLALENEVKKLGEEGAALRGQLDAL-TKQLQRDENEAQSLRQDEQALT 578
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLE 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
438-1017 |
9.05e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 438 QQKRLAQLMVTIQNVTLEQTQRNVALNEMRQRYKEKTQQLADVKTICEQEARIKTLEAQRAQLQAGQPCplcgstshpAV 517
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER---------LE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 518 EAYQALEPGVN-QSRLLALENEVKKLGEEGAALRGQLDALT-KQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQ 595
Cdd:COG4717 150 ELEERLEELRElEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 596 DDIQPWLDAQDEhERQLRLLSQRHELQGQIAAHnQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQ 675
Cdd:COG4717 230 EQLENELEAAAL-EERLKEARLLLLIAAALLAL-LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 676 SWQQRQNELTAlqnriQQLTPILETLPQSDDLPHSEETVALDNWRQVHEQCLALHSQQQTLQqqdvlaaqsLQKAQAQFD 755
Cdd:COG4717 308 QALPALEELEE-----EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---------LEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 756 TALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLVTQTAETLAQHQqhrpdglaLTVTVEQIQQELAQTH 835
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--------LEEELEELEEELEELE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 836 QKLRENTTSQGEIRQQLKQ---DADNRQQQQTLMQQIAQMTQQVEDWGYLNslIGSKEGDKFRKFAQGLTLDNLVHLANQ 912
Cdd:COG4717 446 EELEELREELAELEAELEQleeDGELAELLQELEELKAELRELAEEWAALK--LALELLEEAREEYREERLPPVLERASE 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 913 QLTRL-HGRYLLQRkASEALEVEVVDtwQADAVRDTRTLSGGE----------SFLVslalalalsdlvSHKTRIDSLFL 981
Cdd:COG4717 524 YFSRLtDGRYRLIR-IDEDLSLKVDT--EDGRTRPVEELSRGTreqlylalrlALAE------------LLAGEPLPLIL 588
|
570 580 590
....*....|....*....|....*....|....*.
gi 446621575 982 DEGFGTLDSETLDTALDALDALNASGKTIGVISHVE 1017
Cdd:COG4717 589 DDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEE 624
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-572 |
3.01e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 154 SQGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVAlltpEQVQSLTAslQVLTDEEK 233
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELE----RQLKSLER--QAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 234 QLLTAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSlaqparnlrphwERIAEHSAALAHTRQQI 313
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE------------EKLEELRLEVSELEEEI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 314 EEVNTRLQSTMV----LRASIRHHAANQsAELQQQQQSLNTWLQEHDrfrqwnnelagwraqfSQQTSDREHLRQWQQQL 389
Cdd:TIGR02168 284 EELQKELYALANeisrLEQQKQILRERL-ANLERQLEELEAQLEELE----------------SKLDELAEELAELEEKL 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 390 THAEQKLNTLAAitltltADEVASALAQHAEQRP--LRQRLVALHGQIVPQQKRLAQLMVTIQN--VTLEQTQRNVALNE 465
Cdd:TIGR02168 347 EELKEELESLEA------ELEELEAELEELESRLeeLEEQLETLRSKVAQLELQIASLNNEIERleARLERLEDRRERLQ 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 466 MRQRYKEKTQQLADVKticEQEARIKTLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVnQSRLLALENEVKKLGEE 545
Cdd:TIGR02168 421 QEIEELLKKLEEAELK---ELQAELEELEEELEELQE-------------ELERLEEALEEL-REELEEAEQALDAAERE 483
|
410 420
....*....|....*....|....*..
gi 446621575 546 GAALRGQLDALTKQLQRDENEAQSLRQ 572
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-840 |
2.21e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 154 SQGQFAAFLNAKPKERAELLEE-----------------LTGTE--------IYGQIsamvfeqhksaRTELEKLQAQAS 208
Cdd:COG1196 142 GQGMIDRIIEAKPEERRAIIEEaagiskykerkeeaerkLEATEenlerledILGEL-----------ERQLEPLERQAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 209 gVAlltpEQVQSLTASLQVLtdeEKQLLTAQQQEQQSlnwltRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQP 288
Cdd:COG1196 211 -KA----ERYRELKEELKEL---EAELLLLKLRELEA-----ELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 289 ARNlrphwERIAEHSAALAHTRQQIEEVNTRLQSTMVLRAsirhhaaNQSAELQQQQQSLNTWLQEHDRFRQwnnELAGW 368
Cdd:COG1196 278 ELE-----LELEEAQAEEYELLAELARLEQDIARLEERRR-------ELEERLEELEEELAELEEELEELEE---ELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 369 RAQFSQQTSDREHLRQWQQQLTHAEQKLNTLAAITLTLTADEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLMVT 448
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 449 IQNVTLEQTQRNVALNEMRQRYKEKTQQLADVKTicEQEARIKTLEAQRAQLQAGQpcplcgstshpavEAYQALEPGVN 528
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEE--EEEALLELLAELLEEAALLE-------------AALAELLEELA 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 529 QSRLLALENEVKKLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALtqqWQAVTASLNITLQPQDdiqpwLDAQDEH 608
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY---EAALEAALAAALQNIV-----VEDDEVA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 609 ERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQ 688
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 689 NRIQQLTpILETLPQSDDLPHSEETVALDNwrqvheqclALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQA 768
Cdd:COG1196 640 VTLAGRL-REVTLEGEGGSAGGSLTGGSRR---------ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621575 769 FLAALMDEQTLTQLEQLKQNLENQRRQAQTLVTQTAETLAQHQQHRPDGLAltvTVEQIQQELAQTHQKLRE 840
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP---DLEELERELERLEREIEA 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-579 |
3.07e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 1 MKILSLRLKNLNSLKgewKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlsnVSQSQNDLMTRDTAECL 80
Cdd:PRK02224 1 MRFDRVRLENFKCYA---DADLRLED----GVTVIHGVNGSGKSSLLEACFFALYGSKA----LDDTLDDVITIGAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 81 AEVEFEVKGEAYRAfwsQNRARNQPDgnlqvpRVELARC--ADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQF 158
Cdd:PRK02224 70 IELWFEHAGGEYHI---ERRVRLSGD------RATTAKCvlETPEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 159 AAFLNAKPKERAELLEELTgteiygQISA--MVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTAslqvlTDEEKQLL 236
Cdd:PRK02224 141 NKLINATPSDRQDMIDDLL------QLGKleEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 237 TAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAalSLAQPARNLRphwERIAEHSAALAHTRQQIEEV 316
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE--TLEAEIEDLR---ETIAETEREREELAEEVRDL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 317 NTRLQSTMVLRASIRHHAANQSAELQQQQQSLNTWLQEHDRFRQwnnELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKL 396
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 397 NTLAAiTLTLTADEVASALAQHAEQrplrqrLVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNVALNEMRQRYKEKTQQ 476
Cdd:PRK02224 362 REEAA-ELESELEEAREAVEDRREE------IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 477 LadvkticeQEARiKTLEAQRAQLQAGQpCPLCGstshpaveayQALEPGVNQSRLLALENEVKKLGEEGAALRGQLDAL 556
Cdd:PRK02224 435 L--------RTAR-ERVEEAEALLEAGK-CPECG----------QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEV 494
|
570 580
....*....|....*....|....*....
gi 446621575 557 TKQLQR------DENEAQSLRQDEQALTQ 579
Cdd:PRK02224 495 EERLERaedlveAEDRIERLEERREDLEE 523
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-126 |
3.10e-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: 58.00 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 3 ILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlMTRDTAEcLAE 82
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFS------PLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPK-LIREGEV-RAQ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446621575 83 VEFE---VKGEAYRAFWSQNRARN-----QPDGNLQVPRvELARCADG-KILA 126
Cdd:cd03240 73 VKLAfenANGKKYTITRSLAILENvifchQGESNWPLLD-MRGRCSGGeKVLA 124
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-481 |
4.32e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 60.41 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 6 LRLKNLNSLKGEWkIDFTREPFASNglfAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDtaeCLAEVEF 85
Cdd:PHA02562 7 IRYKNILSVGNQP-IEIQLDKVKKT---LITGKNGAGKSTMLEALTFALFGKPFRDIKKGQLINSINKKD---LLVELWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 86 EVKGEAYRAFwsqnRArnqpdgnlQVPRVELARCaDGKILADK--VKDKLELTATLTGLDYGRFTRSMLLSQGQFAAFLN 163
Cdd:PHA02562 80 EYGEKEYYIK----RG--------IKPNVFEIYC-NGKLLDESasSKDFQKYFEQMLGMNYKSFKQIVVLGTAGYVPFMQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 164 AKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVAlltpEQVqsltASLQVLTDEEKQLLTAQQQEQ 243
Cdd:PHA02562 147 LSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQ----QQI----KTYNKNIEEQRKKNGENIARK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 244 QSlnwltRLDELQQEAsrrqqalQQALAEEEKAQPQLAALSLaqparnlrphweRIAEHSAALAHTRQQIeevnTRLQST 323
Cdd:PHA02562 219 QN-----KYDELVEEA-------KTIKAEIEELTDELLNLVM------------DIEDPSAALNKLNTAA----AKIKSK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 324 MvlrasirhhaanqsaelqqqqqslNTWLQEHDRFRQwNNELAGWRAQFSQQ----TSDREHLRQWQQQLTHAEQKLNTL 399
Cdd:PHA02562 271 I------------------------EQFQKVIKMYEK-GGVCPTCTQQISEGpdriTKIKDKLKELQHSLEKLDTAIDEL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 400 AAItltltadeVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNVALNEMRQRYKEKTQQLAD 479
Cdd:PHA02562 326 EEI--------MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
..
gi 446621575 480 VK 481
Cdd:PHA02562 398 LV 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-384 |
3.11e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 169 RAELLEEltgTEIYGQISAMV--FEQHKSARTELEKLQAQasgVALLTP-----EQVQSLTASLQVLtDEEKQLLTAQQQ 241
Cdd:COG4913 214 REYMLEE---PDTFEAADALVehFDDLERAHEALEDAREQ---IELLEPirelaERYAAARERLAEL-EYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 242 EQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRphweRIAEHSAALAHTRQQIEEVNTRLQ 321
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD----RLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446621575 322 STMVLRASIRHHAANQSAELQQQQQSLNTWLQEHDRFRQW-NNELAGWRAQFSQQTSDREHLRQ 384
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAlEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-841 |
3.66e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 190 FEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQ-EQQSLNWLTRLDELQQEASRRQQALQQ 268
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 269 ALAEEEKAQPQLAALSLAQPARNLRPH--WERIAEHSAALAHTRQQIEEVNTRLQSTMVLRASIRHHAANQSAELQQQQQ 346
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 347 SL-NTWLQEHD-RFRQWNNELAGWRAQFS----QQTSDREHLRQWQQQLTHAEQKLNTLAAITLTL--------TADEVA 412
Cdd:TIGR02168 429 KLeEAELKELQaELEELEEELEELQEELErleeALEELREELEEAEQALDAAERELAQLQARLDSLerlqenleGFSEGV 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 413 SALAQHAEQRPLrqrLVALHGQIVPQQKRLAQLMVT-----IQNVTLE-QTQRNVALNEMRQRYKEKTQQLAdVKTICEQ 486
Cdd:TIGR02168 509 KALLKNQSGLSG---ILGVLSELISVDEGYEAAIEAalggrLQAVVVEnLNAAKKAIAFLKQNELGRVTFLP-LDSIKGT 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 487 EARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGV----------NQSR------------------------- 531
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddldnalELAKklrpgyrivtldgdlvrpggvitgg 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 532 -------LLALENEVKKLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQavtaslnitlqpqdDIQPWLDA 604
Cdd:TIGR02168 665 saktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE--------------ELSRQISA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 605 QDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEEswLATRQQEAQSWQQR---- 680
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ--IEQLKEELKALREAldel 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 681 QNELTALQNRIQQLTPILETLPQSDDLPHSEETVALDNWRQVHEQCLAL-HSQQQTLQQQDVLAAQsLQKAQAQFDTALQ 759
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaAEIEELEELIEELESE-LEALLNERASLEE 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 760 AsvfddqqafLAALMDEQTLTQLEQlkQNLENQRRQAQTLVTQTAETLAQHQQHrpdglaltvtVEQIQQELAQTHQKLR 839
Cdd:TIGR02168 888 A---------LALLRSELEELSEEL--RELESKRSELRRELEELREKLAQLELR----------LEGLEVRIDNLQERLS 946
|
..
gi 446621575 840 EN 841
Cdd:TIGR02168 947 EE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-480 |
6.09e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 89 GEAYRAFWSQNRARNQPDGNLQVPRVELARC-ADGKILADKVKdklELTATLTGLdygrftrsmllsQGQFAAFLNAKPK 167
Cdd:TIGR02168 652 GDLVRPGGVITGGSAKTNSSILERRREIEELeEKIEELEEKIA---ELEKALAEL------------RKELEELEEELEQ 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 168 ERAELLE---ELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQL-LTAQQQEQ 243
Cdd:TIGR02168 717 LRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeAQIEQLKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 244 QSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALS-----LAQPARNLRphwERIAEHSAALAHTRQQIEEVNT 318
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrledLEEQIEELS---EDIESLAAEIEELEELIEELES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 319 RLQSTMVLRASIRHHAANQSAELQQQQQSLNTWLQEHDRFRQWNNELagwraqfsqqtsdREHLRQWQQQLTHAEQKLNT 398
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-------------REKLAQLELRLEGLEVRIDN 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 399 LAAitltlTADEVASALAQHAEQRPlrqrlVALHGQIVPQQKRLAQLMVTIQ---NVTLEqtqrnvALNEMRQ---RYKE 472
Cdd:TIGR02168 941 LQE-----RLSEEYSLTLEEAEALE-----NKIEDDEEEARRRLKRLENKIKelgPVNLA------AIEEYEElkeRYDF 1004
|
....*...
gi 446621575 473 KTQQLADV 480
Cdd:TIGR02168 1005 LTAQKEDL 1012
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-505 |
1.71e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 3 ILSLRLKNLNSLKGEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHET------PRLSN-VSQSQNDlmtRD 75
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPF------SKGFTVISGPNGSGKSNIGDAILFALGLSSskamraERLSDlISNGKNG---QS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 76 TAECLAEVEFEVKGEAYRAFWS-QNRARNQPDGNLQVPRVELARCADGKILAdkvkdklELTATltGLDYGRFTRSMlls 154
Cdd:TIGR02169 73 GNEAYVTVTFKNDDGKFPDELEvVRRLKVTDDGKYSYYYLNGQRVRLSEIHD-------FLAAA--GIYPEGYNVVL--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 155 QGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGV------------------ALLTPE 216
Cdd:TIGR02169 141 QGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKrqqlerlrrerekaeryqALLKEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 217 QVQSLTASLQVLTDEEKQL------LTAQQQEQQSLNwlTRLDELQQEASRRQQALQQ------ALAEEE---------- 274
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKeaierqLASLEEELEKLT--EEISELEKRLEEIEQLLEElnkkikDLGEEEqlrvkekige 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 275 -KAQPQLAALSLAQPARNLRPHWERIAEHSAALAHTRQQIEEVNTRLQSTMVLRASIRHHAANQSAELQQQQQSLNtwlQ 353
Cdd:TIGR02169 299 lEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE---E 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 354 EHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLntlaaitltltadevasalaqHAEQRPLRQRLVALHG 433
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL---------------------SEELADLNAAIAGIEA 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446621575 434 QIVPQQKRL--AQLMVTIQNVTLEQTQRNvaLNEMRQRYKEKTQQLADV-KTICEQEARIKTLEAQRAQLQAGQP 505
Cdd:TIGR02169 435 KINELEEEKedKALEIKKQEWKLEQLAAD--LSKYEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVR 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-564 |
4.85e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 1 MKILSLRLKNLNSLKgEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlSNVSQSQNDLMTRD-TAEC 79
Cdd:PRK03918 1 MKIEELKIKNFRSHK-SSVVEFDD------GINLIIGQNGSGKSSILEAILVGLYWGHG--SKPKGLKKDDFTRIgGSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 80 LAEVEFEVKGEAYRAFWSQNRArnqpdgnlqvprVELARCADG-KILADKVKDKLELTATLtgLDYGRFTRSMLLSQGQF 158
Cdd:PRK03918 72 EIELKFEKNGRKYRIVRSFNRG------------ESYLKYLDGsEVLEEGDSSVREWVERL--IPYHVFLNAIYIRQGEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 159 AAFLNAKpKERAELLEELTGTEIYGQI---SAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQl 235
Cdd:PRK03918 138 DAILESD-ESREKVVRQILGLDDYENAyknLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 236 ltaqqqeqqslnwLTRLDELQQEASRRQQALQQALAEEEKAQPQLaaLSLAQPARNLRphwERIAEHSAALAHTRQQIEE 315
Cdd:PRK03918 216 -------------LPELREELEKLEKEVKELEELKEEIEELEKEL--ESLEGSKRKLE---EKIRELEERIEELKKEIEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 316 VNTRLQSTMVLRASirhhaANQSAELQQQQQSLNTWLQE-HDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQ 394
Cdd:PRK03918 278 LEEKVKELKELKEK-----AEEYIKLSEFYEEYLDELREiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 395 KLNTLaaitltltadevasalaqhaEQRplrqrlVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNvaLNEMRQRYKEKT 474
Cdd:PRK03918 353 RLEEL--------------------EER------HELYEEAKAKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 475 QQLADVKT-ICEQEARIKTLEAQRAQLQ-AGQPCPLCG---STSHPA--VEAYQAlepgvnqsRLLALENEVKKLGEEGA 547
Cdd:PRK03918 405 EEISKITArIGELKKEIKELKKAIEELKkAKGKCPVCGrelTEEHRKelLEEYTA--------ELKRIEKELKEIEEKER 476
|
570
....*....|....*..
gi 446621575 548 ALRGQLDALTKQLQRDE 564
Cdd:PRK03918 477 KLRKELRELEKVLKKES 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-697 |
8.57e-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: 50.06 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 386 QQQLTHAEQKLNTLAAiTLTLTADEVASALAQH----AEQRPLRQRLVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNV 461
Cdd:TIGR02168 676 RREIEELEEKIEELEE-KIAELEKALAELRKELeeleEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 462 ALNEMRQRYKEKTQQLADVKT-ICEQEARIKTLEAQRAQLQagqpcplcgstshpavEAYQALEpgvnqSRLLALENEVK 540
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEeLAEAEAEIEELEAQIEQLK----------------EELKALR-----EALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 541 KLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQP----QDDIQPWLDAQDEHERQLRLLS 616
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieelESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 617 ----------------------QRHELQGQIAAHNQQIIQYQQQIEQRQQQLltaLAGYALTLPQEDEEESWLATRQQEA 674
Cdd:TIGR02168 894 seleelseelreleskrselrrELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340
....*....|....*....|...
gi 446621575 675 qswqqrQNELTALQNRIQQLTPI 697
Cdd:TIGR02168 971 ------RRRLKRLENKIKELGPV 987
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
203-595 |
1.36e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 203 LQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAA 282
Cdd:PRK11281 26 FARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 283 LS--LAQPAR------NLRPHWERIAEHSAALAHTRQQIEEVNTRL--QSTMVLRA-SIRHHAANQSAELQQQQQSLNT- 350
Cdd:PRK11281 106 LKddNDEETRetlstlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAqAALYANSQRLQQIRNLLKGGKVg 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 351 -WLQEHDRFRQWNNELAGWRAQFSQQ--------------TSDREHLRQWQQQLTHAEQKL-NTLAAITLTLTADEVASA 414
Cdd:PRK11281 186 gKALRPSQRVLLQAEQALLNAQNDLQrkslegntqlqdllQKQRDYLTARIQRLEHQLQLLqEAINSKRLTLSEKTVQEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 415 L----AQHAEQRPLRQRLVALHGQI----VPQQKRLAQLM---VTIQNV--TLEQTQRNvaLNEM-----------RQRY 470
Cdd:PRK11281 266 QsqdeAARIQANPLVAQELEINLQLsqrlLKATEKLNTLTqqnLRVKNWldRLTQSERN--IKEQisvlkgslllsRILY 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 471 KEK------------TQQLADVK----TICEQEARIKTLEAQRAQLQAGQPcplcgstshpaveayQALEPGVNQSrLLA 534
Cdd:PRK11281 344 QQQqalpsadlieglADRIADLRleqfEINQQRDALFQPDAYIDKLEAGHK---------------SEVTDEVRDA-LLQ 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446621575 535 LENEVKKLgeegaalrgqLDALTKQLQRDENEAQSLRQDEqaltQQWQAVTASLNITLQPQ 595
Cdd:PRK11281 408 LLDERREL----------LDQLNKQLNNQLNLAINLQLNQ----QQLLSVSDSLQSTLTQQ 454
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
931-1002 |
2.03e-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: 2.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446621575 931 LEVEVVDTWQADAVRDTRTLSGGE-----SFLVSLALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDA 1002
Cdd:pfam13558 14 VEVRDEDGSEVETYRRSGGLSGGEkqllaYLPLAAALAAQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-65 |
2.56e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.97 E-value: 2.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446621575 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 446621575 26 PFASNGLFAITGPTGAGKTTLLDAICLAL 54
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIGLAL 45
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-613 |
6.28e-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: 47.04 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 192 QHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDE---------------EKQLLTAQQQEQQSLnwlTRLDELQ 256
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSElreakrmyedkieelEKQLVLANSELTEAR---TERDQFS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 257 QEASRRQQALQQALAEEEKAQPQLAaLSLAQPARnlrpHWERIAEHSAALAHTRQQIEEVNTRLQSTMVLRASIRHHAAN 336
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELS-LEKEQNKR----LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 337 Q---------------------SAELQQQQQ------------------------SLNTWLQEHDR-FRQWNNELAGWRA 370
Cdd:pfam15921 445 QmerqmaaiqgkneslekvsslTAQLESTKEmlrkvveeltakkmtlessertvsDLTASLQEKERaIEATNAEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 371 QFSQQTSDREHLRQWQQQLTHAEQKLNtlaAITLTLTA-DEVASALAQHAEQrplRQRLVALHGQIV-PQQKRLAQLMVT 448
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDHLRNVQTECE---ALKLQMAEkDKVIEILRQQIEN---MTQLVGQHGRTAgAMQVEKAQLEKE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 449 IQNVTLEQTQRNVALNEMRQRYKEKTQQLAD--------VKTICEQEARIKTLEAQRAQLQagQPCPLCGSTSHPAVEAY 520
Cdd:pfam15921 599 INDRRLELQEFKILKDKKDAKIRELEARVSDlelekvklVNAGSERLRAVKDIKQERDQLL--NEVKTSRNELNSLSEDY 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 521 QAL-----------EPGVN---------QSRLLALENEVKKL-GEEGAAL-------------RGQLDALTKQLQRDENE 566
Cdd:pfam15921 677 EVLkrnfrnkseemETTTNklkmqlksaQSELEQTRNTLKSMeGSDGHAMkvamgmqkqitakRGQIDALQSKIQFLEEA 756
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446621575 567 AQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLR 613
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLK 803
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-55 |
1.05e-04 |
|
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: 1.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446621575 1 MKILSLRLKNLNSLKGewkIDFTrepFASNGLFAITGPTGAGKTTLLDAICLALY 55
Cdd:cd00267 2 IENLSFRYGGRTALDN---VSLT---LKAGEIVALVGPNGSGKSTLLRAIAGLLK 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-773 |
1.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 225 LQVLTDEEKQLLTAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRphwERIAEHSA 304
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE---AELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 305 ALAHTRQQIEEVNTRLQSTMVLRASIRHHAANQSAELQQqqqslnTWLQEHDRFRQWNNELAGWRAQFSQQtsdREHLRQ 384
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQ------LSLATEEELQDLAEELEELQQRLAEL---EEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 385 WQQQLTHAEQKLNTLAAITLTLTADEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNVALN 464
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 465 EMRQRYKEKTQQLADVKTICEQEariktLEAQRAQLQagqpcplcgstshpaveayqaLEPGVNQSRLLALENEVKKLGE 544
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEE-----LEELLAALG---------------------LPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 545 egaaLRGQLDALTKQLQRDENEAQslrqdEQALTQQWQAvtaslnitlqpqDDIQPWLDAQDEHERQLRLLSQRHELQGQ 624
Cdd:COG4717 352 ----LLREAEELEEELQLEELEQE-----IAALLAEAGV------------EDEEELRAALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 625 IAAHnqqiiqyqqqieqrqqqlltalAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRIQQLTPILETLpqs 704
Cdd:COG4717 411 LEEL----------------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL--- 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446621575 705 ddlphsEETVALDNWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAAL 773
Cdd:COG4717 466 ------EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEYFSRL 528
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
318-589 |
2.61e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 318 TRLQSTMVLRASIRHHAANQSAELqqqqqsLNTWLQEhdrFRQWNNELagwRAQFSQQTSD--REHLRQWQQQLTHAEQK 395
Cdd:COG3206 130 EPVKGSNVIEISYTSPDPELAAAV------ANALAEA---YLEQNLEL---RREEARKALEflEEQLPELRKELEEAEAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 396 LNTLAAITLTLTADEVASALAQHAEQrpLRQRLVALHGQIVPQQKRLAQL--MVTIQNVTLEQTQRNVALNEMRQRYKEK 473
Cdd:COG3206 198 LEEFRQKNGLVDLSEEAKLLLQQLSE--LESQLAEARAELAEAEARLAALraQLGSGPDALPELLQSPVIQQLRAQLAEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 474 TQQLADVKTI-CEQEARIKTLEAQRAQLQAgqpcplcgstshpaveAYQALEpgvnQSRLLALENEVKKLGEEGAALRGQ 552
Cdd:COG3206 276 EAELAELSARyTPNHPDVIALRAQIAALRA----------------QLQQEA----QRILASLEAELEALQAREASLQAQ 335
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446621575 553 LDALTKQLQR---DENEAQSLRQDEQALTQQWQAVTASLN 589
Cdd:COG3206 336 LAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLE 375
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
236-499 |
3.30e-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: 44.37 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 236 LTAQQQEQQSLNwlTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSlaqparnlrphwERIAEHSAALAHTRQQIEE 315
Cdd:COG4942 15 AAAQADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALE------------RRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 316 VNTRLQSTmvlrasirhhaANQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQT-SDREHLRQWQQQLTHAEQ 394
Cdd:COG4942 81 LEAELAEL-----------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 395 KLntlaAITLTLTADEVASALAQHAEQrplRQRLVALHGQIVPQQKRLAQlmvtiqnvtlEQTQRNVALNEMRQRYKEKT 474
Cdd:COG4942 150 EQ----AEELRADLAELAALRAELEAE---RAELEALLAELEEERAALEA----------LKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|....*.
gi 446621575 475 QQLADVKTICEQ-EARIKTLEAQRAQ 499
Cdd:COG4942 213 AELAELQQEAEElEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-627 |
7.27e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 412 ASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLMVTIQNVTLEQTQRNVALNEMRQRYKEKTQQLADV-KTICEQEARI 490
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 491 KTLEAQRAQLQA-------------GQPCPLCGSTSHPAVEAYQALE--PGVNQSRlLALENEVKKLGEEGAALRGQLDA 555
Cdd:COG4942 93 AELRAELEAQKEelaellralyrlgRQPPLALLLSPEDFLDAVRRLQylKYLAPAR-REQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621575 556 LTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNitlQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAA 627
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
463-694 |
7.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 463 LNEMRQRYKEKTQQLADVKTICEQEARIKTLEAQRAQLQAGQpcplcgstshpaveayQALEPGVNQSRLLALENEVKKL 542
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLR----------------AALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 543 GEEGAALRGQLDALTKQLQRdeneaqsLRQDEQALTQQWQAvtaslnitlQPQDDIQPWLDAQDEHERQLRLLSQRHE-L 621
Cdd:COG4913 301 RAELARLEAELERLEARLDA-------LREELDELEAQIRG---------NGGDRLEQLEREIERLERELEERERRRArL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446621575 622 QGQIAAhnqqiiqYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEA-QSWQQRQNELTALQNRIQQL 694
Cdd:COG4913 365 EALLAA-------LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAeAALRDLRRELRELEAEIASL 431
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
946-1016 |
8.58e-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: 8.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446621575 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 446621575 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 446621575 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 |
1.29e-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: 1.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 1 MKILSLRLKNLNSLKGEwKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPR 60
Cdd:COG3593 1 MKLEKIKIKNFRSIKDL-SIEL------SDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
191-501 |
1.40e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQEQQSLNWLTRLDELQQEASRR--QQALQQ 268
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRelERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 269 ALAEEEKAQPQLAALSLAQPARNlrphwERIAEHSAALAHTRQQIEEVNTRLQSTMVLRASIRHHaanqsaelqqqqqsl 348
Cdd:pfam17380 369 EIAMEISRMRELERLQMERQQKN-----ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--------------- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 349 ntwlQEHDRFRQWnNELAGWRAQFSQQTSDREHLRqwQQQLTHAEQKLNTLAAITLTLTADEVASALAQHAEQRPLRQRL 428
Cdd:pfam17380 429 ----QEEARQREV-RRLEEERAREMERVRLEEQER--QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446621575 429 VALHGQIVPQQKR---LAQLMVTIQNVTLEQTQRNVALNEMR--QRYKEKTQQLADVKTICEQEARIKTLEAQRAQLQ 501
Cdd:pfam17380 502 EERKQAMIEEERKrklLEKEMEERQKAIYEEERRREAEEERRkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
|
|
| 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 446621575 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 446621575 4 LSLRLKNLNSLKGEWKIDFTRE-------PFASNGLFAITGPTGAGKTTLLDAicLALYHETPRLS 62
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKQllknvsgKAKPGELTAIMGPSGAGKSTLLNA--LAGRRTGLGVS 65
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
220-504 |
2.67e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 220 SLTASLQVLTDEEKQLltaQQQEQQSLNWLtrldELQQEASRRQQALQQALAEEEKAQPQL-AALSLAQPARNLRPHWER 298
Cdd:PRK04863 311 EMARELAELNEAESDL---EQDYQAASDHL----NLVQTALRQQEKIERYQADLEELEERLeEQNEVVEEADEQQEENEA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 299 IAEHS--------AALAHTRQQIEEVNTR-LQSTMVLRASIRHHAANQSAELQQQqqSLNTWLQEhdrFRQWNNELAGWR 369
Cdd:PRK04863 384 RAEAAeeevdelkSQLADYQQALDVQQTRaIQYQQAVQALERAKQLCGLPDLTAD--NAEDWLEE---FQAKEQEATEEL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 370 AQFSQQTSDREHLRQwqqQLTHAEQKLNTLAAITLTLTADEVA-SALAQHAEQRPLRQRLVALHGQIVPQQKRLAQlmvt 448
Cdd:PRK04863 459 LSLEQKLSVAQAAHS---QFEQAYQLVRKIAGEVSRSEAWDVArELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ---- 531
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446621575 449 iqnvtleQTQRNVALNEMRQRYKEKTQQLADVKTI-CEQEARIKTLEAQRAQLQAGQ 504
Cdd:PRK04863 532 -------QQRAERLLAEFCKRLGKNLDDEDELEQLqEELEARLESLSESVSEARERR 581
|
|
| 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 446621575 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 446621575 949 TLSGGESFLVSLALALALSDLVShkTRIDSLFLDEGFGTLDSETLDTAL-DALDALNA-SGKTIGVISHVEAMKERIPVQ 1026
Cdd:cd03240 115 RCSGGEKVLASLIIRLALAETFG--SNCGILALDEPTTNLDEENIEESLaEIIEERKSqKNFQLIVITHDEELVDAADHI 192
|
90
....*....|...
gi 446621575 1027 IKVKKiNGLGYSK 1039
Cdd:cd03240 193 YRVEK-DGRQKSR 204
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-90 |
5.63e-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: 39.88 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621575 3 ILSLRLKNlNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALyhetprlsnVSQSQNDLMTRDTAECLAE 82
Cdd:cd03241 1 LLELSIKN-FALIEELELDFEE------GLTVLTGETGAGKSILLDALSLLL---------GGRASADLIRSGAEKAVVE 64
|
....*...
gi 446621575 83 VEFEVKGE 90
Cdd:cd03241 65 GVFDISDE 72
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-130 |
7.09e-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: 7.09e-03
10 20 30 40 50 60 70 80
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gi 446621575 27 FASNGLFAITGPTGAGKTTLLDAI-CLALYHETPR---LSNVSQSQNDLMTRDTA-----ECLAEvEFEVkgEAYRAFWS 97
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTTSgqiLFNGQPRKPDQFQKCVAyvrqdDILLP-GLTV--RETLTYTA 106
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90 100 110
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gi 446621575 98 QNRARN-QPDGNLQ--VPRVELARCADGKILADKVK 130
Cdd:cd03234 107 ILRLPRkSSDAIRKkrVEDVLLRDLALTRIGGNLVK 142
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