|
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: 1567.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 1 MKILSLRLKNLNSLKGEWKIDFTREPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:PRK10246 1 MKILSLRLKNLNSLKGEWKIDFTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLNNVSQSQNDLMTRDTAECL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:PRK10246 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQAPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQ 240
Cdd:PRK10246 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSTALAHTRQQIEEVNTRL 320
Cdd:PRK10246 241 QQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 321 QSTMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALA 400
Cdd:PRK10246 321 QSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 401 AITLTLTADEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLADV 480
Cdd:PRK10246 401 AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 481 KTICEQETRIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQARLLTLEKEVKKLGEEVATLRGQLDALTKQL 560
Cdd:PRK10246 481 KTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 561 QRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
Cdd:PRK10246 561 QRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 641 QRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQHRQNELTALQNRIQQLTPILETLPQSDELPHSEETVVLENWR 720
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 721 QVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLV 800
Cdd:PRK10246 721 QVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLV 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 801 IQTAETLTQHQQHRPGGLSLTVTVEQIQQELAQTQQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQVEDWG 880
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVEDWG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKASEALEVEVVDTWQADAVRDTRTLSGGESFLVSL 960
Cdd:PRK10246 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVWLANQQLTRLHGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGESFLVSL 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
Cdd:PRK10246 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
|
....*..
gi 446621521 1041 ESAFAMK 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: 990.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 1 MKILSLRLKNLNSLKGEWKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALG----PIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:TIGR00618 77 AELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQ 240
Cdd:TIGR00618 157 FLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSTALAHTRQQIEEVNTRL 320
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 321 QSTMALRASIRHH---AAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLN 397
Cdd:TIGR00618 317 QSKMRSRAKLLMKraaHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 398 ALAAITLTLTAdEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQL 477
Cdd:TIGR00618 397 SLCKELDILQR-EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 478 ADVKTICEQETRIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQARLLTLEKEVKKLGEEVATLRGQLDALT 557
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 558 KQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQ 637
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 638 QIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQHRQNELTALQNRIQQLTPILETLPQSDELPHSEETVVLE 717
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 718 NWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQ 797
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 798 TLVIQTAETLTQHQQHRP-GGLSLTVTVEQIQQELAQTQQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQV 876
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPsDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 877 EDWGYLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKAS--EALEVEVVDTWQADAVRDTRTLSGGE 954
Cdd:TIGR00618 876 DKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNArkYQGLALLVADAYTGSVRPSATLSGGE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 955 SFLVSLALA--LALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKI 1032
Cdd:TIGR00618 956 TFLASLSLAlaLADLLSTSGGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKT 1035
|
....*..
gi 446621521 1033 NGLGYSK 1039
Cdd:TIGR00618 1036 NAGSHVM 1042
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-205 |
9.72e-31 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 120.11 E-value: 9.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 2 KILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRlsnVSQSQNDLMTRDTAECLA 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDD------GLNLIVGPNGAGKSTILEAIRYALYGKARS---RSKLRSDLINVGSEEASV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 82 EVEFEVKGEAYRAFWsqnrarnqpdgnlqvprvelarcadgkiladkvkdkleltatltgldygrftrsmllSQGQFAAF 161
Cdd:COG0419 72 ELEFEHGGKRYRIER---------------------------------------------------------RQGEFAEF 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446621521 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 |
4.12e-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: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 1 MKILSLRLKNLNSLKGEWKIDFTrePFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlmtRDTAECL 80
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFT--GLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSV---FAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 81 AEV--EFEVKGEAYRAFwsqnRARnqpdgnlqvprvelarcadgkiladkvkdkleltatltGLDYGRFTRSMLLSQGQF 158
Cdd:cd03279 76 AEVsfTFQLGGKKYRVE----RSR--------------------------------------GLDYDQFTRIVLLPQGEF 113
|
....
gi 446621521 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 |
1.05e-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: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 945 RDTRTLSGGESFLVSLALAL--ALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKER 1022
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALalSEVLQNRGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKER 198
|
....*....
gi 446621521 1023 IPVQIKVKK 1031
Cdd:cd03279 199 IPQRLEVIK 207
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-206 |
3.28e-22 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 95.26 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 6 LRLKNLNSLKgEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQN-----DLMTRDTAECL 80
Cdd:pfam13476 1 LTIENFRSFR-DQTIDF------SKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFvkgdiRIGLEGKGKAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 81 AEVEFEVKGEA--YRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLEltatltgldygRFTRSMLLSQGQF 158
Cdd:pfam13476 74 VEITFENNDGRytYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKI-----------ILPLLVFLGQERE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446621521 159 AAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQ 206
Cdd:pfam13476 143 EEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-578 |
7.81e-13 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 73.01 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 1 MKILSLRLKNLNSLKgEWKIDFTrepfasNGLFAITGPTGAGKTTLLDAICLALYHETPrlsnvSQSQNDLMTRDTAECL 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHD-DSEIEFD------TGINIITGKNGAGKSSIVDAIRFALFTDKR-----TEKIEDMIKKGKNNLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRvelarcaDGKILADKVKDKLE-LTATLTGLDYGRFTRSMLLSQGQFA 159
Cdd:PRK01156 69 VELEFRIGGHVYQIRRSIERRGKGSRREAYIKK-------DGSIIAEGFDDTTKyIEKNILGISKDVFLNSIFVGQGEMD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 160 AFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTEL-------EKLQAQASGVALLTpEQVQSLTASLQVLTDEE 232
Cdd:PRK01156 142 SLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEIsnidyleEKLKSSNLELENIK-KQIADDEKSHSITLKEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 233 KQL---ITAQQQEQQSLN-WLTRLDELQQEASRRQQALQQA---LAEEEKAQPQLAAL---------SLAQPARN-LRPH 295
Cdd:PRK01156 221 ERLsieYNNAMDDYNNLKsALNELSSLEDMKNRYESEIKTAesdLSMELEKNNYYKELeerhmkiinDPVYKNRNyINDY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 296 WERIAEhstaLAHTRQQIEEVNTRLQSTmalrasirHHAAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQ 375
Cdd:PRK01156 301 FKYKND----IENKKQILSNIDAEINKY--------HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 376 TSDREHLRQWQQQLTHAEQKLNALAAITLT---LTADEVasalaqhaeqrplrqrlvalhgqivpqQKRLAQLQVAIQNV 452
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKiqeIDPDAI---------------------------KKELNEINVKLQDI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 453 TLEQTQRNAALNEMRHRYKEktqqladvkticeqetriktLEAQRAQLQAGQPCPLCGST-----SHPAVEAYQALEPGV 527
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDE--------------------LSRNMEMLNGQSVCPVCGTTlgeekSNHIINHYNEKKSRL 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 446621521 528 NQaRLLTLEKEVKKLGEEVATLRGQLDAL-TKQLQRDENEAQSLRQDEQALT 578
Cdd:PRK01156 482 EE-KIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLE 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
438-1017 |
9.62e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 438 QQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLADVKTICEQETRIKTLEAQRAQLQAGQPCplcgstshpAV 517
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER---------LE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 518 EAYQALEPGVN-QARLLTLEKEVKKLGEEVATLRGQLDALT-KQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQ 595
Cdd:COG4717 150 ELEERLEELRElEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 596 DDIQPWLDAQDEhERQLRLLSQRHELQGQIAAHnQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQ 675
Cdd:COG4717 230 EQLENELEAAAL-EERLKEARLLLLIAAALLAL-LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 676 SWQHRQNELTAlqnriQQLTPILETLPQSDELPHSEETVVLENWRQVHEQCLALHSQQQTLQqqdvlaaqsLQKAQAQFD 755
Cdd:COG4717 308 QALPALEELEE-----EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---------LEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 756 TALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLVIQTAETLTQHQqhrpgglsLTVTVEQIQQELAQTQ 835
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--------LEEELEELEEELEELE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 836 QKLRENTTSQGEIRQQLKQ---DADNRQQQQTLMQQIAQMTQQVEDWGYLNslIGSKEGDKFRKFAQGLTLDNLVHLANQ 912
Cdd:COG4717 446 EELEELREELAELEAELEQleeDGELAELLQELEELKAELRELAEEWAALK--LALELLEEAREEYREERLPPVLERASE 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 913 QLTRL-HGRYLLQRkASEALEVEVVDtwQADAVRDTRTLSGGE----------SFLVslalalalsdlvSHKTRIDSLFL 981
Cdd:COG4717 524 YFSRLtDGRYRLIR-IDEDLSLKVDT--EDGRTRPVEELSRGTreqlylalrlALAE------------LLAGEPLPLIL 588
|
570 580 590
....*....|....*....|....*....|....*.
gi 446621521 982 DEGFGTLDSETLDTALDALDALNASGKTIGVISHVE 1017
Cdd:COG4717 589 DDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEE 624
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-481 |
5.35e-12 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 69.66 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 6 LRLKNLNSLKGEWkIDFTREPFASNglfAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDtaeCLAEVEF 85
Cdd:PHA02562 7 IRYKNILSVGNQP-IEIQLDKVKKT---LITGKNGAGKSTMLEALTFALFGKPFRDIKKGQLINSINKKD---LLVELWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 86 EVKGEAYRAFwsqnRArnqpdgnlQVPRVELARCaDGKILADK--VKDKLELTATLTGLDYGRFTRSMLLSQGQFAAFLN 163
Cdd:PHA02562 80 EYGEKEYYIK----RG--------IKPNVFEIYC-NGKLLDESasSKDFQKYFEQMLGMNYKSFKQIVVLGTAGYVPFMQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 164 AKPKERAELLEELTGTEIygqISAMvfeqhksarTELEKlqaqasgvalltpEQVQSLTASLQVLtDEEKQLITAQQQEQ 243
Cdd:PHA02562 147 LSAPARRKLVEDLLDISV---LSEM---------DKLNK-------------DKIRELNQQIQTL-DMKIDHIQQQIKTY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 244 QslNWLTRLDELQQEASRRQQALQQALAEEEKaqpqlaalslaqparnlrphweriaEHSTALAHTRQQIEEVNTRLQST 323
Cdd:PHA02562 201 N--KNIEEQRKKNGENIARKQNKYDELVEEAK-------------------------TIKAEIEELTDELLNLVMDIEDP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 324 MALRASIRHHAAKQSAELQQQQqslnawlQEHDRFRQwNNELAGWRAQFSQQ----TSDREHLRQWQQQLTHAEQKLNAL 399
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQ-------KVIKMYEK-GGVCPTCTQQISEGpdriTKIKDKLKELQHSLEKLDTAIDEL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 400 AAItltltadeVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLAD 479
Cdd:PHA02562 326 EEI--------MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
..
gi 446621521 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 |
1.77e-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: 68.54 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 154 SQGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVAlltpEQVQSLTAslQVLTDEEK 233
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELE----RQLKSLER--QAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 234 QLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSlaqparnlrphwERIAEHSTALAHTRQQI 313
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE------------EKLEELRLEVSELEEEI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 314 EEVNTRLQSTMALRASIRHHAAKQSAelqqqqqslnawlqehdRFRQWNNELAGWRAQfsqqtsdrehLRQWQQQLTHAE 393
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRE-----------------RLANLERQLEELEAQ----------LEELESKLDELA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 394 QKLNALAAITLTLTAdEVASALAQHAEQRPLRQrlvALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRhrykEK 473
Cdd:TIGR02168 337 EELAELEEKLEELKE-ELESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE----AR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 474 TQQLADVKTICEQETRIKTLEAQRAQLQAgqpcplcgstshpaveayqalepgvNQARLLTLEKEVKKLGEEVATLRGQL 553
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKE-------------------------LQAELEELEEELEELQEELERLEEAL 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446621521 554 DALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQ 617
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-579 |
2.01e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 1 MKILSLRLKNLNSLKgewKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlsnVSQSQNDLMTRDTAECL 80
Cdd:PRK02224 1 MRFDRVRLENFKCYA---DADLRLED----GVTVIHGVNGSGKSSLLEACFFALYGSKA----LDDTLDDVITIGAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 81 AEVEFEVKGEAYRAfwsQNRARNQPDgnlqvpRVELARC--ADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQF 158
Cdd:PRK02224 70 IELWFEHAGGEYHI---ERRVRLSGD------RATTAKCvlETPEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 159 AAFLNAKPKERAELLEELTgteiygQISA--MVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTAslqvlTDEEKQLI 236
Cdd:PRK02224 141 NKLINATPSDRQDMIDDLL------QLGKleEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 237 TAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAalSLAQPARNLRphwERIAEHSTALAHTRQQIEEV 316
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE--TLEAEIEDLR---ETIAETEREREELAEEVRDL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 317 NTRLQSTMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQwnnELAGWRAQFSQQTSDREHLRQWQQQL-THAEQK 395
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLeERAEEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 396 LNALAAITLTLTADEVAsalaqhAEQRplRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTq 475
Cdd:PRK02224 362 REEAAELESELEEAREA------VEDR--REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 476 qlADVKTICEqetrikTLEAQRAQLQAGQpCPLCGstsHPAVEAYQALEPGVNQARLLTLEKEVKKLGEEVATLRGQLDA 555
Cdd:PRK02224 433 --ATLRTARE------RVEEAEALLEAGK-CPECG---QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
570 580
....*....|....*....|....
gi 446621521 556 LtKQLQRDENEAQSLRQDEQALTQ 579
Cdd:PRK02224 501 A-EDLVEAEDRIERLEERREDLEE 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-795 |
2.41e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 154 SQGQFAAFLNAKPKERAELLEELTG-----------------------------TEIYGQIS-----AMVFEQHKSARTE 199
Cdd:COG1196 142 GQGMIDRIIEAKPEERRAIIEEAAGiskykerkeeaerkleateenlerledilGELERQLEplerqAEKAERYRELKEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 200 LEKLQAQASGVAL-LTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWL-TRLDELQQEASRRQQALQQALAEEEKAQ 277
Cdd:COG1196 222 LKELEAELLLLKLrELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEAQAEEYELLAELARLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 278 PQLAALSLAQpaRNLRphwERIAEHSTALAHTRQQIEEVNTRLQstmALRASIRHHAAKQSAELQQQQQSLNAWLQEHDR 357
Cdd:COG1196 302 QDIARLEERR--RELE---ERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 358 FRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALAAITLTLTADEVASALAQHAEQRPLRQRLVAlhgqivp 437
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE------- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 438 QQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLAdvkticEQETRIKTLEAQRAQLQAgqpcplcgstshpAV 517
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA------EAAARLLLLLEAEADYEG-------------FL 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 518 EAYQALEPGVNQARLLTLEKEVKKLGEEVATLRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTAslnitlQPQDD 597
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF------LPLDK 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 598 IQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSW 677
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 678 QHRQNELTALQNRIQQLTPILETLPQSDELPHSEETVVLENWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTA 757
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
650 660 670
....*....|....*....|....*....|....*...
gi 446621521 758 LQASVFDDQQAfLAALMDEQTLTQLEQLKQNLENQRRQ 795
Cdd:COG1196 742 LEEEELLEEEA-LEELPEPPDLEELERELERLEREIEA 778
|
|
| 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 446621521 3 ILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlMTRDTAEcLAE 82
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFS------PLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPK-LIREGEV-RAQ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446621521 83 VEFE---VKGEAYRAFWSQNRARN-----QPDGNLQVPRvELARCADG-KILA 126
Cdd:cd03240 73 VKLAfenANGKKYTITRSLAILENvifchQGESNWPLLD-MRGRCSGGeKVLA 124
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-695 |
8.72e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 169 RAELLEEltgTEIYGQISAMV--FEQHKSARTELEKLQAQasgVALLTP-----EQVQSLTASLQVLtDEEKQLITAQQQ 241
Cdd:COG4913 214 REYMLEE---PDTFEAADALVehFDDLERAHEALEDAREQ---IELLEPirelaERYAAARERLAEL-EYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 242 EQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRphweRIAEHSTALAHTRQQIEEVNTRLQ 321
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD----RLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 322 STMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQW-NNELAGWRAQFSQQTSDREHLRQWQQQLT--------HA 392
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAlEEALAEAEAALRDLRRELRELEAEIASLErrksnipaRL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 393 EQKLNALAAiTLTLTADEV-------------------------------------ASALAQHAEQRPLRQRLVALHgqi 435
Cdd:COG4913 443 LALRDALAE-ALGLDEAELpfvgelievrpeeerwrgaiervlggfaltllvppehYAAALRWVNRLHLRGRLVYER--- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 436 VPQQKRLAQLQVAIQNVTLE--QTQRNAALNEMRHRYkektQQLADVktIC---EQETRiktlEAQRAQLQAGQpcplcg 510
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGklDFKPHPFRAWLEAEL----GRRFDY--VCvdsPEELR----RHPRAITRAGQ------ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 511 sTSHPAV------EAYQALEP---GVNQARLLTLEKEVKKLGEEVATLRGQLDALTKQLQRDENEAQSLRQ--------- 572
Cdd:COG4913 583 -VKGNGTrhekddRRRIRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdei 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 573 DEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQL-RLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 446621521 652 GyaltlpQEDEEESWLATRQQEAQSWQHRQNELTALQNRIQQLT 695
Cdd:COG4913 742 L------ARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-564 |
4.48e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 1 MKILSLRLKNLNSLKgEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlSNVSQSQNDLMTRD-TAEC 79
Cdd:PRK03918 1 MKIEELKIKNFRSHK-SSVVEFDD------GINLIIGQNGSGKSSILEAILVGLYWGHG--SKPKGLKKDDFTRIgGSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 80 LAEVEFEVKGEAYRAFWSQNRArnqpdgnlqvprVELARCADG-KILADKVKDKLELTATLtgLDYGRFTRSMLLSQGQF 158
Cdd:PRK03918 72 EIELKFEKNGRKYRIVRSFNRG------------ESYLKYLDGsEVLEEGDSSVREWVERL--IPYHVFLNAIYIRQGEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 159 AAFLNAKpKERAELLEELTGTEIYGQI---SAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQL 235
Cdd:PRK03918 138 DAILESD-ESREKVVRQILGLDDYENAyknLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 236 ItaqqqeqqslnwltRLDELQQEASRRQQALQQALAEEEKAQPQLaaLSLAQPARNLRphwERIAEHSTALAHTRQQIEE 315
Cdd:PRK03918 217 P--------------ELREELEKLEKEVKELEELKEEIEELEKEL--ESLEGSKRKLE---EKIRELEERIEELKKEIEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 316 VNTRLQSTMALRASirhhaAKQSAELQQQQQSLNAWLQE-HDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQ 394
Cdd:PRK03918 278 LEEKVKELKELKEK-----AEEYIKLSEFYEEYLDELREiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 395 KLNALaaitltltadevasalaqhaEQRplrqrlVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNaaLNEMRHRYKEKT 474
Cdd:PRK03918 353 RLEEL--------------------EER------HELYEEAKAKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 475 QQLADVKT-ICEQETRIKTLEAQRAQLQ-AGQPCPLCG---STSHPA--VEAYqalepgvnQARLLTLEKEVKKLGEEVA 547
Cdd:PRK03918 405 EEISKITArIGELKKEIKELKKAIEELKkAKGKCPVCGrelTEEHRKelLEEY--------TAELKRIEKELKEIEEKER 476
|
570
....*....|....*..
gi 446621521 548 TLRGQLDALTKQLQRDE 564
Cdd:PRK03918 477 KLRKELRELEKVLKKES 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-841 |
7.20e-08 |
|
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: 56.99 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 160 AFLNAKPKERAELLEELTGT-EIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITA 238
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKlDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 239 QQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKaQPQLAALSLAQparnlrphwERIAEHSTALAHTRQQIEEVNT 318
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK-KLEEAELKELQ---------AELEELEEELEELQEELERLEE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 319 RLQSTMALRASIRH---HAAKQSAELQQQQQSLNAWLQEHDRFRQ-------WNNELAGWRAQFSQQTSDREhlrQWQQQ 388
Cdd:TIGR02168 462 ALEELREELEEAEQaldAAERELAQLQARLDSLERLQENLEGFSEgvkallkNQSGLSGILGVLSELISVDE---GYEAA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 389 LTHA-EQKLNALAAITLTlTADEVASALAQHAEQR----PLR----QRLVALHGQIVPQQ-----------KRLAQLQVA 448
Cdd:TIGR02168 539 IEAAlGGRLQAVVVENLN-AAKKAIAFLKQNELGRvtflPLDsikgTEIQGNDREILKNIegflgvakdlvKFDPKLRKA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 449 IQ----NVTLEQTQRNAalNEMRHRYKEktqqladvkticeqETRIKTLEAQRAQ---LQAGQPcplcGSTSHPAVEayq 521
Cdd:TIGR02168 618 LSyllgGVLVVDDLDNA--LELAKKLRP--------------GYRIVTLDGDLVRpggVITGGS----AKTNSSILE--- 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 522 alepgvNQARLLTLEKEVKKLGEEVATLRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQddiqpw 601
Cdd:TIGR02168 675 ------RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV------ 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 602 ldaQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLltalagyaltlpQEDEEEswLATRQQEAQSWQHR- 680
Cdd:TIGR02168 743 ---EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI------------EELEAQ--IEQLKEELKALREAl 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 681 ---QNELTALQNRIQQLTPILETLPQSDELPHSEETVVLENWRQVHEQCLAL-HSQQQTLQQQDVLAAQsLQKAQAQFDT 756
Cdd:TIGR02168 806 delRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaAEIEELEELIEELESE-LEALLNERAS 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 757 ALQAsvfddqqafLAALMDEQTLTQLEQlkQNLENQRRQAQTLVIQTAETLTQHQQHrpgglsltvtVEQIQQELAQTQQ 836
Cdd:TIGR02168 885 LEEA---------LALLRSELEELSEEL--RELESKRSELRRELEELREKLAQLELR----------LEGLEVRIDNLQE 943
|
....*
gi 446621521 837 KLREN 841
Cdd:TIGR02168 944 RLSEE 948
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
203-595 |
1.79e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.69 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 203 LQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAA 282
Cdd:PRK11281 26 FARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 283 LS--LAQPAR------NLRPHWERIAEHSTALAHTRQQIEEVNTRL--QSTMALRA-SIRHHAAKQSAELQQQQQSLNA- 350
Cdd:PRK11281 106 LKddNDEETRetlstlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAqAALYANSQRLQQIRNLLKGGKVg 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 351 -WLQEHDRFRQWNNELAGWRAQFSQQ--------------TSDREHLRQWQQQLTHAEQKL-NALAAITLTLTADEVASA 414
Cdd:PRK11281 186 gKALRPSQRVLLQAEQALLNAQNDLQrkslegntqlqdllQKQRDYLTARIQRLEHQLQLLqEAINSKRLTLSEKTVQEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 415 L----AQHAEQRPLRQRLVALHGQI----VPQQKRLAQL---QVAIQNV--TLEQTQRNaaLNEM-----------RHRY 470
Cdd:PRK11281 266 QsqdeAARIQANPLVAQELEINLQLsqrlLKATEKLNTLtqqNLRVKNWldRLTQSERN--IKEQisvlkgslllsRILY 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 471 KEK------------TQQLADVK----TICEQETRIKTLEAQRAQLQAGQPcplcgstshpaveayQALEPGVNQArLLT 534
Cdd:PRK11281 344 QQQqalpsadlieglADRIADLRleqfEINQQRDALFQPDAYIDKLEAGHK---------------SEVTDEVRDA-LLQ 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446621521 535 LEKEVKKLgeevatlrgqLDALTKQLQRDENEAQSLRQDEqaltQQWQAVTASLNITLQPQ 595
Cdd:PRK11281 408 LLDERREL----------LDQLNKQLNNQLNLAINLQLNQ----QQLLSVSDSLQSTLTQQ 454
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-505 |
7.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 3 ILSLRLKNLNSLKGEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHET------PRLSN-VSQSQNDlmtRD 75
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPF------SKGFTVISGPNGSGKSNIGDAILFALGLSSskamraERLSDlISNGKNG---QS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 76 TAECLAEVEFEVKGEAYRAFWS-QNRARNQPDGNLQVPRVELARCADGKILAdkvkdklELTATltGLDYGRFTRSMlls 154
Cdd:TIGR02169 73 GNEAYVTVTFKNDDGKFPDELEvVRRLKVTDDGKYSYYYLNGQRVRLSEIHD-------FLAAA--GIYPEGYNVVL--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 155 QGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGV------------------ALLTPE 216
Cdd:TIGR02169 141 QGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKrqqlerlrrerekaeryqALLKEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 217 QVQSLTASLQVLTDEEKQL--ITAQQQE-QQSLNWLT-RLDELQQEASRRQQALQQ------ALAEEE-----------K 275
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKeaIERQLASlEEELEKLTeEISELEKRLEEIEQLLEElnkkikDLGEEEqlrvkekigelE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 276 AQPQLAALSLAQPARNLRPHWERIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQqqqsLNAWLQEH 355
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED----LRAELEEV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 356 D-RFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLnalaaitltltadevasalaqHAEQRPLRQRLVALHGQ 434
Cdd:TIGR02169 377 DkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL---------------------SEELADLNAAIAGIEAK 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621521 435 IVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLADV-KTICEQETRIKTLEAQRAQLQAGQP 505
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVR 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-480 |
7.28e-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: 53.52 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 89 GEAYRAFWSQNRARNQPDGNLQVPRVELARC-ADGKILADKVKdklELTATLTGLdygrftrsmllsQGQFAAFLNAKPK 167
Cdd:TIGR02168 652 GDLVRPGGVITGGSAKTNSSILERRREIEELeEKIEELEEKIA---ELEKALAEL------------RKELEELEEELEQ 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 168 ERAELLE---ELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQL-ITAQQQEQ 243
Cdd:TIGR02168 717 LRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeAQIEQLKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 244 QSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALS-----LAQPARNLRphwERIAEHSTALAHTRQQIEEVNT 318
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrledLEEQIEELS---EDIESLAAEIEELEELIEELES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 319 RLQSTMALRASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQWNNELagwraqfsqqtsdREHLRQWQQQLTHAEQKLNA 398
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-------------REKLAQLELRLEGLEVRIDN 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 399 LAAitltlTADEVASALAQHAEQRPlrqrlVALHGQIVPQQKRLAQLQVAIQ---NVTLEQTQRNAALNEmrhRYKEKTQ 475
Cdd:TIGR02168 941 LQE-----RLSEEYSLTLEEAEALE-----NKIEDDEEEARRRLKRLENKIKelgPVNLAAIEEYEELKE---RYDFLTA 1007
|
....*
gi 446621521 476 QLADV 480
Cdd:TIGR02168 1008 QKEDL 1012
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-591 |
3.37e-06 |
|
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: 51.27 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 192 QHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDE---------------EKQLITAQQQEQQSLnwlTRLDELQ 256
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSElreakrmyedkieelEKQLVLANSELTEAR---TERDQFS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 257 QEASRRQQALQQALAEEEKAQPQLAaLSLAQPARnlrpHWERIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAK 336
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELS-LEKEQNKR----LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 337 QSAELQQQQQSLNAWLQEHDRFRqwnnelagwraqfSQQTSDREHLRQWQQQLTHAEQKLNA----LAAITLTLTADEVA 412
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLT-------------AQLESTKEMLRKVVEELTAKKMTLESsertVSDLTASLQEKERA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 413 SAlAQHAEQRPLRQRlVALHGQIVPQQK----RLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLAD--------- 479
Cdd:pfam15921 512 IE-ATNAEITKLRSR-VDLKLQELQHLKnegdHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagamq 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 480 -VKTICEQETRIKTLEAQRAQL----QAGQPCPLCGSTSHPAVEAYQALEPGVNQARLLT-LEKEVKKLGEEVATLRGQL 553
Cdd:pfam15921 590 vEKAQLEKEINDRRLELQEFKIlkdkKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKdIKQERDQLLNEVKTSRNEL 669
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446621521 554 DALTKQ---LQRD-ENEAQSLRQDEQALTQQWQAVTASLNIT 591
Cdd:pfam15921 670 NSLSEDyevLKRNfRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
191-572 |
6.87e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLnwlTRLDELQQEASRRQQALQQAL 270
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL---ELLAELLEEAALLEAALAELL 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 271 AEEEKAQPQLAALSLAQPARNLRPHWERIAEHSTALAHTRQQI-----------EEVNTRLQSTMALRASIRHHAAKQSA 339
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligveaayeAALEAALAAALQNIVVEDDEVAAAAI 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 340 ELQQQQQSLNAWLQEHDRFRQWN-NELAGWRAQFSQQTSDREHLRQWQQQLTH------------AEQKLNALAAITLTL 406
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAaLAAALARGAIGAAVDLVASDLREADARYYvlgdtllgrtlvAARLEAALRRAVTLA 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 407 TADEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLADVKTICEQ 486
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 487 ETRIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQARLLTLEKEVKKLG-------EEVATLRGQLDALTKQ 559
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnllaiEEYEELEERYDFLSEQ 803
|
410
....*....|...
gi 446621521 560 LQRDENEAQSLRQ 572
Cdd:COG1196 804 REDLEEARETLEE 816
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
931-1002 |
1.92e-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: 1.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446621521 931 LEVEVVDTWQADAVRDTRTLSGGE-----SFLVSLALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDA 1002
Cdd:pfam13558 14 VEVRDEDGSEVETYRRSGGLSGGEkqllaYLPLAAALAAQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-65 |
2.39e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.97 E-value: 2.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446621521 26 PFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVS 65
Cdd:pfam13555 18 PIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRARFNKA 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-697 |
2.78e-05 |
|
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: 48.51 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 386 QQQLTHAEQKLNALAAiTLTLTADEVASALAQH----AEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNA 461
Cdd:TIGR02168 676 RREIEELEEKIEELEE-KIAELEKALAELRKELeeleEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 462 ALNEMRHRYKEKTQQLADVKT-ICEQETRIKTLEAQRAQLQagqpcplcgstshpavEAYQALEPGVN--QARLLTLEKE 538
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEeLAEAEAEIEELEAQIEQLK----------------EELKALREALDelRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 539 VKKLGEEVATLRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNitlQPQDDIQPWLDAQDEHERQLRLLS-- 616
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE---ELESELEALLNERASLEEALALLRse 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 617 --------------------QRHELQGQIAAHNQQIIQYQQQIEQRQQQLltaLAGYALTLPQEDEEESWLATRQQEAqs 676
Cdd:TIGR02168 896 leelseelreleskrselrrELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEA-- 970
|
330 340
....*....|....*....|.
gi 446621521 677 wqhrQNELTALQNRIQQLTPI 697
Cdd:TIGR02168 971 ----RRRLKRLENKIKELGPV 987
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-54 |
4.81e-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: 44.66 E-value: 4.81e-05
10 20
....*....|....*....|....*....
gi 446621521 26 PFASNGLFAITGPTGAGKTTLLDAICLAL 54
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIGLAL 45
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-773 |
5.41e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 225 LQVLTDEEKQLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRphwERIAEHST 304
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE---AELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 305 ALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQqslnawLQEHDRFRQWNNELAGWRAQFSQQtsdREHLRQ 384
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAEL---EEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 385 WQQQLTHAEQKLNALAAITLTLTADEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALN 464
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 465 EMRHRYKEKTQQLADVKTICEQEtriktLEAQRAQLqagqpcplcgstshpaveayqalepGVNQARLLTLEKEVKKLGE 544
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEE-----LEELLAAL-------------------------GLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 545 EVATLRGQLDALTKQLQRDENEAQslrqdEQALTQQWQAvtaslnitlqpqDDIQPWLDAQDEHERQLRLLSQRHELQGQ 624
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQE-----IAALLAEAGV------------EDEEELRAALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 625 IAAHnqqiiqyqqqieqrqqqlltalAGYALTLPQEDEEESWLATRQQEAQSWQHRQNELTALQNRIQQLTPILETLPQS 704
Cdd:COG4717 411 LEEL----------------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446621521 705 DElphseetvvLENWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAAL 773
Cdd:COG4717 469 GE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEYFSRL 528
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
318-589 |
9.08e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 318 TRLQSTMALRASIRHHAAKQSAELqqqqqsLNAWLQEhdrFRQWNNELagwRAQFSQQTSD--REHLRQWQQQLTHAEQK 395
Cdd:COG3206 130 EPVKGSNVIEISYTSPDPELAAAV------ANALAEA---YLEQNLEL---RREEARKALEflEEQLPELRKELEEAEAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 396 LNALAAITLTLTADEVASALAQHAEQrpLRQRLVALHGQIVPQQKRLAQL--QVAIQNVTLEQTQRNAALNEMRHRYKEK 473
Cdd:COG3206 198 LEEFRQKNGLVDLSEEAKLLLQQLSE--LESQLAEARAELAEAEARLAALraQLGSGPDALPELLQSPVIQQLRAQLAEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 474 TQQLADVKTI-CEQETRIKTLEAQRAQLQagqpcplcgstshpaveayQALEPGVNQArLLTLEKEVKKLGEEVATLRGQ 552
Cdd:COG3206 276 EAELAELSARyTPNHPDVIALRAQIAALR-------------------AQLQQEAQRI-LASLEAELEALQAREASLQAQ 335
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446621521 553 LDALTKQLQR---DENEAQSLRQDEQALTQQWQAVTASLN 589
Cdd:COG3206 336 LAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLE 375
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-55 |
1.06e-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: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446621521 1 MKILSLRLKNLNSLKGewkIDFTrepFASNGLFAITGPTGAGKTTLLDAICLALY 55
Cdd:cd00267 2 IENLSFRYGGRTALDN---VSLT---LKAGEIVALVGPNGSGKSTLLRAIAGLLK 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
185-618 |
2.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 185 ISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWL-TRLDELQQEASRRQ 263
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 264 QALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSTALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAElqq 343
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE--- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 344 qqqSLNAWLQEHDRFRQwnnELAGWRAQFSQQTSDREHLRQW------QQQLTHAEQKLNALAAITLTLTADEVASALAQ 417
Cdd:COG4717 200 ---ELEELQQRLAELEE---ELEEAQEELEELEEELEQLENEleaaalEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 418 HA--------------------EQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQL 477
Cdd:COG4717 274 TIagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 478 ADVKTIcEQETRIKTLEAQRAQLQAgqpcpLCGSTSHPA----VEAYQALEPGVNQARLLTLEKEVKKLGEEVATLRGQL 553
Cdd:COG4717 354 REAEEL-EEELQLEELEQEIAALLA-----EAGVEDEEElraaLEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446621521 554 DALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNiTLQPQDDIQPWLDAQDEHERQLRLLSQR 618
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELE-QLEEDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
238-500 |
3.24e-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: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 238 AQQQEQQSLNwlTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSlaqparnlrphwERIAEHSTALAHTRQQIEEVN 317
Cdd:COG4942 17 AQADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALE------------RRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 318 TRLQSTmalrasirhhaAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQT-SDREHLRQWQQQLTHAEQKL 396
Cdd:COG4942 83 AELAEL-----------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 397 NALAAITLTLTADEVASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQ 476
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|....
gi 446621521 477 LADVKTICEQETRIKTLEAQRAQL 500
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-795 |
3.50e-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: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 249 LTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERiaehSTALAHTRQQIEEVNTRLQSTMALRA 328
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA----QRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 329 SIRHHAAKQSAELQQQQQSLNAwlQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEqklnALAAITLTLTA 408
Cdd:COG4913 313 RLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL----PASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 409 DEVASALAQ-HAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNvtLEQTQRN--AALNEMRHRYKEKTQQL-ADVKTIC 484
Cdd:COG4913 387 AEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEAEIAS--LERRKSNipARLLALRDALAEALGLDeAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 485 EQetrIKTLEAQRAQlqagqpcplcgstsHPAVEAY---QAL----EPG--------VNQARL---LTLEKeVKKLGEEV 546
Cdd:COG4913 465 EL---IEVRPEEERW--------------RGAIERVlggFALtllvPPEhyaaalrwVNRLHLrgrLVYER-VRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 547 ATLRGQLDALTKQLQRDENEAQS-LRQ------------DEQALTQQWQAVTASLNI-------TLQPQDDI-QPWLDAQ 605
Cdd:COG4913 527 ERPRLDPDSLAGKLDFKPHPFRAwLEAelgrrfdyvcvdSPEELRRHPRAITRAGQVkgngtrhEKDDRRRIrSRYVLGF 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 606 DEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQrqqqlLTALAGYALTLPQEDEEESWLATRQQEAQSWQHR----- 680
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDA-----LQERREALQRLAEYSWDEIDVASAEREIAELEAElerld 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 681 --QNELTALQNRIQQLTPILETLPQSDELPHSEETVVLENWRQVHEQCLALHSQQQTLQQQDVLAAQSLqkAQAQFDTAL 758
Cdd:COG4913 682 asSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAAL 759
|
570 580 590
....*....|....*....|....*....|....*..
gi 446621521 759 QASVFDDQQAFLAALMDEQTlTQLEQLKQNLENQRRQ 795
Cdd:COG4913 760 GDAVERELRENLEERIDALR-ARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-627 |
5.90e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 412 ASALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLADV-KTICEQETRI 490
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 491 KTLEAQRAQLQA-------------GQPCPLCGSTSHPAVEAYQALE--PGVNQARlltlEKEVKKLGEEVATLRGQLDA 555
Cdd:COG4942 93 AELRAELEAQKEelaellralyrlgRQPPLALLLSPEDFLDAVRRLQylKYLAPAR----REQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621521 556 LTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAA 627
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
946-1016 |
9.23e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 9.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446621521 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 446621521 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 446621521 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 |
1.30e-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: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 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 |
1.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 364 ELAGWRAQFSQQTSDREHLRQWQQQLthaEQKLNALAAITLTLTAD-EVASALAQHAEQRPLRQRLVALHGQIVPQQKRL 442
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDAL---QERREALQRLAEYSWDEiDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 443 AQLQvaiqnvtleqtqrnAALNEMRHRYKEKTQQLADVkticeqETRIKTLEAQRAQLQAGqpcpLCGSTSHPAVEAYQA 522
Cdd:COG4913 695 EELE--------------AELEELEEELDELKGEIGRL------EKELEQAEEELDELQDR----LEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 523 LEPGVNQARLLTLEKEVKKlgeevaTLRGQLDALTKQLQRDENEAQSLRQDeqaLTQQWQAVTASLNITLQPQDDIQPWL 602
Cdd:COG4913 751 LEERFAAALGDAVERELRE------NLEERIDALRARLNRAEEELERAMRA---FNREWPAETADLDADLESLPEYLALL 821
|
250 260
....*....|....*....|....*
gi 446621521 603 DAQDE---HERQLRLLSQRHELQGQ 624
Cdd:COG4913 822 DRLEEdglPEYEERFKELLNENSIE 846
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
168-625 |
1.58e-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: 42.63 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 168 ERAELLEELTGT--EIYGQISAMVFEQHKSART--ELEKLQAQASgvalltpeqvqSLTASLQVLTDEEKQLITAQQQEQ 243
Cdd:COG3096 279 ERRELSERALELrrELFGARRQLAEEQYRLVEMarELEELSARES-----------DLEQDYQAASDHLNLVQTALRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 244 QSLNWLTRLDELQQEAsrRQQALQQALAEEEKAQPQlAALSLAQparnlrphwERIAEHSTALAHTRQQIEEVNTR-LQS 322
Cdd:COG3096 348 KIERYQEDLEELTERL--EEQEEVVEEAAEQLAEAE-ARLEAAE---------EEVDSLKSQLADYQQALDVQQTRaIQY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 323 TMALRASIRHHAAKQSAELQQQqqSLNAWLQEHdrfrqwnnelagwRAQFSQQTSDREHLRQ-------WQQQLTHAEQK 395
Cdd:COG3096 416 QQAVQALEKARALCGLPDLTPE--NAEDYLAAF-------------RAKEQQATEEVLELEQklsvadaARRQFEKAYEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 396 LNALAAITLTLTADEVA-SALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQnvTLEQTQRNAAlnemrhrykekt 474
Cdd:COG3096 481 VCKIAGEVERSQAWQTArELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAER--LLEEFCQRIG------------ 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 475 QQLADVKTiceqetriktLEAQRAQLQAgqpcplcgstshpaveayqalepgvnqaRLLTLEKEVKKLGEEVATLRGQLD 554
Cdd:COG3096 547 QQLDAAEE----------LEELLAELEA----------------------------QLEELEEQAAEAVEQRSELRQQLE 588
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446621521 555 ALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLdaqdEHERQL-----RLLSQRHELQGQI 625
Cdd:COG3096 589 QLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLL----EREREAtverdELAARKQALESQI 660
|
|
| 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 446621521 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 446621521 4 LSLRLKNLNSLKGEWKIDFTRE-------PFASNGLFAITGPTGAGKTTLLDAicLALYHETPRLS 62
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKQllknvsgKAKPGELTAIMGPSGAGKSTLLNA--LAGRRTGLGVS 65
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
220-625 |
2.35e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 220 SLTASLQVLTDEEKQLitaQQQEQQSLNWLtrldELQQEASRRQQALQQALAEEEKAQPQL-AALSLAQPARNLRPHWER 298
Cdd:PRK04863 311 EMARELAELNEAESDL---EQDYQAASDHL----NLVQTALRQQEKIERYQADLEELEERLeEQNEVVEEADEQQEENEA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 299 IAEHS--------TALAHTRQQIEEVNTR-LQSTMALRASIRHHAAKQSAELQQQqqSLNAWLQEhdrFRQWNNELAGWR 369
Cdd:PRK04863 384 RAEAAeeevdelkSQLADYQQALDVQQTRaIQYQQAVQALERAKQLCGLPDLTAD--NAEDWLEE---FQAKEQEATEEL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 370 AQFSQQTSDREHLRQwqqQLTHAEQKLNALAAITLTLTADEVA-SALAQHAEQRPLRQRLVALHGQIVPQQKRLAQlqva 448
Cdd:PRK04863 459 LSLEQKLSVAQAAHS---QFEQAYQLVRKIAGEVSRSEAWDVArELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ---- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 449 iqnvtleqtQRNAalNEMRHRYKEKTQQladvkticeQETRIKTLEAQRAQLQAgqpcplcgstshpaveayqalepgvn 528
Cdd:PRK04863 532 ---------QQRA--ERLLAEFCKRLGK---------NLDDEDELEQLQEELEA-------------------------- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 529 qaRLLTLEKEVKKLGEEVATLRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLnitLQPQDDIQpWLDAQDEH 608
Cdd:PRK04863 566 --RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEF---EDSQDVTE-YMQQLLER 639
|
410 420
....*....|....*....|..
gi 446621521 609 ERQLR-----LLSQRHELQGQI 625
Cdd:PRK04863 640 ERELTverdeLAARKQALDEEI 661
|
|
| 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 446621521 1 MKILSLRLKNLNSLKgEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAI 50
Cdd:pfam13175 1 MKIKSIIIKNFRCLK-DTEIDL------DEDLTVLIGKNNSGKSSILEAL 43
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-626 |
2.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 167 KERAELLEELTgtEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTpEQVQSLTASLQV-LTDEEKQLITAQQQEQQS 245
Cdd:COG4913 316 ARLDALREELD--ELEAQIRGNGGDRLEQLEREIERLERELEERERRR-ARLEALLAALGLpLPASAEEFAALRAEAAAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 246 LN-WLTRLDELQQEASRRQQALQQALAEEEKAQPQLAAL-----SLAQPARNLR-------------------------- 293
Cdd:COG4913 393 LEaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLerrksNIPARLLALRdalaealgldeaelpfvgelievrpe 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 294 -PHWERIAE---HSTAL------AHTRQQIEEVNTRlqstmALRASIRHHAAKQSAELQQQQQSLNAWL------QEHDr 357
Cdd:COG4913 473 eERWRGAIErvlGGFALtllvppEHYAAALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDPDSLagkldfKPHP- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 358 FRQWNNELAGWRAQFSQQTSdrehlrqwQQQLTHAEQklnalaAITLT-LTADEvaSALAQHAEQRPLRQRLV----ALH 432
Cdd:COG4913 547 FRAWLEAELGRRFDYVCVDS--------PEELRRHPR------AITRAgQVKGN--GTRHEKDDRRRIRSRYVlgfdNRA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 433 gQIVPQQKRLAQLQVAIQnvtlEQTQRNAALNEMRHRYKEKTQQLADVKTICEQETRIKTLEAQRAQLQagqpcplcgst 512
Cdd:COG4913 611 -KLAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE----------- 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 513 shpavEAYQALEPGvnQARLLTLEKEVKKLGEEVATLRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITL 592
Cdd:COG4913 675 -----AELERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
490 500 510
....*....|....*....|....*....|....*.
gi 446621521 593 QPQDDIQPWLDAQDEHERQLR--LLSQRHELQGQIA 626
Cdd:COG4913 748 RALLEERFAAALGDAVERELRenLEERIDALRARLN 783
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
424-588 |
3.33e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 424 LRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLADVKTICEQETRIKTLEAQRAQLQag 503
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRIS-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 504 qpcplcgstshpaVEAYQALEpgvNQARLLTLEKEVKKLGEEVATLRGQLDALTKQLQRDENEaqsLRQDEQALTQQWQA 583
Cdd:COG1579 107 -------------DLEDEILE---LMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREE 167
|
....*
gi 446621521 584 VTASL 588
Cdd:COG1579 168 LAAKI 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
949-1039 |
3.88e-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: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 949 TLSGGESFLVSLALALALSDLVShkTRIDSLFLDEGFGTLDSETLDTAL-DALDALNA-SGKTIGVISHVEAMKERIPVQ 1026
Cdd:cd03240 115 RCSGGEKVLASLIIRLALAETFG--SNCGILALDEPTTNLDEENIEESLaEIIEERKSqKNFQLIVITHDEELVDAADHI 192
|
90
....*....|...
gi 446621521 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 |
5.83e-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: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 3 ILSLRLKNlNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALyhetprlsnVSQSQNDLMTRDTAECLAE 82
Cdd:cd03241 1 LLELSIKN-FALIEELELDFEE------GLTVLTGETGAGKSILLDALSLLL---------GGRASADLIRSGAEKAVVE 64
|
....*...
gi 446621521 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 27 FASNGLFAITGPTGAGKTTLLDAI-CLALYHETPR---LSNVSQSQNDLMTRDTA-----ECLAEvEFEVkgEAYRAFWS 97
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTTSgqiLFNGQPRKPDQFQKCVAyvrqdDILLP-GLTV--RETLTYTA 106
|
90 100 110
....*....|....*....|....*....|....*.
gi 446621521 98 QNRARN-QPDGNLQ--VPRVELARCADGKILADKVK 130
Cdd:cd03234 107 ILRLPRkSSDAIRKkrVEDVLLRDLALTRIGGNLVK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
191-560 |
8.99e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWLTRLDELQQEASRRQQALQQAL 270
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 271 -------------AEEEKAQPQLAALSLAQPARNLRPHWERIAEHSTALA----------HTRQQIEEVNTRLQSTMALR 327
Cdd:COG1196 522 lagavavligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpldkIRARAALAAALARGAIGAAV 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 328 ASIRHHAAKQSAELQQQQQSLNAWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALAAITLTLT 407
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 408 ADEVASALAQHAEQ-----RPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTLEQTQRNAALNEMRHRYKEKTQQLADVKT 482
Cdd:COG1196 682 EELAERLAEEELELeeallAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621521 483 ICEQETRIKTLEAQRAQLQAGQPCplcgstshpAVEAYQALEpgvnqARLLTLEKEVKKLGEEVATLRG---QLDALTKQ 559
Cdd:COG1196 762 LEELERELERLEREIEALGPVNLL---------AIEEYEELE-----ERYDFLSEQREDLEEARETLEEaieEIDRETRE 827
|
.
gi 446621521 560 L 560
Cdd:COG1196 828 R 828
|
|
| |
