|
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: 1574.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 1 MKILSLRLKNLNSLKGEWKIDFTREPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:PRK10246 1 MKILSLRLKNLNSLKGEWKIDFTAEPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLNNVSQSQNDLMTRDTAECL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:PRK10246 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQAPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
Cdd:PRK10246 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSAALAHTRQQIEEVNTRL 320
Cdd:PRK10246 241 QQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 321 QSTMALRASIRHHAAKQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALA 400
Cdd:PRK10246 321 QSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 401 AITLTLTADEVATALAQHAEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV 480
Cdd:PRK10246 401 AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 481 KTICEQEARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLLALENEVKKLGEEGAALRGQLDALTKQL 560
Cdd:PRK10246 481 KTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 561 QRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
Cdd:PRK10246 561 QRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 641 QRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRIQQLTPILETLPQSDDLPHSEETVALDNWR 720
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 721 QVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLV 800
Cdd:PRK10246 721 QVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLV 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 801 TQTAETLAQHQQHRPDGLALTVTVEQIQQELAQTHQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQVEDWG 880
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVEDWG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKASEALEVEVVDTWQADAVRDTRTLSGGESFLVSL 960
Cdd:PRK10246 881 YLNSLIGSKEGDKFRKFAQGLTLDNLVWLANQQLTRLHGRYLLQRKASEALELEVVDTWQADAVRDTRTLSGGESFLVSL 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
Cdd:PRK10246 961 ALALALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKINGLGYSKL 1040
|
....*..
gi 446621561 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: 1004.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 1 MKILSLRLKNLNSLKGEWKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECL 80
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFTALG----PIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAA 160
Cdd:TIGR00618 77 AELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 161 FLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQ 240
Cdd:TIGR00618 157 FLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 241 QEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSAALAHTRQQIEEVNTRL 320
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 321 QSTMALRASIRHH---AAKQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLN 397
Cdd:TIGR00618 317 QSKMRSRAKLLMKraaHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 398 ALAAITLTLTAdEVATALAQHAEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL 477
Cdd:TIGR00618 397 SLCKELDILQR-EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 478 ADVKTICEQEARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLLALENEVKKLGEEGAALRGQLDALT 557
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 558 KQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAAHNQQIIQYQQ 637
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 638 QIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRIQQLTPILETLPQSDDLPHSEETVALD 717
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 718 NWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQ 797
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 798 TLVTQTAETLAQHQQHRP-DGLALTVTVEQIQQELAQTHQKLRENTTSQGEIRQQLKQDADNRQQQQTLMQQIAQMTQQV 876
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPsDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 877 EDWGYLNSLIGSKEGDKFRKFAQGLTLDNLVHLANQQLTRLHGRYLLQRKAS--EALEVEVVDTWQADAVRDTRTLSGGE 954
Cdd:TIGR00618 876 DKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNArkYQGLALLVADAYTGSVRPSATLSGGE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 955 SFLVSLALA--LALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKERIPVQIKVKKI 1032
Cdd:TIGR00618 956 TFLASLSLAlaLADLLSTSGGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKT 1035
|
....*..
gi 446621561 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 446621561 2 KILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRlsnVSQSQNDLMTRDTAECLA 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDD------GLNLIVGPNGAGKSTILEAIRYALYGKARS---RSKLRSDLINVGSEEASV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 82 EVEFEVKGEAYRAFWsqnrarnqpdgnlqvprvelarcadgkiladkvkdkleltatltgldygrftrsmllSQGQFAAF 161
Cdd:COG0419 72 ELEFEHGGKRYRIER---------------------------------------------------------RQGEFAEF 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446621561 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 |
3.71e-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: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 1 MKILSLRLKNLNSLKGEWKIDFTrePFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlmtRDTAECL 80
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFT--GLDNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSV---FAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 81 AEV--EFEVKGEAYRAFwsqnRARnqpdgnlqvprvelarcadgkiladkvkdkleltatltGLDYGRFTRSMLLSQGQF 158
Cdd:cd03279 76 AEVsfTFQLGGKKYRVE----RSR--------------------------------------GLDYDQFTRIVLLPQGEF 113
|
....
gi 446621561 159 AAFL 162
Cdd:cd03279 114 DRFL 117
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
945-1031 |
9.61e-24 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 100.42 E-value: 9.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 945 RDTRTLSGGESFLVSLALAL--ALSDLVSHKTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISHVEAMKER 1022
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALalSEVLQNRGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKER 198
|
....*....
gi 446621561 1023 IPVQIKVKK 1031
Cdd:cd03279 199 IPQRLEVIK 207
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-206 |
2.25e-22 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 95.64 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 6 LRLKNLNSLKgEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQN-----DLMTRDTAECL 80
Cdd:pfam13476 1 LTIENFRSFR-DQTIDF------SKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFvkgdiRIGLEGKGKAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 81 AEVEFEVKGEA--YRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLEltatltgldygRFTRSMLLSQGQF 158
Cdd:pfam13476 74 VEITFENNDGRytYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKI-----------ILPLLVFLGQERE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446621561 159 AAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQ 206
Cdd:pfam13476 143 EEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-578 |
8.16e-14 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 76.09 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 1 MKILSLRLKNLNSLKgEWKIDFTrepfasNGLFAITGPTGAGKTTLLDAICLALYHETPrlsnvSQSQNDLMTRDTAECL 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHD-DSEIEFD------TGINIITGKNGAGKSSIVDAIRFALFTDKR-----TEKIEDMIKKGKNNLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 81 AEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRvelarcaDGKILADKVKDKLE-LTATLTGLDYGRFTRSMLLSQGQFA 159
Cdd:PRK01156 69 VELEFRIGGHVYQIRRSIERRGKGSRREAYIKK-------DGSIIAEGFDDTTKyIEKNILGISKDVFLNSIFVGQGEMD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 160 AFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTEL-------EKLQAQASGVALLTpEQVQSLTASLQVLTDEE 232
Cdd:PRK01156 142 SLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEIsnidyleEKLKSSNLELENIK-KQIADDEKSHSITLKEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 233 KQLLTAQQQEQQSLNW----LTRLDELQQEASRRQQALQQA---LAEEEKAQPQLAAL---------SLAQPARN-LRPH 295
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNlksaLNELSSLEDMKNRYESEIKTAesdLSMELEKNNYYKELeerhmkiinDPVYKNRNyINDY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 296 WERIAEhsaaLAHTRQQIEEVNTRLQSTmalrasirHHAAKQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQ 375
Cdd:PRK01156 301 FKYKND----IENKKQILSNIDAEINKY--------HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 376 TSDREHLRQWQQQLTHAEQKLNALAAITLT---LTADEVatalaqhaeqrplrqhlvalhgqivpqQKRLAQLQVAIQNV 452
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKiqeIDPDAI---------------------------KKELNEINVKLQDI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 453 TQEQTQRNAALNEMRQRYKEktqqladvkticeqeariktLEAQRAQLQAGQPCPLCGST-----SHPAVEAYQALEPGV 527
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDE--------------------LSRNMEMLNGQSVCPVCGTTlgeekSNHIINHYNEKKSRL 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 446621561 528 NqSRLLALENEVKKLGEEGAALRGQLDAL-TKQLQRDENEAQSLRQDEQALT 578
Cdd:PRK01156 482 E-EKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLE 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
438-1017 |
7.90e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQEARIKTLEAQRAQLQAGQPCplcgstshpAV 517
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER---------LE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 518 EAYQALEPGVN-QSRLLALENEVKKLGEEGAALRGQLDALT-KQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQ 595
Cdd:COG4717 150 ELEERLEELRElEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 596 DDIQPWLDAQDEhERQLRLLSQRHELQGQIAAHnQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQ 675
Cdd:COG4717 230 EQLENELEAAAL-EERLKEARLLLLIAAALLAL-LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 676 SWQQRQNELTAlqnriQQLTPILETLPQSDDLPHSEETVALDNWRQVHEQCLALHSQQQTLQqqdvlaaqsLQKAQAQFD 755
Cdd:COG4717 308 QALPALEELEE-----EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---------LEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 756 TALQASVFDDQQAFLAALMDEQTLTQLEQLKQNLENQRRQAQTLVTQTAETLAQHQqhrpdglaLTVTVEQIQQELAQTH 835
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--------LEEELEELEEELEELE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 836 QKLRENTTSQGEIRQQLKQ---DADNRQQQQTLMQQIAQMTQQVEDWGYLNslIGSKEGDKFRKFAQGLTLDNLVHLANQ 912
Cdd:COG4717 446 EELEELREELAELEAELEQleeDGELAELLQELEELKAELRELAEEWAALK--LALELLEEAREEYREERLPPVLERASE 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 913 QLTRL-HGRYLLQRkASEALEVEVVDtwQADAVRDTRTLSGGE----------SFLVslalalalsdlvSHKTRIDSLFL 981
Cdd:COG4717 524 YFSRLtDGRYRLIR-IDEDLSLKVDT--EDGRTRPVEELSRGTreqlylalrlALAE------------LLAGEPLPLIL 588
|
570 580 590
....*....|....*....|....*....|....*.
gi 446621561 982 DEGFGTLDSETLDTALDALDALNASGKTIGVISHVE 1017
Cdd:COG4717 589 DDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEE 624
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-481 |
2.53e-12 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 70.81 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 6 LRLKNLNSLKGEWkIDFTREPFASNglfAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDtaeCLAEVEF 85
Cdd:PHA02562 7 IRYKNILSVGNQP-IEIQLDKVKKT---LITGKNGAGKSTMLEALTFALFGKPFRDIKKGQLINSINKKD---LLVELWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 86 EVKGEAYRAFwsqnRArnqpdgnlQVPRVELARCaDGKILADK--VKDKLELTATLTGLDYGRFTRSMLLSQGQFAAFLN 163
Cdd:PHA02562 80 EYGEKEYYIK----RG--------IKPNVFEIYC-NGKLLDESasSKDFQKYFEQMLGMNYKSFKQIVVLGTAGYVPFMQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 164 AKPKERAELLEELTGTEIygqISAMvfeqhksarTELEKlqaqasgvalltpEQVQSLTASLQVLtDEEKQLLTAQQQEQ 243
Cdd:PHA02562 147 LSAPARRKLVEDLLDISV---LSEM---------DKLNK-------------DKIRELNQQIQTL-DMKIDHIQQQIKTY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 244 QslNWLTRLDELQQEASRRQQALQQALAEEEKaqpqlaalslaqparnlrphweriaEHSAALAHTRQQIEEVNTRLQST 323
Cdd:PHA02562 201 N--KNIEEQRKKNGENIARKQNKYDELVEEAK-------------------------TIKAEIEELTDELLNLVMDIEDP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 324 MALRASIRHHAAKQSAELQqqqqslnTWLQEHDRFRQwNNELAGWRAQFSQQ----TSDREHLRQWQQQLTHAEQKLNAL 399
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIE-------QFQKVIKMYEK-GGVCPTCTQQISEGpdriTKIKDKLKELQHSLEKLDTAIDEL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 400 AAItltltADEVATalaQHAEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD 479
Cdd:PHA02562 326 EEI-----MDEFNE---QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
..
gi 446621561 480 VK 481
Cdd:PHA02562 398 LV 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-572 |
5.15e-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: 67.00 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 154 SQGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVAlltpEQVQSLTAslQVLTDEEK 233
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELE----RQLKSLER--QAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 234 QLLTAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSlaqparnlrphwERIAEHSAALAHTRQQI 313
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE------------EKLEELRLEVSELEEEI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 314 EEVNTRLQSTMA----LRASIRHHAAKQsAELQQQQQSLNTWLQEHDRFRQ-WNNELAGWRAQFSQQTSDREHLRqwqQQ 388
Cdd:TIGR02168 284 EELQKELYALANeisrLEQQKQILRERL-ANLERQLEELEAQLEELESKLDeLAEELAELEEKLEELKEELESLE---AE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 389 LTHAEQKLNALAAITLTLTA--DEVATALAQhaeqrpLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEM 466
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEqlETLRSKVAQ------LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 467 RQRykektqqladvkticEQEARIKTLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVnQSRLLALENEVKKLGEEG 546
Cdd:TIGR02168 434 ELK---------------ELQAELEELEEELEELQE-------------ELERLEEALEEL-REELEEAEQALDAAEREL 484
|
410 420
....*....|....*....|....*.
gi 446621561 547 AALRGQLDALTKQLQRDENEAQSLRQ 572
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-840 |
6.33e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 154 SQGQFAAFLNAKPKERAELLEE-----------------LTGTE--------IYGQIsamvfeqhksaRTELEKLQAQAS 208
Cdd:COG1196 142 GQGMIDRIIEAKPEERRAIIEEaagiskykerkeeaerkLEATEenlerledILGEL-----------ERQLEPLERQAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 209 gVAlltpEQVQSLTASLQVLtdeEKQLLTAQQQEQQSlnwltRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQP 288
Cdd:COG1196 211 -KA----ERYRELKEELKEL---EAELLLLKLRELEA-----ELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 289 ARNlrphwERIAEHSAALAHTRQQIEevntRLQSTMALRASIRHHAAKQSAELQQQQQSLNTWLQEHDRfrqwnnELAGW 368
Cdd:COG1196 278 ELE-----LELEEAQAEEYELLAELA----RLEQDIARLEERRRELEERLEELEEELAELEEELEELEE------ELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 369 RAQFSQQTSDREHLRQWQQQLTHAEQKLNALAAITLTLTADEVATALAQHAEQRPLRQHLVALHGQIVPQQKRLAQLQVA 448
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 449 IQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTicEQEARIKTLEAQRAQLQAGQpcplcgstshpavEAYQALEPGVN 528
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEE--EEEALLELLAELLEEAALLE-------------AALAELLEELA 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 529 QSRLLALENEVKKLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALtqqWQAVTASLNITLQPQDdiqpwLDAQDEH 608
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY---EAALEAALAAALQNIV-----VEDDEVA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 609 ERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQ 688
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 689 NRIQQLTpILETLPQSDDLPHSEETVALDNwrqvheqclALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQA 768
Cdd:COG1196 640 VTLAGRL-REVTLEGEGGSAGGSLTGGSRR---------ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621561 769 FLAALMDEQTLTQLEQLKQNLENQRRQAQTLVTQTAETLAQHQQHRPDGLAltvTVEQIQQELAQTHQKLRE 840
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP---DLEELERELERLEREIEA 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-579 |
2.86e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 1 MKILSLRLKNLNSLKgewKIDFTREPfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlsnVSQSQNDLMTRDTAECL 80
Cdd:PRK02224 1 MRFDRVRLENFKCYA---DADLRLED----GVTVIHGVNGSGKSSLLEACFFALYGSKA----LDDTLDDVITIGAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 81 AEVEFEVKGEAYRAfwsQNRARNQPDgnlqvpRVELARC--ADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQF 158
Cdd:PRK02224 70 IELWFEHAGGEYHI---ERRVRLSGD------RATTAKCvlETPEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 159 AAFLNAKPKERAELLEELTgteiygQISA--MVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTAslqvlTDEEKQLL 236
Cdd:PRK02224 141 NKLINATPSDRQDMIDDLL------QLGKleEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEE-----KDLHERLN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 237 TAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAalSLAQPARNLRphwERIAEHSAALAHTRQQIEEV 316
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE--TLEAEIEDLR---ETIAETEREREELAEEVRDL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 317 NTRLQSTMALRASIRHHAAKQSAELQQQQQSLNTWLQEHDRFRQwnnELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKL 396
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 397 NALAAiTLTLTADEVATALAQHAEQrplrqhLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQ 476
Cdd:PRK02224 362 REEAA-ELESELEEAREAVEDRREE------IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 477 LadvkticeQEARiKTLEAQRAQLQAGQpCPLCGstshpaveayQALEPGVNQSRLLALENEVKKLGEEGAALRGQLDAL 556
Cdd:PRK02224 435 L--------RTAR-ERVEEAEALLEAGK-CPECG----------QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEV 494
|
570 580
....*....|....*....|....*....
gi 446621561 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 446621561 3 ILSLRLKNLNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDlMTRDTAEcLAE 82
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFS------PLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPK-LIREGEV-RAQ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446621561 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]; |
169-384 |
2.12e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 169 RAELLEEltgTEIYGQISAMV--FEQHKSARTELEKLQAQasgVALLTP-----EQVQSLTASLQVLtDEEKQLLTAQQQ 241
Cdd:COG4913 214 REYMLEE---PDTFEAADALVehFDDLERAHEALEDAREQ---IELLEPirelaERYAAARERLAEL-EYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 242 EQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRphweRIAEHSAALAHTRQQIEEVNTRLQ 321
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD----RLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446621561 322 STMALRASIRHHAAKQSAELQQQQQSLNTWLQEHDRFRQW-NNELAGWRAQFSQQTSDREHLRQ 384
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAlEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-505 |
2.90e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 3 ILSLRLKNLNSLKGEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHET------PRLSN-VSQSQNDlmtRD 75
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPF------SKGFTVISGPNGSGKSNIGDAILFALGLSSskamraERLSDlISNGKNG---QS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 76 TAECLAEVEFEVKGEAYRAFWS-QNRARNQPDGNLQVPRVELARCADGKILAdkvkdklELTATltGLDYGRFTRSMlls 154
Cdd:TIGR02169 73 GNEAYVTVTFKNDDGKFPDELEvVRRLKVTDDGKYSYYYLNGQRVRLSEIHD-------FLAAA--GIYPEGYNVVL--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 155 QGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGV------------------ALLTPE 216
Cdd:TIGR02169 141 QGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKrqqlerlrrerekaeryqALLKEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 217 QVQSLTASLQVLTDEEKQL------LTAQQQEQQSLNwlTRLDELQQEASRRQQALQQ------ALAEEE---------- 274
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKeaierqLASLEEELEKLT--EEISELEKRLEEIEQLLEElnkkikDLGEEEqlrvkekige 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 275 -KAQPQLAALSLAQPARNLRPHWERIAEHSAALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQQSLNtwlQ 353
Cdd:TIGR02169 299 lEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE---E 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 354 EHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLnalaaitltltadevatalaqHAEQRPLRQHLVALHG 433
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL---------------------SEELADLNAAIAGIEA 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446621561 434 QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICEQEARIKTLEAQRAQLQAGQP 505
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVR 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-841 |
4.76e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 190 FEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQ-EQQSLNWLTRLDELQQEASRRQQALQQ 268
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 269 ALAEEEKAQPQLAALSLAQPARNLRPH--WERIAEHSAALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQQ 346
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 347 SL-NTWLQEHD-RFRQWNNELAGWRAQFS----QQTSDREHLRQWQQQLTHAEQKLNALAAITLTL--------TADEVA 412
Cdd:TIGR02168 429 KLeEAELKELQaELEELEEELEELQEELErleeALEELREELEEAEQALDAAERELAQLQARLDSLerlqenleGFSEGV 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 413 TALAQHAEQRPLRQHLVAlhGQIVPQQKRLAQLQVA----IQNVTQE-QTQRNAALNEMRQRYKEKTQQLAdVKTICEQE 487
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLS--ELISVDEGYEAAIEAAlggrLQAVVVEnLNAAKKAIAFLKQNELGRVTFLP-LDSIKGTE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 488 ARIKTLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGV----------NQSR-------------------------- 531
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddldnalELAKklrpgyrivtldgdlvrpggvitggs 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 532 ------LLALENEVKKLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQavtaslnitlqpqdDIQPWLDAQ 605
Cdd:TIGR02168 666 aktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE--------------ELSRQISAL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 606 DEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEEswLATRQQEAQSWQQR----Q 681
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ--IEQLKEELKALREAldelR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 682 NELTALQNRIQQLTPILETLPQSDDLPHSEETVALDNWRQVHEQCLAL-HSQQQTLQQQDVLAAQsLQKAQAQFDTALQA 760
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaAEIEELEELIEELESE-LEALLNERASLEEA 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 761 svfddqqafLAALMDEQTLTQLEQlkQNLENQRRQAQTLVTQTAETLAQHQQHrpdglaltvtVEQIQQELAQTHQKLRE 840
Cdd:TIGR02168 889 ---------LALLRSELEELSEEL--RELESKRSELRRELEELREKLAQLELR----------LEGLEVRIDNLQERLSE 947
|
.
gi 446621561 841 N 841
Cdd:TIGR02168 948 E 948
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
203-462 |
5.66e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 203 LQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAA 282
Cdd:PRK11281 26 FARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 283 LSlaqpARNLRPHWERIAehSAALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQQQQSLNTWLQehdRFRQWN 362
Cdd:PRK11281 106 LK----DDNDEETRETLS--TLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQ---RLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 363 NELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNalaaiTLTLTADEVATAL--AQH----AEQRPLRQHLVALhgQIV 436
Cdd:PRK11281 177 NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQ-----RKSLEGNTQLQDLlqKQRdyltARIQRLEHQLQLL--QEA 249
|
250 260
....*....|....*....|....*.
gi 446621561 437 PQQKRLAQLQvaiQNVTQEQTQRNAA 462
Cdd:PRK11281 250 INSKRLTLSE---KTVQEAQSQDEAA 272
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-564 |
5.95e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 1 MKILSLRLKNLNSLKgEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALYHETPrlSNVSQSQNDLMTRD-TAEC 79
Cdd:PRK03918 1 MKIEELKIKNFRSHK-SSVVEFDD------GINLIIGQNGSGKSSILEAILVGLYWGHG--SKPKGLKKDDFTRIgGSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 80 LAEVEFEVKGEAYRAFWSQNRArnqpdgnlqvprVELARCADG-KILADKVKDKLELTATLtgLDYGRFTRSMLLSQGQF 158
Cdd:PRK03918 72 EIELKFEKNGRKYRIVRSFNRG------------ESYLKYLDGsEVLEEGDSSVREWVERL--IPYHVFLNAIYIRQGEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 159 AAFLNAKpKERAELLEELTGTEIYGQI---SAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQl 235
Cdd:PRK03918 138 DAILESD-ESREKVVRQILGLDDYENAyknLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 236 ltaqqqeqqslnwLTRLDELQQEASRRQQALQQALAEEEKAQPQLaaLSLAQPARNLRphwERIAEHSAALAHTRQQIEE 315
Cdd:PRK03918 216 -------------LPELREELEKLEKEVKELEELKEEIEELEKEL--ESLEGSKRKLE---EKIRELEERIEELKKEIEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 316 VNTRLQSTMALRASirhhaAKQSAELQQQQQSLNTWLQE-HDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQ 394
Cdd:PRK03918 278 LEEKVKELKELKEK-----AEEYIKLSEFYEEYLDELREiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 395 KLNALaaitltltadevatalaqhaEQRplrqhlVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNaaLNEMRQRYKEKT 474
Cdd:PRK03918 353 RLEEL--------------------EER------HELYEEAKAKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 475 QQLADVKT-ICEQEARIKTLEAQRAQLQ-AGQPCPLCG---STSHPA--VEAYQAlepgvnqsRLLALENEVKKLGEEGA 547
Cdd:PRK03918 405 EEISKITArIGELKKEIKELKKAIEELKkAKGKCPVCGrelTEEHRKelLEEYTA--------ELKRIEKELKEIEEKER 476
|
570
....*....|....*..
gi 446621561 548 ALRGQLDALTKQLQRDE 564
Cdd:PRK03918 477 KLRKELRELEKVLKKES 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-435 |
1.15e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 89 GEAYRAFWSQNRARNQPDGNLQVPRVELARC-ADGKILADKVKdklELTATLTGLdygrftrsmllsQGQFAAFLNAKPK 167
Cdd:TIGR02168 652 GDLVRPGGVITGGSAKTNSSILERRREIEELeEKIEELEEKIA---ELEKALAEL------------RKELEELEEELEQ 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 168 ERAELLE---ELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQL-LTAQQQEQ 243
Cdd:TIGR02168 717 LRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeAQIEQLKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 244 QSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALS-----LAQPARNLRphwERIAEHSAALAHTRQQIEEVNT 318
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrledLEEQIEELS---EDIESLAAEIEELEELIEELES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 319 RLQSTMALRASIRHHAAKQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFsqqtsdREHLRQWQQQLTHAEQKLNA 398
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQERLSE 947
|
330 340 350
....*....|....*....|....*....|....*..
gi 446621561 399 LAAITLtltADEVATALAQHAEQRPLRQHLVALHGQI 435
Cdd:TIGR02168 948 EYSLTL---EEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-697 |
2.19e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 386 QQQLTHAEQKLNALAAiTLTLTADEVATALAQH----AEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNA 461
Cdd:TIGR02168 676 RREIEELEEKIEELEE-KIAELEKALAELRKELeeleEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 462 ALNEMRQRYKEKTQQLADVKT-ICEQEARIKTLEAQRAQLQagqpcplcgstshpavEAYQALEpgvnqSRLLALENEVK 540
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEeLAEAEAEIEELEAQIEQLK----------------EELKALR-----EALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 541 KLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQP----QDDIQPWLDAQDEHERQLRLLS 616
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieelESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 617 ----------------------QRHELQGQIAAHNQQIIQYQQQIEQRQQQLltaLAGYALTLPQEDEEESWLATRQQEA 674
Cdd:TIGR02168 894 seleelseelreleskrselrrELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340
....*....|....*....|...
gi 446621561 675 qswqqrQNELTALQNRIQQLTPI 697
Cdd:TIGR02168 971 ------RRRLKRLENKIKELGPV 987
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-613 |
9.90e-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: 49.73 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 192 QHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDE---------------EKQLLTAQQQEQQSLnwlTRLDELQ 256
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSElreakrmyedkieelEKQLVLANSELTEAR---TERDQFS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 257 QEASRRQQALQQALAEEEKAQPQLAaLSLAQPARnlrpHWERIAEHSAALAHTRQQIEEVNTRLQSTMALRASIRHHAAK 336
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELS-LEKEQNKR----LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 337 QSAELQQQQQSLNTWLQEHDRFRqwnnelagwraqfSQQTSDREHLRQWQQQLTHAEQKLNA----LAAITLTLTADEVA 412
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLT-------------AQLESTKEMLRKVVEELTAKKMTLESsertVSDLTASLQEKERA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 413 TAlAQHAEQRPLR----------QHLV--------------ALHGQIVPQQKRLAQLQVAIQNVTQ-------------- 454
Cdd:pfam15921 512 IE-ATNAEITKLRsrvdlklqelQHLKnegdhlrnvqteceALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqv 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 455 EQTQRNAALNEMRQRYKEkTQQLADVK--TICEQEARIKTLEAQRAQL-------------------QAGQPCPLCGSTS 513
Cdd:pfam15921 591 EKAQLEKEINDRRLELQE-FKILKDKKdaKIRELEARVSDLELEKVKLvnagserlravkdikqerdQLLNEVKTSRNEL 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 514 HPAVEAYQAL-----------EPGVN---------QSRLLALENEVKKL-GEEGAAL-------------RGQLDALTKQ 559
Cdd:pfam15921 670 NSLSEDYEVLkrnfrnkseemETTTNklkmqlksaQSELEQTRNTLKSMeGSDGHAMkvamgmqkqitakRGQIDALQSK 749
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446621561 560 LQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLDAQDEHERQLR 613
Cdd:pfam15921 750 IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLK 803
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
931-1002 |
1.99e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 44.15 E-value: 1.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446621561 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 446621561 26 PFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVS 65
Cdd:pfam13555 18 PIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRARFNKA 57
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
251-455 |
2.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 251 RLDELQQEASRRQQALQQALAEEEKAQPQLAALslaqpaRNLRPHWERIAEHSAA---LAHTRQQIEEVNTRLQstmALR 327
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDAL------QERREALQRLAEYSWDeidVASAEREIAELEAELE---RLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 328 ASirhhaakqSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQtsdrehLRQWQQQLTHAEQKLNALAAITLTLT 407
Cdd:COG4913 682 AS--------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE------LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446621561 408 ADEVATALAQHAEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQE 455
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-485 |
3.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 249 LTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWEriAEHSAALAhtRQQIEEVNTRLQSTMALRA 328
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWF--AQRRLELL--EAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 329 SIRHHAAKQSAELQQQQQSLNTwlQEHDRFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEqklnALAAITLTLTA 408
Cdd:COG4913 313 RLEARLDALREELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL----PASAEEFAALR 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446621561 409 DEVATALAQ-HAEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL-ADVKTICE 485
Cdd:COG4913 387 AEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDeAELPFVGE 465
|
|
| 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 446621561 26 PFASNGLFAITGPTGAGKTTLLDAICLAL 54
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIGLAL 45
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-773 |
6.93e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 225 LQVLTDEEKQLLTAQQQEQQSLNWLTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRphwERIAEHSA 304
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE---AELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 305 ALAHTRQQIEEVNTRLQSTMALRASIRHHAAKQSAELQQqqqslnTWLQEHDRFRQWNNELAGWRAQFSQQtsdREHLRQ 384
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQ------LSLATEEELQDLAEELEELQQRLAEL---EEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 385 WQQQLTHAEQKLNALAAITLTLTADEVATALAQHAEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALN 464
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 465 EMRQRYKEKTQQLADVKTICEQEariktLEAQRAQLQagqpcplcgstshpaveayqaLEPGVNQSRLLALENEVKKLGE 544
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEE-----LEELLAALG---------------------LPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 545 egaaLRGQLDALTKQLQRDENEAQslrqdEQALTQQWQAvtaslnitlqpqDDIQPWLDAQDEHERQLRLLSQRHELQGQ 624
Cdd:COG4717 352 ----LLREAEELEEELQLEELEQE-----IAALLAEAGV------------EDEEELRAALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 625 IAAHnqqiiqyqqqieqrqqqlltalAGYALTLPQEDEEESWLATRQQEAQSWQQRQNELTALQNRIQQLTPILETLpqs 704
Cdd:COG4717 411 LEEL----------------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL--- 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446621561 705 ddlphsEETVALDNWRQVHEQCLALHSQQQTLQQQDVLAAQSLQKAQAQFDTALQASVFDDQQAFLAAL 773
Cdd:COG4717 466 ------EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEYFSRL 528
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-55 |
9.68e-05 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 43.77 E-value: 9.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446621561 1 MKILSLRLKNLNSLKGewkIDFTrepFASNGLFAITGPTGAGKTTLLDAICLALY 55
Cdd:cd00267 2 IENLSFRYGGRTALDN---VSLT---LKAGEIVALVGPNGSGKSTLLRAIAGLLK 50
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
236-499 |
1.62e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 236 LTAQQQEQQSLNwlTRLDELQQEASRRQQALQQALAEEEKAQPQLAALSlaqparnlrphwERIAEHSAALAHTRQQIEE 315
Cdd:COG4942 15 AAAQADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALE------------RRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 316 VNTRLQSTmalrasirhhaAKQSAELQQQQQSLNTWLQEHDRFRQWNNELAGWRAQFSQQT-SDREHLRQWQQQLTHAEQ 394
Cdd:COG4942 81 LEAELAEL-----------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 395 KLnalaAITLTLTADEVATALAQHAEQRplrqhlvalhgqiVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKT 474
Cdd:COG4942 150 EQ----AEELRADLAELAALRAELEAER-------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|....*.
gi 446621561 475 QQLADVKTICEQ-EARIKTLEAQRAQ 499
Cdd:COG4942 213 AELAELQQEAEElEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-580 |
1.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 380 EHLRQWQQQLTHAEQKLNALAAITLTltADEVATALAQHAEQRPLRQHLVALHgqivpQQKRLAQLQVAIQNVTQEQTQR 459
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIREL--AERYAAARERLAELEYLRAALRLWF-----AQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 460 NAALNEMRQRYKEKTQQLADVKTICEQ---------EARIKTLEAQRAQLQAgqpcplcgstshpAVEAYQA------LE 524
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGnggdrleqlEREIERLERELEERER-------------RRARLEAllaalgLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 525 PGVNQSRLLALENEVK----KLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALTQQ 580
Cdd:COG4913 375 LPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
220-504 |
1.70e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 220 SLTASLQVLTDEEKQLltaQQQEQQSLNWLtrldELQQEASRRQQALQQALAEEEKAQPQL-AALSLAQPARnlrphwER 298
Cdd:PRK04863 311 EMARELAELNEAESDL---EQDYQAASDHL----NLVQTALRQQEKIERYQADLEELEERLeEQNEVVEEAD------EQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 299 IAEHSAALAHTRQQIEEVNTRL---------QSTMAlrasIRHHAAKQSAElqqqqqSLNTWLQEHDrFRQWNneLAGWR 369
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSQLadyqqaldvQQTRA----IQYQQAVQALE------RAKQLCGLPD-LTADN--AEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 370 AQFsqqtsdREHLRQWQQQLTHAEQKLN---------ALAAITLTLTADEVATALAQHAEQRPLRQH--LVALHGQIVPQ 438
Cdd:PRK04863 445 EEF------QAKEQEATEELLSLEQKLSvaqaahsqfEQAYQLVRKIAGEVSRSEAWDVARELLRRLreQRHLAEQLQQL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446621561 439 QKRLAQLQvaiQNVTQEQTQrNAALNEMRQRYKEKTQQLADVKTI-CEQEARIKTLEAQRAQLQAGQ 504
Cdd:PRK04863 519 RMRLSELE---QRLRQQQRA-ERLLAEFCKRLGKNLDDEDELEQLqEELEARLESLSESVSEARERR 581
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
318-593 |
1.83e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 318 TRLQSTMALRASIRHHAAKQSAELqqqqqsLNTWLQEhdrFRQWNNELagwRAQFSQQTSD--REHLRQWQQQLTHAEQK 395
Cdd:COG3206 130 EPVKGSNVIEISYTSPDPELAAAV------ANALAEA---YLEQNLEL---RREEARKALEflEEQLPELRKELEEAEAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 396 LNALAAITLTLTADEVATALAQhaeqrplrqhlvalhgqivpqqkRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQ 475
Cdd:COG3206 198 LEEFRQKNGLVDLSEEAKLLLQ-----------------------QLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 476 QLADVK---TICEQEARIKTLEAQRAQLQAGqpcplcGSTSHPAVEAYQALEPGVNQSRLLALENEVKKLGEEGAALRGQ 552
Cdd:COG3206 255 ALPELLqspVIQQLRAQLAELEAELAELSAR------YTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446621561 553 LDALTKQLQRDENEAQSLRQDEQ---ALTQQWQAVTASLNITLQ 593
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAelrRLEREVEVARELYESLLQ 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-627 |
1.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 412 ATALAQHAEQRPLRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICEQEARI 490
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 491 KTLEAQRAQLQA-------------GQPCPLCGSTSHPAVEAYQALE--PGVNQSRlLALENEVKKLGEEGAALRGQLDA 555
Cdd:COG4942 93 AELRAELEAQKEelaellralyrlgRQPPLALLLSPEDFLDAVRRLQylKYLAPAR-REQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621561 556 LTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNitlQPQDDIQPWLDAQDEHERQLRLLSQRHELQGQIAA 627
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| 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 446621561 946 DTRTLSGGESFLVSLalalalsdlvshkTRIDSLFLDegFGTLDSETLDTALDALDALnasgktiGVISHV 1016
Cdd:COG0419 155 PIETLSGGERLRLAL-------------ADLLSLILD--FGSLDEERLERLLDALEEL-------AIITHV 203
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
463-694 |
9.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 463 LNEMRQRYKEKTQQLADVKTICEQEARIKTLEAQRAQLQAGQpcplcgstshpaveayQALEPGVNQSRLLALENEVKKL 542
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLR----------------AALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 543 GEEGAALRGQLDALTKQLQRdeneaqsLRQDEQALTQQWQAvtaslnitlQPQDDIQPWLDAQDEHERQLRLLSQRHE-L 621
Cdd:COG4913 301 RAELARLEAELERLEARLDA-------LREELDELEAQIRG---------NGGDRLEQLEREIERLERELEERERRRArL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446621561 622 QGQIAAhnqqiiqYQQQIEQRQQQLLTALAGYALTLPQEDEEESWLATRQQEA-QSWQQRQNELTALQNRIQQL 694
Cdd:COG4913 365 EALLAA-------LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAeAALRDLRRELRELEAEIASL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-502 |
9.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 289 ARNLRPHWERIAEHSAALAHTRQQIEevntRLQSTMALRAsiRHHAAKQSAELQQQQQSLNTWLQEHDRFRQWNNELAGW 368
Cdd:COG4913 227 ADALVEHFDDLERAHEALEDAREQIE----LLEPIRELAE--RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 369 RAQFSQQtsdREHLRQWQQQLTHAEQKLNALAAITLTLTADEVATALAQHAEQRPLRQHLVALHGQivpQQKRLAQLQVA 448
Cdd:COG4913 301 RAELARL---EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR---LEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446621561 449 IQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTicEQEARIKTLEAQRAQLQA 502
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALA--EAEAALRDLRRELRELEA 426
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
357-587 |
9.78e-04 |
|
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: 43.40 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 357 RFRQWNNELAGWRAQFSQQTSDREHLRQWQQQLTHAEQKLNALAAITLTLTADEVATALAQ-HAEQRPLRQHLVALhGQI 435
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAaQEAQAFIQQHGKAL-AQL 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 436 VPQQKRL-------AQLQVAIQNVTQEQTQRNA---ALNEMRQR-----YKEKTQQLADVKTICEQeARIKTLEAQRAQL 500
Cdd:COG3096 923 EPLVAVLqsdpeqfEQLQADYLQAKEQQRRLKQqifALSEVVQRrphfsYEDAVGLLGENSDLNEK-LRARLEQAEEARR 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 501 QAGQPCPLCGSTSHPAVEAYQALEPG--VNQSRLLALENEVKKLG-------------------EEGAALRGQLDALTKQ 559
Cdd:COG3096 1002 EAREQLRQAQAQYSQYNQVLASLKSSrdAKQQTLQELEQELEELGvqadaeaeerarirrdelhEELSQNRSRRSQLEKQ 1081
|
250 260 270
....*....|....*....|....*....|..
gi 446621561 560 LQRDENEAQSL----RQDEQALTQQWQAVTAS 587
Cdd:COG3096 1082 LTRCEAEMDSLqkrlRKAERDYKQEREQVVQA 1113
|
|
| 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 446621561 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 446621561 24 REPFASNGLFAIT--GPTGAGKTTLLDAICLAL 54
Cdd:COG0378 5 RALFAEKGVLAVNlmGSPGSGKTTLLEKTIRAL 37
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
168-625 |
1.21e-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: 43.02 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 168 ERAELLEELTGT--EIYGQISAMVFEQHKSART--ELEKLQAQASgvalltpeqvqSLTASLQVLTDEEKQLLTAQQQEQ 243
Cdd:COG3096 279 ERRELSERALELrrELFGARRQLAEEQYRLVEMarELEELSARES-----------DLEQDYQAASDHLNLVQTALRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 244 QSLNWLTRLDELQQEAsrRQQALQQALAEEEKAQPQlAALSLAQparnlrphwERIAEHSAALAHTRQQIEEVNTR-LQS 322
Cdd:COG3096 348 KIERYQEDLEELTERL--EEQEEVVEEAAEQLAEAE-ARLEAAE---------EEVDSLKSQLADYQQALDVQQTRaIQY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 323 TMALRASIRHHAAKQSAELQQQqqSLNTWLQEHdrfrqwnnelagwRAQFSQQTsdrEHLRQWQQQLT----HAEQKLNA 398
Cdd:COG3096 416 QQAVQALEKARALCGLPDLTPE--NAEDYLAAF-------------RAKEQQAT---EEVLELEQKLSvadaARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 399 LAAitLTLTADEVATALAQHAEQRPLRQHlvalhgqivPQQKRLAQLQVAIQnvtqeqtqrnAALNEMRQRYkektqqla 478
Cdd:COG3096 478 YEL--VCKIAGEVERSQAWQTARELLRRY---------RSQQALAQRLQQLR----------AQLAELEQRL-------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 479 dvkticEQEARIKTLEAQRAQLQAGQpcplcgSTSHPAVEAYQALEpgvnQSRLLALENEVKKLGEEGAALRGQLDALTK 558
Cdd:COG3096 529 ------RQQQNAERLLEEFCQRIGQQ------LDAAEELEELLAEL----EAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446621561 559 QLQRDENEAQSLRQDEQALTQQWQAVTASLNITLQPQDDIQPWLdaqdEHERQL-----RLLSQRHELQGQI 625
Cdd:COG3096 593 RIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLL----EREREAtverdELAARKQALESQI 660
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-60 |
1.23e-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: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 1 MKILSLRLKNLNSLKGEwKIDFtrepfaSNGLFAITGPTGAGKTTLLDAICLALYHETPR 60
Cdd:COG3593 1 MKLEKIKIKNFRSIKDL-SIEL------SDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| 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 446621561 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 446621561 4 LSLRLKNLNSLKGEWKIDFTRE-------PFASNGLFAITGPTGAGKTTLLDAicLALYHETPRLS 62
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKQllknvsgKAKPGELTAIMGPSGAGKSTLLNA--LAGRRTGLGVS 65
|
|
| 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 446621561 1 MKILSLRLKNLNSLKgEWKIDFtrepfaSNGLFAITGPTGAGKTTLLDAI 50
Cdd:pfam13175 1 MKIKSIIIKNFRCLK-DTEIDL------DEDLTVLIGKNNSGKSSILEAL 43
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
424-588 |
3.19e-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: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 424 LRQHLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQEARIKTLEAQRAQLQAg 503
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 504 qpcplcgsTSHPAVEAYQALEpgvnqsrllALENEVKKLGEEGAALRGQLDALTKQLQRDENEaqsLRQDEQALTQQWQA 583
Cdd:COG1579 108 --------LEDEILELMERIE---------ELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREE 167
|
....*
gi 446621561 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 |
3.80e-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 446621561 949 TLSGGESFLVSLALALALSDLVShkTRIDSLFLDEGFGTLDSETLDTAL-DALDALNA-SGKTIGVISHVEAMKERIPVQ 1026
Cdd:cd03240 115 RCSGGEKVLASLIIRLALAETFG--SNCGILALDEPTTNLDEENIEESLaEIIEERKSqKNFQLIVITHDEELVDAADHI 192
|
90
....*....|...
gi 446621561 1027 IKVKKiNGLGYSK 1039
Cdd:cd03240 193 YRVEK-DGRQKSR 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-626 |
5.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 167 KERAELLEELTgtEIYGQISAMVFEQHKSARTELEKLQAQASGVALLTpEQVQSLTASLQV-LTDEEKQLLTAQQQEQQS 245
Cdd:COG4913 316 ARLDALREELD--ELEAQIRGNGGDRLEQLEREIERLERELEERERRR-ARLEALLAALGLpLPASAEEFAALRAEAAAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 246 LN-WLTRLDELQQEASRRQQALQQALAEEEKAQPQLAAL-----SLAQPARNLR-------------------------- 293
Cdd:COG4913 393 LEaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLerrksNIPARLLALRdalaealgldeaelpfvgelievrpe 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 294 -PHWERIAE---HSAAL------AHTRQQIEEVNTRlqstmALRASIRHHAAKQSAELQQQQQSLNTWL------QEHDr 357
Cdd:COG4913 473 eERWRGAIErvlGGFALtllvppEHYAAALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDPDSLagkldfKPHP- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 358 FRQWNNELAGWRAQFSQQTSdrehlrqwQQQLTHAEQklnalaAITLT-LTADEvaTALAQHAEQRPLRQHLV----ALH 432
Cdd:COG4913 547 FRAWLEAELGRRFDYVCVDS--------PEELRRHPR------AITRAgQVKGN--GTRHEKDDRRRIRSRYVlgfdNRA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 433 gQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYkektQQLADVKTICEQEARIKTLEAQRAQLQagqpcplcgst 512
Cdd:COG4913 611 -KLAALEAELAELEEELAEAEERLEALEAELDALQERR----EALQRLAEYSWDEIDVASAEREIAELE----------- 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 513 shpavEAYQALEPGvnQSRLLALENEVKKLGEEGAALRGQLDALTKQLQRDENEAQSLRQDEQALTQQWQAVTASLNITL 592
Cdd:COG4913 675 -----AELERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
490 500 510
....*....|....*....|....*....|....*.
gi 446621561 593 QPQDDIQPWLDAQDEHERQLR--LLSQRHELQGQIA 626
Cdd:COG4913 748 RALLEERFAAALGDAVERELRenLEERIDALRARLN 783
|
|
| 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 446621561 3 ILSLRLKNlNSLKGEWKIDFTRepfasnGLFAITGPTGAGKTTLLDAICLALyhetprlsnVSQSQNDLMTRDTAECLAE 82
Cdd:cd03241 1 LLELSIKN-FALIEELELDFEE------GLTVLTGETGAGKSILLDALSLLL---------GGRASADLIRSGAEKAVVE 64
|
....*...
gi 446621561 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 |
6.65e-03 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 39.18 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446621561 27 FASNGLFAITGPTGAGKTTLLDAI-CLALYHETPR---LSNVSQSQNDLMTRDTA-----ECLAEvEFEVkgEAYRAFWS 97
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTTSgqiLFNGQPRKPDQFQKCVAyvrqdDILLP-GLTV--RETLTYTA 106
|
90 100 110
....*....|....*....|....*....|....*.
gi 446621561 98 QNRARN-QPDGNLQ--VPRVELARCADGKILADKVK 130
Cdd:cd03234 107 ILRLPRkSSDAIRKkrVEDVLLRDLALTRIGGNLVK 142
|
|
| |
