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Conserved domains on  [gi|1474250368|ref|WP_118656998|]
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MULTISPECIES: excinuclease ABC subunit UvrA [Alistipes]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 11415085)

excinuclease ABC subunit UvrA is a DNA-binding ATPase that recognizes DNA adducts in the nucleotide excision repair process catalyzed by the UvrABC excinuclease repair system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
6-931 0e+00

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


:

Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1558.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   6 EEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITGI 85
Cdd:COG0178     2 MMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  86 APAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPLKTAEG 165
Cdd:COG0178    82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 166 QGLIEKLTLLVKEGLQRLYIDGQSLFIEDIIvqADDYAGRADLRIVVDRAKATDDEEtlSRLGDSVATAFLQGDGVCdvI 245
Cdd:COG0178   162 GEHKELLEELRKQGFVRVRVDGEVYDLDEEP--ELDKNKKHTIEVVVDRLVVKEDIR--SRLADSVETALKLGDGLV--I 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 246 VQQADGDRVESFSSRFEL--DGIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDEDLVVPDKNKSIYQDAIACWRGETM 323
Cdd:COG0178   236 VEVVDEGEELLFSEKFACpdCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 324 KWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGNEF------------------FHGLDEFFKFLEGERYKIQYRVM 385
Cdd:COG0178   316 SYYFQLLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEkikfryknrgrrrtyekpFEGVIPFLERRYRETYSEHVREE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 386 LSRYTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLEYLNEVGLG 465
Cdd:COG0178   396 LSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLD 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 466 YLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADT 545
Cdd:COG0178   476 YLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADY 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 546 IIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWNS-YVDVIGARENNLKGIDVKFPLGVMTC 624
Cdd:COG0178   556 IIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGkFLTIKGARENNLKNVDVEIPLGVLTC 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 625 VTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYDDIRKLFAD 704
Cdd:COG0178   636 VTGVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEG-LEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQ 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 705 QPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAV 784
Cdd:COG0178   715 TPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAL 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 785 DLFAAYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTTGLHFHDIR 864
Cdd:COG0178   795 EFFENI-------PKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKR-STGKTLYILDEPTTGLHFHDIR 866
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 865 KLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:COG0178   867 KLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYL 933
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
6-931 0e+00

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1558.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   6 EEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITGI 85
Cdd:COG0178     2 MMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  86 APAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPLKTAEG 165
Cdd:COG0178    82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 166 QGLIEKLTLLVKEGLQRLYIDGQSLFIEDIIvqADDYAGRADLRIVVDRAKATDDEEtlSRLGDSVATAFLQGDGVCdvI 245
Cdd:COG0178   162 GEHKELLEELRKQGFVRVRVDGEVYDLDEEP--ELDKNKKHTIEVVVDRLVVKEDIR--SRLADSVETALKLGDGLV--I 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 246 VQQADGDRVESFSSRFEL--DGIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDEDLVVPDKNKSIYQDAIACWRGETM 323
Cdd:COG0178   236 VEVVDEGEELLFSEKFACpdCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 324 KWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGNEF------------------FHGLDEFFKFLEGERYKIQYRVM 385
Cdd:COG0178   316 SYYFQLLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEkikfryknrgrrrtyekpFEGVIPFLERRYRETYSEHVREE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 386 LSRYTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLEYLNEVGLG 465
Cdd:COG0178   396 LSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLD 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 466 YLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADT 545
Cdd:COG0178   476 YLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADY 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 546 IIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWNS-YVDVIGARENNLKGIDVKFPLGVMTC 624
Cdd:COG0178   556 IIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGkFLTIKGARENNLKNVDVEIPLGVLTC 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 625 VTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYDDIRKLFAD 704
Cdd:COG0178   636 VTGVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEG-LEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQ 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 705 QPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAV 784
Cdd:COG0178   715 TPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAL 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 785 DLFAAYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTTGLHFHDIR 864
Cdd:COG0178   795 EFFENI-------PKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKR-STGKTLYILDEPTTGLHFHDIR 866
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 865 KLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:COG0178   867 KLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYL 933
uvrA PRK00349
excinuclease ABC subunit UvrA;
5-931 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1227.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   5 KEEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITG 84
Cdd:PRK00349    1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  85 IAPAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPL---K 161
Cdd:PRK00349   81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVvrgR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 162 TAEGQGLIEKLTllvKEGLQRLYIDGQSLFIEDIIVQADDYagRADLRIVVDRAKATDDEEtlSRLGDSVATAFLQGDGV 241
Cdd:PRK00349  161 KGEHKKLLENLR---KQGFVRVRVDGEVYDLDEPPKLDKNK--KHTIEVVVDRLVVKEDIR--QRLADSIETALKLSDGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 242 cdVIVQQADGDRVES--FSSRFE--LDGIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDEDLVVPDKNKSIYQDAIAC 317
Cdd:PRK00349  234 --VVVEVMDDPEAEEllFSEKFAcpVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 318 WRGETMKWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGN-----EFFH-----GLDEFFKFLEG------ERYK-- 379
Cdd:PRK00349  312 WSRSSSSYYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgdeeiEFRYkndrgRTRERKHPFEGvipnleRRYRet 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 380 --IQYRVMLSRYTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLE 457
Cdd:PRK00349  392 esEYVREELEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 458 YLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEE 537
Cdd:PRK00349  472 FLVDVGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDE 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 538 EIIRAADTIIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWNS-YVDVIGARENNLKGIDVK 616
Cdd:PRK00349  552 DTIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGkFLKLKGARENNLKNVDVE 631
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 617 FPLGVMTCVTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYD 696
Cdd:PRK00349  632 IPLGKFTCVTGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEG-LEHLDKVIDIDQSPIGRTPRSNPATYTGVFD 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 697 DIRKLFADQPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDIL 776
Cdd:PRK00349  711 PIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVL 790
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 777 ELTVDAAVDLFAAYQdkdainkKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTT 856
Cdd:PRK00349  791 DMTVEEALEFFEAIP-------KIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKR-STGKTLYILDEPTT 862
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 857 GLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:PRK00349  863 GLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
10-919 0e+00

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. 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: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 1094.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  10 IHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITGIAPAI 89
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  90 AIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPL---KTAEGQ 166
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIvrgRKGEFR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 167 GLIEKLTllvKEGLQRLYIDGQSLFIEDIIVQadDYAGRADLRIVVDRAKATddEETLSRLGDSVATAFLQGDGVCDVIV 246
Cdd:TIGR00630 162 KLLEKLR---KQGFARVRVDGEVYPLEDPPKL--EKNKKHTIDVVIDRLTVK--NENRSRLAESVETALRLGDGLLEVEF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 247 QQ---ADGDRVESFSSRFELD--GIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDEDLVVPDKNKSIYQDAIACWRGE 321
Cdd:TIGR00630 235 DDdeeVAESKEELFSEKFACPecGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKS 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 322 TMKWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGNEF-FHGLDEFFKFLEGERYKIQY------------------ 382
Cdd:TIGR00630 315 TTSYYRQMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEeVIVVKYRNGGGETFRYHKPFegvipelerryleteses 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 383 -RVMLSRYTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLEYLNE 461
Cdd:TIGR00630 395 mREYLEKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLID 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 462 VGLGYLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIR 541
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 542 AADTIIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWN-SYVDVIGARENNLKGIDVKFPLG 620
Cdd:TIGR00630 555 AADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNgKFLTLKGARENNLKNITVSIPLG 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 621 VMTCVTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYDDIRK 700
Cdd:TIGR00630 635 LFTCITGVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEG-LEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRE 713
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 701 LFADQPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTV 780
Cdd:TIGR00630 714 LFAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTV 793
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 781 DAAVDLFAAYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTTGLHF 860
Cdd:TIGR00630 794 EEAYEFFEAV-------PSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKR-STGRTLYILDEPTTGLHF 865
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 861 HDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADL 919
Cdd:TIGR00630 866 DDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEV 924
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
602-916 3.27e-124

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 376.95  E-value: 3.27e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 602 VIGARENNLKGIDVKFPLGVMTCVTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIG 681
Cdd:cd03271     3 LKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEG-LEHIDKVIVIDQSPIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 682 KSLRSNPVTYLKAYDDIRKLFadqpyakhngltpshfsfnmaggrceecqgegvikvgmqfmadvelvCESCGGKRFKDE 761
Cdd:cd03271    82 RTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNRE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 762 VLEVKYHGHSIYDILELTVDAAVDLFAAYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKE 841
Cdd:cd03271   115 TLEVRYKGKSIADVLDMTVEEALEFFENI-------PKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKR 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 842 nAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTP 916
Cdd:cd03271   188 -STGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
137-248 4.02e-17

UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 77.91  E-value: 4.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 137 TVADVVNYIAALPSGTRVLVAAPLKTAEGQGLIEKLTLLVKEGLQRLYIDGQSLFIEDIIvQADDYAgRADLRIVVDRAK 216
Cdd:pfam17760   2 TVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEP-KLDKNK-KHTIEVVVDRLV 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1474250368 217 ATDDEEtlSRLGDSVATAFLQGDGVCDVIVQQ 248
Cdd:pfam17760  80 VKEDNR--SRLADSVETALKLGKGLVIVLVLD 109
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
471-571 3.85e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.49  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 471 RLSSTLSGGESQRINLAtslgSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEHEEEIIRAAD--T 545
Cdd:NF000106  140 RAAAKYSGGMRRRLDLA----ASMIGrpAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHelT 215
                          90       100
                  ....*....|....*....|....*.
gi 1474250368 546 IIDigplagyqGGEVMFQGGIDRLAS 571
Cdd:NF000106  216 VID--------RGRVIADGKVDELKT 233
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
6-931 0e+00

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1558.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   6 EEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITGI 85
Cdd:COG0178     2 MMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  86 APAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPLKTAEG 165
Cdd:COG0178    82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 166 QGLIEKLTLLVKEGLQRLYIDGQSLFIEDIIvqADDYAGRADLRIVVDRAKATDDEEtlSRLGDSVATAFLQGDGVCdvI 245
Cdd:COG0178   162 GEHKELLEELRKQGFVRVRVDGEVYDLDEEP--ELDKNKKHTIEVVVDRLVVKEDIR--SRLADSVETALKLGDGLV--I 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 246 VQQADGDRVESFSSRFEL--DGIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDEDLVVPDKNKSIYQDAIACWRGETM 323
Cdd:COG0178   236 VEVVDEGEELLFSEKFACpdCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 324 KWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGNEF------------------FHGLDEFFKFLEGERYKIQYRVM 385
Cdd:COG0178   316 SYYFQLLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEkikfryknrgrrrtyekpFEGVIPFLERRYRETYSEHVREE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 386 LSRYTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLEYLNEVGLG 465
Cdd:COG0178   396 LSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLD 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 466 YLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADT 545
Cdd:COG0178   476 YLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADY 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 546 IIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWNS-YVDVIGARENNLKGIDVKFPLGVMTC 624
Cdd:COG0178   556 IIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGkFLTIKGARENNLKNVDVEIPLGVLTC 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 625 VTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYDDIRKLFAD 704
Cdd:COG0178   636 VTGVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEG-LEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQ 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 705 QPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAV 784
Cdd:COG0178   715 TPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAL 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 785 DLFAAYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTTGLHFHDIR 864
Cdd:COG0178   795 EFFENI-------PKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKR-STGKTLYILDEPTTGLHFHDIR 866
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 865 KLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:COG0178   867 KLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYL 933
uvrA PRK00349
excinuclease ABC subunit UvrA;
5-931 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1227.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   5 KEEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITG 84
Cdd:PRK00349    1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  85 IAPAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPL---K 161
Cdd:PRK00349   81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVvrgR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 162 TAEGQGLIEKLTllvKEGLQRLYIDGQSLFIEDIIVQADDYagRADLRIVVDRAKATDDEEtlSRLGDSVATAFLQGDGV 241
Cdd:PRK00349  161 KGEHKKLLENLR---KQGFVRVRVDGEVYDLDEPPKLDKNK--KHTIEVVVDRLVVKEDIR--QRLADSIETALKLSDGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 242 cdVIVQQADGDRVES--FSSRFE--LDGIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDEDLVVPDKNKSIYQDAIAC 317
Cdd:PRK00349  234 --VVVEVMDDPEAEEllFSEKFAcpVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 318 WRGETMKWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGN-----EFFH-----GLDEFFKFLEG------ERYK-- 379
Cdd:PRK00349  312 WSRSSSSYYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgdeeiEFRYkndrgRTRERKHPFEGvipnleRRYRet 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 380 --IQYRVMLSRYTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLE 457
Cdd:PRK00349  392 esEYVREELEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 458 YLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEE 537
Cdd:PRK00349  472 FLVDVGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDE 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 538 EIIRAADTIIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWNS-YVDVIGARENNLKGIDVK 616
Cdd:PRK00349  552 DTIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGkFLKLKGARENNLKNVDVE 631
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 617 FPLGVMTCVTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYD 696
Cdd:PRK00349  632 IPLGKFTCVTGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEG-LEHLDKVIDIDQSPIGRTPRSNPATYTGVFD 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 697 DIRKLFADQPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDIL 776
Cdd:PRK00349  711 PIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVL 790
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 777 ELTVDAAVDLFAAYQdkdainkKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTT 856
Cdd:PRK00349  791 DMTVEEALEFFEAIP-------KIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKR-STGKTLYILDEPTT 862
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 857 GLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:PRK00349  863 GLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
10-919 0e+00

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. 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: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 1094.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  10 IHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITGIAPAI 89
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  90 AIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPL---KTAEGQ 166
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIvrgRKGEFR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 167 GLIEKLTllvKEGLQRLYIDGQSLFIEDIIVQadDYAGRADLRIVVDRAKATddEETLSRLGDSVATAFLQGDGVCDVIV 246
Cdd:TIGR00630 162 KLLEKLR---KQGFARVRVDGEVYPLEDPPKL--EKNKKHTIDVVIDRLTVK--NENRSRLAESVETALRLGDGLLEVEF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 247 QQ---ADGDRVESFSSRFELD--GIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDEDLVVPDKNKSIYQDAIACWRGE 321
Cdd:TIGR00630 235 DDdeeVAESKEELFSEKFACPecGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKS 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 322 TMKWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGNEF-FHGLDEFFKFLEGERYKIQY------------------ 382
Cdd:TIGR00630 315 TTSYYRQMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEeVIVVKYRNGGGETFRYHKPFegvipelerryleteses 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 383 -RVMLSRYTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLEYLNE 461
Cdd:TIGR00630 395 mREYLEKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLID 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 462 VGLGYLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIR 541
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 542 AADTIIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWN-SYVDVIGARENNLKGIDVKFPLG 620
Cdd:TIGR00630 555 AADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNgKFLTLKGARENNLKNITVSIPLG 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 621 VMTCVTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYDDIRK 700
Cdd:TIGR00630 635 LFTCITGVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEG-LEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRE 713
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 701 LFADQPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTV 780
Cdd:TIGR00630 714 LFAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTV 793
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 781 DAAVDLFAAYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTTGLHF 860
Cdd:TIGR00630 794 EEAYEFFEAV-------PSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKR-STGRTLYILDEPTTGLHF 865
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 861 HDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADL 919
Cdd:TIGR00630 866 DDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEV 924
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
10-920 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 611.83  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   10 IHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITGIAPAI 89
Cdd:PRK00635     6 VRLSGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEGLSPTI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   90 AIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSGREVRSHTVADVVNYIAALPSGTRVLVAAPLKTAEGQGLI 169
Cdd:PRK00635    86 AVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAKDILAIR 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  170 EkltlLVKEGLQRLYIDGQSLFIEDIIvqADDYAGRADLRIVVDraKATDDEETLSRLGDSVATAFLQGDGVCDVIVqqa 249
Cdd:PRK00635   166 E----CLRQGFTKVRIDGEISPIYKFL--TSGIPEDVPVDIVVD--TLIKNESNTARLKVSLFTALDIGHGECSLHF--- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  250 dGDRVESFSSRFELDGI--VFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDeDLVVPDKNKSIYQDAIACWRGETMKWWR 327
Cdd:PRK00635   235 -DNQKRTFSTQATIPETqqTYTPLTPQLFSPHSLEDRCPQCQGSGIFISID-DPSLIQQNLSIEENCCPFAGNCSTYLYH 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  328 DQLVINAPKFDFPIHRPFHELTREEKRLLWKGNE-------FFHG---------------LDEFfkfleGEryKIQYRVM 385
Cdd:PRK00635   313 TIYQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEglvlpvrLFDGtlgkktlthkvwrgvLNEI-----GE--KVRYSNK 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  386 LSRY----TGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDrdgKTVARVLTEIRNRLEYLNE 461
Cdd:PRK00635   386 PSRYlpkgTSATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKS---LSIEEVLQGLKSRLSILID 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  462 VGLGYLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIR 541
Cdd:PRK00635   463 LGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  542 AADTIIDIGPLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWNSYVDVIGARENNLKGIDVKFPLGV 621
Cdd:PRK00635   543 LADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKRTNSLGTLTLSKATKHNLKDLTISLPLGR 622
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  622 MTCVTGVSGSGKSSLVREILYPAIRRELyeTGMKPGDFERLGGDLKRLkgVEIIDQNPiGKSLRSNPVTYLKAYDDIRKL 701
Cdd:PRK00635   623 LTVVTGVSGSGKSSLINDTLVPAVEEFI--EQGFCSNLSIQWGAISRL--VHITRDLP-GRSQRSIPLTYIKAFDDLREL 697
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  702 FADQPYAKHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQfmaDVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVD 781
Cdd:PRK00635   698 FAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDN---RTSIPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAY 774
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  782 AAVDLFAAyqdkdaiNKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnAGGPILFIFDEPTTGLHFH 861
Cdd:PRK00635   775 EAEKFFLD-------EPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAP-SKKPTLYVLDEPTTGLHTH 846
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368  862 DIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADLM 920
Cdd:PRK00635   847 DIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELI 905
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
602-916 3.27e-124

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 376.95  E-value: 3.27e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 602 VIGARENNLKGIDVKFPLGVMTCVTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGdLKRLKGVEIIDQNPIG 681
Cdd:cd03271     3 LKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEG-LEHIDKVIVIDQSPIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 682 KSLRSNPVTYLKAYDDIRKLFadqpyakhngltpshfsfnmaggrceecqgegvikvgmqfmadvelvCESCGGKRFKDE 761
Cdd:cd03271    82 RTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNRE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 762 VLEVKYHGHSIYDILELTVDAAVDLFAAYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKE 841
Cdd:cd03271   115 TLEVRYKGKSIADVLDMTVEEALEFFENI-------PKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKR 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 842 nAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTP 916
Cdd:cd03271   188 -STGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
2-932 2.47e-107

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 366.08  E-value: 2.47e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368    2 QNPKEEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINK-PDVD 80
Cdd:PRK00635   933 PKPPVPADITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQALIKKTPlPSVD 1012
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   81 FITGIAPAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIGRTYSPVSG---REVRSHTVADVV--NYIAALpsgtrVL 155
Cdd:PRK00635  1013 KVTGLSPVIAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGdalRKITPQTIAEELltHYTKGY-----VT 1087
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  156 VAAPLKTAEGqgLIEKLTLLVKEGLQRLYIDGQSLFIEDIIVQADDyagraDLRIVVDRAKATddEETLSRLGDSVATAF 235
Cdd:PRK00635  1088 ITSPIPKEED--LFIYLQEKLKEGFLKLYANEQFYDLDEPLPTSLE-----NPAIVIQHTKIS--EKNLSSLLSSLTLAF 1158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  236 LQGDGVCDVIVQQAdgdRVESFSSRFELD---GIVFEHPSEHMFSFNNPIGACPRCEGYGKVIGIDedlVVPDKNKSIYQ 312
Cdd:PRK00635  1159 SLSSSICLHIEYAG---TSLSLTYRLGWQdssGNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCS---LLPHKEKIAHY 1232
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  313 DAIACWR----GETMKWWRDQLvinaPKFDFPIHRPFHELTREEKRLLWKGNEFFHGLDeffKFLEGERYKIQYRVMLSR 388
Cdd:PRK00635  1233 TPLSLFTlffpNQDPKPVYPLL----KELGIPSIALFQELDTLSFESLCLGTQQHPGLN---ALLMEAMLMESEEPLPPP 1305
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  389 YTGKTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRLDDrdgktVARVLTEIRNRLEYLNEVGLGYLT 468
Cdd:PRK00635  1306 LISKTPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTIHDDE-----EPSIIQDLLNRLTFIDKVGLSYIT 1380
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  469 LDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIID 548
Cdd:PRK00635  1381 LGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIH 1460
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  549 IGPLAGYQGGEVMfqggidrlasakDSLTAKyltgVERIEPPANKRRWNSYVDVIGARENNLKGIDVKFPLGVMTCVTGV 628
Cdd:PRK00635  1461 LGPGSGPQGGYLL------------STSALK----QSQPDLHNTRSSEETPTLSVSLSIHTIQNLNVSAPLHSLVAISGV 1524
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  629 SGSGKSSLVREilypairrELYETGMKpgdfeRLGGDLKRLKGVEIIDQNPIGKSLRSNPVTYLKAYDDIRKLFADQPYA 708
Cdd:PRK00635  1525 SGSGKTSLLLE--------GFYKQACA-----LIEKGPSVFSEIIFLDSHPQISSQRSDISTYFDIAPSLRNFYASLTQA 1591
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  709 KHNGLTPSHFSFNMAGGRCEECQGEGVIKVGMQFMADVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAVDLFA 788
Cdd:PRK00635  1592 KALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFP 1671
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  789 AYqdkdainKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLI---KEnaggPILFIFDEPTTGLHFHDIRK 865
Cdd:PRK00635  1672 FL-------KKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYlppKH----PTLFLLDEIATSLDNQQKSA 1740
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368  866 LLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFLS 932
Cdd:PRK00635  1741 LLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMC 1807
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
10-122 1.69e-65

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 219.44  E-value: 1.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  10 IHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFLGKINKPDVDFITGIAPAI 89
Cdd:cd03270     1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368  90 AIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRIG 122
Cdd:cd03270    81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG 113
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
452-564 2.76e-60

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 205.18  E-value: 2.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 452 IRNRLEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVI 531
Cdd:cd03270   114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368 532 VVEHEEEIIRAADTIIDIGPLAGYQGGEVMFQG 564
Cdd:cd03270   194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
597-932 3.66e-58

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 216.05  E-value: 3.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 597 NSYVDVIGARENNLKGIDVKFPLGVMTCVTGVSGSGKSSLVREILY---------------------------------- 642
Cdd:COG0178     3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYaegqrryveslsayarqflgqmdkpdvdsiegls 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 643 PAI-----------R-------------RELY---------ETG----------M----------------------KPG 657
Cdd:COG0178    83 PAIsieqkttsrnpRstvgtvteiydylRLLFarvgtphcpICGrpvekqtvdqIvdrilalpegtrlqilapvvrgRKG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 658 DFE--------------RLGGDLKRLKGVEIIDQNP------------IGKSLRS-------------NPVTYLKAYDD- 697
Cdd:COG0178   163 EHKelleelrkqgfvrvRVDGEVYDLDEEPELDKNKkhtievvvdrlvVKEDIRSrladsvetalklgDGLVIVEVVDEg 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 698 IRKLFADQPYAKHNG-----LTPSHFSFNMAGGRCEECQG---------------------------------------- 732
Cdd:COG0178   243 EELLFSEKFACPDCGisfeeLEPRLFSFNSPYGACPTCDGlgrvlefdpdlvipdpslslaegaiapwsgpsssyyfqll 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 733 ---------------------------------------------------EGVI-----------KVGM-----QFMAd 745
Cdd:COG0178   323 ealakhygfdldtpwkdlpeeqrdlilygsdekikfryknrgrrrtyekpfEGVIpflerryretySEHVreelsRYMS- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 746 vELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAVDLFAA-----YQDKDA--INKKIIEKLMTLQDVGLGYVKLG 818
Cdd:COG0178   402 -ETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENlelteREAEIAerILKEIRSRLGFLVDVGLDYLTLD 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 819 QSSSTLSGGESQRVKLASFLikenaG----GpILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSAD 894
Cdd:COG0178   481 RSAGTLSGGEAQRIRLATQI-----GsglvG-VLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAAD 554
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 1474250368 895 WVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFLS 932
Cdd:COG0178   555 YIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLS 592
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
4-581 2.42e-54

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 204.49  E-value: 2.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   4 PKEEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAegqrryveslsAYARQFLGKINKP-DVDFI 82
Cdd:COG0178   605 KGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTGVSGSGKSTLVNDILYP-----------ALARKLNGAKEKPgPHDSI 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  83 TG---IAPAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFgrigrtyspvsgrevrshtvadvvnyiAALPsgtrvlvaap 159
Cdd:COG0178   674 EGlehIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELF---------------------------AQTP---------- 716
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 160 lktaegqgliekltllvkEGLQRLYidgqslfiediivqaddYAGRadlrivvdrakatddeetlsrlgdsvataflqgd 239
Cdd:COG0178   717 ------------------EAKARGY-----------------KPGR---------------------------------- 727
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 240 gvcdvivqqadgdrvesfssrfeldgivfehpsehmFSFNNPIGACPRCEGYGkVIGID----EDLVVPdknksiyqdai 315
Cdd:COG0178   728 ------------------------------------FSFNVKGGRCEACQGDG-VIKIEmhflPDVYVP----------- 759
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 316 acwrgetmkwwrdqlvinapkfdfpihrpfheltreekrllwkgneffhgldeffkflegerykiqyrvmlsrytgktvC 395
Cdd:COG0178   760 -------------------------------------------------------------------------------C 760
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 396 PDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRlddrdgktvarvltEIRNRLEYLNEVGLGYLTLDRLSST 475
Cdd:COG0178   761 EVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFENIP--------------KIARKLQTLQDVGLGYIKLGQPATT 826
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 476 LSGGESQRINLATSLG-SSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIGPLAG 554
Cdd:COG0178   827 LSGGEAQRVKLASELSkRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGG 906
                         570       580
                  ....*....|....*....|....*..
gi 1474250368 555 YQGGEVMFQGGIDRLASAKDSLTAKYL 581
Cdd:COG0178   907 DGGGEIVAEGTPEEVAKVKASYTGRYL 933
uvrA PRK00349
excinuclease ABC subunit UvrA;
741-932 1.12e-51

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 196.45  E-value: 1.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 741 QFMadVELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAVDLFAAYQ--DKDA-----INKKIIEKLMTLQDVGLG 813
Cdd:PRK00349  402 KYM--SERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKlsEQEAkiaepILKEIRERLKFLVDVGLD 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 814 YVKLGQSSSTLSGGESQRVKLASfLIKENAGGpILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSA 893
Cdd:PRK00349  480 YLTLSRSAGTLSGGEAQRIRLAT-QIGSGLTG-VLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAA 557
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1474250368 894 DWVIDLGPEAGERGGRVVFEGTPADLMTCRESYTGKFLS 932
Cdd:PRK00349  558 DYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLS 596
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
747-932 7.39e-50

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. 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: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 190.99  E-value: 7.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 747 ELVCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAVDLFAAYQ--DKDA-----INKKIIEKLMTLQDVGLGYVKLGQ 819
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTltPEEKkiaeeVLKEIRERLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 820 SSSTLSGGESQRVKLASFLIKENAGgpILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDL 899
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTG--VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1474250368 900 GPEAGERGGRVVFEGTPADLMTCRESYTGKFLS 932
Cdd:TIGR00630 563 GPGAGEHGGEVVASGTPEEILANPDSLTGQYLS 595
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
600-914 5.41e-48

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 170.52  E-value: 5.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 600 VDVIGARENNLKGIDVKFPLGVMTCVTGVSGSGKSSLVREILYPAIRRELYETgMKPGDFERLGG----DLKRLKGVE-- 673
Cdd:cd03270     1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVES-LSAYARQFLGQmdkpDVDSIEGLSpa 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 674 -IIDQNPIGKSLRSNPVTYLKAYDDIRKLFAdqpyakhngltpshfsfnmaggrceecqgegviKVGmqfmadvelvces 752
Cdd:cd03270    80 iAIDQKTTSRNPRSTVGTVTEIYDYLRLLFA---------------------------------RVG------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 753 cggkrfkdevlevkyhghsiydileltvdaavdlfaayqdkdainkkIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRV 832
Cdd:cd03270   114 -----------------------------------------------IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRI 146
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 833 KLASFLIKENAGgpILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVF 912
Cdd:cd03270   147 RLATQIGSGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVA 224

                  ..
gi 1474250368 913 EG 914
Cdd:cd03270   225 QG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
395-564 2.86e-46

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 166.64  E-value: 2.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 395 CPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGlrlddrdgktVARvlteIRNRLEYLNEVGLGYLTLDRLSS 474
Cdd:cd03271   103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFEN----------IPK----IARKLQTLCDVGLGYIKLGQPAT 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 475 TLSGGESQRINLATSLGSSLVG-SLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIGPLA 553
Cdd:cd03271   169 TLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEG 248
                         170
                  ....*....|.
gi 1474250368 554 GYQGGEVMFQG 564
Cdd:cd03271   249 GDGGGQVVASG 259
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
602-914 4.33e-46

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 163.26  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 602 VIGARENNLKGIDVKFPLGVMTCVTGVSGSGKSSLVREILYPAIRRELYETgmkpgdferlggdlkrlkgveiidqnpig 681
Cdd:cd03238     3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISF----------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 682 kslrsnpvtyLKAYDDIRKLFADQpyakhngltpshfsfnmaggrceecqgegvikvgmqfmadvelvcescggkrfkde 761
Cdd:cd03238    54 ----------LPKFSRNKLIFIDQ-------------------------------------------------------- 67
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 762 vlevkyhghsiydileltvdaavdlfaayqdkdainkkiiekLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKE 841
Cdd:cd03238    68 ------------------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSE 105
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 842 NagGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAGERGGRVVFEG 914
Cdd:cd03238   106 P--PGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
456-564 8.26e-45

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 159.41  E-value: 8.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:cd03238    68 LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
                          90       100
                  ....*....|....*....|....*....
gi 1474250368 536 EEEIIRAADTIIDIGPLAGYQGGEVMFQG 564
Cdd:cd03238   148 NLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
395-908 2.64e-43

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 171.94  E-value: 2.64e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  395 CPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFdglrlddrdgktvarvLTE--IRNRLEYLNEVGLGYLTLDRL 472
Cdd:PRK00635   743 CPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFF----------------LDEpsIHEKIHALCSLGLDYLPLGRP 806
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  473 SSTLSGGESQRINLATSLGS-SLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIGP 551
Cdd:PRK00635   807 LSSLSGGEIQRLKLAYELLApSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGP 886
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  552 LAGYQGGEVMFQGGIDRLASaKDSLTAK----YLTGVERIEP---PANKRRWNSYVDVIGARENNLKGIDVKFPLGVMTC 624
Cdd:PRK00635   887 EGGNLGGYLLASCSPEELIH-LHTPTAKalrpYLSSPQELPYlpdPSPKPPVPADITIKNAYQHNLKHIDLSLPRNALTA 965
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  625 VTGVSGSGKSSLVREILY------------PAIRRELYE----------TGMKP-------------------------- 656
Cdd:PRK00635   966 VTGPSASGKHSLVFDILYaagniayaelfpPYIRQALIKktplpsvdkvTGLSPviaiektsasknsnhsvasaleisng 1045
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  657 --GDFERLG-------GD-LKRLKGVEIIDQ-------------NPIgkSLRSNPVTYL--KAYDDIRKLFA-------D 704
Cdd:PRK00635  1046 leKLFARLGhpysplsGDaLRKITPQTIAEEllthytkgyvtitSPI--PKEEDLFIYLqeKLKEGFLKLYAneqfydlD 1123
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  705 QPYA----------KHNGLTPSH----------------------------------------------------FSFNM 722
Cdd:PRK00635  1124 EPLPtslenpaiviQHTKISEKNlssllssltlafslsssiclhieyagtslsltyrlgwqdssgnlypnittplLSRDH 1203
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  723 AGGRCEECQGEGVI--------------------------------------------KVGMQFMADVEL---------- 748
Cdd:PRK00635  1204 EEGLCPLCHGKGFIlkcsllphkekiahytplslftlffpnqdpkpvypllkelgipsIALFQELDTLSFeslclgtqqh 1283
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  749 ---------------------------VCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAVDLFAAYQDKDA--INKK 799
Cdd:PRK00635  1284 pglnallmeamlmeseeplppplisktPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTIHDDEEpsIIQD 1363
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  800 IIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASfLIKENAGGpILFIFDEPTTGLHFHDIRKLLGAFDALLARGHT 879
Cdd:PRK00635  1364 LLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAK-KISSNLTD-IIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNT 1441
                          730       740
                   ....*....|....*....|....*....
gi 1474250368  880 VVIVEHNMDVIRSADWVIDLGPEAGERGG 908
Cdd:PRK00635  1442 VIATDRSGSLAEHADHLIHLGPGSGPQGG 1470
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-564 8.05e-42

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. 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: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 165.96  E-value: 8.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   4 PKEEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVeslsayarqfLGKINKPDVDFIT 83
Cdd:TIGR00630 608 PGNGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYPALANRLN----------GAKTVPGRYTSIE 677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  84 G---IAPAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRigrtyspvsgrevrshtvadvvnyiaalpsgtrvlvaapl 160
Cdd:TIGR00630 678 GlehLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAE---------------------------------------- 717
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 161 ktaegqgliekltllVKEGLQRLYidgqslfiediivqaddYAGRadlrivvdrakatddeetlsrlgdsvataflqgdg 240
Cdd:TIGR00630 718 ---------------TPEAKVRGY-----------------TPGR----------------------------------- 730
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 241 vcdvivqqadgdrvesfssrfeldgivfehpsehmFSFNNPIGACPRCEGYGkVIGIdEDLVVPDknksIYqdaiacwrg 320
Cdd:TIGR00630 731 -----------------------------------FSFNVKGGRCEACQGDG-VIKI-EMHFLPD----VY--------- 760
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 321 etmkwwrdqlvinapkfdfpihrpfheltreekrllwkgneffhgldeffkflegerykiqyrvmlsrytgkTVCPDCGG 400
Cdd:TIGR00630 761 ------------------------------------------------------------------------VPCEVCKG 768
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 401 GRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGlrlddrdgktvarvLTEIRNRLEYLNEVGLGYLTLDRLSSTLSGGE 480
Cdd:TIGR00630 769 KRYNRETLEVKYKGKNIADVLDMTVEEAYEFFEA--------------VPSISRKLQTLCDVGLGYIRLGQPATTLSGGE 834
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 481 SQRINLATSLGSSLVG-SLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIGPLAGYQGGE 559
Cdd:TIGR00630 835 AQRIKLAKELSKRSTGrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGT 914

                  ....*
gi 1474250368 560 VMFQG 564
Cdd:TIGR00630 915 VVASG 919
uvrA PRK00349
excinuclease ABC subunit UvrA;
4-581 4.19e-41

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 163.71  E-value: 4.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368   4 PKEEKYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAegqrryveslsAYARQFLGKINKP-DVDFI 82
Cdd:PRK00349  609 KGNGKFLKLKGARENNLKNVDVEIPLGKFTCVTGVSGSGKSTLINETLYK-----------ALARKLNGAKKVPgKHKEI 677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  83 TG---IAPAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFgrigrtyspvsgrevrshtvadvvnyiAALPsgtrvlvaap 159
Cdd:PRK00349  678 EGlehLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELF---------------------------AGTP---------- 720
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 160 lktaegqgliekltllvkEGLQRLYidgqslfiediivqaddYAGRadlrivvdrakatddeetlsrlgdsvataflqgd 239
Cdd:PRK00349  721 ------------------EAKARGY-----------------KPGR---------------------------------- 731
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 240 gvcdvivqqadgdrvesfssrfeldgivfehpsehmFSFNNPIGACPRCEGYGkVIGIdEDLVVPDknksIYqdaIACwr 319
Cdd:PRK00349  732 ------------------------------------FSFNVKGGRCEACQGDG-VIKI-EMHFLPD----VY---VPC-- 764
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 320 gETMKwwrdqlvinapkfdfpihrpfheltreekrllwkgneffhgldeffkfleGERYK-----IQYRvmlsrytgktv 394
Cdd:PRK00349  765 -DVCK--------------------------------------------------GKRYNretleVKYK----------- 782
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 395 cpdcgggrlrkeafyvqvgGKHIGELVTMPVDELQRFFdglrlddrdgKTVARvlteIRNRLEYLNEVGLGYLTLDRLSS 474
Cdd:PRK00349  783 -------------------GKNIADVLDMTVEEALEFF----------EAIPK----IARKLQTLVDVGLGYIKLGQPAT 829
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 475 TLSGGESQRINLATSLGSSLVG-SLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIGPLA 553
Cdd:PRK00349  830 TLSGGEAQRVKLAKELSKRSTGkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEG 909
                         570       580
                  ....*....|....*....|....*...
gi 1474250368 554 GYQGGEVMFQGGIDRLASAKDSLTAKYL 581
Cdd:PRK00349  910 GDGGGEIVATGTPEEVAKVEASYTGRYL 937
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
749-931 3.36e-29

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 126.48  E-value: 3.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  749 VCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAVDLFAAYQDKDAINKKIIE----KLMTLQDVGLGYVKLGQSSSTL 824
Cdd:PRK00635   398 SCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKSLSIEEVLQglksRLSILIDLGLPYLTPERALATL 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  825 SGGESQRVKLASFLIKENAGgpILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPEAG 904
Cdd:PRK00635   478 SGGEQERTALAKHLGAELIG--ITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGAG 555
                          170       180
                   ....*....|....*....|....*..
gi 1474250368  905 ERGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:PRK00635   556 IFGGEVLFNGSPREFLAKSDSLTAKYL 582
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
392-584 4.46e-21

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 99.90  E-value: 4.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  392 KTVCPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFDGLRlddrdgktvarvltEIRNRLEYLNEVGLGYLTLDR 471
Cdd:PRK00635  1630 KRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFPFLK--------------KIQKPLQALIDNGLGYLPLGQ 1695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  472 LSSTLSGGESQRINLATSLG-SSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIG 550
Cdd:PRK00635  1696 NLSSLSLSEKIAIKIAKFLYlPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMG 1775
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1474250368  551 PLAGYQGGEVMFQGGIDRLASAKDSLTAKYLTGV 584
Cdd:PRK00635  1776 PGSGKTGGKILFSGPPKDISASKDSLLKTYMCNL 1809
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
451-921 2.73e-20

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 95.74  E-value: 2.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-LEYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGN 528
Cdd:COG1123   118 EARARvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL--ALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGT 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 529 TVIVVEHE-EEIIRAADTIIDIgplagyQGGEVMFQGGIDRLASAKDSLTAKYLTGVERIEPPANKRRWNSYVDVIG--- 604
Cdd:COG1123   195 TVLLITHDlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNlsk 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 605 ---ARENN----LKGIDVKFPLGVMTCVTGVSGSGKSSLVREI--LYPAIRrelyetgmkpGDFERLGGDLKRLKGVEIi 675
Cdd:COG1123   269 rypVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgLLRPTS----------GSILFDGKDLTKLSRRSL- 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 676 dqnpigKSLRSnpvtylkaydDIRKLFADqPYAkhngltpshfSFNmaggrceecqgegvikvgmqfmadvelvcescgg 755
Cdd:COG1123   338 ------RELRR----------RVQMVFQD-PYS----------SLN---------------------------------- 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 756 krfkdevlevkyHGHSIYDILELTVDAAVDLfaayqDKDAINKKIIEklmTLQDVGLGYVKLGQSSSTLSGGESQRVKLA 835
Cdd:COG1123   357 ------------PRMTVGDIIAEPLRLHGLL-----SRAERRERVAE---LLERVGLPPDLADRYPHELSGGQRQRVAIA 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 836 SFLikenAGGPILFIFDEPTTGLhfhDIR---KLLGAFDALLAR-GHTVVIVEHNMDVIRS-ADWVIDLgpeageRGGRV 910
Cdd:COG1123   417 RAL----ALEPKLLILDEPTSAL---DVSvqaQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVM------YDGRI 483
                         490
                  ....*....|.
gi 1474250368 911 VFEGTPADLMT 921
Cdd:COG1123   484 VEDGPTEEVFA 494
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
10-143 3.46e-20

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 91.14  E-value: 3.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  10 IHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAegqrryveslSAYARQFLGKINKPDVDFITG---IA 86
Cdd:cd03271     1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGlehID 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474250368  87 PAIAIEQKVNTRNPRSTVGTSTEIYDYLKLLFGRI--GRTYSPVSgREVRSH--TVADVVN 143
Cdd:cd03271    71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELFCEVckGKRYNRET-LEVRYKgkSIADVLD 130
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
792-924 1.15e-18

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 85.85  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEklmTLQDVGL-GYvkLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAF 870
Cdd:COG1122   107 PREEIRERVEE---ALELVGLeHL--ADRPPHELSGGQKQRVAIAGVL----AMEPEVLVLDEPTAGLDPRGRRELLELL 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 871 DALLARGHTVVIVEHNMD-VIRSADWVIDLgpeageRGGRVVFEGTPADLMTCRE 924
Cdd:COG1122   178 KRLNKEGKTVIIVTHDLDlVAELADRVIVL------DDGRIVADGTPREVFSDYE 226
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
476-558 2.54e-18

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: 83.18  E-value: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 476 LSGGESQRINLA--TSLGSSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIGPLA 553
Cdd:cd03227    78 LSGGEKELSALAliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157

                  ....*
gi 1474250368 554 GYQGG 558
Cdd:cd03227   158 TGVYK 162
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
10-71 6.72e-18

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 82.37  E-value: 6.72e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368  10 IHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQRRYVESLSAYARQFL 71
Cdd:cd03238     1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL 62
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
610-897 1.09e-17

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 82.51  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 610 LKGIDVKFPLGVMTCVTGVSGSGKSSLVREilypairrelyetgmkpgdferLGGDLKRLKGVEIIDqnpiGKSLRSNPV 689
Cdd:cd03225    17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRL----------------------LNGLLGPTSGEVLVD----GKDLTKLSL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 690 TylkaydDIRKlfadqpyakhngltpshfsfnmaggrceecqgegviKVGMQFM-ADVELVCESCGgkrfkDEVlevkyh 768
Cdd:cd03225    71 K------ELRR------------------------------------KVGLVFQnPDDQFFGPTVE-----EEV------ 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 769 ghsiydileltvdaAVDLFAAYQDKDAINKKIIEklmTLQDVGLgYVKLGQSSSTLSGGESQRVKLASFLikenAGGPIL 848
Cdd:cd03225    98 --------------AFGLENLGLPEEEIEERVEE---ALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVL----AMDPDI 155
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1474250368 849 FIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVI 897
Cdd:cd03225   156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVI 205
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
137-248 4.02e-17

UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 77.91  E-value: 4.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 137 TVADVVNYIAALPSGTRVLVAAPLKTAEGQGLIEKLTLLVKEGLQRLYIDGQSLFIEDIIvQADDYAgRADLRIVVDRAK 216
Cdd:pfam17760   2 TVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEP-KLDKNK-KHTIEVVVDRLV 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1474250368 217 ATDDEEtlSRLGDSVATAFLQGDGVCDVIVQQ 248
Cdd:pfam17760  80 VKEDNR--SRLADSVETALKLGKGLVIVLVLD 109
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
777-920 2.23e-16

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 79.34  E-value: 2.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 777 ELTVDAAVDLFAA-YQDKDAINKKIIEKLmtLQDVGLGyVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPT 855
Cdd:COG1131    87 DLTVRENLRFFARlYGLPRKEARERIDEL--LELFGLT-DAADRKVGTLSGGMKQRLGLALALLHD----PELLILDEPT 159
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 856 TGLhfhD---IRKLLGAFDALLARGHTVVIVEHNMDVI-RSADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:COG1131   160 SGL---DpeaRRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAII------DKGRIVADGTPDELK 219
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
451-547 2.26e-16

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 78.66  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRL-EYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNT 529
Cdd:cd03225   110 EIEERVeEALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVL--AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT 186
                          90
                  ....*....|....*....
gi 1474250368 530 VIVVEHEEEIIRA-ADTII 547
Cdd:cd03225   187 IIIVTHDLDLLLElADRVI 205
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
476-549 2.74e-15

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: 74.20  E-value: 2.74e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 476 LSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE-EEIIRAADTIIDI 549
Cdd:cd00267    81 LSGGQRQRVALARALLLN--PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVL 153
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
817-920 1.87e-14

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 77.49  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLIKEnagGPILfIFDEPTTGLhfhDI---RKLLGAFDAlLARGHTVVIVEHNMDVIRSA 893
Cdd:COG4988   467 LGEGGRGLSGGQAQRLALARALLRD---APLL-LLDEPTAHL---DAeteAEILQALRR-LAKGRTVILITHRLALLAQA 538
                          90       100
                  ....*....|....*....|....*..
gi 1474250368 894 DWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:COG4988   539 DRILVL------DDGRIVEQGTHEELL 559
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
824-899 1.94e-14

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: 71.89  E-value: 1.94e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVI-RSADWVIDL 899
Cdd:cd00267    81 LSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAeLAADRVIVL 153
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
792-921 3.88e-14

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 76.10  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEklmTLQDVGLGyVKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFD 871
Cdd:COG1123   115 SRAEARARVLE---LLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMAL----ALDPDLLIADEPTTALDVTTQAEILDLLR 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 872 ALLA-RGHTVVIVEHNMDVI-RSADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:COG1123   187 ELQReRGTTVLLITHDLGVVaEIADRVVVM------DDGRIVEDGPPEEILA 232
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
807-921 9.08e-14

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 71.70  E-value: 9.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHN 886
Cdd:cd03219   128 LERVGLAD-LADRPAGELSYGQQRRLEIARAL----ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHD 202
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1474250368 887 MDVIRS-AD--WVIDLgpeagergGRVVFEGTPADLMT 921
Cdd:cd03219   203 MDVVMSlADrvTVLDQ--------GRVIAEGTPDEVRN 232
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
298-379 1.90e-13

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 67.50  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 298 DEDLVVPDKNKSIYQDAIACWRGETMKWWRDQLVINAPKFDFPIHRPFHELTREEKRLLWKGNEffhglDEFFKFLEGER 377
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSG-----EEIIVFYYSRG 75

                  ..
gi 1474250368 378 YK 379
Cdd:pfam17755  76 GR 77
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
778-936 7.27e-13

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 69.50  E-value: 7.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 778 LTVDAAVDLFAA-YQDKDAINKKIIEKLmtLQDVGLGYVkLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTT 856
Cdd:COG4555    89 LTVRENIRYFAElYGLFDEELKKRIEEL--IELLGLEEF-LDRRVGELSTGMKKKVALARALVHD----PKVLLLDEPTN 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 857 GLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVI-RSADWVIDLgpeageRGGRVVFEGTPADLM--TCRESYTGKFLSL 933
Cdd:COG4555   162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVIL------HKGKVVAQGSLDELReeIGEENLEDAFVAL 235

                  ...
gi 1474250368 934 AEN 936
Cdd:COG4555   236 IGS 238
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
419-547 9.75e-13

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 68.33  E-value: 9.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 419 ELVTMPVDELQRFFDGLRLDDRdgktvARVLteirnrlEYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSL 498
Cdd:cd03235    89 DVVLMGLYGHKGLFRRLSKADK-----AKVD-------EALERVGLSEL-ADRQIGELSGGQQQRVLLARALVQD--PDL 153
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1474250368 499 YILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE-EEIIRAADTII 547
Cdd:cd03235   154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVL 203
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
610-914 1.13e-12

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 67.94  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 610 LKGIDVKFPLGVMTCVTGVSGSGKSSLVREILypairrelyetgmkpgdferlgGDLKRLKGVEIIDQNPIGKSLRSnpV 689
Cdd:cd03235    15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL----------------------GLLKPTSGSIRVFGKPLEKERKR--I 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 690 TYLkayddirklfadqpyakhngltPSHFSFNMaggrceecqgegvikvgmQFMADV-ELVCESCGGKRFkdevlevkyh 768
Cdd:cd03235    71 GYV----------------------PQRRSIDR------------------DFPISVrDVVLMGLYGHKG---------- 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 769 ghsiydileltvdaavdLFAAYQDKDAinKKIIEklmTLQDVGLGYVKLgQSSSTLSGGESQRVKLASFLikenAGGPIL 848
Cdd:cd03235   101 -----------------LFRRLSKADK--AKVDE---ALERVGLSELAD-RQIGELSGGQQQRVLLARAL----VQDPDL 153
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 849 FIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVIDLgpeagerGGRVVFEG 914
Cdd:cd03235   154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLL-------NRTVVASG 213
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
822-921 1.28e-12

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 68.58  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 822 STLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhDI---RKLLGAFDALLARGHTVVIVEHNMDVIRS-ADWVI 897
Cdd:COG1121   138 GELSGGQQQRVLLARAL----AQDPDLLLLDEPFAGV---DAateEALYELLRELRREGKTILVVTHDLGAVREyFDRVL 210
                          90       100
                  ....*....|....*....|....
gi 1474250368 898 DLgpeagerGGRVVFEGTPADLMT 921
Cdd:COG1121   211 LL-------NRGLVAHGPPEEVLT 227
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
824-902 1.64e-12

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: 66.23  E-value: 1.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 824 LSGGESQRVKLASFLIKENAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLGPE 902
Cdd:cd03227    78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
799-920 1.95e-12

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. 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: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 68.03  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 799 KIIEKLMTLQDvglGY-VKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDAlLARG 877
Cdd:cd03253   115 QIHDKIMRFPD---GYdTIVGERGLKLSGGEKQRVAIARAILKN----PPILLLDEATSALDTHTEREIQAALRD-VSKG 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1474250368 878 HTVVIVEHNMDVIRSADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:cd03253   187 RTTIVIAHRLSTIVNADKIIVL------KDGRIVERGTHEELL 223
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
822-921 2.11e-12

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 68.15  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 822 STLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhDIR---KLLGAFDALLA-RGHTVVIVEHNMD-VIRSADWV 896
Cdd:COG1120   136 DELSGGERQRVLIARAL----AQEPPLLLLDEPTSHL---DLAhqlEVLELLRRLAReRGRTVVMVLHDLNlAARYADRL 208
                          90       100
                  ....*....|....*....|....*
gi 1474250368 897 IDLgpeageRGGRVVFEGTPADLMT 921
Cdd:COG1120   209 VLL------KDGRIVAQGPPEEVLT 227
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
780-929 2.87e-12

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 67.76  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 780 VDAAVDLFAAYQDKDAINKKIIEklmTLQDVGLGyVKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLH 859
Cdd:COG0411   113 LAALLRLPRARREEREARERAEE---LLERVGLA-DRADEPAGNLSYGQQRRLEIARAL----ATEPKLLLLDEPAAGLN 184
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 860 FHDIRKLLGAFDALLA-RGHTVVIVEHNMDVIRS-ADWVIDLGpeagerGGRVVFEGTPADLMT---CRESYTGK 929
Cdd:COG0411   185 PEETEELAELIRRLRDeRGITILLIEHDMDLVMGlADRIVVLD------FGRVIAEGTPAEVRAdprVIEAYLGE 253
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
816-921 7.72e-12

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 66.40  E-value: 7.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 816 KLGQSSSTLSGGESQRVKLASFLI----KENAGGPILfIFDEPTTGLhfhDIRKLLgAFDALLAR----GHTVVIVEHNM 887
Cdd:COG4138   119 KLSRPLTQLSGGEWQRVRLAAVLLqvwpTINPEGQLL-LLDEPMNSL---DVAQQA-ALDRLLRElcqqGITVVMSSHDL 193
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1474250368 888 D-VIRSAD--WVIdlgpeageRGGRVVFEGTPADLMT 921
Cdd:COG4138   194 NhTLRHADrvWLL--------KQGKLVASGETAEVMT 222
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
445-564 1.21e-11

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 65.54  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 445 VARVLTEIRNR-LEYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL 523
Cdd:cd03219   113 ARREEREARERaEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATD--PKLLLLDEPAAGLNPEETEELAELIREL 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1474250368 524 RDLGNTVIVVEHEEEIIRA-ADTIIdigplagyqggeVMFQG 564
Cdd:cd03219   190 RERGITVLLVEHDMDVVMSlADRVT------------VLDQG 219
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
816-926 2.27e-11

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 67.94  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 816 KLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLaRGHTVVIVEHNMDVIRSADW 895
Cdd:COG2274   604 VVGEGGSNLSGGQRQRLAIARALLRN----PRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADR 678
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1474250368 896 VIDLgpeageRGGRVVFEGTPADLMTCRESY 926
Cdd:COG2274   679 IIVL------DKGRIVEDGTHEELLARKGLY 703
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
792-931 2.78e-11

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 64.62  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEKLmtlQDVGL-GYVKLgqSSSTLSGGESQRVKLASFLIKEnaggP-ILFiFDEPTTGLhfhD-IRklLG 868
Cdd:COG1127   114 SEAEIRELVLEKL---ELVGLpGAADK--MPSELSGGMRKRVALARALALD----PeILL-YDEPTAGL---DpIT--SA 178
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 869 AFDALL-----ARGHTVVIVEHNMDVIRS-ADWVIDLGpeagerGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:COG1127   179 VIDELIrelrdELGLTSVVVTHDLDSAFAiADRVAVLA------DGKIIAEGTPEELLASDDPWVRQFL 241
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
804-926 3.30e-11

ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 64.45  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 804 LMTLQDVGL-GYVKLGQSSstLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLhfhD-IRKllGAFDALLAR----- 876
Cdd:cd03261   118 LEKLEAVGLrGAEDLYPAE--LSGGMKKRVALARALALD----PELLLYDEPTAGL---DpIAS--GVIDDLIRSlkkel 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1474250368 877 GHTVVIVEHNMDVIRS-ADWVIDLGpeagerGGRVVFEGTPADLMTCRESY 926
Cdd:cd03261   187 GLTSIMVTHDLDTAFAiADRIAVLY------DGKIVAEGTPEELRASDDPL 231
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
777-920 2.49e-10

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). 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.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 61.30  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 777 ELTVDAAVDLfAAYQDKDAINKKIIEKLMT----LQDvglgyvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFD 852
Cdd:cd03224    89 ELTVEENLLL-GAYARRRAKRKARLERVYElfprLKE------RRKQLAGTLSGGEQQMLAIARALMSR----PKLLLLD 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 853 EPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRS-ADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:cd03224   158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVL------ERGRVVLEGTAAELL 220
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
395-920 3.57e-10

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 63.67  E-value: 3.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 395 CPDCGGGRLRKEAFYVQVGGKHIGELVTMPVDELQRFFdGLRLDDRDGKTVARVLTEI--------RNRLEYLNEVGLGY 466
Cdd:TIGR03269  82 CPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTF-ALYGDDTVLDNVLEALEEIgyegkeavGRAVDLIEMVQLSH 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 467 lTLDRLSSTLSGGESQRINLATSLGSSLVgsLYILDEPSIGLHPRdTNRLI--AVLKKLRDLGNTVIVVEHEEEII-RAA 543
Cdd:TIGR03269 161 -RITHIARDLSGGEKQRVVLARQLAKEPF--LFLADEPTGTLDPQ-TAKLVhnALEEAVKASGISMVLTSHWPEVIeDLS 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 544 DTIIDIgplagyQGGEVMFQGgidrlasAKDSLTAKYLTGVERIEPPAN-------------KRRWNSyVD--VIGAren 608
Cdd:TIGR03269 237 DKAIWL------ENGEIKEEG-------TPDEVVAVFMEGVSEVEKECEvevgepiikvrnvSKRYIS-VDrgVVKA--- 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 609 nLKGIDVKFPLGVMTCVTGVSGSGKSSLVREILypairrelyetgmkpGDFERLGGDLKRLKGVEIIDQNPIGKSLRSNP 688
Cdd:TIGR03269 300 -VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIA---------------GVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRA 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 689 VTYLKayddirklFADQPYakhnGLTPshfsfnmaggrceecqgegvikvgmqfmadvelvcescggkrfkdevlevkyh 768
Cdd:TIGR03269 364 KRYIG--------ILHQEY----DLYP----------------------------------------------------- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 769 gHSiyDILE-LTVDAAVDLfaayQDKDAINKKIIeklmTLQDVGLGYVK----LGQSSSTLSGGESQRVKLASFLIKEna 843
Cdd:TIGR03269 379 -HR--TVLDnLTEAIGLEL----PDELARMKAVI----TLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKE-- 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 844 ggPILFIFDEPTTGLhfHDIRKLLGAFDALLAR---GHTVVIVEHNMdvirsaDWVIDLGPEAG-ERGGRVVFEGTPADL 919
Cdd:TIGR03269 446 --PRIVILDEPTGTM--DPITKVDVTHSILKAReemEQTFIIVSHDM------DFVLDVCDRAAlMRDGKIVKIGDPEEI 515

                  .
gi 1474250368 920 M 920
Cdd:TIGR03269 516 V 516
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
451-542 4.59e-10

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 60.45  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRL-EYLNEVGLGYLtLDRLSSTLSGGESQRINLAtslgSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKLRDLG 527
Cdd:COG2884   113 EIRRRVrEVLDLVGLSDK-AKALPHELSGGEQQRVAIA----RALVNrpELLLADEPTGNLDPETSWEIMELLEEINRRG 187
                          90
                  ....*....|....*
gi 1474250368 528 NTVIVVEHEEEIIRA 542
Cdd:COG2884   188 TTVLIATHDLELVDR 202
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
824-911 5.01e-10

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 58.98  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVIDLgpe 902
Cdd:cd03216    83 LSVGERQMVEIARAL----ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVTVL--- 155

                  ....*....
gi 1474250368 903 ageRGGRVV 911
Cdd:cd03216   156 ---RDGRVV 161
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
807-935 5.91e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 61.57  E-value: 5.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDAL-LARGHTVVIVEH 885
Cdd:PRK13634  129 IELVGLPEELLARSPFELSGGQMRRVAIAGVLAME----PEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTH 204
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1474250368 886 NM-DVIRSADWVIDLgpeageRGGRVVFEGTPADLMTCRESYTGKFLSLAE 935
Cdd:PRK13634  205 SMeDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEAIGLDLPE 249
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
450-549 6.38e-10

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 60.20  E-value: 6.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNRLEY-LNEVGLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLG 527
Cdd:cd03255   115 KERRERAEElLERVGLGDR-LNHYPSELSGGQQQRVAIARALAND--PKIILADEPTGNLDSETGKEVMELLRELnKEAG 191
                          90       100
                  ....*....|....*....|..
gi 1474250368 528 NTVIVVEHEEEIIRAADTIIDI 549
Cdd:cd03255   192 TTIVVVTHDPELAEYADRIIEL 213
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
817-926 7.05e-10

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 60.25  E-value: 7.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDAlLARGHTVVIVEHNMDVIRSADWV 896
Cdd:cd03249   133 VGERGSQLSGGQKQRIAIARALLRN----PKILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAHRLSTIRNADLI 207
                          90       100       110
                  ....*....|....*....|....*....|
gi 1474250368 897 IDLGpeagerGGRVVFEGTPADLMTCRESY 926
Cdd:cd03249   208 AVLQ------NGQVVEQGTHDELMAQKGVY 231
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
431-564 7.08e-10

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 58.99  E-value: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 431 FFDGLRLDDRDGKTVARvlteirnRLEY----LNEVGLGYLtLDRLSSTLSGGESQRINLATSLGSslVGSLYILDEPSI 506
Cdd:cd03214    57 LLDGKDLASLSPKELAR-------KIAYvpqaLELLGLAHL-ADRPFNELSGGERQRVLLARALAQ--EPPILLLDEPTS 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 507 GLhprDTNRLIAVLKKLRDL----GNTVIVVEHEEEI-IRAADTIIDIgplagyQGGEVMFQG 564
Cdd:cd03214   127 HL---DIAHQIELLELLRRLarerGKTVVMVLHDLNLaARYADRVILL------KDGRIVAQG 180
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
476-547 1.03e-09

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 58.21  E-value: 1.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 476 LSGGESQRINL--ATSLGSSLVgslyILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH-EEEIIRAADTII 547
Cdd:cd03216    83 LSVGERQMVEIarALARNARLL----ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHrLDEVFEIADRVT 153
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
457-549 1.10e-09

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 62.05  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGyltlDRLS---STLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVV 533
Cdd:PRK10535  127 ELLQRLGLE----DRVEyqpSQLSGGQQQRVSIARALMNG--GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIV 200
                          90
                  ....*....|....*.
gi 1474250368 534 EHEEEIIRAADTIIDI 549
Cdd:PRK10535  201 THDPQVAAQAERVIEI 216
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
807-899 1.13e-09

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 61.92  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGY-VKLGQSSSTLSGGESQRVKLASFLIKenaGGPILfIFDEPTTGLHFHDIRKLLGAFDAlLARGHTVVIVEH 885
Cdd:TIGR02857 441 VAALPQGLdTPIGEGGAGLSGGQAQRLALARAFLR---DAPLL-LLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTH 515
                          90
                  ....*....|....
gi 1474250368 886 NMDVIRSADWVIDL 899
Cdd:TIGR02857 516 RLALAALADRIVVL 529
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
787-888 1.16e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 60.87  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 787 FAAYQ------DKDAI------------NKKIIEKLMTLqdVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPIL 848
Cdd:PRK13651  113 FAEYQlfeqtiEKDIIfgpvsmgvskeeAKKRAAKYIEL--VGLDESYLQRSPFELSGGQKRRVALAGILAME----PDF 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1474250368 849 FIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD 888
Cdd:PRK13651  187 LVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
788-921 1.87e-09

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 59.36  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 788 AAYQDKDAINKKIIEKLMTLQDVgLGYVklGQSSSTLSGGESQRVKLASFLI----KENAGGPILFIfDEPTTGL---HF 860
Cdd:COG4559   101 APHGSSAAQDRQIVREALALVGL-AHLA--GRSYQTLSGGEQQRVQLARVLAqlwePVDGGPRWLFL-DEPTSALdlaHQ 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 861 HDIRKLLGAFdalLARGHTVVIVEH--NMdVIRSADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:COG4559   177 HAVLRLARQL---ARRGGGVVAVLHdlNL-AAQYADRILLL------HQGRLVAQGTPEEVLT 229
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
824-910 2.61e-09

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 57.23  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVIDLgpea 903
Cdd:cd03246    97 LSGGQRQRLGLARALYGN----PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL---- 168

                  ....*..
gi 1474250368 904 geRGGRV 910
Cdd:cd03246   169 --EDGRV 173
cbiO PRK13644
energy-coupling factor transporter ATPase;
805-921 3.17e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 58.85  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 805 MTLQDVGLGYVKLgQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVE 884
Cdd:PRK13644  119 RALAEIGLEKYRH-RSPKTLSGGQGQCVALAGILTME----PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYIT 193
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1474250368 885 HNMDVIRSADWVIDLgpeagERgGRVVFEGTPADLMT 921
Cdd:PRK13644  194 HNLEELHDADRIIVM-----DR-GKIVLEGEPENVLS 224
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
451-540 3.33e-09

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 57.80  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRL-EYLNEVGLGYlTLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNT 529
Cdd:cd03292   112 EIRKRVpAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNS--PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTT 188
                          90
                  ....*....|.
gi 1474250368 530 VIVVEHEEEII 540
Cdd:cd03292   189 VVVATHAKELV 199
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
807-927 3.33e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 59.48  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHN 886
Cdd:PRK13631  160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQ----PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1474250368 887 MD-VIRSADWVIDLGPeagergGRVVFEGTPADLMTCRESYT 927
Cdd:PRK13631  236 MEhVLEVADEVIVMDK------GKILKTGTPYEIFTDQHIIN 271
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
785-921 3.60e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 58.41  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 785 DLFAAYQDKDAINKkIIEKLMtLQDvglgyvKLGQSSSTLSGGESQRVKLA-SFLIKENAGGPI--LFIFDEPTTGLhfh 861
Cdd:PRK03695   96 DKTRTEAVASALNE-VAEALG-LDD------KLGRSVNQLSGGEWQRVRLAaVVLQVWPDINPAgqLLLLDEPMNSL--- 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 862 DIRKlLGAFDALLAR----GHTVVIVEHNMD-VIRSADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:PRK03695  165 DVAQ-QAALDRLLSElcqqGIAVVMSSHDLNhTLRHADRVWLL------KQGKLLASGRRDEVLT 222
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
817-926 3.71e-09

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 60.56  E-value: 3.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLIKeNAggPILfIFDEPTTGLhfhDI---RKLLGAFDALLaRGHTVVIVEHNMDVIRSA 893
Cdd:COG1132   470 VGERGVNLSGGQRQRIAIARALLK-DP--PIL-ILDEATSAL---DTeteALIQEALERLM-KGRTTIVIAHRLSTIRNA 541
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368 894 DWVIDLgpeageRGGRVVFEGTPADLMTCRESY 926
Cdd:COG1132   542 DRILVL------DDGRIVEQGTHEELLARGGLY 568
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
456-551 4.53e-09

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 57.52  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLR-DLGNTVIVVE 534
Cdd:COG4619   111 LELLERLGLPPDILDKPVERLSGGERQRLALIRAL--LLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVS 188
                          90
                  ....*....|....*...
gi 1474250368 535 H-EEEIIRAADTIIDIGP 551
Cdd:COG4619   189 HdPEQIERVADRVLTLEA 206
cbiO PRK13649
energy-coupling factor transporter ATPase;
810-919 5.79e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 58.22  E-value: 5.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 810 VGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNM-D 888
Cdd:PRK13649  132 VGISESLFEKNPFELSGGQMRRVAIAGILAME----PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdD 207
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1474250368 889 VIRSADWVIDLgpeageRGGRVVFEGTPADL 919
Cdd:PRK13649  208 VANYADFVYVL------EKGKLVLSGKPKDI 232
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
807-919 5.82e-09

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. 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: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 57.58  E-value: 5.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAF-DALLARGHTVVIVEH 885
Cdd:cd03256   129 LERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQ----PKLILADEPVASLDPASSRQVMDLLkRINREEGITVIVSLH 203
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474250368 886 NMDVIRS-ADWVIDLgpeageRGGRVVFEGTPADL 919
Cdd:cd03256   204 QVDLAREyADRIVGL------KDGRIVFDGPPAEL 232
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
813-920 6.27e-09

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 59.76  E-value: 6.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 813 GY-VKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhD---IRKLLGAFDALLARGHTVVIVEHNMD 888
Cdd:COG4618   456 GYdTRIGEGGARLSGGQRQRIGLARAL----YGDPRLVVLDEPNSNL---DdegEAALAAAIRALKARGATVVVITHRPS 528
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1474250368 889 VIRSADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:COG4618   529 LLAAVDKLLVL------RDGRVQAFGPRDEVL 554
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
469-571 6.48e-09

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). 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.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 57.06  E-value: 6.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 469 LDRLSSTLSGGESQRinLAtsLGSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEeeiIRAADTI 546
Cdd:cd03224   126 RKQLAGTLSGGEQQM--LA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQN---ARFALEI 198
                          90       100
                  ....*....|....*....|....*..
gi 1474250368 547 IDIgplaGY--QGGEVMFQGGIDRLAS 571
Cdd:cd03224   199 ADR----AYvlERGRVVLEGTAAELLA 221
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
456-549 7.11e-09

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 59.22  E-value: 7.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLT-LDRLSSTLSGGESQRINLATSLGSslVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDlGNTVIVVE 534
Cdd:TIGR02857 438 DEFVAALPQGLDTpIGEGGAGLSGGQAQRLALARAFLR--DAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVT 514
                          90
                  ....*....|....*
gi 1474250368 535 HEEEIIRAADTIIDI 549
Cdd:TIGR02857 515 HRLALAALADRIVVL 529
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
476-547 8.50e-09

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 56.04  E-value: 8.50e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474250368 476 LSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRD-LGNTVIVVEHE-EEIIRAADTII 547
Cdd:cd03229   101 LSGGQQQRVALARALAMD--PDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLADRVV 172
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
823-900 8.70e-09

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 56.50  E-value: 8.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 823 TLSGGESQRVKLASFLIKenagGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVI-RSADWVIDLG 900
Cdd:cd03226   126 SLSGGQKQRLAIAAALLS----GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLLA 200
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
458-547 9.11e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 57.94  E-value: 9.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 458 YLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE- 536
Cdd:PRK13631  159 YLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL--AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTm 236
                          90
                  ....*....|.
gi 1474250368 537 EEIIRAADTII 547
Cdd:PRK13631  237 EHVLEVADEVI 247
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
807-914 9.78e-09

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 55.90  E-value: 9.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLhfhDIR---KLLGAFDAL-LARGHTVVI 882
Cdd:cd03214    82 LELLGLAH-LADRPFNELSGGERQRVLLARALAQE----PPILLLDEPTSHL---DIAhqiELLELLRRLaRERGKTVVM 153
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368 883 VEHNMD-VIRSADWVIDLgpeageRGGRVVFEG 914
Cdd:cd03214   154 VLHDLNlAARYADRVILL------KDGRIVAQG 180
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
798-921 9.81e-09

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 57.09  E-value: 9.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 798 KKIIEKLMTLQDV-GLGyvklGQSSSTLSGGESQRVKLASFLI---KENAGGPILFIfDEPTTGL---HFHDIRKLLGAF 870
Cdd:PRK13548  112 DALVAAALAQVDLaHLA----GRDYPQLSGGEQQRVQLARVLAqlwEPDGPPRWLLL-DEPTSALdlaHQHHVLRLARQL 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 871 DAllARGHTVVIVEHNMDV-IRSADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:PRK13548  187 AH--ERGLAVIVVLHDLNLaARYADRIVLL------HQGRLVADGTPAEVLT 230
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
450-541 1.45e-08

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 56.90  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNR-LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN 528
Cdd:PRK10619  126 QEARERaVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL--AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK 203
                          90
                  ....*....|...
gi 1474250368 529 TVIVVEHEEEIIR 541
Cdd:PRK10619  204 TMVVVTHEMGFAR 216
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
824-899 1.53e-08

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). 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: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 55.08  E-value: 1.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 824 LSGGESQRVKLASFLIKENaggPILfIFDEPTTGLhfhDI---RKLLGAFDAlLARGHTVVIVEHNMDVIRSADWVIDL 899
Cdd:cd03228    97 LSGGQRQRIAIARALLRDP---PIL-ILDEATSAL---DPeteALILEALRA-LAKGKTVIVIAHRLSTIRDADRIIVL 167
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
451-547 1.78e-08

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 55.60  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-LEYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGN 528
Cdd:cd03259   106 EIRARvRELLELVGLEGL-LNRYPHELSGGQQQRVALARALARE--PSLLLLDEPLSALDAKLREELREELKELqRELGI 182
                          90       100
                  ....*....|....*....|
gi 1474250368 529 TVIVVEHE-EEIIRAADTII 547
Cdd:cd03259   183 TTIYVTHDqEEALALADRIA 202
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
817-926 1.80e-08

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 56.34  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLArGHTVVIVEHNMDVIRSADWV 896
Cdd:cd03252   132 VGEQGAGLSGGQRQRIAIARALIHN----PRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRI 206
                          90       100       110
                  ....*....|....*....|....*....|
gi 1474250368 897 IDLgpeageRGGRVVFEGTPADLMTCRESY 926
Cdd:cd03252   207 IVM------EKGRIVEQGSHDELLAENGLY 230
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
807-911 1.82e-08

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 55.82  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDAL-LARGHTVVIVEH 885
Cdd:COG1136   129 LERVGLGD-RLDHRPSQLSGGQQQRVAIARALVNR----PKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTH 203
                          90       100
                  ....*....|....*....|....*.
gi 1474250368 886 NMDVIRSADWVIDLgpeageRGGRVV 911
Cdd:COG1136   204 DPELAARADRVIRL------RDGRIV 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
812-910 1.82e-08

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 55.96  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 812 LGYVKLGQSS----STLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLA-RGHTVVIVEHN 886
Cdd:cd03255   125 LERVGLGDRLnhypSELSGGQQQRVAIARALAND----PKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD 200
                          90       100
                  ....*....|....*....|....
gi 1474250368 887 MDVIRSADWVIDLgpeageRGGRV 910
Cdd:cd03255   201 PELAEYADRIIEL------RDGKI 218
cbiO PRK13643
energy-coupling factor transporter ATPase;
795-919 1.87e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 56.67  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 795 AINKKIIEKLMT--LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDA 872
Cdd:PRK13643  114 GIPKEKAEKIAAekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAME----PEVLVLDEPTAGLDPKARIEMMQLFES 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1474250368 873 LLARGHTVVIVEHNM-DVIRSADWVIDLgpeageRGGRVVFEGTPADL 919
Cdd:PRK13643  190 IHQSGQTVVLVTHLMdDVADYADYVYLL------EKGHIISCGTPSDV 231
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
451-569 2.27e-08

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 56.02  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRLEYLNE-VGLGyLTLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNT 529
Cdd:COG4555   108 ELKKRIEELIElLGLE-EFLDRRVGELSTGMKKKVALARALVHD--PKVLLLDEPTNGLDVMARRLLREILRALKKEGKT 184
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1474250368 530 VIVVEHE-EEIIRAADTIIDIgplagyQGGEVMFQGGIDRL 569
Cdd:COG4555   185 VLFSSHImQEVEALCDRVVIL------HKGKVVAQGSLDEL 219
cbiO PRK13637
energy-coupling factor transporter ATPase;
451-547 2.50e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 56.59  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRL-EYLNEVGLGYLTL-DRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRD-LG 527
Cdd:PRK13637  118 EIENRVkRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVV--AMEPKILILDEPTAGLDPKGRDEILNKIKELHKeYN 195
                          90       100
                  ....*....|....*....|.
gi 1474250368 528 NTVIVVEHE-EEIIRAADTII 547
Cdd:PRK13637  196 MTIILVSHSmEDVAKLADRII 216
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
805-899 2.64e-08

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 57.81  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 805 MTLQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIkeNAGGPILFifDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVE 884
Cdd:PRK10535  127 ELLQRLGLED-RVEYQPSQLSGGQQQRVSIARALM--NGGQVILA--DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVT 201
                          90
                  ....*....|....*
gi 1474250368 885 HNMDVIRSADWVIDL 899
Cdd:PRK10535  202 HDPQVAAQAERVIEI 216
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
786-911 2.70e-08

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 55.44  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 786 LFAAYQDKDAINKKIIEklmTLQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRK 865
Cdd:COG2884   104 LRVTGKSRKEIRRRVRE---VLDLVGLSD-KAKALPHELSGGEQQRVAIARALVNR----PELLLADEPTGNLDPETSWE 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1474250368 866 LLGAFDALLARGHTVVIVEHNMDVIRSADW-VIDLgpeageRGGRVV 911
Cdd:COG2884   176 IMELLEEINRRGTTVLIATHDLELVDRMPKrVLEL------EDGRLV 216
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
791-921 3.33e-08

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 55.76  E-value: 3.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 791 QDKDAINKkiieklmTLQDVGLGYVKlGQSSSTLSGGESQRVKLASFLIKENAggpiLFIFDEPTTGL---HFHDIRKLL 867
Cdd:PRK10253  119 EDEEAVTK-------AMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQETA----IMLLDEPTTWLdisHQIDLLELL 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 868 GAFDAllARGHTVVIVEHNMD-VIRSADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:PRK10253  187 SELNR--EKGYTLAAVLHDLNqACRYASHLIAL------REGKIVAQGAPKEIVT 233
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
824-897 4.45e-08

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 53.56  E-value: 4.45e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRS-ADWVI 897
Cdd:cd03230    96 LSGGMKQRLALAQALLHD----PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVA 166
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
434-542 4.66e-08

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 55.03  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 434 GLRLDDRDGKTVARVLTEIRNRLeylnevGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDT 513
Cdd:cd03299    95 GLKKRKVDKKEIERKVLEIAEML------GIDHL-LNRKPETLSGGEQQRVAIARAL--VVNPKILLLDEPFSALDVRTK 165
                          90       100       110
                  ....*....|....*....|....*....|
gi 1474250368 514 NRLIAVLKKLRD-LGNTVIVVEHEEEIIRA 542
Cdd:cd03299   166 EKLREELKKIRKeFGVTVLHVTHDFEEAWA 195
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
451-569 4.93e-08

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. 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: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 54.88  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRLEYLNEVGLGYLTLDRlSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNT 529
Cdd:cd03256   121 EKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIARALMQQ--PKLILADEPVASLDPASSRQVMDLLKRInREEGIT 197
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1474250368 530 VIVVEHEEEIIRA-ADTIIdigplaGYQGGEVMFQGGIDRL 569
Cdd:cd03256   198 VIVSLHQVDLAREyADRIV------GLKDGRIVFDGPPAEL 232
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
425-535 5.65e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 56.74  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 425 VDELQRFFDGlrlddrdgkTVARVLTEI--RNRL-EYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYIL 501
Cdd:PRK13409  169 VDLIPKVFKG---------KVRELLKKVdeRGKLdEVVERLGLENI-LDRDISELSGGELQRVAIAAAL--LRDADFYFF 236
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1474250368 502 DEPSIGLhprDTNRLIAVLKKLRDL--GNTVIVVEH 535
Cdd:PRK13409  237 DEPTSYL---DIRQRLNVARLIRELaeGKYVLVVEH 269
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
474-573 5.78e-08

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 56.69  E-value: 5.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 474 STLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDlGNTVIVVEHEEEIIRAADTIIDIgpla 553
Cdd:COG4988   472 RGLSGGQAQRLALARALLRD--APLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILVL---- 544
                          90       100
                  ....*....|....*....|
gi 1474250368 554 gyQGGEVMFQGGIDRLASAK 573
Cdd:COG4988   545 --DDGRIVEQGTHEELLAKN 562
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
824-920 6.94e-08

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 56.37  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKenagGPILFIFDEPTTGLHFHDIRKLLGAFDAlLARGHTVVIVEHNMDVIRSADWVIDLgpea 903
Cdd:COG5265   495 LSGGEKQRVAIARTLLK----NPPILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVDADEILVL---- 565
                          90
                  ....*....|....*..
gi 1474250368 904 geRGGRVVFEGTPADLM 920
Cdd:COG5265   566 --EAGRIVERGTHAELL 580
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
476-564 8.84e-08

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: 53.32  E-value: 8.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 476 LSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE--EEIIRAADTIIDIGPla 553
Cdd:cd03213   112 LSGGERKRVSIALELVSN--PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpsSEIFELFDKLLLLSQ-- 187
                          90
                  ....*....|.
gi 1474250368 554 gyqgGEVMFQG 564
Cdd:cd03213   188 ----GRVIYFG 194
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
778-914 9.10e-08

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 53.74  E-value: 9.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 778 LTVDAAVDLFAAYQ---DKDAinKKIIEklMTLQDVGLGYVKlGQSSSTLSGGESQRVKLASFLIkenaGGPILFIFDEP 854
Cdd:cd03264    87 FTVREFLDYIAWLKgipSKEV--KARVD--EVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALV----GDPSILIVDEP 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474250368 855 TTGL---HFHDIRKLLGAfdalLARGHTVVIVEHNM-DVIRSADWVIDLgpeageRGGRVVFEG 914
Cdd:cd03264   158 TAGLdpeERIRFRNLLSE----LGEDRIVILSTHIVeDVESLCNQVAVL------NKGKLVFEG 211
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
822-921 9.14e-08

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 54.25  E-value: 9.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 822 STLSGGESQRVKLASFLIKENaggPILFIfDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVIDLg 900
Cdd:PRK11231  137 TDLSGGQRQRAFLAMVLAQDT---PVVLL-DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVL- 211
                          90       100
                  ....*....|....*....|.
gi 1474250368 901 peageRGGRVVFEGTPADLMT 921
Cdd:PRK11231  212 -----ANGHVMAQGTPEEVMT 227
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
425-535 1.04e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 55.56  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 425 VDELQRFFDGlrlddrdgkTVARVLTEI--RNRLEYLNE-VGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYIL 501
Cdd:COG1245   169 VDLIPKVFKG---------TVRELLEKVdeRGKLDELAEkLGLENI-LDRDISELSGGELQRVAIAAAL--LRDADFYFF 236
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1474250368 502 DEPSIGLhprDTNRLIAVLKKLRDL---GNTVIVVEH 535
Cdd:COG1245   237 DEPSSYL---DIYQRLNVARLIRELaeeGKYVLVVEH 270
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
822-920 1.15e-07

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 54.84  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 822 STLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMdvirsadwvidlgp 901
Cdd:PRK13536  171 SDLSGGMKRRLTLARALIND----PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFM-------------- 232
                          90       100
                  ....*....|....*....|....*...
gi 1474250368 902 EAGER---------GGRVVFEGTPADLM 920
Cdd:PRK13536  233 EEAERlcdrlcvleAGRKIAEGRPHALI 260
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
798-921 1.40e-07

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 53.97  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 798 KKIIEKLmtLQDVGL-GYVKlgQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhD----------IRKL 866
Cdd:TIGR04520 114 RKRVDEA--LKLVGMeDFRD--REPHLLSGGQKQRVAIAGVL----AMRPDIIILDEATSML---DpkgrkevletIRKL 182
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 867 LGafdallARGHTVVIVEHNMDVIRSADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:TIGR04520 183 NK------EEGITVISITHDMEEAVLADRVIVM------NKGKIVAEGTPREIFS 225
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
476-547 1.42e-07

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). 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: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 52.39  E-value: 1.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 476 LSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDlGNTVIVVEHEEEIIRAADTII 547
Cdd:cd03228    97 LSGGQRQRIAIARALLRD--PPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRII 165
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
441-547 1.46e-07

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 52.40  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 441 DGKTVARVLTEIRNRLEYLNEVGLGYltlDRLSS----TLSGGESQRINLAtslgSSLVG--SLYILDEPSIGLHPRDTN 514
Cdd:cd03230    60 LGKDIKKEPEEVKRRIGYLPEEPSLY---ENLTVrenlKLSGGMKQRLALA----QALLHdpELLILDEPTSGLDPESRR 132
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1474250368 515 RLIAVLKKLRDLGNTVIVVEH-EEEIIRAADTII 547
Cdd:cd03230   133 EFWELLRELKKEGKTILLSSHiLEEAERLCDRVA 166
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
782-921 2.02e-07

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 53.16  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 782 AAVDLFAAYQDKDainKKIIEKLMTLqdVGLGYVKlGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFH 861
Cdd:COG1119   107 DSIGLYREPTDEQ---RERARELLEL--LGLAHLA-DRPFGTLSQGEQRRVLIARALVKD----PELLILDEPTAGLDLG 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 862 DIRKLLGAFDALLARGHTVVI-VEHNM-DVIRSADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:COG1119   177 ARELLLALLDKLAAEGAPTLVlVTHHVeEIPPGITHVLLL------KDGRVVAAGPKEEVLT 232
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
818-934 2.11e-07

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 54.58  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 818 GQSSSTLSGGESQRVKLASFLIKeNAggPILfIFDEPTTGLHFHDIRKLLGAFDALLaRGHTVVIVEHNMDVIRSADWVI 897
Cdd:PRK13657  466 GERGRQLSGGERQRLAIARALLK-DP--PIL-ILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRIL 540
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1474250368 898 DLgpeageRGGRVVFEGTPADLMtcreSYTGKFLSLA 934
Cdd:PRK13657  541 VF------DNGRVVESGSFDELV----ARGGRFAALL 567
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
792-899 2.14e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 54.81  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEKLmtlqdvGLGYVkLGQSSSTLSGGESQRVKLASFLIKENAggpiLFIFDEPTTGLhfhDIRKLLGAFD 871
Cdd:PRK13409  188 DERGKLDEVVERL------GLENI-LDRDISELSGGELQRVAIAAALLRDAD----FYFFDEPTSYL---DIRQRLNVAR 253
                          90       100       110
                  ....*....|....*....|....*....|
gi 1474250368 872 AL--LARGHTVVIVEHNMDVIrsaDWVIDL 899
Cdd:PRK13409  254 LIreLAEGKYVLVVEHDLAVL---DYLADN 280
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
779-920 3.40e-07

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 52.50  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 779 TVDAAVDLFAAYQDKDAINKKIIEKLmtlQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGL 858
Cdd:COG1124    97 TVDRILAEPLRIHGLPDREERIAELL---EQVGLPPSFLDRYPHQLSGGQRQRVAIARALILE----PELLLLDEPTSAL 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 859 hfhDI---RKLLGAFDALLA-RGHTVVIVEHNMDVI-RSADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:COG1124   170 ---DVsvqAEILNLLKDLREeRGLTYLFVSHDLAVVaHLCDRVAVM------QNGRIVEELTVADLL 227
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
476-549 3.40e-07

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 51.06  E-value: 3.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 476 LSGGESQRINLATSL-GSSlvgSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDI 549
Cdd:cd03246    97 LSGGQRQRLGLARALyGNP---RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
cbiO PRK13641
energy-coupling factor transporter ATPase;
807-938 3.67e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 52.91  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHN 886
Cdd:PRK13641  129 LKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYE----PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN 204
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 887 M-DVIRSADWVIDLgpeageRGGRVVFEGTPADLMTCRESYTGKFLSLAENSR 938
Cdd:PRK13641  205 MdDVAEYADDVLVL------EHGKLIKHASPKEIFSDKEWLKKHYLDEPATSR 251
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
807-932 3.81e-07

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 52.30  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGyVKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhD---IRKLLGAFDALLARGHTVVIV 883
Cdd:COG1126   121 LERVGLA-DKADAYPAQLSGGQQQRVAIARAL----AMEPKVMLFDEPTSAL---DpelVGEVLDVMRDLAKEGMTMVVV 192
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 884 EHNMDVIRS-ADWVI--DlgpeagerGGRVVFEGTPADLMT-CRESYTGKFLS 932
Cdd:COG1126   193 THEMGFAREvADRVVfmD--------GGRIVEEGPPEEFFEnPQHERTRAFLS 237
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
798-924 3.93e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 52.69  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 798 KKIIEKLMtlQDVGLGYVkLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLH---FHDIRKLLgafDALL 874
Cdd:PRK13632  120 KDIIDDLA--KKVGMEDY-LDKEPQNLSGGQKQRVAIASVL----ALNPEIIIFDESTSMLDpkgKREIKKIM---VDLR 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1474250368 875 ARGH-TVVIVEHNMDVIRSADWVIDLGpeagerGGRVVFEGTPADLMTCRE 924
Cdd:PRK13632  190 KTRKkTLISITHDMDEAILADKVIVFS------EGKLIAQGKPKEILNNKE 234
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
807-901 4.02e-07

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 51.74  E-value: 4.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLAR-GHTVVIVEH 885
Cdd:COG4619   114 LERLGLPPDILDKPVERLSGGERQRLALIRALLLQ----PDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSH 189
                          90
                  ....*....|....*..
gi 1474250368 886 NMDVI-RSADWVIDLGP 901
Cdd:COG4619   190 DPEQIeRVADRVLTLEA 206
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
789-919 4.48e-07

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. 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: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 51.81  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 789 AYQDKDAINKKIIEklmTLQDVGLGYvKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLH---FHDIRK 865
Cdd:cd03258   110 AGVPKAEIEERVLE---LLELVGLED-KADAYPAQLSGGQKQRVGIARAL----ANNPKVLLCDEATSALDpetTQSILA 181
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 866 LLGAFDALLarGHTVVIVEHNMDVIRS-ADWVIDLGpeagerGGRVVFEGTPADL 919
Cdd:cd03258   182 LLRDINREL--GLTIVLITHEMEVVKRiCDRVAVME------KGEVVEEGTVEEV 228
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
823-914 4.71e-07

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 51.51  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 823 TLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVIDLgp 901
Cdd:cd03269   128 ELSKGNQQKVQFIAAVIHD----PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMElVEELCDRVLLL-- 201
                          90
                  ....*....|...
gi 1474250368 902 eageRGGRVVFEG 914
Cdd:cd03269   202 ----NKGRAVLYG 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
451-589 4.96e-07

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 53.37  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRD-LGN 528
Cdd:COG1123   379 ERRERvAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL--ALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGL 456
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 529 TVIVVEHEEEIIRA-ADTIIDIgplagyQGGEVMFQGGIDR-LASAKDSLTAKYLTGVERIEP 589
Cdd:COG1123   457 TYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEvFANPQHPYTRALLAAVPSLDP 513
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
807-921 5.85e-07

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 51.63  E-value: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHN 886
Cdd:PRK09493  121 LAKVGLAE-RAHHYPSELSGGQQQRVAIARAL----AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1474250368 887 MDVIRsadwvidlgpEAGER-----GGRVVFEGTPADLMT 921
Cdd:PRK09493  196 IGFAE----------KVASRlifidKGRIAEDGDPQVLIK 225
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
807-920 6.08e-07

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 51.89  E-value: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHN 886
Cdd:PRK10619  136 LAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME----PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474250368 887 MDVIRS-ADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:PRK10619  212 MGFARHvSSHVIFL------HQGKIEEEGAPEQLF 240
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
451-542 6.73e-07

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. 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: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 51.43  E-value: 6.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-LEYLNEVGLGYLTlDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGN 528
Cdd:cd03258   116 EIEERvLELLELVGLEDKA-DAYPAQLSGGQKQRVGIARALANN--PKVLLCDEATSALDPETTQSILALLRDInRELGL 192
                          90
                  ....*....|....
gi 1474250368 529 TVIVVEHEEEIIRA 542
Cdd:cd03258   193 TIVLITHEMEVVKR 206
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
441-564 1.02e-06

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 50.00  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 441 DGKTVARVLTEIRNRLEYLN-EVGLGYLTL-DRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIA 518
Cdd:cd03247    62 DGVPVSDLEKALSSLISVLNqRPYLFDTTLrNNLGRRFSGGERQRLALARILLQD--APIVLLDEPTVGLDPITERQLLS 139
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1474250368 519 -VLKKLRDlgNTVIVVEHEEEIIRAADTIIDIgplagyQGGEVMFQG 564
Cdd:cd03247   140 lIFEVLKD--KTLIWITHHLTGIEHMDKILFL------ENGKIIMQG 178
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
453-566 1.04e-06

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 50.58  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 453 RNRLEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRD-LGNTVI 531
Cdd:cd03257   123 EAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL--ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLL 200
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1474250368 532 VVEHEEEIIRA-ADTIIdigplagyqggeVMFQGGI 566
Cdd:cd03257   201 FITHDLGVVAKiADRVA------------VMYAGKI 224
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
457-536 1.06e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 51.63  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSLvgSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE 536
Cdd:PRK13651  147 KYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEP--DFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
475-551 1.11e-06

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: 50.30  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 475 TLSGGE------SQRINLATSLGSSLvgSLYILDEPSIGLHP-RDTNRLIAVLKKLRDLGN-TVIVVEHEEEIIRAADTI 546
Cdd:cd03240   115 RCSGGEkvlaslIIRLALAETFGSNC--GILALDEPTTNLDEeNIEESLAEIIEERKSQKNfQLIVITHDEELVDAADHI 192

                  ....*
gi 1474250368 547 IDIGP 551
Cdd:cd03240   193 YRVEK 197
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
464-573 1.11e-06

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 52.53  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 464 LGYLTL--DRlSSTLSGGESQRINLATslgsSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKLRDlGNTVIVVEHEEEI 539
Cdd:COG2274   599 MGYDTVvgEG-GSNLSGGQRQRLAIAR----ALLRnpRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLST 672
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1474250368 540 IRAADTIIDIgplagyQGGEVMFQGGIDRLASAK 573
Cdd:COG2274   673 IRLADRIIVL------DKGRIVEDGTHEELLARK 700
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
434-557 1.13e-06

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. 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: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 50.57  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 434 GLRLDDRDGKTVARVLTEirnrleylneVGLGYLTLdRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDT 513
Cdd:cd03298    98 GLKLTAEDRQAIEVALAR----------VGLAGLEK-RLPGELSGGERQRVALARVLVRD--KPVLLLDEPFAALDPALR 164
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1474250368 514 NRLIAVLKKL-RDLGNTVIVVEHE-EEIIRAADTII--DIGPLAgYQG 557
Cdd:cd03298   165 AEMLDLVLDLhAETKMTVLMVTHQpEDAKRLAQRVVflDNGRIA-AQG 211
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
813-920 1.41e-06

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. 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: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 50.31  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 813 GY-VKLGQSSSTLSGGESQRVKLASFLIKEnagGPILfIFDEPTTGLHFHDIRKLLGAFDALLArGHTVVIVEHNMDVIR 891
Cdd:cd03251   127 GYdTVIGERGVKLSGGQRQRIAIARALLKD---PPIL-ILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIE 201
                          90       100
                  ....*....|....*....|....*....
gi 1474250368 892 SADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:cd03251   202 NADRIVVL------EDGKIVERGTHEELL 224
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
457-574 1.49e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 51.17  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEH 535
Cdd:PRK13634  127 EMIELVGLPEELLARSPFELSGGQMRRVAIAGVL--AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTH 204
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1474250368 536 E-EEIIRAADTIIdigplagyqggeVMFQGGIDRLASAKD 574
Cdd:PRK13634  205 SmEDAARYADQIV------------VMHKGTVFLQGTPRE 232
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
819-921 1.64e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 51.38  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 819 QSSSTLSGGESQRVKLASFLIKENaggPILfIFDEPTTGLHF-HDIRKLLGAFDaLLARGHTVVIVEHNMDV-IRSADWV 896
Cdd:PRK09536  135 RPVTSLSGGERQRVLLARALAQAT---PVL-LLDEPTASLDInHQVRTLELVRR-LVDDGKTAVAAIHDLDLaARYCDEL 209
                          90       100
                  ....*....|....*....|....*
gi 1474250368 897 IDLGpeagerGGRVVFEGTPADLMT 921
Cdd:PRK09536  210 VLLA------DGRVRAAGPPADVLT 228
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
807-897 1.67e-06

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 49.84  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHN 886
Cdd:cd03262   120 LEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMN----PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
                          90
                  ....*....|..
gi 1474250368 887 MDVIRS-ADWVI 897
Cdd:cd03262   195 MGFAREvADRVI 206
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
811-921 1.79e-06

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 51.77  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 811 GLGYVkLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDAlLARGHTVVIVEHNMDVI 890
Cdd:PRK11174  474 GLDTP-IGDQAAGLSVGQAQRLALARALLQP----CQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDL 547
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368 891 RSAD--WVIDlgpeagerGGRVVFEGTPADLMT 921
Cdd:PRK11174  548 AQWDqiWVMQ--------DGQIVQQGDYAELSQ 572
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
823-920 2.49e-06

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 50.17  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 823 TLSGGESQRVKLAsFLIKENAGGPILfifDEPTTGL---HFHDIRKLLGAFDALlaRGHTVVIVEHNMDVI-RSADWVID 898
Cdd:PRK10575  147 SLSGGERQRAWIA-MLVAQDSRCLLL---DEPTSALdiaHQVDVLALVHRLSQE--RGLTVIAVLHDINMAaRYCDYLVA 220
                          90       100
                  ....*....|....*....|..
gi 1474250368 899 LgpeageRGGRVVFEGTPADLM 920
Cdd:PRK10575  221 L------RGGEMIAQGTPAELM 236
cbiO PRK13646
energy-coupling factor transporter ATPase;
807-919 2.58e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 50.16  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDAL-LARGHTVVIVEH 885
Cdd:PRK13646  129 LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL----AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSH 204
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474250368 886 NM-DVIRSADWVIDLgpeageRGGRVVFEGTPADL 919
Cdd:PRK13646  205 DMnEVARYADEVIVM------KEGSIVSQTSPKEL 233
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
451-564 2.67e-06

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. 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, 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: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 49.61  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-LEYLNEVGLGYLTL-DRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLG 527
Cdd:cd03295   109 KIRERaDELLALVGLDPAEFaDRYPHELSGGQQQRVGVARALAAD--PPLLLMDEPFGALDPITRDQLQEEFKRLqQELG 186
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1474250368 528 NTVIVVEHE-EEIIRAADTIidigplAGYQGGEVMFQG 564
Cdd:cd03295   187 KTIVFVTHDiDEAFRLADRI------AIMKNGEIVQVG 218
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
824-921 3.11e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 49.80  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLAR-GHTVVIVEHNMDVIRS-ADWVIDLgp 901
Cdd:PRK13652  138 LSGGEKKRVAIAGVIAME----PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEmADYIYVM-- 211
                          90       100
                  ....*....|....*....|
gi 1474250368 902 eageRGGRVVFEGTPADLMT 921
Cdd:PRK13652  212 ----DKGRIVAYGTVEEIFL 227
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
469-536 3.32e-06

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 49.33  E-value: 3.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 469 LDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLhprDTNRLIAVLKKLRDLG----NTVIVVEHE 536
Cdd:cd03237   109 LDREVPELSGGELQRVAIAACLSKD--ADIYLLDEPSAYL---DVEQRLMASKVIRRFAenneKTAFVVEHD 175
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
459-584 3.33e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 49.71  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 459 LNEVGLGYLTLDRLSST---LSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:PRK14271  144 LTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVN--PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHN 221
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1474250368 536 EEEIIRAADTIidigplAGYQGGEVMFQGGIDRL-ASAKDSLTAKYLTGV 584
Cdd:PRK14271  222 LAQAARISDRA------ALFFDGRLVEEGPTEQLfSSPKHAETARYVAGL 265
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
450-547 3.42e-06

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 48.82  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNR-LEYLNEVGLGYLTLDRLSsTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN 528
Cdd:cd03269   103 EEARRRiDEWLERLELSEYANKRVE-ELSKGNQQKVQFIAAVIHD--PELLILDEPFSGLDPVNVELLKDVIRELARAGK 179
                          90       100
                  ....*....|....*....|
gi 1474250368 529 TVIVVEHE-EEIIRAADTII 547
Cdd:cd03269   180 TVILSTHQmELVEELCDRVL 199
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
824-914 3.74e-06

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 48.90  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVIDLgpe 902
Cdd:cd03266   137 FSTGMRQKVAIARALVHD----PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVL--- 209
                          90
                  ....*....|..
gi 1474250368 903 ageRGGRVVFEG 914
Cdd:cd03266   210 ---HRGRVVYEG 218
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
822-918 4.89e-06

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 50.03  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 822 STLSGGESQRVKLasflIKENAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVIDLg 900
Cdd:COG3845   140 EDLSVGEQQRVEI----LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLReVMAIADRVTVL- 214
                          90
                  ....*....|....*...
gi 1474250368 901 peageRGGRVVFEGTPAD 918
Cdd:COG3845   215 -----RRGKVVGTVDTAE 227
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
425-536 5.09e-06

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 48.90  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 425 VDELQRFFDGLRLDDRDGKTVARVLTEIRNRLEyLNEVglgyltLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEP 504
Cdd:cd03236    96 VDLIPKAVKGKVGELLKKKDERGKLDELVDQLE-LRHV------LDRNIDQLSGGELQRVAIAAALARD--ADFYFFDEP 166
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1474250368 505 SIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE 536
Cdd:cd03236   167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
cbiO PRK13645
energy-coupling factor transporter ATPase;
457-590 5.21e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 49.24  E-value: 5.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEH 535
Cdd:PRK13645  132 ELLKLVQLPEDYVKRSPFELSGGQKRRVALAGII--AMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTH 209
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1474250368 536 E-EEIIRAADTIIdigplagyqggeVMFQGGIDRLASAKDSLTAKYLTGVERIEPP 590
Cdd:PRK13645  210 NmDQVLRIADEVI------------VMHEGKVISIGSPFEIFSNQELLTKIEIDPP 253
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
824-897 5.92e-06

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 47.57  E-value: 5.92e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHF---HDIRKLLGAFDALLarGHTVVIVEHNMD-VIRSADWVI 897
Cdd:cd03229   101 LSGGQQQRVALARALAMD----PDVLLLDEPTSALDPitrREVRALLKSLQAQL--GITVVLVTHDLDeAARLADRVV 172
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
456-590 6.59e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 48.83  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN-TVIVVE 534
Cdd:PRK13632  124 DDLAKKVGMEDY-LDKEPQNLSGGQKQRVAIASVL--ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISIT 200
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 535 HE-EEIIRaADTIIdigplagyqggeVMFQGGIDRLASAKDSLTAKYLTGVERIEPP 590
Cdd:PRK13632  201 HDmDEAIL-ADKVI------------VFSEGKLIAQGKPKEILNNKEILEKAKIDSP 244
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
457-547 6.73e-06

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 48.06  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEH 535
Cdd:cd03297   114 ELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQ--PELLLLDEPFSALDRALRLQLLPELKQIkKNLNIPVIFVTH 190
                          90
                  ....*....|...
gi 1474250368 536 E-EEIIRAADTII 547
Cdd:cd03297   191 DlSEAEYLADRIV 203
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
797-897 8.02e-06

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 47.95  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 797 NKKIIEKLM--TLQDVGL-GYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFH---DIRKLLGAf 870
Cdd:cd03260   112 LKEELDERVeeALRKAALwDEVKDRLHALGLSGGQQQRLCLARALANE----PEVLLLDEPTSALDPIstaKIEELIAE- 186
                          90       100
                  ....*....|....*....|....*...
gi 1474250368 871 dalLARGHTVVIVEHNM-DVIRSADWVI 897
Cdd:cd03260   187 ---LKKEYTIVIVTHNMqQAARVADRTA 211
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
457-540 8.68e-06

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 48.16  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLtLDRLSSTLSGGESQRINLAtslgSSLVGS--LYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVI--V 532
Cdd:COG1119   125 ELLELLGLAHL-ADRPFGTLSQGEQRRVLIA----RALVKDpeLLILDEPTAGLDLGARELLLALLDKLAAEGAPTLvlV 199

                  ....*...
gi 1474250368 533 VEHEEEII 540
Cdd:COG1119   200 THHVEEIP 207
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
469-546 8.77e-06

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 49.25  E-value: 8.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 469 LDRLSSTLSGGESQRINL--ATSLGSSLVgslyILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE-EEIIRAADT 545
Cdd:COG3845   135 PDAKVEDLSVGEQQRVEIlkALYRGARIL----ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKlREVMAIADR 210

                  .
gi 1474250368 546 I 546
Cdd:COG3845   211 V 211
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
817-920 9.19e-06

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). 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: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 47.99  E-value: 9.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLaRGHTVVIVEHNMDVIRSADWV 896
Cdd:cd03254   133 LGENGGNLSQGERQLLAIARAMLRD----PKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKI 207
                          90       100
                  ....*....|....*....|....
gi 1474250368 897 IDLgpeageRGGRVVFEGTPADLM 920
Cdd:cd03254   208 LVL------DDGKIIEEGTHDELL 225
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
807-921 1.00e-05

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. 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, 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: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 48.07  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQS-SSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGL----------HFHDIRKLLgafdalla 875
Cdd:cd03295   118 LALVGLDPAEFADRyPHELSGGQQQRVGVARAL----AADPPLLLMDEPFGALdpitrdqlqeEFKRLQQEL-------- 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1474250368 876 rGHTVVIVEHNMD-VIRSADWVIDLGpeagerGGRVVFEGTPADLMT 921
Cdd:cd03295   186 -GKTIVFVTHDIDeAFRLADRIAIMK------NGEIVQVGTPDEILR 225
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
798-899 1.01e-05

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.40  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 798 KKIIEKLmtlqdvGLGYVkLGQSSSTLSGGESQRVKLASFLIKEnAGgpiLFIFDEPTTGLhfhDIRKLLGAFDAL--LA 875
Cdd:COG1245   194 DELAEKL------GLENI-LDRDISELSGGELQRVAIAAALLRD-AD---FYFFDEPSSYL---DIYQRLNVARLIreLA 259
                          90       100
                  ....*....|....*....|....*
gi 1474250368 876 R-GHTVVIVEHNMDVIrsaDWVIDL 899
Cdd:COG1245   260 EeGKYVLVVEHDLAIL---DYLADY 281
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
457-546 1.14e-05

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 48.86  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGyLTLDRLSSTLSGGESQRINL--ATSLGSSLVgslyILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVE 534
Cdd:COG1129   123 ELLARLGLD-IDPDTPVGDLSVAQQQLVEIarALSRDARVL----ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIS 197
                          90
                  ....*....|...
gi 1474250368 535 HE-EEIIRAADTI 546
Cdd:COG1129   198 HRlDEVFEIADRV 210
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
807-918 1.20e-05

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 47.43  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKENAggpILFIfDEPTTGLHFHD---IRKLLgaFDALLARGHTVVIV 883
Cdd:COG4181   131 LERVGLGH-RLDHYPAQLSGGEQQRVALARAFATEPA---ILFA-DEPTGNLDAATgeqIIDLL--FELNRERGTTLVLV 203
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474250368 884 EHNMDVIRSADWVIDLgpeageRGGRVVfEGTPAD 918
Cdd:COG4181   204 THDPALAARCDRVLRL------RAGRLV-EDTAAT 231
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
824-916 1.22e-05

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 49.28  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLH----FHDIRKLLGafdaLLARGHTVVIVEH--NMDVIRSADWVI 897
Cdd:TIGR00955 167 LSGGERKRLAFASELLTD----PPLLFCDEPTSGLDsfmaYSVVQVLKG----LAQKGKTIICTIHqpSSELFELFDKII 238
                          90
                  ....*....|....*....
gi 1474250368 898 DLGpeagerGGRVVFEGTP 916
Cdd:TIGR00955 239 LMA------EGRVAYLGSP 251
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
824-914 1.25e-05

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: 47.16  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEH--NMDVIRSADWVIDLGP 901
Cdd:cd03213   112 LSGGERKRVSIALELVSN----PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpSSEIFELFDKLLLLSQ 187
                          90
                  ....*....|...
gi 1474250368 902 eagergGRVVFEG 914
Cdd:cd03213   188 ------GRVIYFG 194
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
824-916 1.40e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 47.77  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLAR-GHTVVIVEHNMDVIRSADWVIDLGpe 902
Cdd:PRK13633  145 LSGGQKQRVAIAGIL----AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMD-- 218
                          90
                  ....*....|....
gi 1474250368 903 agerGGRVVFEGTP 916
Cdd:PRK13633  219 ----SGKVVMEGTP 228
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
474-551 1.42e-05

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 47.43  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 474 STLSGGESQRINLAtslgSSLVGS--LYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRA-ADTIIDIG 550
Cdd:COG4778   151 ATFSGGEQQRVNIA----RGFIADppLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVT 226

                  .
gi 1474250368 551 P 551
Cdd:COG4778   227 P 227
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
470-564 1.42e-05

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 47.70  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 470 DRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLhprDTNR---LIAVLKKLRDLGNTVIVVEHE-EEIIRAADT 545
Cdd:PRK11231  133 DRRLTDLSGGQRQRAFLAMVLAQD--TPVVLLDEPTTYL---DINHqveLMRLMRELNTQGKTVVTVLHDlNQASRYCDH 207
                          90
                  ....*....|....*....
gi 1474250368 546 iidigpLAGYQGGEVMFQG 564
Cdd:PRK11231  208 ------LVVLANGHVMAQG 220
cbiO PRK13644
energy-coupling factor transporter ATPase;
450-547 1.48e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 47.67  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNRLEY-LNEVGLGYLTlDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN 528
Cdd:PRK13644  111 IEIRKRVDRaLAEIGLEKYR-HRSPKTLSGGQGQCVALAGIL--TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK 187
                          90
                  ....*....|....*....
gi 1474250368 529 TVIVVEHEEEIIRAADTII 547
Cdd:PRK13644  188 TIVYITHNLEELHDADRII 206
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
801-907 1.54e-05

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 48.86  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 801 IEKLmtlqDVGLGYVkLGQSSSTLSGGESQRVKLASFLIKEnagGPILfIFDEPTTGLHFHDIRKLLGAFDAlLARGHTV 880
Cdd:PRK11176  463 INKM----DNGLDTV-IGENGVLLSGGQRQRIAIARALLRD---SPIL-ILDEATSALDTESERAIQAALDE-LQKNRTS 532
                          90       100
                  ....*....|....*....|....*....
gi 1474250368 881 VIVEHNMDVIRSAD--WVIDLGpEAGERG 907
Cdd:PRK11176  533 LVIAHRLSTIEKADeiLVVEDG-EIVERG 560
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
476-540 1.62e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 47.69  E-value: 1.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 476 LSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEII 540
Cdd:PRK13638  137 LSHGQKKRVAIAGAL--VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
792-938 1.65e-05

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 48.15  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEkLMTLqdVGLGYvKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLgafd 871
Cdd:COG1135   113 PKAEIRKRVAE-LLEL--VGLSD-KADAYPSQLSGGQKQRVGIARAL----ANNPKVLLCDEATSALDPETTRSIL---- 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474250368 872 ALLAR-----GHTVVIVEHNMDVIRS-ADWV--IDlgpeagerGGRVVFEGTPADLMTCRESYTGK-FLSLAENSR 938
Cdd:COG1135   181 DLLKDinrelGLTIVLITHEMDVVRRiCDRVavLE--------NGRIVEQGPVLDVFANPQSELTRrFLPTVLNDE 248
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
470-541 1.65e-05

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 47.32  E-value: 1.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 470 DRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIR 541
Cdd:PRK11124  136 DRFPLHLSGGQQQRVAIARAL--MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVAR 205
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
450-574 1.71e-05

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). 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: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 47.33  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNRL-EYLNEVGLGYLTlDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRD-LG 527
Cdd:cd03296   111 AEIRAKVhELLKLVQLDWLA-DRYPAQLSGGQRQRVALARAL--AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDeLH 187
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1474250368 528 NTVIVVEH-EEEIIRAADTIIdigplagyqggeVMFQGGIDRLASAKD 574
Cdd:cd03296   188 VTTVFVTHdQEEALEVADRVV------------VMNKGRIEQVGTPDE 223
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
451-591 1.75e-05

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 47.77  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-LEYLNEVGLGyltlDRLS---STLSGGESQRINLAtslgSSLVGSLYIL--DEPSIGLHPRDTNRLIAVLKKL- 523
Cdd:COG1135   116 EIRKRvAELLELVGLS----DKADaypSQLSGGQKQRVGIA----RALANNPKVLlcDEATSALDPETTRSILDLLKDIn 187
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 524 RDLGNTVIVVEHEEEIIRA-AD--TIIDigplagyqGGEVMFQGGIDRLASAKDS-LTAKYLTGVERIEPPA 591
Cdd:COG1135   188 RELGLTIVLITHEMDVVRRiCDrvAVLE--------NGRIVEQGPVLDVFANPQSeLTRRFLPTVLNDELPE 251
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
456-553 1.78e-05

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 47.01  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYlTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:PRK09493  118 RELLAKVGLAE-RAHHYPSELSGGQQQRVAIARAL--AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
                          90       100
                  ....*....|....*....|.
gi 1474250368 536 EEEIIRAADT---IIDIGPLA 553
Cdd:PRK09493  195 EIGFAEKVASrliFIDKGRIA 215
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
457-583 1.81e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 47.35  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLTLDRL---SSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVV 533
Cdd:PRK14246  132 ECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARAL--ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS 209
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1474250368 534 EHEEEIIRAADTIIDIgplagYQGGEVMFQGGIDRLASAKDSLTAKYLTG 583
Cdd:PRK14246  210 HNPQQVARVADYVAFL-----YNGELVEWGSSNEIFTSPKNELTEKYVIG 254
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
817-888 1.95e-05

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 46.90  E-value: 1.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVI-VEHNMD 888
Cdd:cd03297   125 LNRYPAQLSGGEKQRVALARALAAQ----PELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIfVTHDLS 193
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
725-939 2.13e-05

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 48.26  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 725 GRCEECQGEGV-IKVGMQfmadvelvCESCGGKRFKDEVLEVKYHGHSIYDILELTVDAAVDLFAAYQDKdainkKIIEK 803
Cdd:TIGR03269  64 ALCEKCGYVERpSKVGEP--------CPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDD-----TVLDN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 804 LM-TLQDVG-------------LGYVKLGQS----SSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLH------ 859
Cdd:TIGR03269 131 VLeALEEIGyegkeavgravdlIEMVQLSHRithiARDLSGGEKQRVVLARQLAKE----PFLFLADEPTGTLDpqtakl 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 860 FHDIRKllgafDALLARGHTVVIVEHNMDVIRS-ADWVIDLgpEAGErggrVVFEGTPADLMTcresytgKFLSLAENSR 938
Cdd:TIGR03269 207 VHNALE-----EAVKASGISMVLTSHWPEVIEDlSDKAIWL--ENGE----IKEEGTPDEVVA-------VFMEGVSEVE 268

                  .
gi 1474250368 939 R 939
Cdd:TIGR03269 269 K 269
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
465-546 2.25e-05

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 48.21  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 465 GYLT-LDRLSSTLSGGESQRINLATSL-GS-SLVgslyILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIR 541
Cdd:COG4618   456 GYDTrIGEGGARLSGGQRQRIGLARALyGDpRLV----VLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA 531

                  ....*
gi 1474250368 542 AADTI 546
Cdd:COG4618   532 AVDKL 536
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
476-535 2.31e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 47.18  E-value: 2.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 476 LSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:PRK15056  143 LSGGQKKRVFLARAIAQQ--GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
824-932 2.33e-05

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 47.05  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRS-ADWVIDLGpe 902
Cdd:PRK11264  145 LSGGQQQRVAIARALAMR----PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMD-- 218
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1474250368 903 agerGGRVVFEGTPADLMTC-RESYTGKFLS 932
Cdd:PRK11264  219 ----QGRIVEQGPAKALFADpQQPRTRQFLE 245
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
767-891 2.51e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 47.38  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 767 YHGHSIYDILELTVDAAVDLFAAYQDKDAINKKIIEKLMTLQDVGLGYVKLGQ----SSSTLSGGEsQRVKLASFLIKEN 842
Cdd:pfam13304 176 ALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGggelPAFELSDGT-KRLLALLAALLSA 254
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1474250368 843 AGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIR 891
Cdd:pfam13304 255 LPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
470-605 2.52e-05

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 47.53  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 470 DRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLhprDTNRLIAVLKKLRDL---GNTVIVVEHE--------EE 538
Cdd:PRK09536  134 DRPVTSLSGGERQRVLLARALAQA--TPVLLLDEPTASL---DINHQVRTLELVRRLvddGKTAVAAIHDldlaarycDE 208
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 539 IIRAAD-TIIDIGP---------LAGYQGGEVMFqgGIDrlaSAKDSLTAKYLTGVERIEPPANKRrwnsyVDVIGA 605
Cdd:PRK09536  209 LVLLADgRVRAAGPpadvltadtLRAAFDARTAV--GTD---PATGAPTVTPLPDPDRTEAAADTR-----VHVVGG 275
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
824-921 2.68e-05

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 47.11  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNM-DVIRSADW--VIDlg 900
Cdd:PRK13537  139 LSGGMKRRLTLARALVND----PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMeEAERLCDRlcVIE-- 212
                          90       100
                  ....*....|....*....|.
gi 1474250368 901 peagerGGRVVFEGTPADLMT 921
Cdd:PRK13537  213 ------EGRKIAEGAPHALIE 227
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
438-535 3.03e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.88  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 438 DDRDGkTVARVLTEIRNRLE---YLNEV----GLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLhp 510
Cdd:PRK13409  411 PDYDG-TVEDLLRSITDDLGssyYKSEIikplQLERL-LDKNVKDLSGGELQRVAIAACL--SRDADLYLLDEPSAHL-- 484
                          90       100
                  ....*....|....*....|....*....
gi 1474250368 511 rDTNRLIAVLKKLRDL----GNTVIVVEH 535
Cdd:PRK13409  485 -DVEQRLAVAKAIRRIaeerEATALVVDH 512
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
463-572 3.11e-05

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 47.92  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 463 GLGYLTLDRlSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRdLGNTVIVVEHEEEIIRA 542
Cdd:PRK11174  474 GLDTPIGDQ-AAGLSVGQAQRLALARALLQP--CQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQ 549
                          90       100       110
                  ....*....|....*....|....*....|
gi 1474250368 543 ADTIIDIgplagyQGGEVMFQGGIDRLASA 572
Cdd:PRK11174  550 WDQIWVM------QDGQIVQQGDYAELSQA 573
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
451-595 3.35e-05

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 47.03  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRLEY-LNEVGLGYLTLDRLSsTLSGGESQRINLAtslgSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKLRDLG 527
Cdd:COG4152   105 EAKRRADEwLERLGLGDRANKKVE-ELSKGNQQKVQLI----AALLHdpELLILDEPFSGLDPVNVELLKDVIRELAAKG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 528 NTVI----VVEHEEEIiraADTIIDIgplagyQGGEVMFQGGID-----------RLASAKDSLTAKYLTGVERIEPPAN 592
Cdd:COG4152   180 TTVIfsshQMELVEEL---CDRIVII------NKGRKVLSGSVDeirrqfgrntlRLEADGDAGWLRALPGVTVVEEDGD 250

                  ...
gi 1474250368 593 KRR 595
Cdd:COG4152   251 GAE 253
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
451-553 3.56e-05

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 46.21  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRL-EYLNEVGLGYLTlDRLSSTLSGGESQRINLATSLgssLVG-SLYILDEPSIGLHPRDTNRLIAVLKKL-RDLG 527
Cdd:cd03265   107 ERRERIdELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSL---VHRpEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFG 182
                          90       100
                  ....*....|....*....|....*....
gi 1474250368 528 NTVIVVEHE-EEIIRAAD--TIIDIGPLA 553
Cdd:cd03265   183 MTILLTTHYmEEAEQLCDrvAIIDHGRII 211
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
457-539 4.15e-05

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 45.93  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYlTLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEH 535
Cdd:PRK10584  129 ALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGR--PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205

                  ....
gi 1474250368 536 EEEI 539
Cdd:PRK10584  206 DLQL 209
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
818-926 4.28e-05

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 47.41  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 818 GQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLhfhDIRKLLGAFDALLARGHTVVIVEHNMDVIRSADWVI 897
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRK----PRVLILDEATSAL---DAECEQLLQESRSRASRTVLLIAHRLSTVERADQIL 684
                          90       100
                  ....*....|....*....|....*....
gi 1474250368 898 DLgpeageRGGRVVFEGTPADLMTCRESY 926
Cdd:TIGR00958 685 VL------KKGSVVEMGTHKQLMEDQGCY 707
cbiO PRK13649
energy-coupling factor transporter ATPase;
457-535 4.99e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 46.28  E-value: 4.99e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 457 EYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:PRK13649  127 EKLALVGISESLFEKNPFELSGGQMRRVAIAGIL--AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
450-535 5.29e-05

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 47.09  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNRLeylnevGLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLhprDTNRLIAVLKKLRDL--- 526
Cdd:COG1245   437 TEIIKPL------GLEKL-LDKNVKDLSGGELQRVAIAACLSRD--ADLYLLDEPSAHL---DVEQRLAVAKAIRRFaen 504
                          90
                  ....*....|
gi 1474250368 527 -GNTVIVVEH 535
Cdd:COG1245   505 rGKTAMVVDH 514
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
456-547 5.44e-05

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 45.21  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLgyltLDRLSS---TLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIV 532
Cdd:cd03262   117 LELLEKVGL----ADKADAypaQLSGGQQQRVAIARAL--AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVV 190
                          90
                  ....*....|....*.
gi 1474250368 533 VEHEEEIIR-AADTII 547
Cdd:cd03262   191 VTHEMGFAReVADRVI 206
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
791-896 5.45e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 45.81  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 791 QDKDAInKKIIEKlmTLQDVGLG---YVKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHF---HDIR 864
Cdd:PRK14246  121 KEKREI-KKIVEE--CLRKVGLWkevYDRLNSPASQLSGGQQQRLTIARAL----ALKPKVLLMDEPTSMIDIvnsQAIE 193
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368 865 KLLGAfdalLARGHTVVIVEHN-MDVIRSADWV 896
Cdd:PRK14246  194 KLITE----LKNEIAIVIVSHNpQQVARVADYV 222
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
819-928 6.09e-05

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 45.64  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 819 QSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSAD--W 895
Cdd:PRK11614  133 QRAGTMSGGEQQMLAIGRALMSQ----PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADrgY 208
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1474250368 896 VIDlgpeagerGGRVVFEGTPADLMT---CRESYTG 928
Cdd:PRK11614  209 VLE--------NGHVVLEDTGDALLAneaVRSAYLG 236
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
450-547 6.29e-05

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 45.44  E-value: 6.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNRLEYLNEV-GLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN 528
Cdd:cd03266   111 DELTARLEELADRlGMEEL-LDRRVGGFSTGMRQKVAIARALVHD--PPVLLLDEPTTGLDVMATRALREFIRQLRALGK 187
                          90       100
                  ....*....|....*....|
gi 1474250368 529 TVIVVEHE-EEIIRAADTII 547
Cdd:cd03266   188 CILFSTHImQEVERLCDRVV 207
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
451-576 6.51e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 45.99  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRLEY-LNEVGLGYLTlDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGN 528
Cdd:PRK13636  117 EVRKRVDNaLKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVL--VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGL 193
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 529 TVIVVEHEeeiiraadtiIDIGPLAGYQG-----GEVMFQGGIDRLASAKDSL 576
Cdd:PRK13636  194 TIIIATHD----------IDIVPLYCDNVfvmkeGRVILQGNPKEVFAEKEML 236
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
469-564 6.54e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 45.78  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 469 LDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN-TVIVVEHEEEIIRAADTII 547
Cdd:PRK13635  134 LNREPHRLSGGQKQRVAIAGVL--ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVI 211
                          90
                  ....*....|....*..
gi 1474250368 548 DIgplagyQGGEVMFQG 564
Cdd:PRK13635  212 VM------NKGEILEEG 222
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
796-890 6.56e-05

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 45.09  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 796 INKKIiekLMTLQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLA 875
Cdd:cd03292   113 IRKRV---PAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNS----PTILIADEPTGNLDPDTTWEIMNLLKKINK 184
                          90
                  ....*....|....*
gi 1474250368 876 RGHTVVIVEHNMDVI 890
Cdd:cd03292   185 AGTTVVVATHAKELV 199
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
443-549 7.14e-05

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 43.59  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 443 KTVARVLTEIRNRLEYLNEVGLGYLtldrlsSTLSGGESQRINLATSLGSSlvGSLYILDEPsiglhprdTNRL----IA 518
Cdd:cd03221    44 KLIAGELEPDEGIVTWGSTVKIGYF------EQLSGGEKMRLALAKLLLEN--PNLLLLDEP--------TNHLdlesIE 107
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368 519 VLKK-LRDLGNTVIVVEHEEEIIRA-ADTIIDI 549
Cdd:cd03221   108 ALEEaLKEYPGTVILVSHDRYFLDQvATKIIEL 140
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
822-903 7.31e-05

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 45.12  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 822 STLSGGESQRVKLASFLIKENaggPILfIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVI-RSADWVIDLG 900
Cdd:COG4778   151 ATFSGGEQQRVNIARGFIADP---PLL-LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVReAVADRVVDVT 226

                  ...
gi 1474250368 901 PEA 903
Cdd:COG4778   227 PFS 229
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
8-46 7.54e-05

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 45.03  E-value: 7.54e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1474250368   8 KYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:COG1136    12 KSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL 50
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
475-549 8.08e-05

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 44.77  E-value: 8.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 475 TLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLI--AVLKKLRDlGNTVIVVEHEEEIIRAADTIIDI 549
Cdd:cd03250   127 NLSGGQKQRISLARAVYSD--ADIYLLDDPLSAVDAHVGRHIFenCILGLLLN-NKTRILVTHQLQLLPHADQIVVL 200
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
20-47 8.12e-05

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). 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: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 44.30  E-value: 8.12e-05
                          10        20
                  ....*....|....*....|....*...
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTLA 47
Cdd:cd03228    18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
773-919 8.42e-05

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 44.80  E-value: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 773 YDIL--ELTVDAAVDLFAAYQdkdAINKKIIEKLM--TLQDVGLgYVKLGQSSSTLSGGESQRVKLASFLIkenaGGPIL 848
Cdd:cd03263    83 FDALfdELTVREHLRFYARLK---GLPKSEIKEEVelLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALI----GGPSV 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 849 FIFDEPTTGLHFHDIRKLlgaFDALLA--RGHTVVIVEHNMDvirsadwvidlgpEAGE--------RGGRVVFEGTPAD 918
Cdd:cd03263   155 LLLDEPTSGLDPASRRAI---WDLILEvrKGRSIILTTHSMD-------------EAEAlcdriaimSDGKLRCIGSPQE 218

                  .
gi 1474250368 919 L 919
Cdd:cd03263   219 L 219
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
807-900 8.68e-05

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 44.79  E-value: 8.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKlGQSSSTLSGGESQRVKLASFLIKenagGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEH- 885
Cdd:cd03231   110 LARVGLNGFE-DRPVAQLSAGQQRRVALARLLLS----GRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHq 184
                          90
                  ....*....|....*
gi 1474250368 886 NMDVIRSADWVIDLG 900
Cdd:cd03231   185 DLGLSEAGARELDLG 199
hmuV PRK13547
heme ABC transporter ATP-binding protein;
817-921 8.73e-05

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 45.20  E-value: 8.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLIK-----ENAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHT-VVIVEHNMDV- 889
Cdd:PRK13547  139 VGRDVTTLSGGELARVQFARVLAQlwpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLa 218
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1474250368 890 IRSADWVIDLGpeagerGGRVVFEGTPADLMT 921
Cdd:PRK13547  219 ARHADRIAMLA------DGAIVAHGAPADVLT 244
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
792-914 9.07e-05

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 44.80  E-value: 9.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEKLMtlqDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGL----------HFH 861
Cdd:cd03257   117 KKEARKEAVLLLLV---GVGLPEEVLNRYPHELSGGQRQRVAIARALALN----PKLLIADEPTSALdvsvqaqildLLK 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1474250368 862 DIRKLLGAfdallarghTVVIVEHNMDVIRS-ADWVIDLgpeageRGGRVVFEG 914
Cdd:cd03257   190 KLQEELGL---------TLLFITHDLGVVAKiADRVAVM------YAGKIVEEG 228
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
469-555 9.08e-05

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: 44.57  E-value: 9.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 469 LDRLSSTLSGGESQRINLATSLG-SSLVGS-------LYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEII 540
Cdd:cd03279   117 LARPVSTLSGGETFLASLSLALAlSEVLQNrggarleALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELK 196
                          90
                  ....*....|....*
gi 1474250368 541 RAADTIIDIGPLAGY 555
Cdd:cd03279   197 ERIPQRLEVIKTPGG 211
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
792-856 9.29e-05

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 43.41  E-value: 9.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 792 DKDAINKKIIEKLMTLQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTT 856
Cdd:pfam00005  90 SKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTK----PKLLLLDEPTA 150
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
457-572 1.06e-04

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 44.78  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLT-LDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLhprDTNRLIAVLKKLRDL--GNTVIVV 533
Cdd:cd03252   119 DFISELPEGYDTiVGEQGAGLSGGQRQRIAIARALIHN--PRILIFDEATSAL---DYESEHAIMRNMHDIcaGRTVIII 193
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1474250368 534 EHEEEIIRAADTIIDIgplagyQGGEVMFQGGIDRLASA 572
Cdd:cd03252   194 AHRLSTVKNADRIIVM------EKGRIVEQGSHDELLAE 226
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
816-910 1.10e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 45.16  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 816 KLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhD------IRKLLGAfdalLARGHTVVIVEHNM-D 888
Cdd:PRK14243  144 KLKQSGLSLSGGQQQRLCIARAI----AVQPEVILMDEPCSAL---DpistlrIEELMHE----LKEQYTIIIVTHNMqQ 212
                          90       100
                  ....*....|....*....|..
gi 1474250368 889 VIRSADWVIDLGPEAGERGGRV 910
Cdd:PRK14243  213 AARVSDMTAFFNVELTEGGGRY 234
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
446-583 1.11e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 44.90  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 446 ARVLTEIRNRLeylnevglgyltlDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRD 525
Cdd:PRK14247  130 AQLWDEVKDRL-------------DAPAGKLSGGQQQRLCIARAL--AFQPEVLLADEPTANLDPENTAKIESLFLELKK 194
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 526 LGNTVIVVEHEEEIIRAADTIidigplAGYQGGEVMFQGGI-DRLASAKDSLTAKYLTG 583
Cdd:PRK14247  195 DMTIVLVTHFPQQAARISDYV------AFLYKGQIVEWGPTrEVFTNPRHELTEKYVTG 247
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
804-897 1.19e-04

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 44.67  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 804 LMTLQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPttglhfhdirklLGAFDAL---------- 873
Cdd:PRK11247  115 LQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHR----PGLLLLDEP------------LGALDALtriemqdlie 177
                          90       100
                  ....*....|....*....|....*...
gi 1474250368 874 ---LARGHTVVIVEHNM-DVIRSADWVI 897
Cdd:PRK11247  178 slwQQHGFTVLLVTHDVsEAVAMADRVL 205
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
819-924 1.28e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 45.00  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 819 QSSSTLSGGESQRVKLASFLIKENAggpiLFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRS-ADWVI 897
Cdd:PRK13638  132 QPIQCLSHGQKKRVAIAGALVLQAR----YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVY 207
                          90       100
                  ....*....|....*....|....*..
gi 1474250368 898 DLgpeageRGGRVVFEGTPADLMTCRE 924
Cdd:PRK13638  208 VL------RQGQILTHGAPGEVFACTE 228
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
792-921 1.30e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 44.68  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEklmTLQDVGL-GYVKlgQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAF 870
Cdd:PRK13639  110 SKEEVEKRVKE---ALKAVGMeGFEN--KPPHHLSGGQKKRVAIAGIL----AMKPEIIVLDEPTSGLDPMGASQIMKLL 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 871 DALLARGHTVVIVEHNMD-VIRSADWVIDLGpeagerGGRVVFEGTPADLMT 921
Cdd:PRK13639  181 YDLNKEGITIIISTHDVDlVPVYADKVYVMS------DGKIIKEGTPKEVFS 226
cbiO PRK13641
energy-coupling factor transporter ATPase;
456-547 1.32e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 44.82  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:PRK13641  126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYE--PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
                          90
                  ....*....|...
gi 1474250368 536 E-EEIIRAADTII 547
Cdd:PRK13641  204 NmDDVAEYADDVL 216
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
807-927 1.34e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 44.74  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLgYVKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGH-TVVIVEH 885
Cdd:PRK13648  127 LKQVDM-LERADYEPNALSGGQKQRVAIAGVL----ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITH 201
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1474250368 886 NMDVIRSADWVIDLGPeagergGRVVFEGTPADLMTCRESYT 927
Cdd:PRK13648  202 DLSEAMEADHVIVMNK------GTVYKEGTPTEIFDHAEELT 237
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
807-920 1.41e-04

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 44.36  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKENaggPILfIFDEPTTGLHF---HDIRKLLgafDALLA-RGHTVVI 882
Cdd:COG3840   114 LERVGLAG-LLDRLPGQLSGGQRQRVALARCLVRKR---PIL-LLDEPFSALDPalrQEMLDLV---DELCReRGLTVLM 185
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1474250368 883 VEHNM-DVIRSADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:COG3840   186 VTHDPeDAARIADRVLLV------ADGRIAADGPTAALL 218
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
14-57 1.42e-04

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: 43.12  E-value: 1.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1474250368  14 GARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLAFDTIFAEGQR 57
Cdd:cd03227     5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
18-46 1.43e-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: 43.00  E-value: 1.43e-04
                          10        20
                  ....*....|....*....|....*....
gi 1474250368  18 HNLKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:cd00267    13 TALDNVSLTLKAGEIVALVGPNGSGKSTL 41
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
824-939 1.51e-04

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 45.45  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhDI---RKLLgafdALLA-----RGHTVVIVEHNMDVIRS-AD 894
Cdd:COG4172   157 LSGGQRQRVMIAMAL----ANEPDLLIADEPTTAL---DVtvqAQIL----DLLKdlqreLGMALLLITHDLGVVRRfAD 225
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1474250368 895 WVIDLgpeageRGGRVVFEGTPADLMTC-RESYTGKFLSlAENSRR 939
Cdd:COG4172   226 RVAVM------RQGEIVEQGPTAELFAApQHPYTRKLLA-AEPRGD 264
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
456-535 1.52e-04

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 45.59  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYL--TLDRLSS-------TLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHpRDTNRLIavLKKLRDL 526
Cdd:PRK11160  447 IEVLQQVGLEKLleDDKGLNAwlgeggrQLSGGEQRRLGIARALLHD--APLLLLDEPTEGLD-AETERQI--LELLAEH 521
                          90
                  ....*....|.
gi 1474250368 527 --GNTVIVVEH 535
Cdd:PRK11160  522 aqNKTVLMITH 532
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
806-904 1.55e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 44.09  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 806 TLQDVGLG---YVKLGqsssTLSGGESQRVKLASFLIkenAGGPIlFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVI 882
Cdd:PRK13539  111 ALEAVGLAplaHLPFG----YLSAGQKRRVALARLLV---SNRPI-WILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
                          90       100
                  ....*....|....*....|..
gi 1474250368 883 VEHNMDVIRSADwVIDLGPEAG 904
Cdd:PRK13539  183 ATHIPLGLPGAR-ELDLGPFAA 203
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
821-894 1.65e-04

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 43.57  E-value: 1.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474250368 821 SSTLSGGESQRVKLAsfliKENAGGPILFIFDEPTTGLHFH---DIRKLLgafDALLARGHTVVIVEHNMD-VIRSAD 894
Cdd:cd03215   102 SSLLSGGNQQKVVLA----RWLARDPRVLILDEPTRGVDVGakaEIYRLI---RELADAGKAVLLISSELDeLLGLCD 172
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
20-46 1.66e-04

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 43.61  E-value: 1.66e-04
                          10        20
                  ....*....|....*....|....*..
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:cd03250    21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
415-524 1.67e-04

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 44.29  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 415 KHIGELVTMPVDELqrffdgLRLDDRDgkTVARVLteirnrlEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSl 494
Cdd:PRK10419  106 KTVREIIREPLRHL------LSLDKAE--RLARAS-------EMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVE- 169
                          90       100       110
                  ....*....|....*....|....*....|
gi 1474250368 495 vGSLYILDEPSIGLHPRDTNRLIAVLKKLR 524
Cdd:PRK10419  170 -PKLLILDEAVSNLDLVLQAGVIRLLKKLQ 198
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
443-565 1.76e-04

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 44.23  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 443 KTVARVLTEIRNR--LEYLNEVGLGYLTLDRLSsTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPrDTNRLiaVL 520
Cdd:PRK09984  119 RTCFSWFTREQKQraLQALTRVGMVHFAHQRVS-TLSGGQQQRVAIARALMQQ--AKVILADEPIASLDP-ESARI--VM 192
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1474250368 521 KKLRDL----GNTVIVVEHE-EEIIRAADTIIDIgplagyQGGEVMFQGG 565
Cdd:PRK09984  193 DTLRDInqndGITVVVTLHQvDYALRYCERIVAL------RQGHVFYDGS 236
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
449-573 1.79e-04

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 45.50  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 449 LTEIRNRLEYLNevgLGYLT-LDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDlg 527
Cdd:TIGR01193 587 IAEIKDDIENMP---LGYQTeLSEEGSSISGGQKQRIALARALLTD--SKVLILDESTSNLDTITEKKIVNNLLNLQD-- 659
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1474250368 528 NTVIVVEHEEEIIRAADTIIDIgplagyQGGEVMFQGGIDRLASAK 573
Cdd:TIGR01193 660 KTIIFVAHRLSVAKQSDKIIVL------DHGKIIEQGSHDELLDRN 699
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
412-541 1.89e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 44.69  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 412 VGGKHIGELVTMPVDELQRFFDGLRLDDRDGKTVARVLTEIRNRLEYLNEVGLGY-LTLDRLSStlsgGESQRINLATSL 490
Cdd:pfam13304 176 ALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGeLPAFELSD----GTKRLLALLAAL 251
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 491 GSSL-VGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIR 541
Cdd:pfam13304 252 LSALpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
473-544 1.91e-04

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 44.10  E-value: 1.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 473 SSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE-EEIIRAAD 544
Cdd:PRK11614  135 AGTMSGGEQQMLAIGRALMSQ--PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNaNQALKLAD 205
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
456-542 2.04e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 45.08  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN-TVIVVE 534
Cdd:PRK15134  406 IAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARAL--ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFIS 483

                  ....*...
gi 1474250368 535 HEEEIIRA 542
Cdd:PRK15134  484 HDLHVVRA 491
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
786-933 2.07e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 44.45  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 786 LFAA--YQDKD--AINKKIIEKLM------TLQDVGLGYVKlGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPT 855
Cdd:PRK13636   95 LFSAsvYQDVSfgAVNLKLPEDEVrkrvdnALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVME----PKVLVLDEPT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 856 TGLH---FHDIRKLLgaFDALLARGHTVVIVEHNMDVIR-SADWVIDLgpeageRGGRVVFEGTPADLMTCRESYTGKFL 931
Cdd:PRK13636  170 AGLDpmgVSEIMKLL--VEMQKELGLTIIIATHDIDIVPlYCDNVFVM------KEGRVILQGNPKEVFAEKEMLRKVNL 241

                  ..
gi 1474250368 932 SL 933
Cdd:PRK13636  242 RL 243
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
469-546 2.18e-04

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 43.40  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 469 LDRLSSTLSGGESQRInlatSLGSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEHEE-EIIRAAD 544
Cdd:cd03301   124 LDRKPKQLSGGQRQRV----ALGRAIVRepKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQvEAMTMAD 199

                  ..
gi 1474250368 545 TI 546
Cdd:cd03301   200 RI 201
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
457-582 2.21e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 44.02  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEH 535
Cdd:PRK13652  120 SALHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVI--AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTH 196
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1474250368 536 EEEII-RAADTIIDIgplagyQGGEVMFQGGIDRLASAKDSLTAKYLT 582
Cdd:PRK13652  197 QLDLVpEMADYIYVM------DKGRIVAYGTVEEIFLQPDLLARVHLD 238
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
817-917 2.30e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 44.24  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGH-TVVIVEHNMDVIRSADW 895
Cdd:PRK13635  134 LNREPHRLSGGQKQRVAIAGVL----ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADR 209
                          90       100
                  ....*....|....*....|..
gi 1474250368 896 VIDLgpeageRGGRVVFEGTPA 917
Cdd:PRK13635  210 VIVM------NKGEILEEGTPE 225
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
456-548 2.38e-04

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 44.03  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIV-VE 534
Cdd:TIGR02769 131 AELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVK--PKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLfIT 208
                          90
                  ....*....|....
gi 1474250368 535 HEeeiIRAADTIID 548
Cdd:TIGR02769 209 HD---LRLVQSFCQ 219
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
817-921 2.60e-04

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 44.32  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 817 LGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHdiRK--LLGAFDALLARGHT-VVIVEHNMD-VIRS 892
Cdd:COG4148   127 LDRRPATLSGGERQRVAIGRAL----LSSPRLLLMDEPLAALDLA--RKaeILPYLERLRDELDIpILYVSHSLDeVARL 200
                          90       100
                  ....*....|....*....|....*....
gi 1474250368 893 ADWVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:COG4148   201 ADHVVLL------EQGRVVASGPLAEVLS 223
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
450-533 2.65e-04

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 43.34  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNRLEY-LNEVGLGYlTLDRLSSTLSGGESQRINLAtslgSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKklrDL 526
Cdd:cd03264   105 KEVKARVDEvLELVNLGD-RAKKKIGSLSGGMRRRVGIA----QALVGdpSILIVDEPTAGLDPEERIRFRNLLS---EL 176

                  ....*..
gi 1474250368 527 GNTVIVV 533
Cdd:cd03264   177 GEDRIVI 183
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
457-556 2.75e-04

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 44.80  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLtLDRL------SSTLSGGESQRINLATSLgsslvgsLY-----ILDEPSIGLhprDTNRLIAVLKKLRD 525
Cdd:COG4178   462 EALEAVGLGHL-AERLdeeadwDQVLSLGEQQRLAFARLL-------LHkpdwlFLDEATSAL---DEENEAALYQLLRE 530
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1474250368 526 L--GNTVIVVEHEEEIIRAADTIIDIGPLAGYQ 556
Cdd:COG4178   531 ElpGTTVISVGHRSTLAAFHDRVLELTGDGSWQ 563
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
463-547 3.03e-04

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 44.09  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 463 GLGYLtLDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEP--SIGLhPRdTNRLIAVLKKLRDLGNTVIV-VEHE-EE 538
Cdd:PRK11144  117 GIEPL-LDRYPGSLSGGEKQRVAIGRALLTA--PELLLMDEPlaSLDL-PR-KRELLPYLERLAREINIPILyVSHSlDE 191

                  ....*....
gi 1474250368 539 IIRAADTII 547
Cdd:PRK11144  192 ILRLADRVV 200
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
610-687 3.36e-04

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 42.84  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 610 LKGIDVKFPLGVMTCVTGVSGSGKSSLVREILypairrelyetgmkpGDFERLGGDLKRLKGVEIIDQNP--IGKSLRSN 687
Cdd:cd03250    21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALL---------------GELEKLSGSVSVPGSIAYVSQEPwiQNGTIREN 85
cbiO PRK13643
energy-coupling factor transporter ATPase;
457-535 3.42e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 43.57  E-value: 3.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 457 EYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:PRK13643  126 EKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL--AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
447-535 3.48e-04

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 43.38  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 447 RVLTEIRNRLEYLNE-VGLGYLtLDRLSSTLSGGESQRINLATSL-----GSSLVGSLYILDEPSIGLHPRDTNRLIAVL 520
Cdd:PRK03695   98 TRTEAVASALNEVAEaLGLDDK-LGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAGQLLLLDEPMNSLDVAQQAALDRLL 176
                          90
                  ....*....|....*
gi 1474250368 521 KKLRDLGNTVIVVEH 535
Cdd:PRK03695  177 SELCQQGIAVVMSSH 191
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
793-883 3.56e-04

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: 43.03  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 793 KDAINKKIIEkLMTLQDVGLGYVKlGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLH---FHDIRKLLga 869
Cdd:cd03234   115 SDAIRKKRVE-DVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWD----PKVLILDEPTSGLDsftALNLVSTL-- 186
                          90
                  ....*....|....
gi 1474250368 870 fdALLARGHTVVIV 883
Cdd:cd03234   187 --SQLARRNRIVIL 198
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
433-568 3.56e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 43.38  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 433 DGLRLDDRDGKTV--------ARVLTEIRNR-LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSL--GSSLVgslyIL 501
Cdd:PRK11701  100 DGLRMQVSAGGNIgerlmavgARHYGDIRATaGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLvtHPRLV----FM 175
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 502 DEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEHEEEIIR-AADTIIDIgplagyQGGEVMFQGGIDR 568
Cdd:PRK11701  176 DEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARlLAHRLLVM------KQGRVVESGLTDQ 238
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
476-536 3.57e-04

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 42.56  E-value: 3.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 476 LSGGESQRINLATSLGSSlvGSLYILDEPSIGLhprDTNRLIAVLKKLRDL----GNTVIVVEHE 536
Cdd:cd03222    72 LSGGELQRVAIAAALLRN--ATFYLFDEPSAYL---DIEQRLNAARAIRRLseegKKTALVVEHD 131
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
451-547 3.68e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 43.54  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRLEY-LNEVGLgYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGN 528
Cdd:PRK13633  120 EIRERVDEsLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGIL--AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGI 196
                          90
                  ....*....|....*....
gi 1474250368 529 TVIVVEHEEEIIRAADTII 547
Cdd:PRK13633  197 TIILITHYMEEAVEADRII 215
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
799-920 4.03e-04

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 43.56  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 799 KIIEKLmtlqdvGLGYVkLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLAR-G 877
Cdd:TIGR02142 114 RVIELL------GIGHL-LGRLPGRLSGGEKQRVAIGRALLSS----PRLLLMDEPLAALDDPRKYEILPYLERLHAEfG 182
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1474250368 878 HTVVIVEHNMD-VIRSADWVIDLgpeageRGGRVVFEGTPADLM 920
Cdd:TIGR02142 183 IPILYVSHSLQeVLRLADRVVVL------EDGRVAAAGPIAEVW 220
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
451-591 4.53e-04

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 43.64  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-LEYLNEVGLGYLTlDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGN 528
Cdd:PRK11153  116 EIKARvTELLELVGLSDKA-DRYPAQLSGGQKQRVAIARALASN--PKVLLCDEATSALDPATTRSILELLKDInRELGL 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474250368 529 TVIVVEHEEEIIRA-AD--TIIDigplagyqGGEVMFQGG-IDRLASAKDSLTAKYLTGVERIEPPA 591
Cdd:PRK11153  193 TIVLITHEMDVVKRiCDrvAVID--------AGRLVEQGTvSEVFSHPKHPLTREFIQSTLHLDLPE 251
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
456-536 4.55e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 42.88  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 456 LEYLNEVGLGYLTLDRlSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVE 534
Cdd:PRK11629  127 LEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNN--PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVT 203

                  ..
gi 1474250368 535 HE 536
Cdd:PRK11629  204 HD 205
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
20-47 4.55e-04

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 41.48  E-value: 4.55e-04
                          10        20
                  ....*....|....*....|....*...
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTLA 47
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL 28
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
791-914 4.66e-04

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. 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: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 42.48  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 791 QDKDAINKkiieklmTLQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKENaggPILfIFDEPTTGLH---FHDIRKLL 867
Cdd:cd03298   104 EDRQAIEV-------ALARVGLAG-LEKRLPGELSGGERQRVALARVLVRDK---PVL-LLDEPFAALDpalRAEMLDLV 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1474250368 868 GAFDAllARGHTVVIVEHNM-DVIRSADWVIDLGpeagerGGRVVFEG 914
Cdd:cd03298   172 LDLHA--ETKMTVLMVTHQPeDAKRLAQRVVFLD------NGRIAAQG 211
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
474-535 4.73e-04

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 43.89  E-value: 4.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 474 STLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDlGNTVIVVEH 535
Cdd:TIGR02868 470 ARLSGGERQRLALARALLAD--APILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITH 528
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
451-536 4.90e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 43.14  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRL-EYLNEVGL-GYLtlDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN 528
Cdd:PRK13639  113 EVEKRVkEALKAVGMeGFE--NKPPHHLSGGQKKRVAIAGIL--AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGI 188

                  ....*...
gi 1474250368 529 TVIVVEHE 536
Cdd:PRK13639  189 TIIISTHD 196
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
20-47 5.11e-04

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 42.45  E-value: 5.11e-04
                          10        20
                  ....*....|....*....|....*...
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTLA 47
Cdd:cd03225    17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
460-549 5.27e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 460 NEVGLGYLtldrlsstlSGGESQRINLATSLGSSL--VG--SLYILDEPSIGLHPRDTNRLIAVLKK-LRDLGNtVIVVE 534
Cdd:PRK03918  782 KERPLTFL---------SGGERIALGLAFRLALSLylAGniPLLILDEPTPFLDEERRRKLVDIMERyLRKIPQ-VIIVS 851
                          90
                  ....*....|....*
gi 1474250368 535 HEEEIIRAADTIIDI 549
Cdd:PRK03918  852 HDEELKDAADYVIRV 866
cbiO PRK13640
energy-coupling factor transporter ATPase;
798-919 5.62e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 42.86  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 798 KKIIEKLmtLQDVG-LGYVKlgQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLA- 875
Cdd:PRK13640  121 IKIVRDV--LADVGmLDYID--SEPANLSGGQKQRVAIAGIL----AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKk 192
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1474250368 876 RGHTVVIVEHNMDVIRSADWVIDLGPeagergGRVVFEGTPADL 919
Cdd:PRK13640  193 NNLTVISITHDIDEANMADQVLVLDD------GKLLAQGSPVEI 230
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
816-921 5.86e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.50  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 816 KLGQSSSTLSGGESQRVKLASFLIKENAggpILfIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRS-AD 894
Cdd:PRK15439  133 DLDSSAGSLEVADRQIVEILRGLMRDSR---IL-ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQlAD 208
                          90       100
                  ....*....|....*....|....*..
gi 1474250368 895 WVIDLgpeageRGGRVVFEGTPADLMT 921
Cdd:PRK15439  209 RISVM------RDGTIALSGKTADLST 229
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
807-934 5.90e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 43.54  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVI-VEH 885
Cdd:PRK15134  409 MEEVGLDPETRHRYPAEFSGGQRQRIAIARALILK----PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLfISH 484
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1474250368 886 NMDVIRS-ADWVIDLgpeageRGGRVVFEGTPADLMTC-RESYTGKFLSLA 934
Cdd:PRK15134  485 DLHVVRAlCHQVIVL------RQGEVVEQGDCERVFAApQQEYTRQLLALS 529
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
814-910 5.91e-04

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 42.46  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 814 YVKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARgHTVVIVEHNMDVIRSA 893
Cdd:cd03248   141 DTEVGEKGSQLSGGQKQRVAIARALIRN----PQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVERA 215
                          90
                  ....*....|....*..
gi 1474250368 894 DWVIDLgpeageRGGRV 910
Cdd:cd03248   216 DQILVL------DGGRI 226
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
807-905 6.07e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 42.39  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYVKLGQSSSTLSGGESQRVKLA---SFLikenaggPILFIFDEPTTGLHFHDIRKLLGAFDAlLARGHTVVI- 882
Cdd:PRK10247  121 LERFALPDTILTKNIAELSGGEKQRISLIrnlQFM-------PKVLLLDEITSALDESNKHNVNEIIHR-YVREQNIAVl 192
                          90       100
                  ....*....|....*....|....
gi 1474250368 883 -VEHNMDVIRSADWVIDLGPEAGE 905
Cdd:PRK10247  193 wVTHDKDEINHADKVITLQPHAGE 216
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
20-47 6.09e-04

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 43.67  E-value: 6.09e-04
                          10        20
                  ....*....|....*....|....*...
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTLA 47
Cdd:COG2274   491 LDNISLTIKPGERVAIVGRSGSGKSTLL 518
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
14-46 6.49e-04

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. 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: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 42.56  E-value: 6.49e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1474250368  14 GARVHNLKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:cd03256    11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTL 43
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
807-921 6.72e-04

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 42.63  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLG---YVKLGQssstLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLhfhD--IRKLLGafDALLA----RG 877
Cdd:cd03294   145 LELVGLEgweHKYPDE----LSGGMQQRVGLARAL----AVDPDILLMDEAFSAL---DplIRREMQ--DELLRlqaeLQ 211
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1474250368 878 HTVVIVEHNMD-VIRSADWVidlgpeAGERGGRVVFEGTPADLMT 921
Cdd:cd03294   212 KTIVFITHDLDeALRLGDRI------AIMKDGRLVQVGTPEEILT 250
PTZ00243 PTZ00243
ABC transporter; Provisional
817-920 6.86e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 43.61  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  817 LGQSSSTLSGGESQRVKLASFLIKENAggpiLFIFDEPTTGLHFHDIRK-----LLGAFdallaRGHTVVIVEHNMDVIR 891
Cdd:PTZ00243   776 IGEKGVNLSGGQKARVSLARAVYANRD----VYLLDDPLSALDAHVGERvveecFLGAL-----AGKTRVLATHQVHVVP 846
                           90       100
                   ....*....|....*....|....*....
gi 1474250368  892 SADWVIDLGpeagerGGRVVFEGTPADLM 920
Cdd:PTZ00243   847 RADYVVALG------DGRVEFSGSSADFM 869
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
434-547 7.98e-04

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 42.17  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 434 GLRLDDRDGKTVARVLTEirnrlEYLNEVGLGYLTLDRLSST-LSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRD 512
Cdd:cd03260   104 GLRLHGIKLKEELDERVE-----EALRKAALWDEVKDRLHALgLSGGQQQRLCLARAL--ANEPEVLLLDEPTSALDPIS 176
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1474250368 513 TNRLIAVLKKLRDlGNTVIVVEHE-EEIIRAADTII 547
Cdd:cd03260   177 TAKIEELIAELKK-EYTIVIVTHNmQQAARVADRTA 211
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
458-536 8.59e-04

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 42.28  E-value: 8.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 458 YLNEVGLGYLTlDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRD-LGNTVIVVEHE 536
Cdd:PRK11300  137 WLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQ--PEILMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHD 213
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
457-504 8.94e-04

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 40.71  E-value: 8.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 457 EYLNEVGLGYL---TLDRLSSTLSGGESQRINLATSLgssLVGS-LYILDEP 504
Cdd:pfam00005 100 EALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARAL---LTKPkLLLLDEP 148
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
457-535 8.99e-04

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 42.19  E-value: 8.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474250368 457 EYLNEVGLGYLTlDRLSSTLSGGESQRINLATSLGSSlvGSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEH 535
Cdd:PRK10895  120 ELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAAN--PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
822-890 9.11e-04

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 41.97  E-value: 9.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 822 STLSGGESQRVKLASFLIKENAggpiLFIFDEPTTGLhfhDIRKLLGA---FDALLARGHTVVIVEHNMDVI 890
Cdd:cd03236   138 DQLSGGELQRVAIAAALARDAD----FYFFDEPSSYL---DIKQRLNAarlIRELAEDDNYVLVVEHDLAVL 202
cbiO PRK13646
energy-coupling factor transporter ATPase;
476-547 9.44e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 42.07  E-value: 9.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474250368 476 LSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLR-DLGNTVIVVEHE-EEIIRAADTII 547
Cdd:PRK13646  146 MSGGQMRKIAIVSIL--AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVI 217
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
848-919 9.67e-04

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 42.70  E-value: 9.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 848 LFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMD-VIRSADWVIDLgpeageRGGRVVFEGTPADL 919
Cdd:COG1129   161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDeVFEIADRVTVL------RDGRLVGTGPVAEL 227
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
816-897 9.86e-04

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 41.55  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 816 KLGQSSSTLSGGESQRVKLASFLIKENAggpILFIfDEPTTGLHFHDIRKLL--GAFDALLARGHTVVIVEHNMDVIRSA 893
Cdd:cd03290   133 EIGERGINLSGGQRQRICVARALYQNTN---IVFL-DDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPHA 208

                  ....
gi 1474250368 894 DWVI 897
Cdd:cd03290   209 DWII 212
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
450-547 1.04e-03

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 42.32  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 450 TEIRNRLEYLNEV-GLGYLtLDRLSSTLSGGESQRInlatSLGSSLVG--SLYILDEPSIGLHP--RDTNRL-IAVLKKl 523
Cdd:PRK11000  108 EEINQRVNQVAEVlQLAHL-LDRKPKALSGGQRQRV----AIGRTLVAepSVFLLDEPLSNLDAalRVQMRIeISRLHK- 181
                          90       100
                  ....*....|....*....|....*
gi 1474250368 524 rDLGNTVIVVEHEE-EIIRAADTII 547
Cdd:PRK11000  182 -RLGRTMIYVTHDQvEAMTLADKIV 205
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
434-574 1.08e-03

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. 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: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 41.84  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 434 GLRLDDRDGKtvarvltEIRNRL-EYLNEVGLGYLtLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRD 512
Cdd:cd03300    96 GLRLKKLPKA-------EIKERVaEALDLVQLEGY-ANRKPSQLSGGQQQRVAIARAL--VNEPKVLLLDEPLGALDLKL 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474250368 513 TNRLIAVLKKL-RDLGNTVIVVEH-EEEIIRAADTIIdigplagyqggeVMFQGGIDRLASAKD 574
Cdd:cd03300   166 RKDMQLELKRLqKELGITFVFVTHdQEEALTMSDRIA------------VMNKGKIQQIGTPEE 217
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
476-540 1.16e-03

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 41.36  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474250368 476 LSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPrDTNRLIA-VLKKLRDLGNTVIVVEHEEEII 540
Cdd:cd03217   105 FSGGEKKRNEILQLL--LLEPDLAILDEPDSGLDI-DALRLVAeVINKLREEGKSVLIITHYQRLL 167
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
824-891 1.24e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 41.54  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIR 891
Cdd:PRK11124  142 LSGGQQQRVAIARALMME----PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVAR 205
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
476-544 1.27e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 476 LSGGESQRINLatslgsSLVGSLY----------------ILDEPSIGLHPRDTNRLIAVLKKLRDLG-NTVIVVEHEEE 538
Cdd:PRK02224  782 LSGGERALFNL------SLRCAIYrllaegiegdaplpplILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHDDE 855

                  ....*.
gi 1474250368 539 IIRAAD 544
Cdd:PRK02224  856 LVGAAD 861
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
451-584 1.28e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 41.75  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRLEY-LNEVGLGYLTLDRLS---STLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRDL 526
Cdd:PRK14267  121 ELDERVEWaLKKAALWDEVKDRLNdypSNLSGGQRQRLVIARAL--AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE 198
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474250368 527 GNTVIVVEHEEEIIRAAD--------TIIDIGPlagyqgGEVMFQggidrlaSAKDSLTAKYLTGV 584
Cdd:PRK14267  199 YTIVLVTHSPAQAARVSDyvaflylgKLIEVGP------TRKVFE-------NPEHELTEKYVTGA 251
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
792-918 1.33e-03

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 41.55  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEklmTLQDVGLGYVkLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHfhdiRKLLGAFD 871
Cdd:cd03299   102 DKKEIERKVLE---IAEMLGIDHL-LNRKPETLSGGEQQRVAIARALVVN----PKILLLDEPFSALD----VRTKEKLR 169
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 872 ALLARGH-----TVVIVEHNMDVIRS-ADWVIDLgpeageRGGRVVFEGTPAD 918
Cdd:cd03299   170 EELKKIRkefgvTVLHVTHDFEEAWAlADKVAIM------LNGKLIQVGKPEE 216
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
822-921 1.35e-03

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 41.49  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 822 STLSGGESQRVKLASFLIKENaggPILfIFDEPTTGLH---FHDIRKLLGafDALLARGHTVVIVEHNM-DVIRSAD--W 895
Cdd:PRK10771  128 GQLSGGQRQRVALARCLVREQ---PIL-LLDEPFSALDpalRQEMLTLVS--QVCQERQLTLLMVSHSLeDAARIAPrsL 201
                          90       100
                  ....*....|....*....|....*.
gi 1474250368 896 VIDlgpeagerGGRVVFEGTPADLMT 921
Cdd:PRK10771  202 VVA--------DGRIAWDGPTDELLS 219
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
818-899 1.41e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 40.92  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 818 GQSSSTLSGGESQRVKLASFLIKENAggpiLFIFDEPTTGLHFHDIRKLlgaFD----ALLARGHTVVIVEHNMDVIRSA 893
Cdd:cd03250   122 GEKGINLSGGQKQRISLARAVYSDAD----IYLLDDPLSAVDAHVGRHI---FEncilGLLLNNKTRILVTHQLQLLPHA 194

                  ....*.
gi 1474250368 894 DWVIDL 899
Cdd:cd03250   195 DQIVVL 200
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
764-886 1.42e-03

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 40.97  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 764 EVKYHGHsiyDILELTVD--AAVDLFAAYQDKDAINKKIIEKLmtLQDVGLGyvklgqssstLSGGESQRVKLASFLIKE 841
Cdd:cd03217    58 EILFKGE---DITDLPPEerARLGIFLAFQYPPEIPGVKNADF--LRYVNEG----------FSGGEKKRNEILQLLLLE 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1474250368 842 naggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHN 886
Cdd:cd03217   123 ----PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY 163
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
758-917 1.46e-03

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 41.24  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 758 FKDEVLEVKYHGhSIYDIL-ELTVDAAVDlfaAYQDKDAINKKIIEKLMTlqdvglgyvklgQSSSTLSGGESQRVKLAS 836
Cdd:cd03237    65 YKPQYIKADYEG-TVRDLLsSITKDFYTH---PYFKTEIAKPLQIEQILD------------REVPELSGGELQRVAIAA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 837 FLIKENAggpiLFIFDEPTTGLhfhDIRKLLGAFDAL----LARGHTVVIVEHnmDVIRsADWVIDlgpeagerggRV-V 911
Cdd:cd03237   129 CLSKDAD----IYLLDEPSAYL---DVEQRLMASKVIrrfaENNEKTAFVVEH--DIIM-IDYLAD----------RLiV 188

                  ....*.
gi 1474250368 912 FEGTPA 917
Cdd:cd03237   189 FEGEPS 194
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
14-46 1.47e-03

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 41.27  E-value: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1474250368  14 GARVHNLKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:COG4181    22 AGELTILKGISLEVEAGESVAIVGASGSGKSTL 54
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
8-46 1.74e-03

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 40.94  E-value: 1.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1474250368   8 KYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:cd03255     8 KTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL 46
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
824-919 1.85e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 41.26  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIRS-ADWVIDLgpe 902
Cdd:PRK13647  139 LSYGQKKRVAIAGVL----AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVL--- 211
                          90
                  ....*....|....*..
gi 1474250368 903 ageRGGRVVFEGTPADL 919
Cdd:PRK13647  212 ---KEGRVLAEGDKSLL 225
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
459-574 1.89e-03

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 41.61  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 459 LNEVGLGYLTlDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEH-E 536
Cdd:PRK10851  121 LEMVQLAHLA-DRYPAQLSGGQKQRVALARAL--AVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHdQ 197
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1474250368 537 EEIIRAADTIIdigplagyqggeVMFQGGIDRLASAKD 574
Cdd:PRK10851  198 EEAMEVADRVV------------VMSQGNIEQAGTPDQ 223
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
457-589 1.94e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 40.91  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLTlDRLSSTLSGGESQRINLATSL----GSSLVGSLYILDEPSIGLHPRDTnrlIAVLKKLRDL----GN 528
Cdd:PRK13548  117 AALAQVDLAHLA-GRDYPQLSGGEQQRVQLARVLaqlwEPDGPPRWLLLDEPTSALDLAHQ---HHVLRLARQLaherGL 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 529 TVIVVEHEEEI-IRAADTIIdigplagyqggeVMFQGGIDRLASAKDSLTAKYLTGVERIEP 589
Cdd:PRK13548  193 AVIVVLHDLNLaARYADRIV------------LLHQGRLVADGTPAEVLTPETLRRVYGADV 242
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
436-549 1.95e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 41.97  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 436 RLDDRDGktvarvlTEIRNRLEY-LNEVGLGYLTLDRLSSTLSGGESQRINLAtslgSSLVGS--LYILDEPsiglhprd 512
Cdd:COG0488   119 EFEALGG-------WEAEARAEEiLSGLGFPEEDLDRPVSELSGGWRRRVALA----RALLSEpdLLLLDEP-------- 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1474250368 513 TNRL----IAVLKK-LRDLGNTVIVVEHEEEII-RAADTIIDI 549
Cdd:COG0488   180 TNHLdlesIEWLEEfLKNYPGTVLVVSHDRYFLdRVATRILEL 222
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
792-918 1.98e-03

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 41.32  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEkLMTLqdVGLGyVKLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLgafd 871
Cdd:PRK11153  113 PKAEIKARVTE-LLEL--VGLS-DKADRYPAQLSGGQKQRVAIARAL----ASNPKVLLCDEATSALDPATTRSIL---- 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1474250368 872 ALLAR-----GHTVVIVEHNMDVIRS-AD--WVIDlgpeagerGGRVVFEGTPAD 918
Cdd:PRK11153  181 ELLKDinrelGLTIVLITHEMDVVKRiCDrvAVID--------AGRLVEQGTVSE 227
cbiO PRK13650
energy-coupling factor transporter ATPase;
449-574 2.01e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 41.26  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 449 LTEIRNRL-EYLNEVGLGYLTlDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGLHPRDTNRLIAVLKKLRD-L 526
Cdd:PRK13650  114 HEEMKERVnEALELVGMQDFK-EREPARLSGGQKQRVAIAGAV--AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdY 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1474250368 527 GNTVIVVEHEEEIIRAADTIIdigplagyqggeVMFQGGIDRLASAKD 574
Cdd:PRK13650  191 QMTVISITHDLDEVALSDRVL------------VMKNGQVESTSTPRE 226
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
451-566 2.01e-03

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 41.62  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRL-EYLNEVGLGYLtLDRLSSTLSGGESQRINLATSL--GSSLVgslyILDEPSIGLHPRDTNRLIAVLKKL-RDL 526
Cdd:COG3842   111 EIRARVaELLELVGLEGL-ADRYPHQLSGGQQQRVALARALapEPRVL----LLDEPLSALDAKLREEMREELRRLqREL 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1474250368 527 GNTVIVVEHE-EEIIRAADTIIdigplagyqggeVMFQGGI 566
Cdd:COG3842   186 GITFIYVTHDqEEALALADRIA------------VMNDGRI 214
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
447-569 2.05e-03

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 40.57  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 447 RVLTEIRNRLEYLNEVGLGYLtLDRLSSTLSGGESQRINLATSL-GSSlvgSLYILDEPSIGLHPRDTNRLIAVLKKLRD 525
Cdd:cd03263   106 PKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALiGGP---SVLLLDEPTSGLDPASRRAIWDLILEVRK 181
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1474250368 526 lGNTVIVVEHE-EEIIRAADtiiDIGPLAgyqGGEVMFQGGIDRL 569
Cdd:cd03263   182 -GRSIILTTHSmDEAEALCD---RIAIMS---DGKLRCIGSPQEL 219
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
822-888 2.10e-03

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 40.58  E-value: 2.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474250368 822 STLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLAR-GHTVVIVEHNMD 888
Cdd:cd03259   129 HELSGGQQQRVALARALARE----PSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQE 192
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
824-937 2.10e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 41.61  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFH---DIRKLLGAFDALLARGhtVVIVEHNMDVIRS-ADWVidl 899
Cdd:PRK15134  157 LSGGERQRVMIAMALLTR----PELLIADEPTTALDVSvqaQILQLLRELQQELNMG--LLFITHNLSIVRKlADRV--- 227
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1474250368 900 gpeAGERGGRVVFEGTPADLMTC-RESYTGKFLSlAENS 937
Cdd:PRK15134  228 ---AVMQNGRCVEQNRAATLFSApTHPYTQKLLN-SEPS 262
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
500-642 2.11e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 41.58  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 500 ILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE-EEIIRAADTIidigplagyqggEVMFQGGIdRLASAKDSL-- 576
Cdd:PRK15439  163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRI------------SVMRDGTI-ALSGKTADLst 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 577 -----------TAKYLTGVER--IEPPANKRRWNSYVDVIgaRENNLKG---IDVKFPL--GVMTCVTGVSGSGKSSLVr 638
Cdd:PRK15439  230 ddiiqaitpaaREKSLSASQKlwLELPGNRRQQAAGAPVL--TVEDLTGegfRNISLEVraGEILGLAGVVGAGRTELA- 306

                  ....
gi 1474250368 639 EILY 642
Cdd:PRK15439  307 ETLY 310
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
20-47 2.25e-03

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 40.78  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|....*...
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTLA 47
Cdd:COG1122    17 LDDVSLSIEKGEFVAIIGPNGSGKSTLL 44
PLN03211 PLN03211
ABC transporter G-25; Provisional
824-925 2.45e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 41.79  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLA-SFLIKenaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEH--NMDVIRSADWVIDLG 900
Cdd:PLN03211  207 ISGGERKRVSIAhEMLIN-----PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHqpSSRVYQMFDSVLVLS 281
                          90       100
                  ....*....|....*....|....*
gi 1474250368 901 PeagergGRVVFEGTPADLMTCRES 925
Cdd:PLN03211  282 E------GRCLFFGKGSDAMAYFES 300
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
801-888 2.48e-03

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 41.92  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368  801 IEKLM--TLQDVGLGyVKLGQSSSTLSGGESQRVKLASFLIkenaGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGH 878
Cdd:TIGR01257 2047 IEKVAnwSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALI----GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
                           90
                   ....*....|
gi 1474250368  879 TVVIVEHNMD 888
Cdd:TIGR01257 2122 AVVLTSHSME 2131
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
20-46 2.61e-03

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 40.33  E-value: 2.61e-03
                          10        20
                  ....*....|....*....|....*..
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:COG2401    46 LRDLNLEIEPGEIVLIVGASGSGKSTL 72
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
791-858 2.65e-03

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 40.32  E-value: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474250368 791 QDKDAINKKIIEKLMTLQDVGLgyvkLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGL 858
Cdd:cd03301   102 VPKDEIDERVREVAELLQIEHL----LDRKPKQLSGGQRQRVALGRAIVRE----PKVFLMDEPLSNL 161
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
459-564 2.75e-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: 40.33  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 459 LNEVGLGYLTLDRLSStLSGGESQRINLATSLGSSLVgsLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE-- 536
Cdd:cd03234   128 LRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPK--VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpr 204
                          90       100
                  ....*....|....*....|....*...
gi 1474250368 537 EEIIRAADTIIDIgplagyQGGEVMFQG 564
Cdd:cd03234   205 SDLFRLFDRILLL------SSGEIVYSG 226
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
824-911 2.88e-03

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. 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: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 40.15  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPttglhfhdirklLGAFDALLAR-------------GHTVVIVEHNMD-V 889
Cdd:cd03293   132 LSGGMRQRVALARALAVD----PDVLLLDEP------------FSALDALTREqlqeelldiwretGKTVLLVTHDIDeA 195
                          90       100
                  ....*....|....*....|..
gi 1474250368 890 IRSADWVIDLGPeageRGGRVV 911
Cdd:cd03293   196 VFLADRVVVLSA----RPGRIV 213
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
473-555 2.90e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 39.44  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 473 SSTLSGGESQRINLATSLgssLVGSLY-ILDEPSIGLhprDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTIIDIGP 551
Cdd:cd03223    89 DDVLSGGEQQRLAFARLL---LHKPKFvFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162

                  ....
gi 1474250368 552 LAGY 555
Cdd:cd03223   163 EGGW 166
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
816-895 2.98e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 40.41  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 816 KLGQSSSTLSGGESQRVKLASFLikenAGGPILFIFDEPTTGLHFHDIRKLLGAFDALLARGH-TVVIVEHNM-DVIRSA 893
Cdd:PRK14258  143 KIHKSALDLSGGQQQRLCIARAL----AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLhQVSRLS 218

                  ..
gi 1474250368 894 DW 895
Cdd:PRK14258  219 DF 220
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
824-891 2.98e-03

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 40.38  E-value: 2.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474250368 824 LSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHDIRKLLGAFDALLARGHTVVIVEHNMDVIR 891
Cdd:COG4161   142 LSGGQQQRVAIARALMME----PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFAR 205
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
20-47 3.78e-03

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 40.90  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|....*...
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTLA 47
Cdd:COG4988   353 LDGLSLTIPPGERVALVGPSGAGKSTLL 380
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
471-571 3.85e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.49  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 471 RLSSTLSGGESQRINLAtslgSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKL-RDLGNTVIVVEHEEEIIRAAD--T 545
Cdd:NF000106  140 RAAAKYSGGMRRRLDLA----ASMIGrpAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHelT 215
                          90       100
                  ....*....|....*....|....*.
gi 1474250368 546 IIDigplagyqGGEVMFQGGIDRLAS 571
Cdd:NF000106  216 VID--------RGRVIADGKVDELKT 233
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
824-917 3.90e-03

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 39.48  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 824 LSGGESQRVKLASFLIKENAggpiLFIFDEPTTGLhfhDIRKLLGAFDAL----LARGHTVVIVEHNMDVIrsaDWVIDL 899
Cdd:cd03222    72 LSGGELQRVAIAAALLRNAT----FYLFDEPSAYL---DIEQRLNAARAIrrlsEEGKKTALVVEHDLAVL---DYLSDR 141
                          90
                  ....*....|....*...
gi 1474250368 900 gpeagerggRVVFEGTPA 917
Cdd:cd03222   142 ---------IHVFEGEPG 150
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
476-571 3.96e-03

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 40.80  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 476 LSGGESQRInlatSLGSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE--EEIIRAADTIIDIGp 551
Cdd:TIGR00955 167 LSGGERKRL----AFASELLTdpPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMA- 241
                          90       100
                  ....*....|....*....|
gi 1474250368 552 lagyqGGEVMFQGGIDRLAS 571
Cdd:TIGR00955 242 -----EGRVAYLGSPDQAVP 256
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
802-915 4.01e-03

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 40.00  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 802 EKLMTLQDVGLGYVKlGQSSSTLSGGESQRVKLASFLIKENAggpiLFIFDEPTTGLHFHDIRKLLGAF-DALLARGHTV 880
Cdd:PRK09984  132 RALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQAK----VILADEPIASLDPESARIVMDTLrDINQNDGITV 206
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1474250368 881 VIVEHNMD-VIRSADWVIDLgpeageRGGRVVFEGT 915
Cdd:PRK09984  207 VVTLHQVDyALRYCERIVAL------RQGHVFYDGS 236
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
476-547 4.08e-03

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 39.62  E-value: 4.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474250368 476 LSGGESQRINLATSLGSSLvgSLYILDEP--SIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHEEEIIRAADTII 547
Cdd:cd03290   141 LSGGQRQRICVARALYQNT--NIVFLDDPfsALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWII 212
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
792-919 4.44e-03

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 40.44  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIE--KLMTLQDVglgyvkLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLhfhdirkllga 869
Cdd:COG3839   106 PKAEIDRRVREaaELLGLEDL------LDRKPKQLSGGQRQRVALGRALVRE----PKVFLLDEPLSNL----------- 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474250368 870 fDALL-------------ARGHTVVIVEHN-MDVIRSADWVIDLgpeageRGGRVVFEGTPADL 919
Cdd:COG3839   165 -DAKLrvemraeikrlhrRLGTTTIYVTHDqVEAMTLADRIAVM------NDGRIQQVGTPEEL 221
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
457-643 4.97e-03

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 40.58  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 457 EYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLGSSLvgSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE 536
Cdd:TIGR02633 123 NLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA--RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHK 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 537 -EEIIRAADTIIDI--GPLAGYQGGEVMFQGGIDRLASAKDsLTAKYLTGVERIEPPANKRRWNSYVDVIGARENNLKgi 613
Cdd:TIGR02633 201 lNEVKAVCDTICVIrdGQHVATKDMSTMSEDDIITMMVGRE-ITSLYPHEPHEIGDVILEARNLTCWDVINPHRKRVD-- 277
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1474250368 614 DVKFPL--GVMTCVTGVSGSGKSSLVREIL--YP 643
Cdd:TIGR02633 278 DVSFSLrrGEILGVAGLVGAGRTELVQALFgaYP 311
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
8-47 5.18e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 39.41  E-value: 5.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1474250368   8 KYIHVKGARVHNLKNIEVKIPHNQLVVITGLSGSGKSTLA 47
Cdd:cd03257     9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLA 48
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
777-919 5.22e-03

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 39.28  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 777 ELTVDAAVDLFAA-YQDKDAINKKIIEKLmtLQDVGLGYVKlGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPT 855
Cdd:cd03265    87 ELTGWENLYIHARlYGVPGAERRERIDEL--LDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHR----PEVLFLDEPT 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1474250368 856 TGLHFHD-------IRKLLGAFDAllarghTVVIVEHNMDvirSADWVIDlgPEAGERGGRVVFEGTPADL 919
Cdd:cd03265   160 IGLDPQTrahvweyIEKLKEEFGM------TILLTTHYME---EAEQLCD--RVAIIDHGRIIAEGTPEEL 219
PLN03211 PLN03211
ABC transporter G-25; Provisional
476-536 5.75e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 40.63  E-value: 5.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 476 LSGGESQRINLATSLgssLVG-SLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE 536
Cdd:PLN03211  207 ISGGERKRVSIAHEM---LINpSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
18-46 6.05e-03

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 39.05  E-value: 6.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 1474250368  18 HNLKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:cd03262    14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTL 42
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
807-887 6.31e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 39.41  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 807 LQDVGLGYvKLGQSSSTLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFHD---IRKLLGAFDAllARGHTVVIV 883
Cdd:PRK11629  130 LAAVGLEH-RANHRPSELSGGERQRVAIARALVNN----PRLVLADEPTGNLDARNadsIFQLLGELNR--LQGTAFLVV 202

                  ....
gi 1474250368 884 EHNM 887
Cdd:PRK11629  203 THDL 206
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
451-554 6.49e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 39.31  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNR-------LEYLNEVGLGYLTLDRLSSTLSGGESQRINLATSLgsSLVGSLYILDEPSIGL---HPRDTNRLIAVL 520
Cdd:PRK10247  106 QIRNQqpdpaifLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVLLLDEITSALdesNKHNVNEIIHRY 183
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1474250368 521 kkLRDLGNTVIVVEHEEEIIRAADTIIDIGPLAG 554
Cdd:PRK10247  184 --VREQNIAVLWVTHDKDEINHADKVITLQPHAG 215
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
20-46 6.52e-03

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 6.52e-03
                          10        20
                  ....*....|....*....|....*..
gi 1474250368  20 LKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:COG2884    18 LSDVSLEIEKGEFVFLTGPSGAGKSTL 44
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
18-46 6.59e-03

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 39.09  E-value: 6.59e-03
                          10        20
                  ....*....|....*....|....*....
gi 1474250368  18 HNLKNIEVKIPHNQLVVITGLSGSGKSTL 46
Cdd:cd03260    14 HALKDISLDIPKGEITALIGPSGCGKSTL 42
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
476-546 6.62e-03

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 40.30  E-value: 6.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474250368 476 LSGGESQRINLATSLGSSLvgSLYILDEPSIGLHPRDTNRLIAVLKKLRDLGNTVIVVEHE-EEIIRAADTI 546
Cdd:PRK13549  144 LGLGQQQLVEIAKALNKQA--RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTI 213
cbiO PRK13640
energy-coupling factor transporter ATPase;
459-547 7.32e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 39.40  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 459 LNEVG-LGYLtlDRLSSTLSGGESQRINLATSLGsslVG-SLYILDEPSIGLHPRDTNRLIAVLKKLRDLGN-TVIVVEH 535
Cdd:PRK13640  128 LADVGmLDYI--DSEPANLSGGQKQRVAIAGILA---VEpKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITH 202
                          90
                  ....*....|..
gi 1474250368 536 EEEIIRAADTII 547
Cdd:PRK13640  203 DIDEANMADQVL 214
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
792-919 8.17e-03

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 39.36  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 792 DKDAINKKIIEKLMTLQDVGLGYVKLGQssstLSGGESQRVKLASFLIKEnaggPILFIFDEPTTGLHFH---DIRKLLG 868
Cdd:COG1118   106 SKAEIRARVEELLELVQLEGLADRYPSQ----LSGGQRQRVALARALAVE----PEVLLLDEPFGALDAKvrkELRRWLR 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 869 afdALLAR-GHTVVIVEHNMD-VIRSADWVIDLgpeageRGGRVVFEGTPADL 919
Cdd:COG1118   178 ---RLHDElGGTTVFVTHDQEeALELADRVVVM------NQGRIEQVGTPDEV 221
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
451-547 8.67e-03

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 39.29  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474250368 451 EIRNRLEYLNE-VGLGYLtLDRLSSTLSGGESQRInlatSLGSSLVG--SLYILDEPSIGLHPRDTNRLIAVLKKL-RDL 526
Cdd:COG3839   109 EIDRRVREAAElLGLEDL-LDRKPKQLSGGQRQRV----ALGRALVRepKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRL 183
                          90       100
                  ....*....|....*....|..
gi 1474250368 527 GNTVIVVEHE-EEIIRAADTII 547
Cdd:COG3839   184 GTTTIYVTHDqVEAMTLADRIA 205
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
625-677 9.67e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 37.87  E-value: 9.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1474250368 625 VTGVSGSGKSSLVREILYPAIRRELYETGMKPGDFERLGGDLKRLKGVEIIDQ 677
Cdd:pfam13191  29 LTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTREGLLRQ 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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