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Conserved domains on  [gi|940388401|ref|WP_054982959|]
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MULTISPECIES: excinuclease ABC subunit UvrA [Pseudoalteromonas]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 11478512)

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 PRK00349
excinuclease ABC subunit UvrA;
1-939 0e+00

excinuclease ABC subunit UvrA;


:

Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1988.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   1 MENIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 161 EHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVAYMDDS 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 241 TIEEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNPELSLAGGAIKGWDKR-SFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 320 MLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQTKIAFNYRNDRGDLITRNHEFEGVLNNMNRRYRETESNSVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 400 YQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLSFLINVGLNYLS 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 560 IGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQERNPTSDKWLELFGATGNNLKNVDLKIPFGLLTCITG 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCVTG 642
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 640 VSGSGKSTLINDTLFKLAHTELNGATTaEAAPYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAGTQE 719
Cdd:PRK00349 643 VSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTPE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 720 ARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDYF 799
Cdd:PRK00349 722 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 801
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD 879
Cdd:PRK00349 802 EAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVD 881
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 880 HGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVAECERSHTGHYLKPLL 939
Cdd:PRK00349 882 KGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-939 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1988.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   1 MENIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 161 EHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVAYMDDS 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 241 TIEEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNPELSLAGGAIKGWDKR-SFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 320 MLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQTKIAFNYRNDRGDLITRNHEFEGVLNNMNRRYRETESNSVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 400 YQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLSFLINVGLNYLS 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 560 IGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQERNPTSDKWLELFGATGNNLKNVDLKIPFGLLTCITG 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCVTG 642
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 640 VSGSGKSTLINDTLFKLAHTELNGATTaEAAPYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAGTQE 719
Cdd:PRK00349 643 VSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTPE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 720 ARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDYF 799
Cdd:PRK00349 722 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 801
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD 879
Cdd:PRK00349 802 EAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVD 881
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 880 HGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVAECERSHTGHYLKPLL 939
Cdd:PRK00349 882 KGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-939 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1914.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   1 MENIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRKG 160
Cdd:COG0178   83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 161 EHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVAYMDDS 240
Cdd:COG0178  163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDEG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 241 tiEEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNPELSLAGGAIKGWDKRSF-YYFQ 319
Cdd:COG0178  243 --EELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSsYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 320 MLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQtKIAFNYRNdRGDLITRNHEFEGVLNNMNRRYRETESNSVREELAK 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDE-KIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 400 YQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLSFLINVGLNYLS 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIID 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 560 IGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQERNPTSDKWLELFGATGNNLKNVDLKIPFGLLTCITG 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 640 VSGSGKSTLINDTLFKLAHTELNGATTaEAAPYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAGTQE 719
Cdd:COG0178  639 VSGSGKSTLVNDILYPALARKLNGAKE-KPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPE 717
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 720 ARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDYF 799
Cdd:COG0178  718 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 797
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD 879
Cdd:COG0178  798 ENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVD 877
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 880 HGNTIVVIEHNLDVVKTADWVVDLgpeggagggEILIAGTPEEVAECERSHTGHYLKPLL 939
Cdd:COG0178  878 KGNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
3-924 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: 1635.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401    3 NIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   83 ISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRKGEH 162
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  163 VKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVAYMDDSTI 242
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  243 ---EEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNPELSLAGGAIKGWDK-RSFYYF 318
Cdd:TIGR00630 241 aesKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKsTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  319 QMLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQTKIAFNYRNDRGDLITRNHEFEGVLNNMNRRYRETESNSVREELA 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  399 KYQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLSFLINVGLNYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  479 SLERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHII 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  559 DIGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQERNPTSDKWLELFGATGNNLKNVDLKIPFGLLTCIT 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  639 GVSGSGKSTLINDTLFKLAHTELNGATTaEAAPYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAGTQ 718
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKT-VPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETP 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  719 EARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDY 798
Cdd:TIGR00630 720 EAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEF 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  799 FDKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVVLHRLR 878
Cdd:TIGR00630 800 FEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLV 879
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*.
gi 940388401  879 DHGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVA 924
Cdd:TIGR00630 880 DKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
612-920 3.52e-150

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: 443.98  E-value: 3.52e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 612 LELFGATGNNLKNVDLKIPFGLLTCITGVSGSGKSTLINDTLFKLAHTELNGATTAeAAPYKSISGLDHFDKVIDIDQSP 691
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQ-PGNHDRIEGLEHIDKVIVIDQSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 692 IGRTPRSNPATYTGIFTGIRELFagtqearsrgykvgrfsfnvkggrceacqgdgvikvemhflpdvyvpCDVCKGARYN 771
Cdd:cd03271   80 IGRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYN 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 772 RETLEVQYKGKNIHQVLEMTVEDAHDYFDKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKT 851
Cdd:cd03271  113 RETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKT 192
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 852 LYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTP 920
Cdd:cd03271  193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
130-238 1.46e-50

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 173.05  E-value: 1.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  130 QTISQMVDTVLALPEGTKLMLLAPVVKDRKGEHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKV 209
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 940388401  210 KDGQQQRLAESFETALEMSGGVANVAYMD 238
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
622-903 8.07e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 62.25  E-value: 8.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLindtLFKLAHTELNGATTAEAAPYKSISGLdhfdkvidIDQSPIgrtPRSNPA 701
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTL----LKVLAGVLRPTSGTVRRAGGARVAYV--------PQRSEV---PDSLPL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 702 TytgiftgIRELFAgtqearsrgykVGRFSfnvKGGRCEacqgdgvikvemhflpdvyvpcdvckgaRYNRETlevqykg 781
Cdd:NF040873  73 T-------VRDLVA-----------MGRWA---RRGLWR----------------------------RLTRDD------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 782 knihqvlEMTVEDAhdyfdkipaiarklktLMDVGLSYIRlGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTG 861
Cdd:NF040873  97 -------RAAVDDA----------------LERVGLADLA-GRQLGELSGGQRQRALLAQGLAQE---ADLLLLDEPTTG 149
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 940388401 862 LHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
832-898 2.63e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 47.86  E-value: 2.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 832 GEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL-DVVKTAD 898
Cdd:NF040905 143 GKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLnEIRRVAD 207
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-939 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1988.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   1 MENIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 161 EHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVAYMDDS 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 241 TIEEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNPELSLAGGAIKGWDKR-SFYYFQ 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 320 MLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQTKIAFNYRNDRGDLITRNHEFEGVLNNMNRRYRETESNSVREELAK 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 400 YQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLSFLINVGLNYLS 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIID 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 560 IGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQERNPTSDKWLELFGATGNNLKNVDLKIPFGLLTCITG 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCVTG 642
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 640 VSGSGKSTLINDTLFKLAHTELNGATTaEAAPYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAGTQE 719
Cdd:PRK00349 643 VSGSGKSTLINETLYKALARKLNGAKK-VPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTPE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 720 ARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDYF 799
Cdd:PRK00349 722 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 801
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD 879
Cdd:PRK00349 802 EAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVD 881
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 880 HGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVAECERSHTGHYLKPLL 939
Cdd:PRK00349 882 KGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-939 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1914.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   1 MENIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLS 80
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRKG 160
Cdd:COG0178   83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 161 EHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVAYMDDS 240
Cdd:COG0178  163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDEG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 241 tiEEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNPELSLAGGAIKGWDKRSF-YYFQ 319
Cdd:COG0178  243 --EELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSsYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 320 MLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQtKIAFNYRNdRGDLITRNHEFEGVLNNMNRRYRETESNSVREELAK 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDE-KIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 400 YQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLSFLINVGLNYLS 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIID 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 560 IGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQERNPTSDKWLELFGATGNNLKNVDLKIPFGLLTCITG 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 640 VSGSGKSTLINDTLFKLAHTELNGATTaEAAPYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAGTQE 719
Cdd:COG0178  639 VSGSGKSTLVNDILYPALARKLNGAKE-KPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPE 717
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 720 ARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDYF 799
Cdd:COG0178  718 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 797
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD 879
Cdd:COG0178  798 ENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVD 877
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 880 HGNTIVVIEHNLDVVKTADWVVDLgpeggagggEILIAGTPEEVAECERSHTGHYLKPLL 939
Cdd:COG0178  878 KGNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
3-924 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: 1635.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401    3 NIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPA 82
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   83 ISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRKGEH 162
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  163 VKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVAYMDDSTI 242
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  243 ---EEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNPELSLAGGAIKGWDK-RSFYYF 318
Cdd:TIGR00630 241 aesKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKsTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  319 QMLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQTKIAFNYRNDRGDLITRNHEFEGVLNNMNRRYRETESNSVREELA 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  399 KYQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLSFLINVGLNYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  479 SLERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHII 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  559 DIGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQERNPTSDKWLELFGATGNNLKNVDLKIPFGLLTCIT 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  639 GVSGSGKSTLINDTLFKLAHTELNGATTaEAAPYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAGTQ 718
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKT-VPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETP 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  719 EARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDY 798
Cdd:TIGR00630 720 EAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEF 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  799 FDKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVVLHRLR 878
Cdd:TIGR00630 800 FEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLV 879
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*.
gi 940388401  879 DHGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVA 924
Cdd:TIGR00630 880 DKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1-939 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 648.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401    1 MENIEVR--GARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEG 78
Cdd:PRK00635    1 MPSLPVRlsGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   79 LSPAISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKdr 158
Cdd:PRK00635   81 LSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPA-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  159 kgEHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKVKDGQQQRLAESFETALEMSGGVANVaymd 238
Cdd:PRK00635  159 --KDILAIRECLRQGFTKVRIDGEISPIYKFLTSGIPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSL---- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  239 DSTIEEMLFSANFACPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFDPNRVVHNpELS-------LAGGAikgwd 311
Cdd:PRK00635  233 HFDNQKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISIDDPSLIQQ-NLSieenccpFAGNC----- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  312 kRSFYYFQMLQAVAEHYNFDLDVPFEKLAKESQKIILegSGQTKIAFNYRNDRGDL--ITRNHE-FEGVLNNMNRRYRET 388
Cdd:PRK00635  307 -STYLYHTIYQSLADSLGFSLSTPWKDLSPEIQNIFL--YGKEGLVLPVRLFDGTLgkKTLTHKvWRGVLNEIGEKVRYS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  389 ESNSvrEELAKYQTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEamdFFEGLSLTGQKAQIAEKILKEIRDRLS 468
Cdd:PRK00635  384 NKPS--RYLPKGTSATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQE---LFIFLSQLPSKSLSIEEVLQGLKSRLS 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  469 FLINVGLNYLSLERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDE 548
Cdd:PRK00635  459 ILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDE 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  549 DAIRAADHIIDIGPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPqERNPTSDKWLELFGATGNNLKNVDLK 628
Cdd:PRK00635  539 QMISLADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIP-EKRTNSLGTLTLSKATKHNLKDLTIS 617
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  629 IPFGLLTCITGVSGSGKSTLINDTLFKLAHTELNGattaEAAPYKSISGlDHFDKVIDIDQSPIGRTPRSNPATYTGIFT 708
Cdd:PRK00635  618 LPLGRLTVVTGVSGSGKSSLINDTLVPAVEEFIEQ----GFCSNLSIQW-GAISRLVHITRDLPGRSQRSIPLTYIKAFD 692
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  709 GIRELFAGTQEARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPdvyVPCDVCKGARYNRETLEVQYKGKNIHQVL 788
Cdd:PRK00635  693 DLRELFAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNIADIL 769
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  789 EMTVEDAHDYFDKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIE 868
Cdd:PRK00635  770 EMTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHTHDIK 849
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401  869 QLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVAECErSHTGHYLKPLL 939
Cdd:PRK00635  850 ALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELIHLH-TPTAKALRPYL 919
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
612-920 3.52e-150

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: 443.98  E-value: 3.52e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 612 LELFGATGNNLKNVDLKIPFGLLTCITGVSGSGKSTLINDTLFKLAHTELNGATTAeAAPYKSISGLDHFDKVIDIDQSP 691
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQ-PGNHDRIEGLEHIDKVIVIDQSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 692 IGRTPRSNPATYTGIFTGIRELFagtqearsrgykvgrfsfnvkggrceacqgdgvikvemhflpdvyvpCDVCKGARYN 771
Cdd:cd03271   80 IGRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYN 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 772 RETLEVQYKGKNIHQVLEMTVEDAHDYFDKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKT 851
Cdd:cd03271  113 RETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKT 192
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 852 LYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTP 920
Cdd:cd03271  193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-938 5.67e-108

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 368.00  E-value: 5.67e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401    4 IEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQflSLMEK---PDVDHIEGLS 80
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQ--ALIKKtplPSVDKVTGLS 1018
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLMFARVGEPRCPTHDLPLAAQTISQMVDTVLALPEGTKLMLLAPVVKDRkg 160
Cdd:PRK00635 1019 PVIAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPIPKEE-- 1096
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  161 EHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKhtiEVVVDRFKVKDGQQQRLAESFETALEMSGGVaNVAYMDDS 240
Cdd:PRK00635 1097 DLFIYLQEKLKEGFLKLYANEQFYDLDEPLPTSLENP---AIVIQHTKISEKNLSSLLSSLTLAFSLSSSI-CLHIEYAG 1172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  241 TIEEMLFSANFAcPTCGYAMTELEPRLFSFNNPAGACQSCDGLGVRQYFD----PNRVVHNPELSLAggaikgwdkRSFY 316
Cdd:PRK00635 1173 TSLSLTYRLGWQ-DSSGNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCSllphKEKIAHYTPLSLF---------TLFF 1242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  317 ---YFQMLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQtkiafnyrndrgdlitrNHEFEGVLnnMNRRYRETESNSV 393
Cdd:PRK00635 1243 pnqDPKPVYPLLKELGIPSIALFQELDTLSFESLCLGTQQ-----------------HPGLNALL--MEAMLMESEEPLP 1303
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  394 REELAkyqtSQACPSCHGSRLRQEARHVFIGQTNLPAITTmsigEAMDFFEGLSLTGQKAQiAEKILKEIRDRLSFLINV 473
Cdd:PRK00635 1304 PPLIS----KTPCNQCQGLGVYTYAHCVRIHNTSLSDIYQ----EDVTFLKKFLLTIHDDE-EPSIIQDLLNRLTFIDKV 1374
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  474 GLNYLSLERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRA 553
Cdd:PRK00635 1375 GLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEH 1454
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  554 ADHIIDIGPGAGVHGGHIIaqgtrddilatkDSVTGQFLSGVRKIEVPQERNPTSDKWLelfgaTGNNLKNVDLKIPFGL 633
Cdd:PRK00635 1455 ADHLIHLGPGSGPQGGYLL------------STSALKQSQPDLHNTRSSEETPTLSVSL-----SIHTIQNLNVSAPLHS 1517
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  634 LTCITGVSGSGKSTLINDTLFKLAHTELNgattaeaapyksiSGLDHFDKVIDIDQSPIGRTPRSNPATYTGIFTGIREL 713
Cdd:PRK00635 1518 LVAISGVSGSGKTSLLLEGFYKQACALIE-------------KGPSVFSEIIFLDSHPQISSQRSDISTYFDIAPSLRNF 1584
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  714 FAGTQEARSRGYKVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVE 793
Cdd:PRK00635 1585 YASLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIE 1664
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  794 DAHDYFDKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGKTLYILDEPTTGLHFADIEQLLVV 873
Cdd:PRK00635 1665 EVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKSALLVQ 1744
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940388401  874 LHRLRDHGNTIVVIEHNLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVAECERSHTGHYLKPL 938
Cdd:PRK00635 1745 LRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCNL 1809
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
4-116 4.06e-75

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: 245.63  E-value: 4.06e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   4 IEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAI 83
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401  84 SIEQKSTSHNPRSTVGTITEIYDYLRLMFARVG 116
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG 113
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
463-575 4.94e-69

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: 229.07  E-value: 4.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 463 IRDRLSFLINVGLNYLSLERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVI 542
Cdd:cd03270  114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401 543 VVEHDEDAIRAADHIIDIGPGAGVHGGHIIAQG 575
Cdd:cd03270  194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
608-935 1.33e-54

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 205.26  E-value: 1.33e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 608 SDKWLELFGATGNNLKNVDLKIPFGLLTCITGVSGSGKSTLINDTLFklahtelngattAEA--------APY------- 672
Cdd:COG0178    2 MMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIY------------AEGqrryveslSAYarqflgq 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 673 ------KSISGLdhfDKVIDIDQSPIGRTPRSNPATYTGIF-----------------TG--------------IRELFA 715
Cdd:COG0178   70 mdkpdvDSIEGL---SPAISIEQKTTSRNPRSTVGTVTEIYdylrllfarvgtphcpiCGrpvekqtvdqivdrILALPE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 716 GT--------------------QEARSRGY-------------------------------------------------- 725
Cdd:COG0178  147 GTrlqilapvvrgrkgehkellEELRKQGFvrvrvdgevydldeepeldknkkhtievvvdrlvvkedirsrladsveta 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 726 -KVGR------------------------------------FSFNVKGGRCEACQG---------------------DGV 747
Cdd:COG0178  227 lKLGDglvivevvdegeellfsekfacpdcgisfeeleprlFSFNSPYGACPTCDGlgrvlefdpdlvipdpslslaEGA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 748 IKV------------------EMHF--------LPD-------------------------------------------- 757
Cdd:COG0178  307 IAPwsgpsssyyfqllealakHYGFdldtpwkdLPEeqrdlilygsdekikfryknrgrrrtyekpfegvipflerryre 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 758 --------------VYVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDYFDKIP------AIARK--------L 809
Cdd:COG0178  387 tysehvreelsrymSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLEltereaEIAERilkeirsrL 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 810 KTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGkTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEH 889
Cdd:COG0178  467 GFLVDVGLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVG-VLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEH 545
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*.
gi 940388401 890 NLDVVKTADWVVDLGPEGGAGGGEILIAGTPEEVAECERSHTGHYL 935
Cdd:COG0178  546 DEDTIRAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYL 591
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
130-238 1.46e-50

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 173.05  E-value: 1.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  130 QTISQMVDTVLALPEGTKLMLLAPVVKDRKGEHVKLLEQLASQGYIRARIDGEVCDLSDPPTLELHKKHTIEVVVDRFKV 209
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 940388401  210 KDGQQQRLAESFETALEMSGGVANVAYMD 238
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
290-399 2.18e-49

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 169.96  E-value: 2.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  290 DPNRVVHNPELSLAGGAIKGWDK-RSFYYFQMLQAVAEHYNFDLDVPFEKLAKESQKIILEGSGQTKIAFNYrNDRGDLI 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKkRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYY-SRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 940388401  369 TRNHEFEGVLNNMNRRYRETESNSVREELAK 399
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
759-935 2.70e-48

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: 185.99  E-value: 2.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  759 YVPCDVCKGARYNRETLEVQYKGKNIHQVLEMTVEDAHDYFDKIP------AIARK--------LKTLMDVGLSYIRLGQ 824
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTltpeekKIAEEvlkeirerLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  825 AATTLSGGEAQRVKLARELSKRDTGkTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDLG 904
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIG 563
                         170       180       190
                  ....*....|....*....|....*....|.
gi 940388401  905 PEGGAGGGEILIAGTPEEVAECERSHTGHYL 935
Cdd:TIGR00630 564 PGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
612-903 1.34e-47

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: 169.36  E-value: 1.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 612 LELFGATGNNLKNVDLKIPFGLLTCITGVSGSGKSTLINDTLFKLAHTELNGATTAEAA--------P-YKSISGLDhfd 682
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARqflgqmdkPdVDSIEGLS--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 683 KVIDIDQSPIGRTPRSNPATYTGIFTGIRELFAgtqearsrgyKVGrfsfnvkggrceacqgdgvikvemhflpdvyvpc 762
Cdd:cd03270   78 PAIAIDQKTTSRNPRSTVGTVTEIYDYLRLLFA----------RVG---------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 763 dvckgarynretlevqykgknihqvlemtvedahdyfdkipaIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARE 842
Cdd:cd03270  114 ------------------------------------------IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQ 151
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 843 LSKRDTGkTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:cd03270  152 IGSGLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
406-576 2.79e-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: 2.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 406 CPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEGLSltgqkaqiaekilkEIRDRLSFLINVGLNYLSLERSAD 485
Cdd:cd03271  103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENIP--------------KIARKLQTLCDVGLGYIKLGQPAT 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 486 TLSGGEAQRIRLASQIGAGLVG-VMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIIDIGPGA 564
Cdd:cd03271  169 TLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEG 248
                        170
                 ....*....|..
gi 940388401 565 GVHGGHIIAQGT 576
Cdd:cd03271  249 GDGGGQVVASGT 260
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
465-575 9.68e-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: 162.11  E-value: 9.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 465 DRLSFLINVGLNYLSLERSADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVV 544
Cdd:cd03238   66 DQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
                         90       100       110
                 ....*....|....*....|....*....|.
gi 940388401 545 EHDEDAIRAADHIIDIGPGAGVHGGHIIAQG 575
Cdd:cd03238  146 EHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
612-903 4.40e-40

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: 145.93  E-value: 4.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 612 LELFGATGNNLKNVDLKIPFGLLTCITGVSGSGKSTLINDTLFKLAHTELNGATTAEAApyksisgldhfDKVIDIDQsp 691
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSR-----------NKLIFIDQ-- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 692 igrtprsnpatytgiftgirelfagtqearsrgykvgrfsfnvkggrceacqgdgvikvemhflpdvyvpcdvckgaryn 771
Cdd:cd03238      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 772 retlevqykgknihqvlemtvedahdyfdkipaiarkLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTGkT 851
Cdd:cd03238   68 -------------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPG-T 109
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940388401 852 LYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:cd03238  110 LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
401-715 1.79e-39

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 159.61  E-value: 1.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  401 QTSQACPSCHGSRLRQEARHVFIGQTNLPAITTMSIGEAMDFFEglsltgQKAQIAEKIlkeirdrlSFLINVGLNYLSL 480
Cdd:PRK00635  738 RTSIPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFL------DEPSIHEKI--------HALCSLGLDYLPL 803
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  481 ERSADTLSGGEAQRIRLASQIGAGLVG-VMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIID 559
Cdd:PRK00635  804 GRPLSSLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLE 883
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  560 IGPGAGVHGGHIIAQGTRDDiLATKDSVTGQ----FLSGVRKIEVPQERNPTSDKWLELF--GATGNNLKNVDLKIPFGL 633
Cdd:PRK00635  884 LGPEGGNLGGYLLASCSPEE-LIHLHTPTAKalrpYLSSPQELPYLPDPSPKPPVPADITikNAYQHNLKHIDLSLPRNA 962
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  634 LTCITGVSGSGKSTLINDTLF---KLAHTELNGATTAEA----APYKSISGLDHFDKVIDIDQSPIGRTPRSNPATYTGI 706
Cdd:PRK00635  963 LTAVTGPSASGKHSLVFDILYaagNIAYAELFPPYIRQAlikkTPLPSVDKVTGLSPVIAIEKTSASKNSNHSVASALEI 1042

                  ....*....
gi 940388401  707 FTGIRELFA 715
Cdd:PRK00635 1043 SNGLEKLFA 1051
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
453-901 9.64e-19

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: 90.73  E-value: 9.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 453 AQIAEKIL------KEIRDR-LSFLINVGLNYLsLERSADTLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGL---HQR 522
Cdd:COG1123  103 DQIAEALEnlglsrAEARARvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL-ALDPDLL-IADEPTTALdvtTQA 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 523 DNDRLLQTLVhlRDLGNTVIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDILATKDSVtGQFLSGVRKIEVP 601
Cdd:COG1123  180 EILDLLRELQ--RERGTTVLLITHDlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQAL-AAVPRLGAARGRA 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 602 QERNPTSDKWLEL------FGATGNN----LKNVDLKIPFGLLTCITGVSGSGKSTLIndtlfklahtelngattaeaap 671
Cdd:COG1123  251 APAAAAAEPLLEVrnlskrYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLA---------------------- 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 672 yKSISGLDHFDK-VIDIDQSPIGRTPRSNPATYTG----IFtgirelfagtQEARSrgykvgrfSFNvkggrceacqgdg 746
Cdd:COG1123  309 -RLLLGLLRPTSgSILFDGKDLTKLSRRSLRELRRrvqmVF----------QDPYS--------SLN------------- 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 747 vikvemhflpdvyvpcdvckgARynretlevqykgknihqvleMTVED-------AHDYFDKiPAIARKLKTLMD-VGLS 818
Cdd:COG1123  357 ---------------------PR--------------------MTVGDiiaeplrLHGLLSR-AERRERVAELLErVGLP 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 819 YIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD-HGNTIVVIEHNLDVVKT- 896
Cdd:COG1123  395 PDLADRYPHELSGGQRQRVAIARALA---LEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYi 471

                 ....*
gi 940388401 897 ADWVV 901
Cdd:COG1123  472 ADRVA 476
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
4-65 9.70e-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: 81.99  E-value: 9.70e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401   4 IEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFL 65
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL 62
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
4-112 2.09e-17

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: 83.05  E-value: 2.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   4 IEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAegqrryveslSAYARQFLSLMEKPDVDHIEGL---S 80
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGLehiD 70
                         90       100       110
                 ....*....|....*....|....*....|..
gi 940388401  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLMF 112
Cdd:cd03271   71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELF 102
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
829-903 9.97e-16

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: 75.36  E-value: 9.97e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 829 LSGGEAQRVKLARELSKRDTgktLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTA-DWVVDL 903
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD---LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
461-585 1.34e-15

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: 76.99  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDR-LSFLINVGLNYLsLERSADTLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGLHQRDNDRLLQTLVHLR 535
Cdd:COG1122  109 EEIRERvEEALELVGLEHL-ADRPPHELSGGQKQRVAIAGVL------AMepevLVLDEPTAGLDPRGRRELLELLKRLN 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940388401 536 DLGNTVIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDILATKD 585
Cdd:COG1122  182 KEGKTVIIVTHDlDLVAELADRVIVL------DDGRIVADGTPREVFSDYE 226
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
485-562 2.06e-15

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: 74.70  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 485 DTLSGGEAQRIRLASQIG--AGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIIDIGP 562
Cdd:cd03227   76 LQLSGGEKELSALALILAlaSLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
785-901 1.20e-14

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: 73.66  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 785 HQVLEMTVED------AHDYFDKIPAIARKLKTLMDVGLSyIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEP 858
Cdd:cd03225   86 DQFFGPTVEEevafglENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLA---MDPDILLLDEP 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 940388401 859 TTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKT-ADWVV 901
Cdd:cd03225  162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVI 205
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
828-927 1.42e-14

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 74.36  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 828 TLSGGEAQRVKLAREL-SKRDtgktLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKT-ADWVVDLgp 905
Cdd:COG1121  139 ELSGGQQQRVLLARALaQDPD----LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLL-- 212
                         90       100
                 ....*....|....*....|..
gi 940388401 906 eggagGGEILIAGTPEEVAECE 927
Cdd:COG1121  213 -----NRGLVAHGPPEEVLTPE 229
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
622-903 5.19e-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: 75.95  E-value: 5.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLINdTLFKLAHTElNGATTAEAAPYKSISGLDHFDKVIDIDQSPigrtprsnpa 701
Cdd:COG4988  353 LDGLSLTIPPGERVALVGPSGAGKSTLLN-LLLGFLPPY-SGSILINGVDLSDLDPASWRRQIAWVPQNP---------- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 702 tytgiftgirELFAGTQEArsrgykvgrfsfNVKGGRCEAcqgdgvikvemhflpdvyvpcdvckgaryNRETLEvqykg 781
Cdd:COG4988  421 ----------YLFAGTIRE------------NLRLGRPDA-----------------------------SDEELE----- 444
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 782 knihQVLEMTveDAHDYFDKIPAiarklktlmdvGLSYiRLGQAATTLSGGEAQRVKLARE-LSKRDtgktLYILDEPTT 860
Cdd:COG4988  445 ----AALEAA--GLDEFVAALPD-----------GLDT-PLGEGGRGLSGGQAQRLALARAlLRDAP----LLLLDEPTA 502
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 940388401 861 GLhfaDIE---QLLVVLHRLRdHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:COG4988  503 HL---DAEteaEILQALRRLA-KGRTVILITHRLALLAQADRILVL 544
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
455-563 6.61e-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: 70.35  E-value: 6.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 455 IAEKILKEIRDRLSFLinvglnylslersaDTLSGGEAQRIRLASQIgAGLVGVmYVLDEPSIGLHQRDNDRLLQTLVHL 534
Cdd:cd00267   63 IAKLPLEELRRRIGYV--------------PQLSGGQRQRVALARAL-LLNPDL-LLLDEPTSGLDPASRERLLELLREL 126
                         90       100       110
                 ....*....|....*....|....*....|
gi 940388401 535 RDLGNTVIVVEHD-EDAIRAADHIIDIGPG 563
Cdd:cd00267  127 AEEGRTVIIVTHDpELAELAADRVIVLKDG 156
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
815-901 1.66e-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: 70.64  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 815 VGLSYI---RLGQaattLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL 891
Cdd:cd03235  120 VGLSELadrQIGE----LSGGQQQRVLLARALVQD---PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDL 192
                         90
                 ....*....|.
gi 940388401 892 D-VVKTADWVV 901
Cdd:cd03235  193 GlVLEYFDRVL 203
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
815-903 3.23e-13

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: 68.54  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 815 VGLSYIRLGQAATTLSGGEAQRVKLARELSKRDT-GKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDV 893
Cdd:cd03227   64 VAAVSAELIFTRLQLSGGEKELSALALILALASLkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                         90
                 ....*....|
gi 940388401 894 VKTADWVVDL 903
Cdd:cd03227  144 AELADKLIHI 153
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
461-575 3.34e-13

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: 68.62  E-value: 3.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDRLSF----LINVGLNYLSlERSADTLSGGEAQRIRLAsqigAGLVGV--MYVLDEPSIGL---HQrdnDRLLQTL 531
Cdd:cd03214   69 KELARKIAYvpqaLELLGLAHLA-DRPFNELSGGERQRVLLA----RALAQEppILLLDEPTSHLdiaHQ---IELLELL 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 940388401 532 VHL-RDLGNTVIVVEHDED-AIRAADHIIDIgpgagvHGGHIIAQG 575
Cdd:cd03214  141 RRLaRERGKTVVMVLHDLNlAARYADRVILL------KDGRIVAQG 180
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
457-558 4.65e-13

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: 69.03  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 457 EKILKEIRDRLSFlinVGLNYLsLERSADTLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGLHQRDNDRLLQTLV 532
Cdd:cd03225  109 EEIEERVEEALEL---VGLEGL-RDRSPFTLSGGQKQRVAIAGVL------AMdpdiLLLDEPTAGLDPAGRRELLELLK 178
                         90       100
                 ....*....|....*....|....*..
gi 940388401 533 HLRDLGNTVIVVEHD-EDAIRAADHII 558
Cdd:cd03225  179 KLKAEGKTIIIVTHDlDLLLELADRVI 205
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
815-924 1.00e-12

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: 68.62  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 815 VGLSYiRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVV 894
Cdd:cd03219  131 VGLAD-LADRPAGELSYGQQRRLEIARALA---TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVV 206
                         90       100       110
                 ....*....|....*....|....*....|..
gi 940388401 895 -KTADWVVDLGPEGgagggeiLIA-GTPEEVA 924
Cdd:cd03219  207 mSLADRVTVLDQGR-------VIAeGTPDEVR 231
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
785-923 1.71e-12

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: 67.74  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 785 HQVLEMTVED--AhdyF---------DKIPAIARKlkTLMDVGLSYIRlGQAATTLSGGEAQRVKLARELSkrdTGKTLY 853
Cdd:COG1122   86 DQLFAPTVEEdvA---FgpenlglprEEIRERVEE--ALELVGLEHLA-DRPPHELSGGQKQRVAIAGVLA---MEPEVL 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 854 ILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLD-VVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:COG1122  157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVL------DDGRIVADGTPREV 221
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
829-901 1.03e-11

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: 63.99  E-value: 1.03e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388401 829 LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLD-VVKTADWVV 901
Cdd:cd03216   83 LSVGERQMVEIARALA---RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVT 153
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
622-903 1.44e-11

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 65.06  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLINdtlfklahtelngattaeaapykSISGLDHFD--KVIdIDQSPIGRTPRsn 699
Cdd:COG1136   24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-----------------------ILGGLDRPTsgEVL-IDGQDISSLSE-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 700 patytgiftgiRELfagtqeARSRGYKVGrF---SFNVkggrceacqgdgvikvemhfLPdvyvpcdvckgarynretle 776
Cdd:COG1136   78 -----------REL------ARLRRRHIG-FvfqFFNL--------------------LP-------------------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 777 vqykgknihqvlEMTVED----AHDYFDKIPAIARK--LKTLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgK 850
Cdd:COG1136  100 ------------ELTALEnvalPLLLAGVSRKERREraRELLERVGLGD-RLDHRPSQLSGGQQQRVAIARALVNR---P 163
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 851 TLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:COG1136  164 KLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAARADRVIRL 217
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
474-584 2.20e-11

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: 67.48  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 474 GLNYLSLERSAdTLSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLHQRDNDRLLQTLVHLRDlGNTVIVVEHD 547
Cdd:COG4988  462 GLDTPLGEGGR-GLSGGQAQRLALArallrdAPL--------LLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHR 531
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 940388401 548 EDAIRAADHIIDigpgagVHGGHIIAQGTRDDILATK 584
Cdd:COG4988  532 LALLAQADRILV------LDDGRIVEQGTHEELLAKN 562
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
821-894 2.25e-11

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: 64.38  E-value: 2.25e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRDtgkTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVV 894
Cdd:cd03224  125 RRKQLAGTLSGGEQQMLAIARALMSRP---KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFA 195
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
622-923 3.33e-11

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: 64.68  E-value: 3.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLIndtlfklahtelngattaeaapyKSISGLDHFDK-VIDIDQSPIGRTPRsnp 700
Cdd:COG1120   17 LDDVSLSLPPGEVTALLGPNGSGKSTLL-----------------------RALAGLLKPSSgEVLLDGRDLASLSR--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 701 atytgiftgiRELfagtqeARSRGY----KVGRFSFNVKggrcEAcqgdgvikVEMhflpdvyvpcdvckgARYNretle 776
Cdd:COG1120   71 ----------REL------ARRIAYvpqePPAPFGLTVR----EL--------VAL---------------GRYP----- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 777 vqykgkniHQVLeMTVEDAHDYfdkiPAIARKLKTlmdVGLSYIRlGQAATTLSGGEAQRVKLARELSkRDTGktLYILD 856
Cdd:COG1120  103 --------HLGL-FGRPSAEDR----EAVEEALER---TGLEHLA-DRPVDELSGGERQRVLIARALA-QEPP--LLLLD 162
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401 857 EPTTGLhfaDI---EQLLVVLHRL-RDHGNTIVVIEHNLD-VVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:COG1120  163 EPTSHL---DLahqLEVLELLRRLaRERGRTVVMVLHDLNlAARYADRLVLL------KDGRIVAQGPPEEV 225
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
789-901 3.50e-11

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 64.31  E-value: 3.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 789 EMTVEDAHDYF------DKIPAIARKLKTLMDVGLSyIRLGQAATTLSGGEAQRVKLARELSKR-DtgktLYILDEPTTG 861
Cdd:COG1131   87 DLTVRENLRFFarlyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDpE----LLILDEPTSG 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 940388401 862 LhfaDIE---QLLVVLHRLRDHGNTIVVIEHNLDVV-KTADWVV 901
Cdd:COG1131  162 L---DPEarrELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVA 202
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
622-903 8.07e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 62.25  E-value: 8.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLindtLFKLAHTELNGATTAEAAPYKSISGLdhfdkvidIDQSPIgrtPRSNPA 701
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTL----LKVLAGVLRPTSGTVRRAGGARVAYV--------PQRSEV---PDSLPL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 702 TytgiftgIRELFAgtqearsrgykVGRFSfnvKGGRCEacqgdgvikvemhflpdvyvpcdvckgaRYNRETlevqykg 781
Cdd:NF040873  73 T-------VRDLVA-----------MGRWA---RRGLWR----------------------------RLTRDD------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 782 knihqvlEMTVEDAhdyfdkipaiarklktLMDVGLSYIRlGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTG 861
Cdd:NF040873  97 -------RAAVDDA----------------LERVGLADLA-GRQLGELSGGQRQRALLAQGLAQE---ADLLLLDEPTTG 149
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 940388401 862 LHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
804-923 1.43e-10

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: 64.92  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 804 AIARKLKTLMDVGLSyIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGN 882
Cdd:COG1123  119 ARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALD---PDLLIADEPTTALDVTTQAEILDLLRELqRERGT 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 883 TIVVIEHNLDVV-KTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:COG1123  195 TVLLITHDLGVVaEIADRVVVM------DDGRIVEDGPPEEI 230
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
776-892 1.50e-10

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 61.76  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 776 EVQYKGKNI---------HQV---------LEMTVED----AHDYFDKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGE 833
Cdd:COG4619   56 EIYLDGKPLsampppewrRQVayvpqepalWGGTVRDnlpfPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGE 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401 834 AQRVKLARELSkrdTGKTLYILDEPTTGL---HFADIEQLLvvLHRLRDHGNTIVVIEHNLD 892
Cdd:COG4619  136 RQRLALIRALL---LQPDVLLLDEPTSALdpeNTRRVEELL--REYLAEEGRAVLWVSHDPE 192
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
776-892 2.30e-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: 60.53  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 776 EVQYKGKNIHQVlemtvedahdyfdKIPAIARK---LKTLMD-VGLSYIRlGQAATTLSGGEAQRVKLARELSkRDTgkT 851
Cdd:cd03214   55 EILLDGKDLASL-------------SPKELARKiayVPQALElLGLAHLA-DRPFNELSGGERQRVLLARALA-QEP--P 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 852 LYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLD 892
Cdd:cd03214  118 ILLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLN 159
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
790-895 4.04e-10

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: 60.98  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 790 MTVED-------AHDYFDKIPAIARK-LKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTG 861
Cdd:cd03257   99 MTIGEqiaeplrIHGKLSKKEARKEAvLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA---LNPKLLIADEPTSA 175
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 940388401 862 LhfaDI---EQLLVVLHRLRD-HGNTIVVIEHNLDVVK 895
Cdd:cd03257  176 L---DVsvqAQILDLLKKLQEeLGLTLLFITHDLGVVA 210
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
481-610 4.59e-10

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 61.18  E-value: 4.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 481 ERSADTLSGGEAQRIRLASQIGAGLVGVMyvLDEPSIGL---HQRDNDRLLQtlvHLRDLGNTVIVVEHD-EDAIRAADH 556
Cdd:PRK11231 133 DRRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQVELMRLMR---ELNTQGKTVVTVLHDlNQASRYCDH 207
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 557 IIDIgpgagvHGGHIIAQGTRDDILatkdsvTGQFLSGVRKIEVPQERNPTSDK 610
Cdd:PRK11231 208 LVVL------ANGHVMAQGTPEEVM------TPGLLRTVFDVEAEIHPEPVSGT 249
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
821-925 6.37e-10

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 62.86  E-value: 6.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIEQLLVVLHRLRDH--GNTIVVIEHNLDVVKTAD 898
Cdd:COG4987  464 WLGEGGRRLSGGERRRLALARALLRD---APILLLDEPTEGL---DAATEQALLADLLEAlaGRTVLLITHRLAGLERMD 537
                         90       100
                 ....*....|....*....|....*..
gi 940388401 899 WVVDLgpeggaGGGEILIAGTPEEVAE 925
Cdd:COG4987  538 RILVL------EDGRIVEQGTHEELLA 558
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
829-903 6.65e-10

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: 58.93  E-value: 6.65e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 829 LSGGEAQRVKLARE-LSKRDtgktLYILDEPTTGLhfaDIE---QLLVVLHRLRDhGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:cd03228   97 LSGGQRQRIAIARAlLRDPP----ILILDEATSAL---DPEteaLILEALRALAK-GKTVIVIAHRLSTIRDADRIIVL 167
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
486-582 6.79e-10

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: 62.84  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 486 TLSGGEAQRIRLASqigAglvgvMY------VLDEPSIGLhqrDND---RLLQTLVHLRDLGNTVIVVEHDEDAIRAADH 556
Cdd:COG4618  467 RLSGGQRQRIGLAR---A-----LYgdprlvVLDEPNSNL---DDEgeaALAAAIRALKARGATVVVITHRPSLLAAVDK 535
                         90       100
                 ....*....|....*....|....*.
gi 940388401 557 IIDIgpgagvHGGHIIAQGTRDDILA 582
Cdd:COG4618  536 LLVL------RDGRVQAFGPRDEVLA 555
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
473-593 7.29e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 61.19  E-value: 7.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 473 VGLNYLSLERSADTLSGGEAQRIRLAsqigaglvGV------MYVLDEPSIGLHQRDNDRLLQTLVHL-RDLGNTVIVVE 545
Cdd:PRK13634 132 VGLPEELLARSPFELSGGQMRRVAIA--------GVlamepeVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVT 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 940388401 546 HD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDILATKDSVTGQFLS 593
Cdd:PRK13634 204 HSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEAIGLD 246
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
461-582 7.58e-10

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: 60.14  E-value: 7.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDRLSFLIN-VGLNYLsLERSADTLSGGEAQRIrlasQIGAGLVG--VMYVLDEPSIGLHQRDNDRLLQTLVHLRDL 537
Cdd:cd03219  118 REARERAEELLErVGLADL-ADRPAGELSYGQQRRL----EIARALATdpKLLLLDEPAAGLNPEETEELAELIRELRER 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 940388401 538 GNTVIVVEHDEDAIRA-ADHIIdigpgagV-HGGHIIAQGTRDDILA 582
Cdd:cd03219  193 GITVLLVEHDMDVVMSlADRVT-------VlDQGRVIAEGTPDEVRN 232
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
622-903 9.65e-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: 59.43  E-value: 9.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLINdtlfklahtelngattaeaapykSISGLDhfdkvididqspigrTPRSNPA 701
Cdd:cd03255   20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN-----------------------ILGGLD---------------RPTSGEV 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 702 TYTGI-FTGIRElfagTQEARSRGYKVGrFSFnvkggrceacQgdgvikvEMHFLPD------VYVPCDVCKGARYNREt 774
Cdd:cd03255   62 RVDGTdISKLSE----KELAAFRRRHIG-FVF----------Q-------SFNLLPDltalenVELPLLLAGVPKKERR- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 775 levqykgKNIHQVLEMtvedahdyfdkipaiarklktlmdVGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYI 854
Cdd:cd03255  119 -------ERAEELLER------------------------VGLGD-RLNHYPSELSGGQQQRVAIARALAND---PKIIL 163
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940388401 855 LDEPTTGL---HFADIEQLLVVLHrlRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:cd03255  164 ADEPTGNLdseTGKEVMELLRELN--KEAGTTIVVVTHDPELAEYADRIIEL 213
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
473-581 1.22e-09

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 60.19  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 473 VGLNYLSlERSADTLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGL---HQRDNDRLLQTLVHLRDLgnTVIVVEHDED 549
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQD--SRCLLLDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHDIN 209
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401 550 -AIRAADHIIdigpgaGVHGGHIIAQGTRDDIL 581
Cdd:PRK10575 210 mAARYCDYLV------ALRGGEMIAQGTPAELM 236
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
461-591 1.72e-09

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: 59.05  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDR-LSFLINVGLnylslERSAD----TLSGGEAQRIRLASQIGAGLVGVMYvlDEPSIGLHQRDNDRLLQTLVHLR 535
Cdd:cd03261  111 EEIREIvLEKLEAVGL-----RGAEDlypaELSGGMKKRVALARALALDPELLLY--DEPTAGLDPIASGVIDDLIRSLK 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 536 D-LGNTVIVVEHDEDAIRA-ADHIidigpgAGVHGGHIIAQGTRDDILATKDSVTGQF 591
Cdd:cd03261  184 KeLGLTSIMVTHDLDTAFAiADRI------AVLYDGKIVAEGTPEELRASDDPLVRQF 235
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
615-903 2.42e-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: 60.76  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  615 FGATGNNLKNVDLKIPFGLLTCITGVSGSGKSTLINDTLFKLAHTE----LNGATTAEAAPYksisglDHFDKVIDIDQS 690
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEgsiaVNGVPLADADAD------SWRDQIAWVPQH 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  691 PIgrtprsnpatytgiftgireLFAGTqearsrgykvgrFSFNVKGGRCEAcqgdgvikvemhflpdvyvpcdvckgary 770
Cdd:TIGR02857 405 PF--------------------LFAGT------------IAENIRLARPDA----------------------------- 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  771 nretlevqyKGKNIHQVLEMTveDAHDYfdkIPAIARKLKTlmdvglsyiRLGQAATTLSGGEAQRVKLARELSKrdtGK 850
Cdd:TIGR02857 424 ---------SDAEIREALERA--GLDEF---VAALPQGLDT---------PIGEGGAGLSGGQAQRLALARAFLR---DA 477
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 940388401  851 TLYILDEPTTGLhfaDIEQLLVVLHRLRD--HGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:TIGR02857 478 PLLLLDEPTAHL---DAETEAEVLEALRAlaQGRTVLLVTHRLALAALADRIVVL 529
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
404-563 2.51e-09

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 58.29  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 404 QACPSCHGSRLRQEARHVFigQTnlPAITTMSIGEAMDF---FEGLSLTGQKAqiaekilkeirdrLSFLINVGLNYLSL 480
Cdd:COG4619   62 KPLSAMPPPEWRRQVAYVP--QE--PALWGGTVRDNLPFpfqLRERKFDRERA-------------LELLERLGLPPDIL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 481 ERSADTLSGGEAQRIRLAS------QIgaglvgvmYVLDEPSIGLHQrDNDRLLQTLVH--LRDLGNTVIVVEHDEDAI- 551
Cdd:COG4619  125 DKPVERLSGGERQRLALIRalllqpDV--------LLLDEPTSALDP-ENTRRVEELLReyLAEEGRAVLWVSHDPEQIe 195
                        170
                 ....*....|..
gi 940388401 552 RAADHIIDIGPG 563
Cdd:COG4619  196 RVADRVLTLEAG 207
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
461-583 3.36e-09

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: 58.47  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDRLSFLIN-VGLNYLSL-ERSADTLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNDRLLQTLVHL-RDL 537
Cdd:cd03295  108 EKIRERADELLAlVGLDPAEFaDRYPHELSGGQQQRVGVARALAAD--PPLLLMDEPFGALDPITRDQLQEEFKRLqQEL 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 940388401 538 GNTVIVVEHD-EDAIRAADHIidigpgAGVHGGHIIAQGTRDDILAT 583
Cdd:cd03295  186 GKTIVFVTHDiDEAFRLADRI------AIMKNGEIVQVGTPDEILRS 226
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
473-575 4.00e-09

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: 57.54  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 473 VGLNYLSlERSADTLSGGEAQRIRLAsQIgagLVG--VMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHD-ED 549
Cdd:cd03235  120 VGLSELA-DRQIGELSGGQQQRVLLA-RA---LVQdpDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDlGL 194
                         90       100
                 ....*....|....*....|....*.
gi 940388401 550 AIRAADHIIDIgpgagvhGGHIIAQG 575
Cdd:cd03235  195 VLEYFDRVLLL-------NRTVVASG 213
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
829-903 5.14e-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: 56.46  E-value: 5.14e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:cd03246   97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
777-902 6.20e-09

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: 57.80  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 777 VQYKGKNIHQVLEMTVED----------AHDYFDKIPAIARKLKTLMDvglsyirlgQAATTLSGGEAQRVKLARELSKr 846
Cdd:cd03237   63 VSYKPQYIKADYEGTVRDllssitkdfyTHPYFKTEIAKPLQIEQILD---------REVPELSGGELQRVAIAACLSK- 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 847 DTgkTLYILDEPTTGLhfaDIEQLLV---VLHRLRDHGN-TIVVIEHnlDVVkTADWVVD 902
Cdd:cd03237  133 DA--DIYLLDEPSAYL---DVEQRLMaskVIRRFAENNEkTAFVVEH--DII-MIDYLAD 184
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
829-901 1.20e-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: 55.48  E-value: 1.20e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 829 LSGGEAQRVKLARELSKR-DtgktLYILDEPTTGLhfaDIE---QLLVVLHRLRDHGNTIVVIEHNLDVV-KTADWVV 901
Cdd:cd03230   96 LSGGMKQRLALAQALLHDpE----LLILDEPTSGL---DPEsrrEFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
459-582 1.49e-08

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: 56.29  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 459 ILKEIRDRLsflinvglnylslersADTLSGGEAQriRLAsqIGAGLVG--VMYVLDEPSIGLHQRDNDRLLQTLVHLRD 536
Cdd:cd03224  121 RLKERRKQL----------------AGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRD 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 940388401 537 LGNTVIVVEHDED-AIRAADH--IIDigpgagvhGGHIIAQGTRDDILA 582
Cdd:cd03224  181 EGVTILLVEQNARfALEIADRayVLE--------RGRVVLEGTAAELLA 221
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
801-894 1.65e-08

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: 56.35  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 801 KIPAIARKLKTLMD-VGLSYIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLhfaDI---EQLLVVLHR 876
Cdd:COG1124  110 GLPDREERIAELLEqVGLPPSFLDRYPHQLSGGQRQRVAIARALI---LEPELLLLDEPTSAL---DVsvqAEILNLLKD 183
                         90
                 ....*....|....*....
gi 940388401 877 LR-DHGNTIVVIEHNLDVV 894
Cdd:COG1124  184 LReERGLTYLFVSHDLAVV 202
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
434-582 2.04e-08

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: 57.99  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 434 MSIGEAMDffEGLSLTGQKAQiaekilKEIRDRLSFLIN-VGLNYLSLERSADTLSGGEAQRIRLASQIGAG--LVgvmy 510
Cdd:COG1123  359 MTVGDIIA--EPLRLHGLLSR------AERRERVAELLErVGLPPDLADRYPHELSGGQRQRVAIARALALEpkLL---- 426
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 511 VLDEPSIGL---HQRdndRLLQTLVHLRD-LGNTVIVVEHDEDAIRA-ADHIIdigpgagV-HGGHIIAQGTRDDILA 582
Cdd:COG1123  427 ILDEPTSALdvsVQA---QILNLLRDLQReLGLTYLFISHDLAVVRYiADRVA-------VmYDGRIVEDGPTEEVFA 494
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
622-860 2.09e-08

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: 54.19  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  622 LKNVDLKIPFGLLTCITGVSGSGKSTLIndtlfklahtelngattaeaapyKSISGLDHFDK-VIDIDQSPIGRTPRsnp 700
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL-----------------------KLIAGLLSPTEgTILLDGQDLTDDER--- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  701 atytgiftgirelfagtqeaRSRGYKVGRFSfnvkggrceacQgdgvikvEMHFLPDVYVpcdvckgarynRETL-EVQY 779
Cdd:pfam00005  55 --------------------KSLRKEIGYVF-----------Q-------DPQLFPRLTV-----------RENLrLGLL 85
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  780 KGKNIHQVLEMTVEDAhdyfdkipaiarkLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPT 859
Cdd:pfam00005  86 LKGLSKREKDARAEEA-------------LEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTK---PKLLLLDEPT 149

                  .
gi 940388401  860 T 860
Cdd:pfam00005 150 A 150
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
804-892 2.61e-08

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 57.34  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 804 AIARKLKTLMD-VGLSyIRLGQAATTLSGGEAQRVKLARELSKRdtGKTLyILDEPTTGLHFADIEQLLVVLHRLRDHGN 882
Cdd:COG1129  116 AMRRRARELLArLGLD-IDPDTPVGDLSVAQQQLVEIARALSRD--ARVL-ILDEPTASLTEREVERLFRIIRRLKAQGV 191
                         90
                 ....*....|
gi 940388401 883 TIVVIEHNLD 892
Cdd:COG1129  192 AIIYISHRLD 201
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
473-612 2.90e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 55.93  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 473 VGLNYLSlERSADTLSGGEAQRIRLA---SQI--GAGLVGVMYvLDEPSIGL---HQRDNDRLLQTLVHLRdlGNTVIVV 544
Cdd:PRK13548 122 VDLAHLA-GRDYPQLSGGEQQRVQLArvlAQLwePDGPPRWLL-LDEPTSALdlaHQHHVLRLARQLAHER--GLAVIVV 197
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 545 EHDED-AIRAADHIIDIgpgagvHGGHIIAQGTRDDILatkdsvTGQFLSGVRKIEVPQERNPTSDKWL 612
Cdd:PRK13548 198 LHDLNlAARYADRIVLL------HQGRLVADGTPAEVL------TPETLRRVYGADVLVQPHPETGAPL 254
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
827-923 3.18e-08

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 55.89  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 827 TTLSGGEAQRVKLAREL-----SKRDTGKTLyILDEPTTGLhfaDI---EQLLVVLHRLRDHGNTIVVIEH--NLdVVKT 896
Cdd:COG4559  132 QTLSGGEQQRVQLARVLaqlwePVDGGPRWL-FLDEPTSAL---DLahqHAVLRLARQLARRGGGVVAVLHdlNL-AAQY 206
                         90       100
                 ....*....|....*....|....*..
gi 940388401 897 ADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:COG4559  207 ADRILLL------HQGRLVAQGTPEEV 227
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
784-895 3.18e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 57.25  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 784 IHQ----VLEMTV--------EDAH----DYfDKIPAIARKLktLMDVGLS---YIRLGQaattLSGGEAQRVKLARELS 844
Cdd:PRK13549  87 IHQelalVKELSVleniflgnEITPggimDY-DAMYLRAQKL--LAQLKLDinpATPVGN----LGLGQQQLVEIAKALN 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940388401 845 KRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVK 895
Cdd:PRK13549 160 KQ---ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
785-892 4.34e-08

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: 54.57  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 785 HQVLEMTVED-----AHDYFDKIPAIARKLKTLmdvGLSYIRLgQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPT 859
Cdd:cd03226   82 YQLFTDSVREelllgLKELDAGNEQAETVLKDL---DLYALKE-RHPLSLSGGQKQRLAIAAALL---SGKDLLIFDEPT 154
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401 860 TGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLD 892
Cdd:cd03226  155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYE 187
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
829-887 4.78e-08

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: 53.98  E-value: 4.78e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 829 LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVI 887
Cdd:cd03215  105 LSGGNQQKVVLARWLA---RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
445-566 4.91e-08

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: 54.19  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 445 GLSLTGQKAQIAEKILKEIrdrlsflinvGLNYLSlERSADTLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDN 524
Cdd:cd03226   96 GLKELDAGNEQAETVLKDL----------DLYALK-ERHPLSLSGGQKQRLAIAAALLSG--KDLLIFDEPTSGLDYKNM 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 940388401 525 DRLLQTLVHLRDLGNTVIVVEHDED-AIRAADHIIDIGPGAGV 566
Cdd:cd03226  163 ERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
622-903 5.13e-08

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: 56.77  E-value: 5.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLINdTLFKLahtelngattaeaapYKSISGLDHFDKvIDIDQspIgrtprsNPA 701
Cdd:COG2274  491 LDNISLTIKPGERVAIVGRSGSGKSTLLK-LLLGL---------------YEPTSGRILIDG-IDLRQ--I------DPA 545
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 702 TYTGIFTGIR---ELFAGT-QEarsrgykvgrfsfNVKGGRCEAcqgdgvikvemhflpdvyvpcdvckgarynreTLEv 777
Cdd:COG2274  546 SLRRQIGVVLqdvFLFSGTiRE-------------NITLGDPDA--------------------------------TDE- 579
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 778 qykgkNIHQVLEMTveDAHDYFDKIPaiaRKLKTLmdvglsyirLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDE 857
Cdd:COG2274  580 -----EIIEAARLA--GLHDFIEALP---MGYDTV---------VGEGGSNLSGGQRQRLAIARALLRN---PRILILDE 637
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 940388401 858 PTTGLhfaDIEQLLVVLHRLRD--HGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:COG2274  638 ATSAL---DAETEAIILENLRRllKGRTVIIIAHRLSTIRLADRIIVL 682
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
821-900 5.66e-08

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: 56.68  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARelskrdtgkTLY------ILDEPTTGLHfADIEQLLV-VLHRLRDHGNTIVVIEHNLDV 893
Cdd:COG4618  460 RIGEGGARLSGGQRQRIGLAR---------ALYgdprlvVLDEPNSNLD-DEGEAALAaAIRALKARGATVVVITHRPSL 529

                 ....*..
gi 940388401 894 VKTADWV 900
Cdd:COG4618  530 LAAVDKL 536
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
487-597 7.49e-08

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 56.27  E-value: 7.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIIDIgpgagv 566
Cdd:PRK10535 145 LSGGQQQRVSIARALMNG--GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI------ 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 940388401 567 HGGHII----AQGTRDDILATKDSVT-----GQFLSGVRK 597
Cdd:PRK10535 217 RDGEIVrnppAQEKVNVAGGTEPVVNtasgwRQFVSGFRE 256
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
802-903 8.30e-08

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 56.27  E-value: 8.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 802 IPAI----------ARKLKTLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLL 871
Cdd:PRK10535 109 VPAVyaglerkqrlLRAQELLQRLGLED-RVEYQPSQLSGGQQQRVSIARALM---NGGQVILADEPTGALDSHSGEEVM 184
                         90       100       110
                 ....*....|....*....|....*....|..
gi 940388401 872 VVLHRLRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:PRK10535 185 AILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
784-901 8.49e-08

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 55.80  E-value: 8.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 784 IHQ----VLEMTV--------EDAHDYFDKIPAIARKLKTLMD-VGLSyIRLGQAATTLSGGEAQRVKLARELSkRDTgK 850
Cdd:COG3845   85 VHQhfmlVPNLTVaenivlglEPTKGGRLDRKAARARIRELSErYGLD-VDPDAKVEDLSVGEQQRVEILKALY-RGA-R 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940388401 851 TLyILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKT-ADWVV 901
Cdd:COG3845  162 IL-ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVT 212
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
474-584 1.11e-07

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: 55.61  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 474 GLNYLSLERSAdTLSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLHQRDNDRLLQTLVHLRDlGNTVIVVEHD 547
Cdd:COG2274  600 GYDTVVGEGGS-NLSGGQRQRLAIArallrnPRI--------LILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHR 669
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 940388401 548 EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDILATK 584
Cdd:COG2274  670 LSTIRLADRIIVL------DKGRIVEDGTHEELLARK 700
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
827-891 1.29e-07

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 54.01  E-value: 1.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401 827 TTLSGGEAQRVKLAR---ELSKRDTGKTLYILDEPTTGLhfaDI---EQLLVVLHRL-RDHGNTIVVIEHNL 891
Cdd:PRK13548 133 PQLSGGEQQRVQLARvlaQLWEPDGPPRWLLLDEPTSAL---DLahqHHVLRLARQLaHERGLAVIVVLHDL 201
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
824-923 1.32e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 54.85  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 824 QAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDV-VKTADWVVD 902
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQA---TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVL 211
                         90       100
                 ....*....|....*....|.
gi 940388401 903 LgpeggaGGGEILIAGTPEEV 923
Cdd:PRK09536 212 L------ADGRVRAAGPPADV 226
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
439-581 1.55e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 53.40  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 439 AMDFFEGLSL---TGQKAQIAEKILKEIRDRLsflinvGLNYLsLERSADTLSGGEAQRIRLAS---QI--GAGLVGVMY 510
Cdd:PRK03695  83 AMPVFQYLTLhqpDKTRTEAVASALNEVAEAL------GLDDK-LGRSVNQLSGGEWQRVRLAAvvlQVwpDINPAGQLL 155
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940388401 511 VLDEPSIGL---HQRDNDRLLQtlvHLRDLGNTVIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDIL 581
Cdd:PRK03695 156 LLDEPMNSLdvaQQAALDRLLS---ELCQQGIAVVMSSHDlNHTLRHADRVWLL------KQGKLLASGRRDEVL 221
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
774-891 1.66e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.20  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 774 TLEVQYKGKNIHQVLEMTVEDahdYFDKIPA----------IARKLK--TLMDvglsyirlgQAATTLSGGEAQRVKLAR 841
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVED---LLRSITDdlgssyykseIIKPLQleRLLD---------KNVKDLSGGELQRVAIAA 466
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940388401 842 ELSKR-DtgktLYILDEPTTGLhfaDIEQLLVV---LHRL-RDHGNTIVVIEHNL 891
Cdd:PRK13409 467 CLSRDaD----LYLLDEPSAHL---DVEQRLAVakaIRRIaEEREATALVVDHDI 514
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
828-901 1.79e-07

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: 53.32  E-value: 1.79e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940388401 828 TLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL-DVVKTADWVV 901
Cdd:COG4555  132 ELSTGMKKKVALARALVHD---PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMqEVEALCDRVV 203
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
805-891 1.88e-07

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 53.31  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 805 IARKLKtLMDvglsyiRLGQAATTLSGGEAQRVKLAREL-----SKRDTGKtLYILDEPTTGLhfaDIEQ---LLVVLHR 876
Cdd:COG4138  110 LAEALG-LED------KLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEGQ-LLLLDEPMNSL---DVAQqaaLDRLLRE 178
                         90
                 ....*....|....*
gi 940388401 877 LRDHGNTIVVIEHNL 891
Cdd:COG4138  179 LCQQGITVVMSSHDL 193
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
790-901 1.96e-07

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 53.90  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 790 MTVED-------AHDYFDKIPAIARKLKTLMDVGLSY--IRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTT 860
Cdd:COG0444  103 MTVGDqiaeplrIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGGMRQRVMIARALA---LEPKLLIADEPTT 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 940388401 861 GLHfADIE-QLLVVLHRL-RDHGNTIVVIEHNLDVVK-TADWVV 901
Cdd:COG0444  180 ALD-VTIQaQILNLLKDLqRELGLAILFITHDLGVVAeIADRVA 222
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
829-901 2.05e-07

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: 51.80  E-value: 2.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFA---DIEQLLVVLHRLrdHGNTIVVIEHNLDVVKT-ADWVV 901
Cdd:cd03229  101 LSGGQQQRVALARALAMD---PDVLLLDEPTSALDPItrrEVRALLKSLQAQ--LGITVVLVTHDLDEAARlADRVV 172
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
829-889 2.47e-07

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: 52.17  E-value: 2.47e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEH 889
Cdd:cd03213  112 LSGGERKRVSIALELVSN---PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
786-889 2.56e-07

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 52.79  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 786 QVLEMTVEDAHDyfdkipaIARKLktLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfa 865
Cdd:PRK09493 104 RVRGASKEEAEK-------QAREL--LAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVK---PKLMLFDEPTSAL--- 167
                         90       100
                 ....*....|....*....|....*..
gi 940388401 866 DIE---QLLVVLHRLRDHGNTIVVIEH 889
Cdd:PRK09493 168 DPElrhEVLKVMQDLAEEGMTMVIVTH 194
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
783-895 2.57e-07

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 52.36  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 783 NIHQVLEMTVEDAHDYFDKIPAIarklktLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGL 862
Cdd:COG2884   99 NVALPLRVTGKSRKEIRRRVREV------LDLVGLSD-KAKALPHELSGGEQQRVAIARALVNR---PELLLADEPTGNL 168
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401 863 HFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVK 895
Cdd:COG2884  169 DPETSWEIMELLEEINRRGTTVLIATHDLELVD 201
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
829-927 2.79e-07

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: 52.50  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLhfaD------IEQLlvvLHRLRD-HGNTIVVIEHNLD-VVKTADWV 900
Cdd:cd03261  137 LSGGMKKRVALARALA---LDPELLLYDEPTAGL---DpiasgvIDDL---IRSLKKeLGLTSIMVTHDLDtAFAIADRI 207
                         90       100
                 ....*....|....*....|....*..
gi 940388401 901 VDLgpeggaGGGEILIAGTPEEVAECE 927
Cdd:cd03261  208 AVL------YDGKIVAEGTPEELRASD 228
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
772-903 2.85e-07

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: 52.49  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 772 RETLEVQYKGKNIHQVLEMT-VEDAHDYFDKIPAiarklktlmdvGLSYIrLGQAATTLSGGEAQRVKLARELSkrdTGK 850
Cdd:cd03252   93 RDNIALADPGMSMERVIEAAkLAGAHDFISELPE-----------GYDTI-VGEQGAGLSGGQRQRIAIARALI---HNP 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940388401 851 TLYILDEPTTGLhfaDIEQLLVVLHRLRD--HGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:cd03252  158 RILIFDEATSAL---DYESEHAIMRNMHDicAGRTVIIIAHRLSTVKNADRIIVM 209
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
784-902 3.01e-07

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 54.08  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 784 IHQVLEMTveDAHDYFDKIPAiarklktlmdvGLSYIrLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLH 863
Cdd:PRK11174 455 LQQALENA--WVSEFLPLLPQ-----------GLDTP-IGDQAAGLSVGQAQRLALARALLQP---CQLLLLDEPTASLD 517
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 940388401 864 fADIEQLlvVLHRLRD--HGNTIVVIEHNLDVVKTAD--WVVD 902
Cdd:PRK11174 518 -AHSEQL--VMQALNAasRRQTTLMVTHQLEDLAQWDqiWVMQ 557
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
828-892 3.02e-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: 52.78  E-value: 3.02e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 828 TLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGN-TIVVIEHNLD 892
Cdd:COG1119  142 TLSQGEQRRVLIARALVKD---PELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVE 204
cbiO PRK13645
energy-coupling factor transporter ATPase;
793-901 3.03e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 53.09  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 793 EDAHDYFDKIPaiarKLKTLMDVGLSYIRlgQAATTLSGGEAQRVKLARELSKrdTGKTLyILDEPTTGLHFADIEQLLV 872
Cdd:PRK13645 121 ENKQEAYKKVP----ELLKLVQLPEDYVK--RSPFELSGGQKRRVALAGIIAM--DGNTL-VLDEPTGGLDPKGEEDFIN 191
                         90       100       110
                 ....*....|....*....|....*....|.
gi 940388401 873 VLHRL-RDHGNTIVVIEHNLD-VVKTADWVV 901
Cdd:PRK13645 192 LFERLnKEYKKRIIMVTHNMDqVLRIADEVI 222
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
779-893 3.05e-07

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: 52.75  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 779 YKGKNIHQVLEMTVEDAHD------YFDKIPAIAR--------------KLKTLMDV-GLSYIrLGQAATTLSGGEAQRV 837
Cdd:cd03236   70 FRGSELQNYFTKLLEGDVKvivkpqYVDLIPKAVKgkvgellkkkdergKLDELVDQlELRHV-LDRNIDQLSGGELQRV 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 838 KLARELSkRDTgkTLYILDEPTTGLhfaDIEQLL---VVLHRLRDHGNTIVVIEHNLDV 893
Cdd:cd03236  149 AIAAALA-RDA--DFYFFDEPSSYL---DIKQRLnaaRLIRELAEDDNYVLVVEHDLAV 201
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
487-619 3.10e-07

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 52.85  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASQIGAGLVGVMYvlDEPSIGlhqrDNDRLLQTLVHLRD-----LGNTVIVVEHD-EDAIRAADHIIDI 560
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMF--DEPFVG----QDPITMGVLVKLISelnsaLGVTCVVVSHDvPEVLSIADHAYIV 217
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 561 GpgagvhGGHIIAQGTRDDILATKDSVTGQFLSGVRKIEVPQeRNPTSDKWLELFGATG 619
Cdd:PRK11831 218 A------DKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPF-RYPAGDYHADLLGGGS 269
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
800-894 3.61e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 53.17  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRD 879
Cdd:PRK13651 137 SKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAME---PDFLVFDEPTAGLDPQGVKEILEIFDNLNK 213
                         90
                 ....*....|....*
gi 940388401 880 HGNTIVVIEHNLDVV 894
Cdd:PRK13651 214 QGKTIILVTHDLDNV 228
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
622-889 3.91e-07

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: 52.05  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLindtLFKLAhtelngattaeaapyksisGLDhfdkvididqspigrTPRSNPA 701
Cdd:COG4181   28 LKGISLEVEAGESVAIVGASGSGKSTL----LGLLA-------------------GLD---------------RPTSGTV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 702 TYTGiftgiRELFAGTQEARS--RGYKVGrF---SFnvkggrceacqgdgvikvemHFLP------DVYVPCDVcKGARy 770
Cdd:COG4181   70 RLAG-----QDLFALDEDARArlRARHVG-FvfqSF--------------------QLLPtltaleNVMLPLEL-AGRR- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 771 nretlevqykgknihqvlemtveDAHdyfdkipAIARKLktLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSkrdTGK 850
Cdd:COG4181  122 -----------------------DAR-------ARARAL--LERVGLGH-RLDHYPAQLSGGEQQRVALARAFA---TEP 165
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 940388401 851 TLYILDEPTTGLHFAD---IEQLLVVLHrlRDHGNTIVVIEH 889
Cdd:COG4181  166 AILFADEPTGNLDAATgeqIIDLLFELN--RERGTTLVLVTH 205
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
805-896 4.03e-07

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: 51.64  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 805 IARKLKTLMD-VGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNT 883
Cdd:cd03292  113 IRKRVPAALElVGLSH-KHRALPAELSGGEQQRVAIARAIVNS---PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTT 188
                         90
                 ....*....|...
gi 940388401 884 IVVIEHNLDVVKT 896
Cdd:cd03292  189 VVVATHAKELVDT 201
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
824-923 4.33e-07

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 52.32  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 824 QAATTLSGGEAQRVKLARELSKrDTgkTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLD-VVKTADWVVD 902
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAMVLAQ-DT--PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVV 210
                         90       100
                 ....*....|....*....|..
gi 940388401 903 LGPEGgagggeiLIA-GTPEEV 923
Cdd:PRK11231 211 LANGH-------VMAqGTPEEV 225
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
773-891 5.22e-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: 53.63  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 773 ETLEVQYKGKNIHQVLEMTVED--AHDYFDKIPA------IARKL--KTLMDvglsyirlgQAATTLSGGEAQRVKLARE 842
Cdd:COG1245  399 EDLKISYKPQYISPDYDGTVEEflRSANTDDFGSsyykteIIKPLglEKLLD---------KNVKDLSGGELQRVAIAAC 469
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 843 LSKR-DtgktLYILDEPTTGLhfaDIEQLLVV---LHRL-RDHGNTIVVIEHNL 891
Cdd:COG1245  470 LSRDaD----LYLLDEPSAHL---DVEQRLAVakaIRRFaENRGKTAMVVDHDI 516
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
821-903 6.32e-07

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: 51.28  E-value: 6.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAA-TTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKT-AD 898
Cdd:COG4778  144 RLWDLPpATFSGGEQQRVNIARGFIAD---PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvAD 220

                 ....*
gi 940388401 899 WVVDL 903
Cdd:COG4778  221 RVVDV 225
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
480-575 6.53e-07

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: 50.98  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASqigaGLV---GVMyVLDEPSIGLHQRDNDRLLQTLVHL-RDLGNTVIVVEHD-EDAIRAA 554
Cdd:cd03259  124 LNRYPHELSGGQQQRVALAR----ALArepSLL-LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDqEEALALA 198
                         90       100
                 ....*....|....*....|.
gi 940388401 555 DHIidigpgAGVHGGHIIAQG 575
Cdd:cd03259  199 DRI------AVMNEGRIVQVG 213
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
487-558 6.90e-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: 50.07  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLhqrDND---RLLQTLVHLRDlGNTVIVVEHDEDAIRAADHI 557
Cdd:cd03228   97 LSGGQRQRIAIArallrdPPI--------LILDEATSAL---DPEteaLILEALRALAK-GKTVIVIAHRLSTIRDADRI 164

                 .
gi 940388401 558 I 558
Cdd:cd03228  165 I 165
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
768-898 7.54e-07

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 51.42  E-value: 7.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 768 ARYNRETLEVQYKGKNIHQvlEMTVE----------DAHDYFDKIPAIARKLKTLMDvglsyiRLGQAATTLSGGEAQRV 837
Cdd:PRK11614  75 AKIMREAVAIVPEGRRVFS--RMTVEenlamggffaERDQFQERIKWVYELFPRLHE------RRIQRAGTMSGGEQQML 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401 838 KLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLD-VVKTAD 898
Cdd:PRK11614 147 AIGRALMSQ---PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLAD 205
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
480-601 9.20e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 51.53  E-value: 9.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGN-TVIVVEHDEDAIRAADHII 558
Cdd:PRK13632 136 LDKEPQNLSGGQKQRVAIASVL--ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVI 213
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 940388401 559 DIGpgagvhGGHIIAQGTRDDILATKdsvtgQFLSgVRKIEVP 601
Cdd:PRK13632 214 VFS------EGKLIAQGKPKEILNNK-----EILE-KAKIDSP 244
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
822-903 9.26e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.50  E-value: 9.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 822 LGQAATTLSGGEAQRVKLARELSkRDTgkTLYILDEPTTGLhfaDIEQLLVVLHRLRD--HGNTIVVIEHNLDVVktaDW 899
Cdd:PRK13409 206 LDRDISELSGGELQRVAIAAALL-RDA--DFYFFDEPTSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVL---DY 276

                 ....
gi 940388401 900 VVDL 903
Cdd:PRK13409 277 LADN 280
cbiO PRK13644
energy-coupling factor transporter ATPase;
776-923 9.83e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 51.53  E-value: 9.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 776 EVQYKGKNIHQVLEMTVEDAHdyfdkIPAIarKLKTLMDVGLSYIRLGQ----AATTLSGGEAQRVKLARELSKRdtgKT 851
Cdd:PRK13644  87 ETQFVGRTVEEDLAFGPENLC-----LPPI--EIRKRVDRALAEIGLEKyrhrSPKTLSGGQGQCVALAGILTME---PE 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401 852 LYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM------DRGKIVLEGEPENV 222
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
487-560 1.05e-06

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: 52.29  E-value: 1.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401  487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNDRLLQTLVHLRDlGNTVIVVEHDEDAIRAADHIIDI 560
Cdd:TIGR02857 459 LSGGQAQRLALARAFlrDAPLL----LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
786-895 1.18e-06

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 51.12  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 786 QVLEMTVEDAHDyfdkipaiaRKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFA 865
Cdd:PRK10619 119 QVLGLSKQEARE---------RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME---PEVLLFDEPTSALDPE 186
                         90       100       110
                 ....*....|....*....|....*....|
gi 940388401 866 DIEQLLVVLHRLRDHGNTIVVIEHNLDVVK 895
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEMGFAR 216
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
829-895 1.36e-06

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: 50.27  E-value: 1.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 829 LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDVVK 895
Cdd:cd03258  141 LSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVK 205
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
815-889 1.41e-06

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 50.17  E-value: 1.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 815 VGLSYiRLGQAATTLSGGEAQRVKLAR-ELSKRDtgktLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEH 889
Cdd:COG4133  119 VGLAG-LADLPVRQLSAGQKRRVALARlLLSPAP----LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
829-923 1.46e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.78  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGN-TIVVIEHNLDVVKTADWVVDLgpeg 907
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQ---PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVM---- 213
                         90
                 ....*....|....*.
gi 940388401 908 gaGGGEILIAGTPEEV 923
Cdd:PRK13635 214 --NKGEILEEGTPEEI 227
cbiO PRK13641
energy-coupling factor transporter ATPase;
467-630 1.48e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 50.98  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 467 LSFLINVGLNYLSLERSADTLSGGEAQRIRLAsqigaglvGVM------YVLDEPSIGLHQRDNDRLLQTLVHLRDLGNT 540
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIA--------GVMayepeiLCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 541 VIVVEHDEDAIraADHIIDIgpgAGVHGGHIIAQGTRDDILATKDSVTGQFLSgvrkievpqerNPTSDKWLELFGATGN 620
Cdd:PRK13641 198 VILVTHNMDDV--AEYADDV---LVLEHGKLIKHASPKEIFSDKEWLKKHYLD-----------EPATSRFASKLEKGGF 261
                        170
                 ....*....|
gi 940388401 621 NLKNVDLKIP 630
Cdd:PRK13641 262 KFSEMPLTID 271
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
803-895 1.48e-06

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: 51.75  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  803 PAIARKLKTLM-DVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHG 881
Cdd:TIGR02633 115 NAMYLRAKNLLrELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ---ARLLILDEPSSSLTEKETEILLDIIRDLKAHG 191
                          90
                  ....*....|....
gi 940388401  882 NTIVVIEHNLDVVK 895
Cdd:TIGR02633 192 VACVYISHKLNEVK 205
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
821-891 1.59e-06

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: 51.98  E-value: 1.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401  821 RLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLhRLRDHGNTIVVIEHNL 891
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALL---ADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
458-547 1.65e-06

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: 51.71  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 458 KILKEIRDRLSfLINVglnylsLERSADTLSGGEAQRIrlasQIGAGLV--GVMYVLDEPSIGL--HQRDN-DRLLQTLV 532
Cdd:COG1245  191 GKLDELAEKLG-LENI------LDRDISELSGGELQRV----AIAAALLrdADFYFFDEPSSYLdiYQRLNvARLIRELA 259
                         90
                 ....*....|....*
gi 940388401 533 hlrDLGNTVIVVEHD 547
Cdd:COG1245  260 ---EEGKYVLVVEHD 271
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
821-901 1.78e-06

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: 50.23  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIEQLLVV---LHRLRDhGNTIVVIEHNLDVVKTA 897
Cdd:cd03249  132 LVGERGSQLSGGQKQRIAIARALLRN---PKILLLDEATSAL---DAESEKLVqeaLDRAMK-GRTTIVIAHRLSTIRNA 204

                 ....
gi 940388401 898 DWVV 901
Cdd:cd03249  205 DLIA 208
cbiO PRK13637
energy-coupling factor transporter ATPase;
462-576 1.78e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 50.82  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 462 EIRDRLSFLIN-VGLNYLSL-ERSADTLSGGEAQRIRLAsqigaGLVGVM---YVLDEPSIGLHQRDNDRLLQTLVHLRD 536
Cdd:PRK13637 118 EIENRVKRAMNiVGLDYEDYkDKSPFELSGGQKRRVAIA-----GVVAMEpkiLILDEPTAGLDPKGRDEILNKIKELHK 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 537 -LGNTVIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGT 576
Cdd:PRK13637 193 eYNMTIILVSHSmEDVAKLADRIIVM------NKGKCELQGT 228
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
783-927 1.92e-06

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 49.85  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 783 NIHQVLEMTVEDahdyfDKIpaIARKLKTLM-DVGLSYIRLgQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTG 861
Cdd:cd03218   95 NILAVLEIRGLS-----KKE--REEKLEELLeEFHITHLRK-SKASSLSGGERRRVEIARALA---TNPKFLLLDEPFAG 163
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940388401 862 ---LHFADIEQLlvvLHRLRDHGNTIVVIEHN----LDVVKTADWVVDlgpeggaggGEILIAGTPEEVAECE 927
Cdd:cd03218  164 vdpIAVQDIQKI---IKILKDRGIGVLITDHNvretLSITDRAYIIYE---------GKVLAEGTPEEIAANE 224
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
473-549 1.92e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 50.86  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 473 VGLNYLSLERSADTLSGGEAQRIRLAsqigaGLVGV---MYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDED 549
Cdd:PRK13651 152 VGLDESYLQRSPFELSGGQKRRVALA-----GILAMepdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
829-927 2.25e-06

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: 49.98  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLARelskrdtgkTL-----YIL-DEPTTGLhfaD------IEQLlvvLHRLRD-HGNTIVVIEHNLD-VV 894
Cdd:COG1127  142 LSGGMRKRVALAR---------ALaldpeILLyDEPTAGL---DpitsavIDEL---IRELRDeLGLTSVVVTHDLDsAF 206
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401 895 KTADWVVDLgpeggaGGGEILIAGTPEEVAECE 927
Cdd:COG1127  207 AIADRVAVL------ADGKIIAEGTPEELLASD 233
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
829-923 2.57e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 50.08  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKT-ADWVVDLgpeg 907
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMK---PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVM---- 210
                         90
                 ....*....|....*.
gi 940388401 908 gaGGGEILIAGTPEEV 923
Cdd:PRK13639 211 --SDGKIIKEGTPKEV 224
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
474-581 3.20e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 49.60  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 474 GLNYLSLErSADTLSGGEAQRIRLAsQIGAGLVGVMyVLDEPSIGL---HQRDndrLLQTLVHL-RDLGNTVIVVEHD-E 548
Cdd:PRK10253 132 GITHLADQ-SVDTLSGGQRQRAWIA-MVLAQETAIM-LLDEPTTWLdisHQID---LLELLSELnREKGYTLAAVLHDlN 205
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401 549 DAIRAADHIIdigpgaGVHGGHIIAQGTRDDIL 581
Cdd:PRK10253 206 QACRYASHLI------ALREGKIVAQGAPKEIV 232
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
821-901 4.03e-06

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: 48.87  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGL--HFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTAD 898
Cdd:cd03290  133 EIGERGINLSGGQRQRICVARALYQN---TNIVFLDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHAD 209

                 ...
gi 940388401 899 WVV 901
Cdd:cd03290  210 WII 212
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
480-562 4.05e-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: 48.76  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGE------AQRIRLASQIGAGLvGVMyVLDEPSIGLhqrDNDRLLQTLV-----HLRDLGNTVIVVEHDE 548
Cdd:cd03240  109 LLDMRGRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNL---DEENIEESLAeiieeRKSQKNFQLIVITHDE 183
                         90
                 ....*....|....
gi 940388401 549 DAIRAADHIIDIGP 562
Cdd:cd03240  184 ELVDAADHIYRVEK 197
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
808-903 5.06e-06

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: 50.17  E-value: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 808 KLKTLMD-VGLSYIrLGQAATTLSGGEAQRVKLARELSkRDTgkTLYILDEPTTGLhfaDIEQLLVV---LHRLRDHGNT 883
Cdd:COG1245  192 KLDELAEkLGLENI-LDRDISELSGGELQRVAIAAALL-RDA--DFYFFDEPSSYL---DIYQRLNVarlIRELAEEGKY 264
                         90       100
                 ....*....|....*....|
gi 940388401 884 IVVIEHNLDVVktaDWVVDL 903
Cdd:COG1245  265 VLVVEHDLAIL---DYLADY 281
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
487-564 5.42e-06

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: 47.60  E-value: 5.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASqigaglvgVMY------VLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIIDI 560
Cdd:cd03246   97 LSGGQRQRLGLAR--------ALYgnprilVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168

                 ....
gi 940388401 561 GPGA 564
Cdd:cd03246  169 EDGR 172
cbiO PRK13645
energy-coupling factor transporter ATPase;
450-588 5.60e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 49.24  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 450 GQKAQIAEKILKEIRDrlsfLINVGLNYLslERSADTLSGGEAQRIRLASQIgaGLVGVMYVLDEPSIGLHQRDNDRLLQ 529
Cdd:PRK13645 120 GENKQEAYKKVPELLK----LVQLPEDYV--KRSPFELSGGQKRRVALAGII--AMDGNTLVLDEPTGGLDPKGEEDFIN 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 530 TLVHL-RDLGNTVIVVEHDEDAI-RAADHIIDIgpgagvHGGHIIAQGTRDDILATKDSVT 588
Cdd:PRK13645 192 LFERLnKEYKKRIIMVTHNMDQVlRIADEVIVM------HEGKVISIGSPFEIFSNQELLT 246
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
801-901 5.63e-06

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 48.60  E-value: 5.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 801 KIPAIARKlktlmdVGLSYI--RL-GQaattLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL 877
Cdd:COG3840  109 QVEQALER------VGLAGLldRLpGQ----LSGGQRQRVALARCLVRK---RPILLLDEPFSALDPALRQEMLDLVDEL 175
                         90       100
                 ....*....|....*....|....*.
gi 940388401 878 -RDHGNTIVVIEHNL-DVVKTADWVV 901
Cdd:COG3840  176 cRERGLTVLMVTHDPeDAARIADRVL 201
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
829-903 6.05e-06

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: 46.67  E-value: 6.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 829 LSGGEAQRVKLARELSKRDtgkTLYILDEPTTGLhfaDIEQLLVVLHRLRDHGNTIVVIEHNLDVV-KTADWVVDL 903
Cdd:cd03221   71 LSGGEKMRLALAKLLLENP---NLLLLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYFLdQVATKIIEL 140
cbiO PRK13640
energy-coupling factor transporter ATPase;
810-923 6.14e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 49.03  E-value: 6.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 810 KTLMDVG-LSYIRLGQAatTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGN-TIVVI 887
Cdd:PRK13640 126 DVLADVGmLDYIDSEPA--NLSGGQKQRVAIAGILA---VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISI 200
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 940388401 888 EHNLDVVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13640 201 THDIDEANMADQVLVL------DDGKLLAQGSPVEI 230
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
794-903 6.52e-06

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 49.93  E-value: 6.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  794 DAHDYFDkipaIARKLKTLMDVglsyIRL--GQA-ATTLSGGEAQRVKLAREL-SKRDtgktLYILDEPTTGLhfaDIEQ 869
Cdd:TIGR03719 132 DAADAWD----LDSQLEIAMDA----LRCppWDAdVTKLSGGERRRVALCRLLlSKPD----MLLLDEPTNHL---DAES 196
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 940388401  870 LLVVLHRLRDHGNTIVVIEHN---LDVVktADWVVDL 903
Cdd:TIGR03719 197 VAWLERHLQEYPGTVVAVTHDryfLDNV--AGWILEL 231
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
801-923 7.58e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 49.08  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 801 KIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRDTgktLYILDEPTTGLHFADIEQLLVVLHRLRDH 880
Cdd:PRK13631 149 KSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE---ILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 940388401 881 GNTIVVIEHNLD-VVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13631 226 NKTVFVITHTMEhVLEVADEVIVM------DKGKILKTGTPYEI 263
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
612-690 8.02e-06

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 48.03  E-value: 8.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 612 LELFGATGNN-----LKNVDLKIPFGLLTCITGVSGSGKSTLIndtlfKLAHTELNGATTA------EAAPYKSISGLDH 680
Cdd:COG2401   31 LEAFGVELRVveryvLRDLNLEIEPGEIVLIVGASGSGKSTLL-----RLLAGALKGTPVAgcvdvpDNQFGREASLIDA 105
                         90
                 ....*....|
gi 940388401 681 FDKVIDIDQS 690
Cdd:COG2401  106 IGRKGDFKDA 115
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
827-903 8.02e-06

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: 47.85  E-value: 8.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 827 TTLSGGEAQRVKLAREL-SKRDtgktLYILDEPTTGLHfADIEQLL---VVLHRLRDhGNTIVVIEHNLDVVKTADWVVD 902
Cdd:cd03250  126 INLSGGQKQRISLARAVySDAD----IYLLDDPLSAVD-AHVGRHIfenCILGLLLN-NKTRILVTHQLQLLPHADQIVV 199

                 .
gi 940388401 903 L 903
Cdd:cd03250  200 L 200
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
785-923 8.05e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 48.86  E-value: 8.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 785 HQVLEMTV---------------EDAHdyfdkipAIARKLKTLmdVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtg 849
Cdd:PRK13634  96 HQLFEETVekdicfgpmnfgvseEDAK-------QKAREMIEL--VGLPEELLARSPFELSGGQMRRVAIAGVLAME--- 163
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 850 KTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNL-DVVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMeDAARYADQIVVM------HKGTVFLQGTPREI 233
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
481-591 8.50e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 49.07  E-value: 8.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 481 ERSADTLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGLhqrDNDRLLQTLVHLRDL---GNTVIVVEHDED-AIRAADH 556
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARAL-AQATPVL-LLDEPTASL---DINHQVRTLELVRRLvddGKTAVAAIHDLDlAARYCDE 208
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 940388401 557 IidigpgAGVHGGHIIAQGTRDDILaTKDSVTGQF 591
Cdd:PRK09536 209 L------VLLADGRVRAAGPPADVL-TADTLRAAF 236
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
467-565 9.10e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 47.79  E-value: 9.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 467 LSFLINVGLNYLSLERSADTLSGGEAQRIRLASQIGAgLVGVMyVLDEPSIGLHQrDNDRLLQTLVH--LRDLGNTVIVV 544
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQF-MPKVL-LLDEITSALDE-SNKHNVNEIIHryVREQNIAVLWV 194
                         90       100
                 ....*....|....*....|.
gi 940388401 545 EHDEDAIRAADHIIDIGPGAG 565
Cdd:PRK10247 195 THDKDEINHADKVITLQPHAG 215
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
824-926 9.21e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 48.46  E-value: 9.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 824 QAATTLSGGEAQRVKLARELSKRdtGKTLyILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVV-KTADWVVD 902
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQ--ARYL-LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYV 208
                         90       100
                 ....*....|....*....|....
gi 940388401 903 LgpeggaGGGEILIAGTPEEVAEC 926
Cdd:PRK13638 209 L------RQGQILTHGAPGEVFAC 226
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
789-903 9.40e-06

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 49.29  E-value: 9.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 789 EMTVEDAHDYFDKIPAIARKLktlmdvGLSYIRLGQAATTLSGGEAQRVKLAREL-SKRDtgktLYILDEPTTGLhfaDI 867
Cdd:COG0488  119 EFEALGGWEAEARAEEILSGL------GFPEEDLDRPVSELSGGWRRRVALARALlSEPD----LLLLDEPTNHL---DL 185
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 940388401 868 EQLLVVLHRLRDHGNTIVVIEHN---LDvvKTADWVVDL 903
Cdd:COG0488  186 ESIEWLEEFLKNYPGTVLVVSHDryfLD--RVATRILEL 222
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
395-607 1.03e-05

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: 48.26  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  395 EELAKYQTSQAcpschgSRLRQEARHVF---IGQTNLPAITTMSIGEAMDFFEGLSLTGQKAQIAEkILKEirdrlsfli 471
Cdd:TIGR02769  73 QDLYQLDRKQR------RAFRRDVQLVFqdsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAE-LLDM--------- 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  472 nVGLNYLSLERSADTLSGGEAQRIRLASQIGAG--LVgvmyVLDEPSIGLhqrdnDRLLQT--LVHLRDL----GNTVIV 543
Cdd:TIGR02769 137 -VGLRSEDADKLPRQLSGGQLQRINIARALAVKpkLI----VLDEAVSNL-----DMVLQAviLELLRKLqqafGTAYLF 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388401  544 VEHDedaIRAADHIIDigPGAGVHGGHIIAQGTRDDILATKDSVTGQFLSGVRKiEVPQERNPT 607
Cdd:TIGR02769 207 ITHD---LRLVQSFCQ--RVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSAVLP-EHPVRRSIT 264
cbiO PRK13643
energy-coupling factor transporter ATPase;
450-585 1.04e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 48.19  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 450 GQKAQIAEKILKEirdRLSFlinVGLNYLSLERSADTLSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNDRLLQ 529
Cdd:PRK13643 114 GIPKEKAEKIAAE---KLEM---VGLADEFWEKSPFELSGGQMRRVAIAGILA--MEPEVLVLDEPTAGLDPKARIEMMQ 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 940388401 530 TLVHLRDLGNTVIVVEH-DEDAIRAADHIIDIgpgagvHGGHIIAQGTRDDILATKD 585
Cdd:PRK13643 186 LFESIHQSGQTVVLVTHlMDDVADYADYVYLL------EKGHIISCGTPSDVFQEVD 236
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
453-571 1.16e-05

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: 47.48  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 453 AQIAEKILKEIRDR-LSFLINVGLNYLsLERSADTLSGGEAQRIRLASqigAGLVGVMYVL-DEPSIGLHQRDNDRLLQT 530
Cdd:cd03255  107 LLLAGVPKKERRERaEELLERVGLGDR-LNHYPSELSGGQQQRVAIAR---ALANDPKIILaDEPTGNLDSETGKEVMEL 182
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 531 LVHL-RDLGNTVIVVEHDEDAIRAADHIIDIgpgagvHGGHI 571
Cdd:cd03255  183 LRELnKEAGTTIVVVTHDPELAEYADRIIEL------RDGKI 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
828-931 1.20e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 47.82  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 828 TLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLR-DHGNTIVVIEHNLDVVKTADWVVDLgpe 906
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLA---LNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVM--- 215
                         90       100
                 ....*....|....*....|....*
gi 940388401 907 ggaGGGEILIAGTPEEVAECERSHT 931
Cdd:PRK13648 216 ---NKGTVYKEGTPTEIFDHAEELT 237
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
822-924 1.23e-05

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: 48.57  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  822 LGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNT-IVVIEHNLD-VVKTADW 899
Cdd:TIGR02142 125 LGRLPGRLSGGEKQRVAIGRALL---SSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQeVLRLADR 201
                          90       100
                  ....*....|....*....|....*
gi 940388401  900 VVDLgpeggaGGGEILIAGTPEEVA 924
Cdd:TIGR02142 202 VVVL------EDGRVAAAGPIAEVW 220
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
807-892 1.29e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 47.70  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 807 RKLKTLMDVGLSYIRlGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIEQLLVVLHRLRD----HGN 882
Cdd:PRK09984 132 RALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQ---AKVILADEPIASL---DPESARIVMDTLRDinqnDGI 204
                         90
                 ....*....|
gi 940388401 883 TIVVIEHNLD 892
Cdd:PRK09984 205 TVVVTLHQVD 214
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
805-895 1.30e-05

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: 47.56  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 805 IARKLKTLMDVGLS---YIRlgqaATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL-RDH 880
Cdd:cd03256  122 KQRALAALERVGLLdkaYQR----ADQLSGGQQQRVAIARALMQQ---PKLILADEPVASLDPASSRQVMDLLKRInREE 194
                         90
                 ....*....|....*
gi 940388401 881 GNTIVVIEHNLDVVK 895
Cdd:cd03256  195 GITVIVSLHQVDLAR 209
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
812-891 1.37e-05

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 49.05  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 812 LMDVGLSYIR---------LGQAATTLSGGEAQRVKLARELsKRDtgKTLYILDEPTTGLHfADIEQLlvVLHRLRDH-- 880
Cdd:PRK11160 450 LQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARAL-LHD--APLLLLDEPTEGLD-AETERQ--ILELLAEHaq 523
                         90
                 ....*....|.
gi 940388401 881 GNTIVVIEHNL 891
Cdd:PRK11160 524 NKTVLMITHRL 534
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
452-581 1.38e-05

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: 47.33  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 452 KAQIAEKIlKEIRDRLsflinvGLNYLsLERSADTLSGGEAQRIRLASqigaGLV--GVMYVLDEPSIGLHQRDNDRLLQ 529
Cdd:cd03299  103 KKEIERKV-LEIAEML------GIDHL-LNRKPETLSGGEQQRVAIAR----ALVvnPKILLLDEPFSALDVRTKEKLRE 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 530 TLVHLRD-LGNTVIVVEHD-EDAIRAADHIidigpgAGVHGGHIIAQGTRDDIL 581
Cdd:cd03299  171 ELKKIRKeFGVTVLHVTHDfEEAWALADKV------AIMLNGKLIQVGKPEEVF 218
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
821-901 1.45e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 48.55  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGN-TIVVIEHNLDVV-KTAD 898
Cdd:PRK15134 149 RLTDYPHQLSGGERQRVMIAMALLTR---PELLIADEPTTALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVrKLAD 225

                 ...
gi 940388401 899 WVV 901
Cdd:PRK15134 226 RVA 228
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-547 1.46e-05

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: 47.75  E-value: 1.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 480 LERSADTLSGGEAQRIRLASQIGAGlvGVMYVLDEPS--IGLHQRDN-DRLLQTLVhlrDLGNTVIVVEHD 547
Cdd:cd03236  133 LDRNIDQLSGGELQRVAIAAALARD--ADFYFFDEPSsyLDIKQRLNaARLIRELA---EDDNYVLVVEHD 198
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
829-901 1.53e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 47.57  E-value: 1.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388401 829 LSGGEAQRVKLARELSKRdtGKTLyILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVVKT-ADWVV 901
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQ--GQVI-LLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTV 213
hmuV PRK13547
heme ABC transporter ATP-binding protein;
482-606 1.55e-05

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 47.51  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 482 RSADTLSGGEAQRIRLA---SQI---GAGLVGVMY-VLDEPSIGLHQRDNDRLLQTLVHL-RDLGNTVIVVEHDED-AIR 552
Cdd:PRK13547 141 RDVTTLSGGELARVQFArvlAQLwppHDAAQPPRYlLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNlAAR 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 553 AADHIidigpgAGVHGGHIIAQGTRDDILaTKDSVTGQFLSGVRKIEVPQERNP 606
Cdd:PRK13547 221 HADRI------AMLADGAIVAHGAPADVL-TPAHIARCYGFAVRLVDAGDGVPP 267
cbiO PRK13649
energy-coupling factor transporter ATPase;
801-923 1.59e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 47.82  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 801 KIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDH 880
Cdd:PRK13649 118 QEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAME---PKILVLDEPTAGLDPKGRKELMTLFKKLHQS 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 940388401 881 GNTIVVIEHNL-DVVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13649 195 GMTIVLVTHLMdDVANYADFVYVL------EKGKLVLSGKPKDI 232
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
821-901 1.71e-05

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 48.62  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIE---QLLVVLHRLRdHGNTIVVIEHNLDVVKTA 897
Cdd:COG1132  469 VVGERGVNLSGGQRQRIAIARALLKD---PPILILDEATSAL---DTEteaLIQEALERLM-KGRTTIVIAHRLSTIRNA 541

                 ....
gi 940388401 898 DWVV 901
Cdd:COG1132  542 DRIL 545
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
829-902 1.72e-05

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: 46.41  E-value: 1.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIEQLLV---VLHRLRDHGN-TIVVIEHNLDVvktADWVVD 902
Cdd:cd03222   72 LSGGELQRVAIAAALLRN---ATFYLFDEPSAYL---DIEQRLNaarAIRRLSEEGKkTALVVEHDLAV---LDYLSD 140
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
829-901 1.73e-05

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: 46.15  E-value: 1.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388401 829 LSGGEAQRVKLARELsKRDTgkTLYILDEPTTGLHFADIEQLL-VVLHRLRDhgNTIVVIEHNLDVVKTADWVV 901
Cdd:cd03247   99 FSGGERQRLALARIL-LQDA--PIVLLDEPTVGLDPITERQLLsLIFEVLKD--KTLIWITHHLTGIEHMDKIL 167
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
454-581 1.73e-05

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: 47.39  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 454 QIAEKILKEirdrlsflinVGLNYLSlERSADTLSGGEAQRIrlasQIGAGLVG--VMYVLDEPSIGL--HQRdnDRLLQ 529
Cdd:COG1119  121 ERARELLEL----------LGLAHLA-DRPFGTLSQGEQRRV----LIARALVKdpELLILDEPTAGLdlGAR--ELLLA 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 530 TLVHLRDLGNTVIV-VEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDIL 581
Cdd:COG1119  184 LLDKLAAEGAPTLVlVTHHvEEIPPGITHVLLL------KDGRVVAAGPKEEVL 231
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
445-575 1.84e-05

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: 46.72  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 445 GLSLTGQKAQIAEKILKEirdrlsflinVGLNYLsLERSADTLSGGEAQRIRLASQigagLV---GVMyVLDEPSIGLHQ 521
Cdd:cd03298   98 GLKLTAEDRQAIEVALAR----------VGLAGL-EKRLPGELSGGERQRVALARV----LVrdkPVL-LLDEPFAALDP 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 522 RDNDRLLQTLVHL-RDLGNTVIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQG 575
Cdd:cd03298  162 ALRAEMLDLVLDLhAETKMTVLMVTHQpEDAKRLAQRVVFL------DNGRIAAQG 211
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
455-601 1.85e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 47.92  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 455 IAEKILK-EIRDRLSFLIN-VGLNYLSLERSADTLSGGEAQRIRLasqigAGLVGV---MYVLDEPSIGLHQRDNDRLLQ 529
Cdd:PRK13631 143 VALGVKKsEAKKLAKFYLNkMGLDDSYLERSPFGLSGGQKRRVAI-----AGILAIqpeILIFDEPTAGLDPKGEHEMMQ 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940388401 530 TLVHLRDLGNTVIVVEHD-EDAIRAADHIIDIGPgagvhgGHIIAQGTRDDILATKDSVTgqflsgVRKIEVP 601
Cdd:PRK13631 218 LILDAKANNKTVFVITHTmEHVLEVADEVIVMDK------GKILKTGTPYEIFTDQHIIN------STSIQVP 278
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
789-901 1.87e-05

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 46.83  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 789 EMTVEDAHDYFDKIPAIARKL--KTLMDVGLSYIRlGQAATTLSGGEAQRVKLARE-LSKRDtgktLYILDEPTTGLHFA 865
Cdd:cd03268   86 NLTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALAlLGNPD----LLILDEPTNGLDPD 160
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 940388401 866 DIEQLLVVLHRLRDHGNTIVVIEHNL-DVVKTADWVV 901
Cdd:cd03268  161 GIKELRELILSLRDQGITVLISSHLLsEIQKVADRIG 197
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
14-41 1.90e-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: 45.84  E-value: 1.90e-05
                         10        20
                 ....*....|....*....|....*...
gi 940388401  14 LKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
824-891 2.03e-05

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: 46.79  E-value: 2.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 824 QAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGL---HFADIEQLLVVLHrlRDHgnTIVVIEHNL 891
Cdd:cd03260  137 LHALGLSGGQQQRLCLARALANE---PEVLLLDEPTSALdpiSTAKIEELIAELK--KEY--TIVIVTHNM 200
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
14-40 2.11e-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: 46.31  E-value: 2.11e-05
                         10        20
                 ....*....|....*....|....*..
gi 940388401  14 LKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
cbiO PRK13637
energy-coupling factor transporter ATPase;
805-923 2.13e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 47.35  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 805 IARKLKTLMD-VGLSYIRL-GQAATTLSGGEAQRVKLARELSKRDtgKTLyILDEPTTGLHFADIEQLLVVLHRLRD-HG 881
Cdd:PRK13637 119 IENRVKRAMNiVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEP--KIL-ILDEPTAGLDPKGRDEILNKIKELHKeYN 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 940388401 882 NTIVVIEHNL-DVVKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13637 196 MTIILVSHSMeDVAKLADRIIVM------NKGKCELQGTPREV 232
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
823-903 2.29e-05

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: 46.70  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 823 GQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIEQLLVVLHRLRD--HGNTIVVIEHNLDVVKTADWV 900
Cdd:cd03248  145 GEKGSQLSGGQKQRVAIARALIRN---PQVLILDEATSAL---DAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQI 218

                 ...
gi 940388401 901 VDL 903
Cdd:cd03248  219 LVL 221
GguA NF040905
sugar ABC transporter ATP-binding protein;
832-898 2.63e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 47.86  E-value: 2.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 832 GEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL-DVVKTAD 898
Cdd:NF040905 143 GKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLnEIRRVAD 207
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
486-584 2.74e-05

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 47.85  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 486 TLSGGEAQRIRLA------SQIgaglvgvmYVLDEPSIGLhqrD--NDRLLQTlvHLRDL--GNTVIVVEHDEDAIRAAD 555
Cdd:COG1132  476 NLSGGQRQRIAIArallkdPPI--------LILDEATSAL---DteTEALIQE--ALERLmkGRTTIVIAHRLSTIRNAD 542
                         90       100       110
                 ....*....|....*....|....*....|
gi 940388401 556 HIIdigpgagV-HGGHIIAQGTRDDILATK 584
Cdd:COG1132  543 RIL-------VlDDGRIVEQGTHEELLARG 565
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
787-925 3.24e-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: 47.49  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  787 VLEMTVEDAHDY-FDKIPAIARKLKTLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfa 865
Cdd:TIGR03269 127 VLDNVLEALEEIgYEGKEAVGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKE---PFLFLADEPTGTL--- 199
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388401  866 DIEQLLVVLHRLRDhgntiVVIEHNLDVVKTADW---VVDLGPEGG-AGGGEILIAGTPEEVAE 925
Cdd:TIGR03269 200 DPQTAKLVHNALEE-----AVKASGISMVLTSHWpevIEDLSDKAIwLENGEIKEEGTPDEVVA 258
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
805-891 3.34e-05

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 46.46  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 805 IARKLKtLMDvglsyiRLGQAATTLSGGEAQRVKLA-------RELSKRdtGKTLyILDEPTTGLhfaDIEQ---LLVVL 874
Cdd:PRK03695 110 VAEALG-LDD------KLGRSVNQLSGGEWQRVRLAavvlqvwPDINPA--GQLL-LLDEPMNSL---DVAQqaaLDRLL 176
                         90
                 ....*....|....*..
gi 940388401 875 HRLRDHGNTIVVIEHNL 891
Cdd:PRK03695 177 SELCQQGIAVVMSSHDL 193
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
446-558 3.55e-05

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: 45.26  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 446 LSLTGQKAQIAEKILKEIRDRLSFLI-NVGL-NYLS-LERSADTLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIG 518
Cdd:cd03229   57 ILIDGEDLTDLEDELPPLRRRIGMVFqDFALfPHLTvLENIALGLSGGQQQRVALARAL------AMdpdvLLLDEPTSA 130
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 519 LHQRDNDRLLQTLVHLRD-LGNTVIVVEHD-EDAIRAADHII 558
Cdd:cd03229  131 LDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLADRVV 172
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
801-894 3.59e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 47.03  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 801 KIPAiARKlktlmdvglsyiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDH 880
Cdd:PRK09473 147 KMPE-ARK------------RMKMYPHEFSGGMRQRVMIAMALLCR---PKLLIADEPTTALDVTVQAQIMTLLNELKRE 210
                         90
                 ....*....|....*
gi 940388401 881 GNT-IVVIEHNLDVV 894
Cdd:PRK09473 211 FNTaIIMITHDLGVV 225
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
800-901 3.59e-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: 45.98  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGL-----SYIRlgqaatTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVL 874
Cdd:cd03262  108 SKAEAEERALELLEKVGLadkadAYPA------QLSGGQQQRVAIARALAMN---PKVMLFDEPTSALDPELVGEVLDVM 178
                         90       100
                 ....*....|....*....|....*...
gi 940388401 875 HRLRDHGNTIVVIEHNLDVV-KTADWVV 901
Cdd:cd03262  179 KDLAEEGMTMVVVTHEMGFArEVADRVI 206
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
14-41 3.64e-05

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: 45.92  E-value: 3.64e-05
                         10        20
                 ....*....|....*....|....*...
gi 940388401  14 LKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
433-575 3.84e-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: 45.96  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 433 TMSIGEAmdFFEGLSLtgQKAQIAEKILKEIRDRLsfLINVGLNYLSLERSADTLSGGEAQRIRLASQIGAG--LVgvmy 510
Cdd:cd03257   98 RMTIGEQ--IAEPLRI--HGKLSKKEARKEAVLLL--LVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNpkLL---- 167
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 511 VLDEPSIGLHQRDNDRLLQTLVHLRD-LGNTVIVVEHDEDAIRA-ADHIIdigpgagV-HGGHIIAQG 575
Cdd:cd03257  168 IADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKiADRVA-------VmYAGKIVEEG 228
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
480-582 4.11e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 46.55  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLasqigAGLVGV---MYVLDEPSIGLHQRDNDRLLQTLVHLRDLGN-TVIVVEHDEDAIRAAD 555
Cdd:PRK13635 134 LNREPHRLSGGQKQRVAI-----AGVLALqpdIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQAD 208
                         90       100
                 ....*....|....*....|....*..
gi 940388401 556 HIIDIgpgagvHGGHIIAQGTRDDILA 582
Cdd:PRK13635 209 RVIVM------NKGEILEEGTPEEIFK 229
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
770-891 4.36e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 47.31  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 770 YNRETLEVQYKGKN----------------IHQVL----EMTVedAHDYF--------------DKIPAIARKLktLMDV 815
Cdd:PRK10762  54 YTRDAGSILYLGKEvtfngpkssqeagigiIHQELnlipQLTI--AENIFlgrefvnrfgridwKKMYAEADKL--LARL 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 816 GLSYiRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL 891
Cdd:PRK10762 130 NLRF-SSDKLVGELSIGEQQMVEIAKVLS---FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
828-903 4.81e-05

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: 44.84  E-value: 4.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 828 TLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIEQLLVVLHRLRDHGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:cd03223   91 VLSGGEQQRLAFARLLLHK---PKFVFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL 160
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
806-901 5.00e-05

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 45.82  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 806 ARKLKTLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLH-FADIE--QLLVVLhrLRDHGN 882
Cdd:PRK11247 112 DAALQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHR---PGLLLLDEPLGALDaLTRIEmqDLIESL--WQQHGF 185
                         90       100
                 ....*....|....*....|
gi 940388401 883 TIVVIEHNL-DVVKTADWVV 901
Cdd:PRK11247 186 TVLLVTHDVsEAVAMADRVL 205
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
2-40 5.04e-05

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: 45.64  E-value: 5.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 940388401   2 ENIEVR-GARTHNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:cd03256    4 ENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTL 43
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
14-41 5.35e-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: 44.18  E-value: 5.35e-05
                          10        20
                  ....*....|....*....|....*...
gi 940388401   14 LKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL 28
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
484-594 6.55e-05

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 45.26  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 484 ADTLSGGEAQRIrlasQIGAGLVGV--MYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDED-AIRAADHiidi 560
Cdd:PRK11614 135 AGTMSGGEQQML----AIGRALMSQprLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADR---- 206
                         90       100       110
                 ....*....|....*....|....*....|....
gi 940388401 561 gpGAGVHGGHIIAQGTRDDILATkDSVTGQFLSG 594
Cdd:PRK11614 207 --GYVLENGHVVLEDTGDALLAN-EAVRSAYLGG 237
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
462-597 6.71e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 45.73  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 462 EIRDR-LSFLINVGLNYLSLERSADTLSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNT 540
Cdd:PRK10619 127 EARERaVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALA--MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 541 VIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDILAT-KDSVTGQFLSGVRK 597
Cdd:PRK10619 205 MVVVTHEmGFARHVSSHVIFL------HQGKIEEEGAPEQLFGNpQSPRLQQFLKGSLK 257
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
823-901 6.73e-05

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 46.64  E-value: 6.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401  823 GQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHfADIEQLLVVLHRLRDHgnTIVVIEHNLDVVKTADWVV 901
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRK---PRVLILDEATSALD-AECEQLLQESRSRASR--TVLLIAHRLSTVERADQIL 684
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
790-887 6.92e-05

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: 44.88  E-value: 6.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 790 MTVEDAHDYFDKIPAI------ARKLKTLMDVGLsYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLh 863
Cdd:cd03264   87 FTVREFLDYIAWLKGIpskevkARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD---PSILIVDEPTAGL- 161
                         90       100
                 ....*....|....*....|....
gi 940388401 864 faDIEQLLVVLHRLRDHGNTIVVI 887
Cdd:cd03264  162 --DPEERIRFRNLLSELGEDRIVI 183
PTZ00243 PTZ00243
ABC transporter; Provisional
822-903 7.04e-05

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 47.08  E-value: 7.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  822 LGQAATTLSGGEAQRVKLAREL-SKRDtgktLYILDEPTTGLHfADIEQLLV---VLHRLrdHGNTIVVIEHNLDVVKTA 897
Cdd:PTZ00243  776 IGEKGVNLSGGQKARVSLARAVyANRD----VYLLDDPLSALD-AHVGERVVeecFLGAL--AGKTRVLATHQVHVVPRA 848

                  ....*.
gi 940388401  898 DWVVDL 903
Cdd:PTZ00243  849 DYVVAL 854
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
821-890 7.87e-05

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 45.16  E-value: 7.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPT------TGLHFADieqLLVVLHrlRDHGNTIVVIEHN 890
Cdd:PRK10584 139 RLDHLPAQLSGGEQQRVALARAFNGR---PDVLFADEPTgnldrqTGDKIAD---LLFSLN--REHGTTLILVTHD 206
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
782-923 7.94e-05

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: 45.02  E-value: 7.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 782 KNIHQVLEMTVEDAHDYFDKIPAIARKLktlmdvGLSYIrLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTG 861
Cdd:cd03299   90 KNIAYGLKKRKVDKKEIERKVLEIAEML------GIDHL-LNRKPETLSGGEQQRVAIARALV---VNPKILLLDEPFSA 159
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388401 862 LHFADIEQLLVVLHRLRDHGNTIVV-IEHNLDVVKT-ADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:cd03299  160 LDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIM------LNGKLIQVGKPEEV 217
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
781-895 8.68e-05

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 45.30  E-value: 8.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 781 GKNIHQVLeMTVEDAHdyFDKIPAIArkLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTT 860
Cdd:PRK11701 109 GGNIGERL-MAVGARH--YGDIRATA--GDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLV---THPRLVFMDEPTG 180
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 940388401 861 GLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDVVK 895
Cdd:PRK11701 181 GLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVAR 216
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
787-901 9.20e-05

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 45.01  E-value: 9.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 787 VLEMTVEDAHDYFDKIpaiarkLKTLmdvglsyiRLGQAATT----LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGL 862
Cdd:PRK11124 110 VLGLSKDQALARAEKL------LERL--------RLKPYADRfplhLSGGQQQRVAIARALMME---PQVLLFDEPTAAL 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 940388401 863 hfaDIE---QLLVVLHRLRDHGNTIVVIEHNLDVV-KTADWVV 901
Cdd:PRK11124 173 ---DPEitaQIVSIIRELAETGITQVIVTHEVEVArKTASRVV 212
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
829-894 9.43e-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: 44.67  E-value: 9.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVV 894
Cdd:cd03266  137 FSTGMRQKVAIARALVHD---PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEV 199
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1-40 9.63e-05

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 43.77  E-value: 9.63e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 940388401   1 MENIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:cd00267    2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTL 41
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
622-650 1.01e-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: 44.38  E-value: 1.01e-04
                         10        20
                 ....*....|....*....|....*....
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLIN 650
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSLLS 49
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
487-589 1.03e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 45.07  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASqIGAGLVGVMyVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRA-ADHIIDIGpgag 565
Cdd:PRK13639 138 LSGGQKKRVAIAG-ILAMKPEII-VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMS---- 211
                         90       100
                 ....*....|....*....|....
gi 940388401 566 vhGGHIIAQGTRDDILATKDSVTG 589
Cdd:PRK13639 212 --DGKIIKEGTPKEVFSDIETIRK 233
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
828-903 1.04e-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: 44.41  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 828 TLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFA---DIEQLLVVLHRLRdhGNTIVVIEHNL-DVVKTADWVVDL 903
Cdd:cd03298  128 ELSGGERQRVALARVLVRD---KPVLLLDEPFAALDPAlraEMLDLVLDLHAET--KMTVLMVTHQPeDAKRLAQRVVFL 202
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
434-558 1.05e-04

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 45.79  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 434 MSIGEAMDFfeGLSLTG-QKAQIAEKIlKEIRDRLSflinvgLNYLsLERSADTLSGGeaQRIRLAsqIGAGLVG--VMY 510
Cdd:PRK11000  90 LSVAENMSF--GLKLAGaKKEEINQRV-NQVAEVLQ------LAHL-LDRKPKALSGG--QRQRVA--IGRTLVAepSVF 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940388401 511 VLDEPSIGLHQ--RDNDRLLQTLVHLRdLGNTVIVVEHDE-DAIRAADHII 558
Cdd:PRK11000 156 LLDEPLSNLDAalRVQMRIEISRLHKR-LGRTMIYVTHDQvEAMTLADKIV 205
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
787-892 1.11e-04

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 45.79  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 787 VLEMTVED--AHDYFDKIP----------AIARKLKTLMDvglSY-IR---LGQAATTLSGGEAQRVKLARELSKRdtgK 850
Cdd:COG3845  348 VPDMSVAEnlILGRYRRPPfsrggfldrkAIRAFAEELIE---EFdVRtpgPDTPARSLSGGNQQKVILARELSRD---P 421
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 851 TLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLD 892
Cdd:COG3845  422 KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLD 463
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
462-580 1.23e-04

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: 44.64  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 462 EIRDRLSFLIN-VGLNYLSlERSADTLSGGEAQRIRLASQIgAGLVGVMyVLDEPSIGLHQRDNDRLLQTLVHLRD-LGN 539
Cdd:cd03296  112 EIRAKVHELLKlVQLDWLA-DRYPAQLSGGQRQRVALARAL-AVEPKVL-LLDEPFGALDAKVRKELRRWLRRLHDeLHV 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 540 TVIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDI 580
Cdd:cd03296  189 TTVFVTHDqEEALEVADRVVVM------NKGRIEQVGTPDEV 224
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
801-903 1.24e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 44.32  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 801 KIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELskRDTGKTLyILDEPTTGLHFADIEQLLVVLHRL-RD 879
Cdd:PRK10247 110 QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVL-LLDEITSALDESNKHNVNEIIHRYvRE 186
                         90       100
                 ....*....|....*....|....
gi 940388401 880 HGNTIVVIEHNLDVVKTADWVVDL 903
Cdd:PRK10247 187 QNIAVLWVTHDKDEINHADKVITL 210
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
806-892 1.31e-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: 44.94  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 806 ARKLKTLMDVGL-----SYIRlgqaatTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLH---FADIEQLLVVLHrl 877
Cdd:cd03294  139 ERAAEALELVGLegwehKYPD------ELSGGMQQRVGLARALA---VDPDILLMDEAFSALDpliRREMQDELLRLQ-- 207
                         90
                 ....*....|....*
gi 940388401 878 RDHGNTIVVIEHNLD 892
Cdd:cd03294  208 AELQKTIVFITHDLD 222
PLN03211 PLN03211
ABC transporter G-25; Provisional
815-889 1.36e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 45.64  E-value: 1.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940388401 815 VGLSYIRlgqaatTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEH 889
Cdd:PLN03211 199 IGNSFIR------GISGGERKRVSIAHEML---INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
622-887 1.39e-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: 44.18  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLINdtlfklahtelngattaeaapykSISGLDHFDkvididqspigrtprsnpa 701
Cdd:cd03234   23 LNDVSLHVESGQVMAILGSSGSGKTTLLD-----------------------AISGRVEGG------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 702 tytGIFTGiRELFAGtqEARSRGYKVGRFSFnvkggrceacqgdgvikVEMH--FLPDVYVpcdvckgarynRETLevQY 779
Cdd:cd03234   61 ---GTTSG-QILFNG--QPRKPDQFQKCVAY-----------------VRQDdiLLPGLTV-----------RETL--TY 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 780 KGknihqVLEMTVEDAHDYFDKIPAIARklktLMDVGLSYIRlGQAATTLSGGEAQRVKLARELSkRDTGktLYILDEPT 859
Cdd:cd03234  105 TA-----ILRLPRKSSDAIRKKRVEDVL----LRDLALTRIG-GNLVKGISGGERRRVSIAVQLL-WDPK--VLILDEPT 171
                        250       260
                 ....*....|....*....|....*...
gi 940388401 860 TGLHFADIEQLLVVLHRLRdHGNTIVVI 887
Cdd:cd03234  172 SGLDSFTALNLVSTLSQLA-RRNRIVIL 198
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
828-892 1.44e-04

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: 44.21  E-value: 1.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 828 TLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGN-TIVVIEHNLD 892
Cdd:cd03297  131 QLSGGEKQRVALARALAAQ---PELLLLDEPFSALDRALRLQLLPELKQIKKNLNiPVIFVTHDLS 193
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
817-928 1.47e-04

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 44.50  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 817 LSYIR--LGQAattLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHN---- 890
Cdd:PRK10895 127 IEHLRdsMGQS---LSGGERRRVEIARALA---ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvret 200
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 940388401 891 LDVVKTAdWVVDLGPeggagggeiLIA-GTPEEVAECER 928
Cdd:PRK10895 201 LAVCERA-YIVSQGH---------LIAhGTPTEILQDEH 229
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
487-558 1.53e-04

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: 43.19  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940388401 487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRA-ADHII 558
Cdd:cd03216   83 LSVGERQMVEIARALarNARLL----ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVT 153
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
822-901 1.54e-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: 45.09  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 822 LGQAATTLSGGEAQRVKLAREL--SKRdtgktLYILDEPTTGLHFADIEQLLVVLHRLRDHGNT-IVVIEHNLD-VVKTA 897
Cdd:COG4148  127 LDRRPATLSGGERQRVAIGRALlsSPR-----LLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDeVARLA 201

                 ....
gi 940388401 898 DWVV 901
Cdd:COG4148  202 DHVV 205
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
6-51 1.56e-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: 1.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 940388401   6 VRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQR 51
Cdd:cd03227    3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
807-903 1.58e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 44.65  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 807 RKLKTLMD-----VGL---SYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFA---DIEQLLVVLH 875
Cdd:PRK14246 124 REIKKIVEeclrkVGLwkeVYDRLNSPASQLSGGQQQRLTIARALALK---PKVLLMDEPTSMIDIVnsqAIEKLITELK 200
                         90       100
                 ....*....|....*....|....*....
gi 940388401 876 RlrdhGNTIVVIEHN-LDVVKTADWVVDL 903
Cdd:PRK14246 201 N----EIAIVIVSHNpQQVARVADYVAFL 225
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
454-556 1.65e-04

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 43.89  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 454 QIAEKILKEIRDRLSFLIN-VGLnyLSLERS-ADTLSGGEAQRIRLASqigaGLVG--VMYVLDEPSIGLHQRDNDRLLQ 529
Cdd:COG2884  105 RVTGKSRKEIRRRVREVLDlVGL--SDKAKAlPHELSGGEQQRVAIAR----ALVNrpELLLADEPTGNLDPETSWEIME 178
                         90       100
                 ....*....|....*....|....*..
gi 940388401 530 TLVHLRDLGNTVIVVEHDEDAIRAADH 556
Cdd:COG2884  179 LLEEINRRGTTVLIATHDLELVDRMPK 205
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-559 1.84e-04

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: 44.32  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 480 LERSADTLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIglHQRDNDRLLQTLVHLRDLGN---TVIVVEHDedaIRAA 554
Cdd:cd03237  109 LDREVPELSGGELQRVAIAACLSkdADI----YLLDEPSA--YLDVEQRLMASKVIRRFAENnekTAFVVEHD---IIMI 179

                 ....*
gi 940388401 555 DHIID 559
Cdd:cd03237  180 DYLAD 184
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
828-894 1.88e-04

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: 43.81  E-value: 1.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940388401 828 TLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVV 894
Cdd:cd03269  128 ELSKGNQQKVQFIAAVIHD---PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELV 191
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
824-900 1.97e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 45.04  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 824 QAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHF---ADIEQLlvvLHRLRDHGNTIVVIEHNLD-VVKTADW 899
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEAS---PQLLIVDEPTRGVDVsarNDIYQL---IRSIAAQNVAVLFISSDLEeIEQMADR 472

                 .
gi 940388401 900 V 900
Cdd:PRK15439 473 V 473
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
487-575 2.05e-04

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: 43.07  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNDRLLQTLV-HLRDlgNTVIVVEHDEDAIRAADHIIDIgpg 563
Cdd:cd03247   99 FSGGERQRLALARILlqDAPIV----LLDEPTVGLDPITERQLLSLIFeVLKD--KTLIWITHHLTGIEHMDKILFL--- 169
                         90
                 ....*....|..
gi 940388401 564 agvHGGHIIAQG 575
Cdd:cd03247  170 ---ENGKIIMQG 178
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
14-41 2.22e-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: 45.21  E-value: 2.22e-04
                         10        20
                 ....*....|....*....|....*...
gi 940388401  14 LKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:COG2274  491 LDNISLTIKPGERVAIVGRSGSGKSTLL 518
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
825-903 2.36e-04

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: 43.25  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 825 AATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLlvvLHRLRDH----GNTIVVIEHNLDVVKTADWV 900
Cdd:cd03231  122 PVAQLSAGQQRRVALARLLL---SGRPLWILDEPTTALDKAGVARF---AEAMAGHcargGMVVLTTHQDLGLSEAGARE 195

                 ...
gi 940388401 901 VDL 903
Cdd:cd03231  196 LDL 198
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
462-547 2.49e-04

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: 44.78  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 462 EIRDRLsflinvGLNYLsLERSADTLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrD-NDRLLQTLV---HLR 535
Cdd:COG1245  438 EIIKPL------GLEKL-LDKNVKDLSGGELQRVAIAACLSrdADL----YLLDEPSAHL---DvEQRLAVAKAirrFAE 503
                         90
                 ....*....|..
gi 940388401 536 DLGNTVIVVEHD 547
Cdd:COG1245  504 NRGKTAMVVDHD 515
cbiO PRK13640
energy-coupling factor transporter ATPase;
457-580 2.74e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 44.02  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 457 EKILKEIRDRLSfliNVG-LNYLSLERSadTLSGGEAQRIRLasqigAGLVGV---MYVLDEPSIGLHQRDNDRLLQTLV 532
Cdd:PRK13640 118 PEMIKIVRDVLA---DVGmLDYIDSEPA--NLSGGQKQRVAI-----AGILAVepkIIILDESTSMLDPAGKEQILKLIR 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 940388401 533 HLRDLGN-TVIVVEHDEDAIRAADHIIDIgpgagvHGGHIIAQGTRDDI 580
Cdd:PRK13640 188 KLKKKNNlTVISITHDIDEANMADQVLVL------DDGKLLAQGSPVEI 230
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
821-891 2.79e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 43.61  E-value: 2.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHgNTIVVIEHNL 891
Cdd:PRK14239 141 RLHDSALGLSGGQQQRVCIARVLA---TSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSM 207
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
829-923 2.82e-04

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: 43.57  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLhfaDIE---QLLVVLHRL-RDHGNTIVVIEHNLDVVKTADWVVDLg 904
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMR---PDIIILDEATSML---DPKgrkEVLETIRKLnKEEGITVISITHDMEEAVLADRVIVM- 209
                          90
                  ....*....|....*....
gi 940388401  905 peggaGGGEILIAGTPEEV 923
Cdd:TIGR04520 210 -----NKGKIVAEGTPREI 223
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
622-898 2.99e-04

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: 43.37  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLINdTLFKLahtelngattaeaapYKSISGLDHFD----KVIDID--QSPIGRT 695
Cdd:cd03253   17 LKDVSFTIPAGKKVAIVGPSGSGKSTILR-LLFRF---------------YDVSSGSILIDgqdiREVTLDslRRAIGVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 696 PRSNPatytgiftgireLFAGTQEarsrgykvgrfsFNVKGGRCEACQGDgVIKVemhflpdvyvpcdvCKGARynretl 775
Cdd:cd03253   81 PQDTV------------LFNDTIG------------YNIRYGRPDATDEE-VIEA--------------AKAAQ------ 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 776 evqykgknIHqvlemtvedahdyfDKIPAIARKLKTlmdvglsyiRLGQAATTLSGGEAQRVKLARELSKrdtGKTLYIL 855
Cdd:cd03253  116 --------IH--------------DKIMRFPDGYDT---------IVGERGLKLSGGEKQRVAIARAILK---NPPILLL 161
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 940388401 856 DEPTTGLhfaDIEQLLVVLHRLRD--HGNTIVVIEHNLDVVKTAD 898
Cdd:cd03253  162 DEATSAL---DTHTEREIQAALRDvsKGRTTIVIAHRLSTIVNAD 203
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
829-889 3.00e-04

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 44.65  E-value: 3.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401  829 LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEH 889
Cdd:TIGR00955 167 LSGGERKRLAFASELL---TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
461-581 3.08e-04

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 43.98  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDRLSFLIN-VGLNYLSlERSADTLSGGEAQRI---R-LASQIGAGLvgvmyvLDEPSIGL------HQRdndRLLQ 529
Cdd:COG1118  108 AEIRARVEELLElVQLEGLA-DRYPSQLSGGQRQRValaRaLAVEPEVLL------LDEPFGALdakvrkELR---RWLR 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 530 TLvhLRDLGNTVIVVEHD-EDAIRAADHIIdigpgagV-HGGHIIAQGTRDDIL 581
Cdd:COG1118  178 RL--HDELGGTTVFVTHDqEEALELADRVV-------VmNQGRIEQVGTPDEVY 222
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
823-892 3.09e-04

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 43.82  E-value: 3.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 823 GQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLD 892
Cdd:PRK10253 138 DQSVDTLSGGQRQRAWIAMVLAQE---TAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLN 205
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
486-564 3.36e-04

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: 43.19  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 486 TLSGGEAQRIRLAsqigAGLVG---VMyVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRA-ADHIIDIG 561
Cdd:COG4778  152 TFSGGEQQRVNIA----RGFIAdppLL-LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVT 226

                 ...
gi 940388401 562 PGA 564
Cdd:COG4778  227 PFS 229
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
487-563 3.46e-04

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: 41.67  E-value: 3.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 487 LSGGEAQRIRLASqigAGLVGV-MYVLDEPSIGLhqrDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRA-ADHIIDIGPG 563
Cdd:cd03221   71 LSGGEKMRLALAK---LLLENPnLLLLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
cbiO PRK13646
energy-coupling factor transporter ATPase;
776-901 3.47e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 43.61  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 776 EVQYKGKNIHQVLEMTVEDAHDYfdkipaiarklktLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYIL 855
Cdd:PRK13646 106 EIIFGPKNFKMNLDEVKNYAHRL-------------LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA---MNPDIIVL 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 940388401 856 DEPTTGLHFADIEQLLVVLHRLR-DHGNTIVVIEHNL-DVVKTADWVV 901
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMnEVARYADEVI 217
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
810-903 3.52e-04

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 43.22  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  810 KTLMDVGLSYIRLGQAA----TTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTI 884
Cdd:TIGR01184  92 RAIVEEHIALVGLTEAAdkrpGQLSGGMKQRVAIARALSIR---PKVLLLDEPFGALDALTRGNLQEELMQIwEEHRVTV 168
                          90       100
                  ....*....|....*....|
gi 940388401  885 VVIEHNLD-VVKTADWVVDL 903
Cdd:TIGR01184 169 LMVTHDVDeALLLSDRVVML 188
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
812-895 3.60e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 44.39  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 812 LMDVGLSyIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL 891
Cdd:PRK09700 130 LLRVGLK-VDLDEKVANLSISHKQMLEIAKTLM---LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKL 205

                 ....
gi 940388401 892 DVVK 895
Cdd:PRK09700 206 AEIR 209
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
801-900 3.72e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 44.27  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 801 KIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELsKRDTgkTLYILDEPTTGLHFADIEQLLVVLHRLRDH 880
Cdd:PRK15439 113 KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL-MRDS--RILILDEPTASLTPAETERLFSRIRELLAQ 189
                         90       100
                 ....*....|....*....|.
gi 940388401 881 GNTIVVIEHNL-DVVKTADWV 900
Cdd:PRK15439 190 GVGIVFISHKLpEIRQLADRI 210
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
486-582 3.88e-04

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 42.96  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 486 TLSGGEAQRIRLASQIGAGLVGVMyvLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDedaIRaadHIIDIGPGAG 565
Cdd:PRK10895 137 SLSGGERRRVEIARALAANPKFIL--LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN---VR---ETLAVCERAY 208
                         90
                 ....*....|....*...
gi 940388401 566 -VHGGHIIAQGTRDDILA 582
Cdd:PRK10895 209 iVSQGHLIAHGTPTEILQ 226
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
484-548 3.91e-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: 44.27  E-value: 3.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940388401  484 ADTLSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNDRLLQTLVHLRDlGNTVIVVEHDE 548
Cdd:TIGR02868 469 GARLSGGERQRLALARALlaDAPIL----LLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
457-547 3.92e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 44.03  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 457 EKILKEIRDRL--SFLIN-----VGLNYLsLERSADTLSGGEAQRIRLASQIG--AGLvgvmYVLDEPSIGLhqrD-NDR 526
Cdd:PRK13409 418 EDLLRSITDDLgsSYYKSeiikpLQLERL-LDKNVKDLSGGELQRVAIAACLSrdADL----YLLDEPSAHL---DvEQR 489
                         90       100
                 ....*....|....*....|....
gi 940388401 527 LLQTLV---HLRDLGNTVIVVEHD 547
Cdd:PRK13409 490 LAVAKAirrIAEEREATALVVDHD 513
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
828-927 4.09e-04

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 43.24  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 828 TLSGGEAQRVKLAReLSKRDTGKTLyiLDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDV-VKTADWVVDLGP 905
Cdd:PRK10575 147 SLSGGERQRAWIAM-LVAQDSRCLL--LDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMaARYCDYLVALRG 223
                         90       100
                 ....*....|....*....|...
gi 940388401 906 EGgagggeiLIA-GTPEEVAECE 927
Cdd:PRK10575 224 GE-------MIAqGTPAELMRGE 239
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
4-40 4.22e-04

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: 42.87  E-value: 4.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 940388401   4 IEVRGART-----HNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:cd03261    1 IELRGLTKsfggrTVLKGVDLDVRRGEILAIIGPSGSGKSTL 42
cbiO PRK13643
energy-coupling factor transporter ATPase;
815-923 4.27e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 43.18  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 815 VGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL-DV 893
Cdd:PRK13643 131 VGLADEFWEKSPFELSGGQMRRVAIAGILAME---PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMdDV 207
                         90       100       110
                 ....*....|....*....|....*....|
gi 940388401 894 VKTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13643 208 ADYADYVYLL------EKGHIISCGTPSDV 231
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
829-901 4.36e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 44.18  E-value: 4.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940388401 829 LSGGEAQRVKLARELSKrdtGKTLYILDEPTTGLHFADIEQLLVVLHRLRdHGNTIVVIEHNLDVVKTADWVV 901
Cdd:PRK13657 472 LSGGERQRLAIARALLK---DPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRIL 540
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
812-880 4.54e-04

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 42.35  E-value: 4.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401  812 LMDVGLSYIRlGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLlvvLHRLRDH 880
Cdd:TIGR01189 112 LAAVGLTGFE-DLPAAQLSAGQQRRLALARLWL---SRRPLWILDEPTTALDKAGVALL---AGLLRAH 173
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
8-40 4.64e-04

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: 42.48  E-value: 4.64e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 940388401   8 GARTHNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:cd03255   14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL 46
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
813-889 4.86e-04

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 43.85  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 813 MDVGLSYIrLGQAATTLSGGEAQRVKLARELsKRDTgkTLYILDEPTTGLHF-------ADIEQL------LVVLHRLR- 878
Cdd:PRK11176 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARAL-LRDS--PILILDEATSALDTeseraiqAALDELqknrtsLVIAHRLSt 541
                         90
                 ....*....|..
gi 940388401 879 -DHGNTIVVIEH 889
Cdd:PRK11176 542 iEKADEILVVED 553
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
2-41 4.94e-04

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: 41.82  E-value: 4.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 940388401   2 ENIEVR--GARTHNLKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:cd03246    4 ENVSFRypGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLA 45
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
806-895 4.97e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 43.93  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 806 ARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLR-DHGNTI 884
Cdd:PRK15134 403 QQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILK---PSLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAY 479
                         90
                 ....*....|.
gi 940388401 885 VVIEHNLDVVK 895
Cdd:PRK15134 480 LFISHDLHVVR 490
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
487-548 5.10e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 42.46  E-value: 5.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940388401 487 LSGGEAQRIRLASQIgAGLVGVMYVlDEPSIGLHQRDNDRLLQTLVHL-RDLGNTVIVVEHDE 548
Cdd:PRK10584 147 LSGGEQQRVALARAF-NGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
829-890 5.16e-04

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 43.29  E-value: 5.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGL--HFADIEQLLVV--LHRLrdhGNTIVVIEHN 890
Cdd:PRK11607 150 LSGGQRQRVALARSLAKR---PKLLLLDEPMGALdkKLRDRMQLEVVdiLERV---GVTCVMVTHD 209
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
827-903 5.16e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 43.57  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 827 TTLSGGEAQRVKLAREL-SKRDtgktLYILDEPTTGLhfaDIEQLLVVLHRLRDHGNTIVVIEHN---LDVVktADWVVD 902
Cdd:PRK11819 162 TKLSGGERRRVALCRLLlEKPD----MLLLDEPTNHL---DAESVAWLEQFLHDYPGTVVAVTHDryfLDNV--AGWILE 232

                 .
gi 940388401 903 L 903
Cdd:PRK11819 233 L 233
hmuV PRK13547
heme ABC transporter ATP-binding protein;
822-926 5.35e-04

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 42.89  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 822 LGQAATTLSGGEAQRVKLARELSK------RDTGKTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDV- 893
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFARVLAQlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLa 218
                         90       100       110
                 ....*....|....*....|....*....|...
gi 940388401 894 VKTADWVVDLGPEGGAGGGEILIAGTPEEVAEC 926
Cdd:PRK13547 219 ARHADRIAMLADGAIVAHGAPADVLTPAHIARC 251
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
810-903 5.40e-04

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 43.64  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 810 KTLMDVGLSYI--RLGQAA---TTLSGGEAQRVKLAR-ELSKRDtgktLYILDEPTTGLhfaDIEQLLVVLHRLRDH--G 881
Cdd:COG4178  462 EALEAVGLGHLaeRLDEEAdwdQVLSLGEQQRLAFARlLLHKPD----WLFLDEATSAL---DEENEAALYQLLREElpG 534
                         90       100
                 ....*....|....*....|..
gi 940388401 882 NTIVVIEHNLDVVKTADWVVDL 903
Cdd:COG4178  535 TTVISVGHRSTLAAFHDRVLEL 556
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
455-547 5.41e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 42.50  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 455 IAEKILKEIRDR-LSFLINVGLNYLSLERSADtLSGGEAQRIRLASqigaGLVG--VMYVLDEPSIGLHQRDNDRLLQTL 531
Cdd:PRK11629 114 IGKKKPAEINSRaLEMLAAVGLEHRANHRPSE-LSGGERQRVAIAR----ALVNnpRLVLADEPTGNLDARNADSIFQLL 188
                         90
                 ....*....|....*..
gi 940388401 532 VHL-RDLGNTVIVVEHD 547
Cdd:PRK11629 189 GELnRLQGTAFLVVTHD 205
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
486-584 5.46e-04

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: 42.53  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 486 TLSGGEAQRIRLASQIgaglvgV----MYVLDEPSIGLhqrDND--RLLQ-TLVHLRdLGNTVIVVEHDEDAIRAADHII 558
Cdd:cd03249  139 QLSGGQKQRIAIARAL------LrnpkILLLDEATSAL---DAEseKLVQeALDRAM-KGRTTIVIAHRLSTIRNADLIA 208
                         90       100
                 ....*....|....*....|....*.
gi 940388401 559 digpgaGVHGGHIIAQGTRDDILATK 584
Cdd:cd03249  209 ------VLQNGQVVEQGTHDELMAQK 228
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
807-895 5.76e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 42.50  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 807 RKLKTLMDVGLSYiRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGL--HFAD-IEQLLVVLHRLrdHGNT 883
Cdd:PRK11629 125 RALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNN---PRLVLADEPTGNLdaRNADsIFQLLGELNRL--QGTA 198
                         90
                 ....*....|..
gi 940388401 884 IVVIEHNLDVVK 895
Cdd:PRK11629 199 FLVVTHDLQLAK 210
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
803-895 5.91e-04

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 43.14  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 803 PAIARKLKTLMD-VGLSyirlGQAA---TTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRL- 877
Cdd:COG1135  115 AEIRKRVAELLElVGLS----DKADaypSQLSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTRSILDLLKDIn 187
                         90
                 ....*....|....*...
gi 940388401 878 RDHGNTIVVIEHNLDVVK 895
Cdd:COG1135  188 RELGLTIVLITHEMDVVR 205
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
471-566 6.03e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 471 INVGLNYLSLERSADTLSGGEaqRI------RLA-SQIGAGLVGVMyVLDEPSIGLHQRDNDRLLQTLV-HLRDLGNtVI 542
Cdd:PRK03918 773 VKLFVVYQGKERPLTFLSGGE--RIalglafRLAlSLYLAGNIPLL-ILDEPTPFLDEERRRKLVDIMErYLRKIPQ-VI 848
                         90       100
                 ....*....|....*....|....
gi 940388401 543 VVEHDEDAIRAADHIIDIGPGAGV 566
Cdd:PRK03918 849 IVSHDEELKDAADYVIRVSLEGGV 872
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
829-892 6.29e-04

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: 42.07  E-value: 6.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401 829 LSGGEAQRVKLARELSKRdtGKTLyILDEPttglhFA--------DIEQLLVVLhrLRDHGNTIVVIEHNLD 892
Cdd:cd03293  132 LSGGMRQRVALARALAVD--PDVL-LLDEP-----FSaldaltreQLQEELLDI--WRETGKTVLLVTHDID 193
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
4-40 6.30e-04

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: 42.27  E-value: 6.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 940388401   4 IEVR------GARTHnLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:COG1127    6 IEVRnltksfGDRVV-LDGVSLDVPRGEILAIIGGSGSGKSVL 47
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
333-592 6.44e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 43.86  E-value: 6.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  333 DVPFEKLAKESQKIILE-GSGQTKIA------FNYRNDRgdLITRNHEFEGVLNNMNRRYRETESNSVREELAKYQTSQA 405
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGEtGSGKSTVMsllmrfYDLKNDH--HIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKE 1263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  406 CPSCHGSRL------------------RQEARHVFIGQTNLPAITTMSIGEAMDF-FEGLSLTGQKAQIAEKILKEIRDR 466
Cdd:PTZ00265 1264 GGSGEDSTVfknsgkilldgvdicdynLKDLRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEFIES 1343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  467 L--SFLINVGlnylsleRSADTLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGN-TVIV 543
Cdd:PTZ00265 1344 LpnKYDTNVG-------PYGKSLSGGQKQRIAIARALLRE--PKILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIIT 1414
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 940388401  544 VEHDEDAIRAADHIIdIGPGAGVHGGHIIAQGTRDDILATKDSVTGQFL 592
Cdd:PTZ00265 1415 IAHRIASIKRSDKIV-VFNNPDRTGSFVQAHGTHEELLSVQDGVYKKYV 1462
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
474-580 6.48e-04

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 43.29  E-value: 6.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 474 GLNYLSLERSAdTLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNDRLLQTLVHLRdLGNTVIVVEHDEDAIRA 553
Cdd:PRK11174 474 GLDTPIGDQAA-GLSVGQAQRLALARALLQP--CQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQ 549
                         90       100
                 ....*....|....*....|....*..
gi 940388401 554 ADHIIDIgpgagvHGGHIIAQGTRDDI 580
Cdd:PRK11174 550 WDQIWVM------QDGQIVQQGDYAEL 570
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
806-889 6.55e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 42.90  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 806 ARKLKTLMDVGLSYIRLGQAATT----LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLhfaDIEQLLVVLHRLRD-- 879
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARALI---NDPQLLILDEPTTGL---DPHARHLIWERLRSll 219
                         90
                 ....*....|.
gi 940388401 880 -HGNTIVVIEH 889
Cdd:PRK13536 220 aRGKTILLTTH 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
804-887 6.62e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 43.47  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 804 AIARKLKTLMDVGLSyiRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLhfaDI---EQLLVVLHRLRDH 880
Cdd:COG1129  372 ALAEEYIKRLRIKTP--SPEQPVGNLSGGNQQKVVLAKWLA---TDPKVLILDEPTRGI---DVgakAEIYRLIRELAAE 443

                 ....*..
gi 940388401 881 GNTIVVI 887
Cdd:COG1129  444 GKAVIVI 450
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
487-585 6.85e-04

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 43.28  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASQI--GAGLVgvmyVLDEPSIGLHQRDNDRLLQTLV-HLRDlgNTVIVVEHDEDAIRAADHIIDIGpg 563
Cdd:PRK11160 476 LSGGEQRRLGIARALlhDAPLL----LLDEPTEGLDAETERQILELLAeHAQN--KTVLMITHRLTGLEQFDRICVMD-- 547
                         90       100
                 ....*....|....*....|..
gi 940388401 564 agvhGGHIIAQGTRDDILATKD 585
Cdd:PRK11160 548 ----NGQIIEQGTHQELLAQQG 565
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
433-580 7.50e-04

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 42.75  E-value: 7.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 433 TMSIGEAMDFfeGLSLTGQ-KAQIAEKIlKEIRDRLsflinvGLNYLsLERSADTLSGGEAQRIrlAsqIGAGLV---GV 508
Cdd:COG3839   89 HMTVYENIAF--PLKLRKVpKAEIDRRV-REAAELL------GLEDL-LDRKPKQLSGGQRQRV--A--LGRALVrepKV 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 509 mYVLDEPsigL-----HQRDNDRL-LQTLvhLRDLGNTVIVVEHD-EDAIRAADHIIdigpgagV-HGGHIIAQGTRDDI 580
Cdd:COG3839  155 -FLLDEP---LsnldaKLRVEMRAeIKRL--HRRLGTTTIYVTHDqVEAMTLADRIA-------VmNDGRIQQVGTPEEL 221
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
478-656 7.71e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.12  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 478 LSLERSADTLSGGEAQRIrlasQIGAGLV--GVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRA-A 554
Cdd:PRK15439 132 LDLDSSAGSLEVADRQIV----EILRGLMrdSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQlA 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 555 DHIIDIGPGAGVHGGHiIAQGTRDDIL-ATKDSVTGQFLSGVRK--IEVPQER--NPTSDKWLELFGATGNNLKNVDLKI 629
Cdd:PRK15439 208 DRISVMRDGTIALSGK-TADLSTDDIIqAITPAAREKSLSASQKlwLELPGNRrqQAAGAPVLTVEDLTGEGFRNISLEV 286
                        170       180
                 ....*....|....*....|....*..
gi 940388401 630 PFGLLTCITGVSGSGKSTLInDTLFKL 656
Cdd:PRK15439 287 RAGEILGLAGVVGAGRTELA-ETLYGL 312
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
829-901 7.77e-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: 43.13  E-value: 7.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388401 829 LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLhfaDI---EQLLVVLHRL-RDHGNTIVVIEHNLDVV-KTADWVV 901
Cdd:COG4172  157 LSGGQRQRVMIAMALA---NEPDLLIADEPTTAL---DVtvqAQILDLLKDLqRELGMALLLITHDLGVVrRFADRVA 228
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-40 1.01e-03

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 41.57  E-value: 1.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 940388401   1 MEN-IEVRG---------ARTHNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:COG1136    1 MSPlLELRNltksygtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL 50
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
821-899 1.03e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 41.95  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGN-TIVVIEHNL-DVVKTAD 898
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVK---PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLhQVSRLSD 219

                 .
gi 940388401 899 W 899
Cdd:PRK14258 220 F 220
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
829-896 1.08e-03

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 42.61  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401  829 LSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLhfaDIEQLLVVLHRLRDHGNTIVVIEHN---LDVVKT 896
Cdd:TIGR03719 444 LSGGERNRVHLAKTLK---SGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISHDrwfLDRIAT 508
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
804-891 1.10e-03

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 41.66  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 804 AIARKLKTLMDVGL-----SYIRlgqaatTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLR 878
Cdd:PRK11264 121 ATARARELLAKVGLagketSYPR------RLSGGQQQRVAIARALAMR---PEVILFDEPTSALDPELVGEVLNTIRQLA 191
                         90
                 ....*....|...
gi 940388401 879 DHGNTIVVIEHNL 891
Cdd:PRK11264 192 QEKRTMVIVTHEM 204
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
487-580 1.11e-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: 41.02  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGN-TVIVVEHDEDAIR-AADHIIDIGPGA 564
Cdd:cd03222   72 LSGGELQRVAIAAALLRN--ATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDyLSDRIHVFEGEP 149
                         90
                 ....*....|....*.
gi 940388401 565 GVHGGHIIAQGTRDDI 580
Cdd:cd03222  150 GVYGIASQPKGTREGI 165
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
815-923 1.19e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 41.71  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 815 VGLSYIRlGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDV 893
Cdd:PRK13652 125 LGLEELR-DRVPHHLSGGEKKRVAIAGVIAME---PQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDL 200
                         90       100       110
                 ....*....|....*....|....*....|.
gi 940388401 894 V-KTADWVVDLgpeggaGGGEILIAGTPEEV 923
Cdd:PRK13652 201 VpEMADYIYVM------DKGRIVAYGTVEEI 225
cbiO PRK13641
energy-coupling factor transporter ATPase;
809-898 1.28e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 41.74  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 809 LKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIE 888
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYE---PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT 202
                         90
                 ....*....|.
gi 940388401 889 HNL-DVVKTAD 898
Cdd:PRK13641 203 HNMdDVAEYAD 213
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
411-593 1.29e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 41.54  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 411 GSRLRQEARHVFiGQTNL-PAITTM-SIGEAMDFFEGLSLTGQKAQiAEKILKEIRdrlsflinvglnylsLERSADT-- 486
Cdd:PRK11124  77 IRELRRNVGMVF-QQYNLwPHLTVQqNLIEAPCRVLGLSKDQALAR-AEKLLERLR---------------LKPYADRfp 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 --LSGGEAQRIRLASQIgaglvgVM--YVL--DEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHD-EDAIRAADHIID 559
Cdd:PRK11124 140 lhLSGGQQQRVAIARAL------MMepQVLlfDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEvEVARKTASRVVY 213
                        170       180       190
                 ....*....|....*....|....*....|....
gi 940388401 560 IgpgagvHGGHIIAQGTRDDILATKDSVTGQFLS 593
Cdd:PRK11124 214 M------ENGHIVEQGDASCFTQPQTEAFKNYLS 241
CP_lyasePhnL TIGR02324
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...
486-562 1.37e-03

phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.


Pssm-ID: 131377 [Multi-domain]  Cd Length: 224  Bit Score: 41.22  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  486 TLSGGEAQRIRLASqigaGLVgVMY---VLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRA-ADHIIDIG 561
Cdd:TIGR02324 149 TFSGGEQQRVNIAR----GFI-ADYpilLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRVMDVT 223

                  .
gi 940388401  562 P 562
Cdd:TIGR02324 224 P 224
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
776-895 1.46e-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: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 776 EVQYKGKNIhqvLEMTVED--------AHDYFDKIPAIarklkTLMDVgLSYIRLGqaattLSGGEAQRVKLARELSKRd 847
Cdd:cd03217   58 EILFKGEDI---TDLPPEErarlgiflAFQYPPEIPGV-----KNADF-LRYVNEG-----FSGGEKKRNEILQLLLLE- 122
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940388401 848 tgKTLYILDEPTTGLhfaDIEQLLVV---LHRLRDHGNTIVVIEHN---LDVVK 895
Cdd:cd03217  123 --PDLAILDEPDSGL---DIDALRLVaevINKLREEGKSVLIITHYqrlLDYIK 171
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
819-903 1.49e-03

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 42.40  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 819 YIRLGQAATTLSGGEAQRVKLARELSkrDTGKTLyILDEPTtglhfADI----EQLLV-VLHRLRDHgNTIVVIEHNLDV 893
Cdd:PRK10790 467 YTPLGEQGNNLSVGQKQLLALARVLV--QTPQIL-ILDEAT-----ANIdsgtEQAIQqALAAVREH-TTLVVIAHRLST 537
                         90
                 ....*....|
gi 940388401 894 VKTADWVVDL 903
Cdd:PRK10790 538 IVEADTILVL 547
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
7-40 1.49e-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: 1.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 940388401   7 RGARTHNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:COG4181   21 GAGELTILKGISLEVEAGESVAIVGASGSGKSTL 54
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
824-894 1.54e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 41.51  E-value: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388401 824 QAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD-HGNTIVVIEHNLDVV 894
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMV---TQPEILMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLV 217
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
829-895 1.58e-03

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 41.71  E-value: 1.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLARELSKRDTgktlyIL--DEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDVVK 895
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPK-----VLlcDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVK 205
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
828-901 1.65e-03

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 41.78  E-value: 1.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 828 TLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNT-IVVIEHNLD-VVKTADWVV 901
Cdd:PRK11144 128 SLSGGEKQRVAIGRALL---TAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDeILRLADRVV 200
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
462-580 1.66e-03

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: 41.01  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 462 EIRDRLSFLINVGLNYLSLERsADTLSGGEAQRI---RLASQ----IGAglvgvmyvlDEPSIGLHQRDNDRLLQTLVHL 534
Cdd:cd03256  121 EKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVaiaRALMQqpklILA---------DEPVASLDPASSRQVMDLLKRI 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 940388401 535 -RDLGNTVIVVEHDEDAIRA-ADHIIdigpgaGVHGGHIIAQGTRDDI 580
Cdd:cd03256  191 nREEGITVIVSLHQVDLAREyADRIV------GLKDGRIVFDGPPAEL 232
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
784-892 1.66e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 42.21  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 784 IHQ----VLEMTVED---------AHDYFDKIPAIARKLKTLMDVGLSyIRLGQAATTLSGGEAQRVKLARELSkRDTgk 850
Cdd:PRK11288  84 IYQelhlVPEMTVAEnlylgqlphKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALA-RNA-- 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940388401 851 TLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNLD 892
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME 201
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
14-40 1.80e-03

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 40.81  E-value: 1.80e-03
                         10        20
                 ....*....|....*....|....*..
gi 940388401  14 LKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:COG2884   18 LSDVSLEIEKGEFVFLTGPSGAGKSTL 44
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
622-650 1.90e-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: 40.92  E-value: 1.90e-03
                         10        20
                 ....*....|....*....|....*....
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLIN 650
Cdd:cd03293   20 LEDISLSVEEGEFVALVGPSGCGKSTLLR 48
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
790-895 1.97e-03

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 41.62  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 790 MTV-----EDAHDYFDKIPA--IARKLKTLMD-VGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTG 861
Cdd:PRK15079 115 MTIgeiiaEPLRTYHPKLSRqeVKDRVKAMMLkVGLLPNLINRYPHEFSGGQCQRIGIARALILE---PKLIICDEPVSA 191
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 940388401 862 LHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDVVK 895
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK 226
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
485-565 2.28e-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: 39.83  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 485 DTLSGGEAQRIRLASqigaglvgVMY------VLDEPSIGLHQRDNDRLLQtlvHLRDLGNTVIVVEHDEDAIRAADHII 558
Cdd:cd03223   90 DVLSGGEQQRLAFAR--------LLLhkpkfvFLDEATSALDEESEDRLYQ---LLKELGITVISVGHRPSLWKFHDRVL 158

                 ....*..
gi 940388401 559 DIGPGAG 565
Cdd:cd03223  159 DLDGEGG 165
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
3-41 2.29e-03

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 41.54  E-value: 2.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 940388401   3 NIEVR-------GARTHNLKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:PRK11176 341 DIEFRnvtftypGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
473-580 2.30e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 40.74  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 473 VGLNYLSlERSADTLSGGEAQRIRLASQIGAGLVGVMyvLDEPSIGLHQRDNDRLLQTLVHLRD-LGNTVIVVEHDEDAI 551
Cdd:PRK11300 141 VGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPEILM--LDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLV 217
                         90       100       110
                 ....*....|....*....|....*....|
gi 940388401 552 RA-ADHIIDIGPGAGvhgghiIAQGTRDDI 580
Cdd:PRK11300 218 MGiSDRIYVVNQGTP------LANGTPEEI 241
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
803-892 2.56e-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: 40.20  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 803 PAIARKLKTLMD-VGLSyIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL-RDH 880
Cdd:cd03259  105 AEIRARVRELLElVGLE-GLLNRYPHELSGGQQQRVALARALARE---PSLLLLDEPLSALDAKLREELREELKELqREL 180
                         90
                 ....*....|..
gi 940388401 881 GNTIVVIEHNLD 892
Cdd:cd03259  181 GITTIYVTHDQE 192
cbiO PRK13646
energy-coupling factor transporter ATPase;
460-588 2.64e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 40.92  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 460 LKEIRDR-LSFLINVGLNYLSLERSADTLSGGEAQRIRLASqIGAGLVGVMyVLDEPSIGLHQRDNDRLLQTLVHLR-DL 537
Cdd:PRK13646 118 LDEVKNYaHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVS-ILAMNPDII-VLDEPTAGLDPQSKRQVMRLLKSLQtDE 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940388401 538 GNTVIVVEHD-EDAIRAADHIIDIgpgagvHGGHIIAQGTRDDILATKDSVT 588
Cdd:PRK13646 196 NKTIILVSHDmNEVARYADEVIVM------KEGSIVSQTSPKELFKDKKKLA 241
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
12-40 2.66e-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: 40.21  E-value: 2.66e-03
                         10        20
                 ....*....|....*....|....*....
gi 940388401  12 HNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:cd03262   14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTL 42
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
487-582 2.72e-03

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: 40.55  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASqigaGLVG--VMYVLDEPSIGLhQRDNDRLLQTLVHLRDLGNTVIVVEHDEDAIRAADHIIDIgpga 564
Cdd:cd03252  139 LSGGQRQRIAIAR----ALIHnpRILIFDEATSAL-DYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVM---- 209
                         90
                 ....*....|....*...
gi 940388401 565 gvHGGHIIAQGTRDDILA 582
Cdd:cd03252  210 --EKGRIVEQGSHDELLA 225
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
786-901 2.93e-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: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 786 QVLEMTVEDAHDYFDKIpaiarklktlmdvgLSYIRLGQAATT----LSGGEAQRVKLARELSKRdtgKTLYILDEPTTG 861
Cdd:COG4161  109 KVLGLSKEQAREKAMKL--------------LARLRLTDKADRfplhLSGGQQQRVAIARALMME---PQVLLFDEPTAA 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 940388401 862 LHFADIEQLLVVLHRLRDHGNTIVVIEHNLDVV-KTADWVV 901
Cdd:COG4161  172 LDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVV 212
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
482-547 2.97e-03

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 40.64  E-value: 2.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 482 RSADTLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHD 547
Cdd:PRK15056 138 RQIGELSGGQKKRVFLARAIAQQ--GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
806-901 3.19e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 41.38  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 806 ARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHF---ADIEQLLVVLHRLRDHGn 882
Cdd:PRK10261 146 AKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR---PAVLIADEPTTALDVtiqAQILQLIKVLQKEMSMG- 221
                         90       100
                 ....*....|....*....|
gi 940388401 883 tIVVIEHNLDVV-KTADWVV 901
Cdd:PRK10261 222 -VIFITHDMGVVaEIADRVL 240
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
800-895 3.28e-03

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 40.44  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 800 DKIPAIARKLKTLMDVGLSYIRLGQAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRD 879
Cdd:PRK10419 123 DKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALA---VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQ 199
                         90
                 ....*....|....*..
gi 940388401 880 HGNT-IVVIEHNLDVVK 895
Cdd:PRK10419 200 QFGTaCLFITHDLRLVE 216
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
829-887 3.28e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 41.15  E-value: 3.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLAREL-SKRDtgktLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVI 887
Cdd:PRK10938 136 LSTGETRKTLLCQALmSEPD----LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
461-563 3.53e-03

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: 40.08  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDRLSFLIN-VGLNYLSLERSADtLSGGEAQRIRLASQIGAGlvGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGN 539
Cdd:cd03292  111 REIRKRVPAALElVGLSHKHRALPAE-LSGGEQQRVAIARAIVNS--PTILIADEPTGNLDPDTTWEIMNLLKKINKAGT 187
                         90       100
                 ....*....|....*....|....*
gi 940388401 540 TVIVVEHDEDAIRAADH-IIDIGPG 563
Cdd:cd03292  188 TVVVATHAKELVDTTRHrVIALERG 212
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
637-703 3.56e-03

p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase family consists of several highly homologous proteins, including IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. They are found in higher eukaryotes where they play a role in immune resistance against intracellular pathogens. p47 proteins exist at low resting levels in mouse cells, but are strongly induced by Type II interferon (IFN-gamma). ITGP is critical for resistance to Toxoplasma gondii infection and in involved in inhibition of Coxsackievirus-B3-induced apoptosis. TGTP was shown to limit vesicular stomatitis virus (VSV) infection of fibroblasts in vitro. IRG-47 is involved in resistance to T. gondii infection. LRG-47 has been implicated in resistance to T. gondii, Listeria monocytogenes, Leishmania, and mycobacterial infections. IIGP1 has been shown to localize to the ER and to the Golgi membranes in IFN-induced cells and inflamed tissues. In macrophages, IIGP1 interacts with hook3, a microtubule binding protein that participates in the organization of the cis-Golgi compartment.


Pssm-ID: 206690  Cd Length: 197  Bit Score: 39.62  E-value: 3.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940388401 637 ITGVSGSGKSTLINdTLFKLAHTELNGA------TTAEAAPYKSisglDHFDKVIDIDQSPIGrTPRSNPATY 703
Cdd:cd04104    6 VTGESGAGKSSFIN-ALRGIGHEEEGAAptgvveTTMKRTPYPH----PKFPNVTLWDLPGIG-STAFPPDDY 72
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
787-861 3.80e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 40.76  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 787 VLEMTVED-----AHDYFDKIPAIARKLKTLMDVGlSYIRL--------GQAATTLSGGEAQRVKLARELSKRDtgKTLy 853
Cdd:PRK10762 342 VLGMSVKEnmsltALRYFSRAGGSLKHADEQQAVS-DFIRLfniktpsmEQAIGLLSGGNQQKVAIARGLMTRP--KVL- 417

                 ....*...
gi 940388401 854 ILDEPTTG 861
Cdd:PRK10762 418 ILDEPTRG 425
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
487-582 3.82e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 40.10  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 487 LSGGEAQRIRLASQIGagLVGVMYVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVEHDED-AIRAADHIIDIgpgag 565
Cdd:PRK13647 139 LSYGQKKRVAIAGVLA--MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVL----- 211
                         90       100
                 ....*....|....*....|..
gi 940388401 566 vHGGHIIAQG-----TRDDILA 582
Cdd:PRK13647 212 -KEGRVLAEGdksllTDEDIVE 232
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
3-41 3.95e-03

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: 40.66  E-value: 3.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 940388401   3 NIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:COG1123   11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLA 49
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
473-558 4.02e-03

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 473 VGLNYLSLERSADT----LSGGEAQRIRLASQigagLV---GVMyVLDEPSIGLHQRDNDRLLQTLVHLRDLGNTVIVVE 545
Cdd:cd03234  126 VLLRDLALTRIGGNlvkgISGGERRRVSIAVQ----LLwdpKVL-ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI 200
                         90
                 ....*....|....*
gi 940388401 546 HD--EDAIRAADHII 558
Cdd:cd03234  201 HQprSDLFRLFDRIL 215
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
622-901 4.32e-03

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 39.98  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 622 LKNVDLKIPFGLLTCITGVSGSGKSTLIndtlfklahtelngattaeaapyKSISGLDHFDK-VIDIDQSPIGRTPRSnp 700
Cdd:COG1126   17 LKGISLDVEKGEVVVIIGPSGSGKSTLL-----------------------RCINLLEEPDSgTITVDGEDLTDSKKD-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 701 atytgiftgIRELfagtqeaRSRgykVGR-F-SFNVkggrceacqgdgvikvemhFlpdvyvPcdvckgaryNRETLEvq 778
Cdd:COG1126   72 ---------INKL-------RRK---VGMvFqQFNL-------------------F------P---------HLTVLE-- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 779 ykgkNI----HQVLEMTVEDAHdyfdkipAIARKLktLMDVGLSyirlGQA---ATTLSGGEAQRVKLARELS---Krdt 848
Cdd:COG1126   97 ----NVtlapIKVKKMSKAEAE-------ERAMEL--LERVGLA----DKAdayPAQLSGGQQQRVAIARALAmepK--- 156
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940388401 849 gktlYIL-DEPTTGLhfaDIE---QLLVVLHRLRDHGNTIVVIEHNL----DVvktADWVV 901
Cdd:COG1126  157 ----VMLfDEPTSAL---DPElvgEVLDVMRDLAKEGMTMVVVTHEMgfarEV---ADRVV 207
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
435-580 4.81e-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: 39.66  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 435 SIGEAMDFFEGLSLTGQKAQIAEKILKEIRDRLsflinvgLNYLSLERSAD----TLSGGEAQRIrlasQIGAGLVGV-- 508
Cdd:cd03265   83 SVDDELTGWENLYIHARLYGVPGAERRERIDEL-------LDFVGLLEAADrlvkTYSGGMRRRL----EIARSLVHRpe 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388401 509 MYVLDEPSIGL--HQRDND-RLLQTLVhlRDLGNTVIVVEHD-EDAIRAADHIidigpgAGVHGGHIIAQGTRDDI 580
Cdd:cd03265  152 VLFLDEPTIGLdpQTRAHVwEYIEKLK--EEFGMTILLTTHYmEEAEQLCDRV------AIIDHGRIIAEGTPEEL 219
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
829-923 5.09e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 40.07  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRL-RDHGNTIVVIEHNLDVVKTADWVVDLgpeg 907
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMR---PECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVM---- 217
                         90
                 ....*....|....*.
gi 940388401 908 gaGGGEILIAGTPEEV 923
Cdd:PRK13633 218 --DSGKVVMEGTPKEI 231
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
821-903 5.15e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 39.90  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKRdtgKTLYILDEPTTGL---HFADIEQLLVVLHRlrdhGNTIVVIEH-NLDVVKT 896
Cdd:PRK14247 139 RLDAPAGKLSGGQQQRLCIARALAFQ---PEVLLADEPTANLdpeNTAKIESLFLELKK----DMTIVLVTHfPQQAARI 211

                 ....*..
gi 940388401 897 ADWVVDL 903
Cdd:PRK14247 212 SDYVAFL 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
461-569 5.45e-03

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: 39.20  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 461 KEIRDRLS-FLINVGLNYLsLERSADTLSGGEAQRIRLASQIGA--GLVgvmyVLDEPSIGLHQRDNDRLLQTLVHL-RD 536
Cdd:cd03297  106 REDRISVDeLLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAqpELL----LLDEPFSALDRALRLQLLPELKQIkKN 180
                         90       100       110
                 ....*....|....*....|....*....|....
gi 940388401 537 LGNTVIVVEHD-EDAIRAADHIIDIGPGAGVHGG 569
Cdd:cd03297  181 LNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYIG 214
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
804-892 5.47e-03

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 39.69  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 804 AIARKLktLMDVGLS-----YIRlgqaatTLSGGEAQRVKLARELSkrdTGKTLYILDEPttglhFA--DI---EQLLVV 873
Cdd:COG1116  117 ERAREL--LELVGLAgfedaYPH------QLSGGMRQRVAIARALA---NDPEVLLMDEP-----FGalDAltrERLQDE 180
                         90       100
                 ....*....|....*....|
gi 940388401 874 LHRL-RDHGNTIVVIEHNLD 892
Cdd:COG1116  181 LLRLwQETGKTVLFVTHDVD 200
PTZ00243 PTZ00243
ABC transporter; Provisional
14-40 6.19e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 40.53  E-value: 6.19e-03
                          10        20
                  ....*....|....*....|....*..
gi 940388401   14 LKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTL 702
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
829-924 6.21e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 39.33  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 829 LSGGEAQRVKLARELSKRdtgKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGN-TIVVIEHNLDVV--KTaDWVVDLgp 905
Cdd:PRK09544 121 LSGGETQRVLLARALLNR---PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHDLHLVmaKT-DEVLCL-- 194
                         90
                 ....*....|....*....
gi 940388401 906 eggagGGEILIAGTPEEVA 924
Cdd:PRK09544 195 -----NHHICCSGTPEVVS 208
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
14-41 6.74e-03

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 40.15  E-value: 6.74e-03
                         10        20
                 ....*....|....*....|....*...
gi 940388401  14 LKDISLTIPRDKLIVITGLSGSGKSSLA 41
Cdd:COG1132  356 LKDISLTIPPGETVALVGPSGSGKSTLV 383
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
3-40 7.01e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 39.17  E-value: 7.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 940388401   3 NIEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:COG2401   35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTL 72
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
824-901 7.14e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 39.89  E-value: 7.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 824 QAATTLSGGEAQRVKLARELSkrdTGKTLYILDEPTTGLHFADIEQLLVVLHRLRDHGNTIVVIEHNL-DVVKTADWVV 901
Cdd:PRK11288 392 QLIMNLSGGNQQKAILGRWLS---EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLGVADRIV 467
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
4-105 7.44e-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: 39.03  E-value: 7.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401   4 IEVRGARTHNLKDISLTIPRDKLIVITGLSGSGKSSLAFDTL----YAEGQRRYV-ESLSAYARQFLSLMEKpdvdhieg 78
Cdd:cd03257   11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILgllkPTSGSIIFDgKDLLKLSRRLRKIRRK-------- 82
                         90       100       110
                 ....*....|....*....|....*....|
gi 940388401  79 lspAIS-IEQKS-TSHNPRSTVGT-ITEIY 105
Cdd:cd03257   83 ---EIQmVFQDPmSSLNPRMTIGEqIAEPL 109
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
390-584 7.66e-03

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: 40.11  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  390 SNSVREELAK-----YQTSQACPSCHGSRLRQEARHVFIGQTNL----PAITTMSIgeamdfFEGLSLTGQKAQIAEKIL 460
Cdd:TIGR01193 509 SGSGKSTLAKllvgfFQARSGEILLNGFSLKDIDRHTLRQFINYlpqePYIFSGSI------LENLLLGAKENVSQDEIW 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401  461 K-----EIRDRLSfliNVGLNY-LSLERSADTLSGGEAQRIRLASQIgagLV-GVMYVLDEPSIGLHQRDNDRLLQTLVH 533
Cdd:TIGR01193 583 AaceiaEIKDDIE---NMPLGYqTELSEEGSSISGGQKQRIALARAL---LTdSKVLILDESTSNLDTITEKKIVNNLLN 656
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 940388401  534 LRDlgNTVIVVEHDEDAIRAADHIIdigpgaGVHGGHIIAQGTRDDILATK 584
Cdd:TIGR01193 657 LQD--KTIIFVAHRLSVAKQSDKII------VLDHGKIIEQGSHDELLDRN 699
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
821-901 8.66e-03

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: 38.75  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 821 RLGQAATTLSGGEAQRVKLARELSKrdtGKTLYILDEPTTGLhfaDIEQLLVV---LHRLRDhGNTIVVIEHNLDVVKTA 897
Cdd:cd03251  131 VIGERGVKLSGGQRQRIAIARALLK---DPPILILDEATSAL---DTESERLVqaaLERLMK-NRTTFVIAHRLSTIENA 203

                 ....
gi 940388401 898 DWVV 901
Cdd:cd03251  204 DRIV 207
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
482-580 9.15e-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: 38.76  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 482 RSADTLSGGEAQRIRLASQIgaglvgVM----YVLDEPSIGLHQRDNDRLLQTLVHL-RDLGNTVIVVEHD-EDAIRAAD 555
Cdd:cd03300  126 RKPSQLSGGQQQRVAIARAL------VNepkvLLLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDqEEALTMSD 199
                         90       100
                 ....*....|....*....|....*
gi 940388401 556 HIidigpgAGVHGGHIIAQGTRDDI 580
Cdd:cd03300  200 RI------AVMNKGKIQQIGTPEEI 218
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
444-575 9.18e-03

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; 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 to 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 the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 38.85  E-value: 9.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388401 444 EGLSLTGQKAQIAEKILKEIRDRLSFLINVGLnylSLERSADTLSGGeaQRIRlaSQIGAGLV---GVMYvLDEPSIGLH 520
Cdd:cd03267  114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEE---LLDTPVRQLSLG--QRMR--AEIAAALLhepEILF-LDEPTIGLD 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 940388401 521 ---QRDNDRLLQTLVhlRDLGNTVIVVEHDEDAIRA-ADHIIDIgpgagvHGGHIIAQG 575
Cdd:cd03267  186 vvaQENIRNFLKEYN--RERGTTVLLTSHYMKDIEAlARRVLVI------DKGRLLYDG 236
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
7-40 9.73e-03

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: 38.72  E-value: 9.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 940388401   7 RGARTHNLKDISLTIPRDKLIVITGLSGSGKSSL 40
Cdd:cd03258   14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL 47
 
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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