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Conserved domains on  [gi|15600424|ref|NP_253918|]
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ABC transporter ATP-binding protein/permease [Pseudomonas aeruginosa PAO1]

Protein Classification

ABC transporter ATP-binding protein/permease( domain architecture ID 16678421)

ABC transporter ATP-binding protein/permease similar to Escherichia coli ribosome-associated ATPase, which is involved in modulating protein synthesis and oxidative phosphorylation; also similar to transporters that can confer drug resistance

CATH:  3.40.50.300
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-915 0e+00

ribosome-associated ATPase/putative transporter RbbA;


:

Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 1887.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAY 87
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQGLGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:NF033858  81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  168 DEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGTQSLESAFIAL 247
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  248 LPESKRAGHHRLVIPPRPQSEGAPrIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS 327
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPADDDDE-PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  328 EGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLP 407
Cdd:NF033858 320 EGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  408 LGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASD 487
Cdd:NF033858 400 LGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  488 TPDELVRQRGLPTLEATFIAYLEEAAGAAAPAQPAEAPAVAEQPGDGQeRQAQRERFSPLRLFSYARREAMELRRDPIRL 567
Cdd:NF033858 480 TPAALVAARGAATLEEAFIAYLEEAAGAAAAPAAAAAPAAAAAAPAAP-APAPRRRFSLRRLLAYARREALELLRDPIRL 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  568 TLALLGTALLMFIIGYGINMDVEDLSWAVLDRDQTTTSQAYALNIAGSRYFVEHAPITDPDDLDRRLRSGELSLAVEIPP 647
Cdd:NF033858 559 TFALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPP 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  648 NFGRDLKRGSDPAIGVWIDGAMPTRANTVLGYVQGLHTSYLADLSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPAVI 727
Cdd:NF033858 639 GFGRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLARERGGAAAASPATIETRYRYNPDFKSLPAMVPAVI 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  728 PLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKGSFLALTIGA 807
Cdd:NF033858 719 PLLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGA 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  808 FLYVVTSTGLGLFLSTFMRSQIAAVFGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGAFSKSLGLS 887
Cdd:NF033858 799 LLYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFA 878
                        890       900
                 ....*....|....*....|....*...
gi 15600424  888 DLWAYYLPLAASIVVLTLLSVACLKKQE 915
Cdd:NF033858 879 DLWPSFLALAAFIPVLLGLSVLLLKKQE 906
 
Name Accession Description Interval E-value
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-915 0e+00

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 1887.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAY 87
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQGLGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:NF033858  81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  168 DEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGTQSLESAFIAL 247
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  248 LPESKRAGHHRLVIPPRPQSEGAPrIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS 327
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPADDDDE-PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  328 EGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLP 407
Cdd:NF033858 320 EGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  408 LGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASD 487
Cdd:NF033858 400 LGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  488 TPDELVRQRGLPTLEATFIAYLEEAAGAAAPAQPAEAPAVAEQPGDGQeRQAQRERFSPLRLFSYARREAMELRRDPIRL 567
Cdd:NF033858 480 TPAALVAARGAATLEEAFIAYLEEAAGAAAAPAAAAAPAAAAAAPAAP-APAPRRRFSLRRLLAYARREALELLRDPIRL 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  568 TLALLGTALLMFIIGYGINMDVEDLSWAVLDRDQTTTSQAYALNIAGSRYFVEHAPITDPDDLDRRLRSGELSLAVEIPP 647
Cdd:NF033858 559 TFALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPP 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  648 NFGRDLKRGSDPAIGVWIDGAMPTRANTVLGYVQGLHTSYLADLSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPAVI 727
Cdd:NF033858 639 GFGRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLARERGGAAAASPATIETRYRYNPDFKSLPAMVPAVI 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  728 PLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKGSFLALTIGA 807
Cdd:NF033858 719 PLLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGA 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  808 FLYVVTSTGLGLFLSTFMRSQIAAVFGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGAFSKSLGLS 887
Cdd:NF033858 799 LLYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFA 878
                        890       900
                 ....*....|....*....|....*...
gi 15600424  888 DLWAYYLPLAASIVVLTLLSVACLKKQE 915
Cdd:NF033858 879 DLWPSFLALAAFIPVLLGLSVLLLKKQE 906
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
275-506 3.82e-100

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 312.38  E-value: 3.82e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:COG1131   1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:COG1131  81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglpTLEATFI 506
Cdd:COG1131 161 GLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR----LLEDVFL 228
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
275-483 3.68e-72

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: 234.98  E-value: 3.68e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03230   1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLvlharlfhlpadgiparvgemlrrfdlekvadelpnDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03230  81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03230 125 GLDPESRREFWELLREL-KKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
17-248 4.65e-55

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 192.99  E-value: 4.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMPQGlgKNL 96
Cdd:TIGR01188   2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--REPRKVRRSIGIVPQY--ASV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    97 YPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:TIGR01188  78 DEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424   177 LSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAFIALL 248
Cdd:TIGR01188 158 RTRRAIWDYIRALK--EEGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQ 228
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
265-502 3.56e-53

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 188.89  E-value: 3.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  265 PQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA 344
Cdd:PRK13536  32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  345 TRRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  425 EILILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQR-GLPTLE 502
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEHiGCQVIE 270
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
578-908 1.56e-37

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 144.07  E-value: 1.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   578 MFIIGYGINmDVEDLSWAVLDRDQTTTSQAYALNIAGSRYFVEHAPITDPDDLDRRLRSGELSLAVEIPPNFGRDLKRGS 657
Cdd:pfam12698  19 GLIFSNAVN-DPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLLKGE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   658 DPAIGVWIDGAMPTRANTVLGYVQGLHTSYLA-DLSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPaVIPLLLIMIPA 736
Cdd:pfam12698  98 SATVTVYINSSNLLVSKLILNALQSLLQQLNAsALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIILIGA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   737 MLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFrVPLKGSFLALtIGAFLYVVTSTG 816
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIG-IPFGNLGLLL-LLFLLYGLAYIA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   817 LGLFLSTFMRSQIAAVFGVAIATMIPAIQFSGLIhPVSSLEGAAAWIGKLYPTSHFLVVSRgAFSKSLGLSDLWAYYLPL 896
Cdd:pfam12698 255 LGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLF-PLEDPPSFLQWIFSIIPFFSPIDGLL-RLIYGDSLWEIAPSLIIL 332
                         330
                  ....*....|..
gi 15600424   897 AASIVVLTLLSV 908
Cdd:pfam12698 333 LLFAVVLLLLAL 344
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-241 5.78e-30

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 122.15  E-value: 5.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    1 MTAGGSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVgkssllallAGARKMQDGEIRVLDGDMRDRR---- 76
Cdd:NF000106   6 ISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---------A**RGALPAHV*GPDAGRRPWRf*tw 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   77 --HRRAVCPRIA-YMPQGLGKNlyPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLG 153
Cdd:NF000106  77 caNRRALRRTIG*HRPVR*GRR--ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV--RDGATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELK 232

                 ....*....
gi 15600424  233 ERTGTQSLE 241
Cdd:NF000106 233 TKVGGRTLQ 241
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
267-502 2.22e-26

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 111.75  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  267 SEGApRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTtmkmltGLLPASEGTCALFGQPVD-----AS 341
Cdd:NF000106   7 SNGA-RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHV*GPDAGRRPWRf*twcAN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  342 DMATRRRVG-YMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAV 420
Cdd:NF000106  80 RRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  421 IHKPEILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELVRQRGLP 499
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGGR 238

                 ...
gi 15600424  500 TLE 502
Cdd:NF000106 239 TLQ 241
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
17-212 2.63e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.93  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrhrravcpRIAYMPQGLGKNL 96
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA------------RVAYVPQRSEVPD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   97 YPTLSVFENVD--FFGR--LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:NF040873  69 SLPLTVRDLVAmgRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15600424  173 GVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERFD 212
Cdd:NF040873 149 GLDAESRERIIALLAEEHA--RGATVVVVTHDLELVRRAD 186
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
283-478 6.50e-24

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 100.00  E-value: 6.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpvdasdMATRRRVGYMSQAFSLYAEL 362
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR----------RAGGARVAYVPQRSEVPDSL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  363 --SVRQNLVL----HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:NF040873  71 plTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15600424  437 DPVARDGFWELMVELsRRDGVTIFISTHFMNEAQRCDRISLM 478
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
276-482 6.11e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.76  E-value: 6.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMATRRRVGY-- 351
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIvi 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 MSQAFSLYAELSVRQNLVL---HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:NF040905  83 IHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELsRRDGVT-IFIStHFMNE-AQRCDRISLMHAGK 482
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLEL-KAQGITsIIIS-HKLNEiRRVADSITVLRDGR 216
GguA NF040905
sugar ABC transporter ATP-binding protein;
11-483 5.15e-12

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.43  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG--ARKMQDGEIrVLDG------DMRDRRHRravc 82
Cdd:NF040905   4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyPHGSYEGEI-LFDGevcrfkDIRDSEAL---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   83 pRIAYMPQGLGknLYPTLSVFENVdFFGRLFGH----DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCAL 158
Cdd:NF040905  79 -GIVIIHQELA--LIPYLSIAENI-FLGNERAKrgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  159 IHDPDLLILDEPTTGV-DPLSRNqFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATgtpqeLRERTG 236
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAA-LLDLLLELKA--QGITSIIISHKLNEIRRVaDSITVLRDGRTIET-----LDCRAD 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  237 TQSlESAFIALLpeSKRAGHHRLviPPRpqsegAPRI---AIEAEGLTCR---FGDFVAVDHVSFRIERGEIFGFLGSNG 310
Cdd:NF040905 227 EVT-EDRIIRGM--VGRDLEDRY--PER-----TPKIgevVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMG 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  311 CGKsTTMKMltGLLPAS-----EGTCALFGQPVDASDM--ATRRRVGYMSQ---AFSLYAELSVRQNLVLhARLFHLPAD 380
Cdd:NF040905 297 AGR-TELAM--SVFGRSygrniSGTVFKDGKEVDVSTVsdAIDAGLAYVTEdrkGYGLNLIDDIKRNITL-ANLGKVSRR 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  381 GIPARVGEMlrrfdleKVADELPNDLPL---GIRQ---RLS--------LAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:NF040905 373 GVIDENEEI-------KVAEEYRKKMNIktpSVFQkvgNLSggnqqkvvLSKWLFTDPDVLILDEPTRGIDVGAKYEIYT 445
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 15600424  447 LMVELSRRDGVTIFISTHfMNEA-QRCDRISLMHAGKV 483
Cdd:NF040905 446 IINELAAEGKGVIVISSE-LPELlGMCDRIYVMNEGRI 482
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
299-464 3.55e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.98  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    299 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFgqpvdasdmatrrrvgymsqafslyaelsvrqnlvlharlfhlp 378
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    379 aDGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAviHKPEILILDEPTSGVDPVARDGFWELMV-----ELSR 453
Cdd:smart00382  37 -DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK--LKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKS 113
                          170
                   ....*....|.
gi 15600424    454 RDGVTIFISTH 464
Cdd:smart00382 114 EKNLTVILTTN 124
 
Name Accession Description Interval E-value
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-915 0e+00

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 1887.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAY 87
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQGLGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:NF033858  81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  168 DEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGTQSLESAFIAL 247
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  248 LPESKRAGHHRLVIPPRPQSEGAPrIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS 327
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPADDDDE-PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  328 EGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLP 407
Cdd:NF033858 320 EGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  408 LGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASD 487
Cdd:NF033858 400 LGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  488 TPDELVRQRGLPTLEATFIAYLEEAAGAAAPAQPAEAPAVAEQPGDGQeRQAQRERFSPLRLFSYARREAMELRRDPIRL 567
Cdd:NF033858 480 TPAALVAARGAATLEEAFIAYLEEAAGAAAAPAAAAAPAAAAAAPAAP-APAPRRRFSLRRLLAYARREALELLRDPIRL 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  568 TLALLGTALLMFIIGYGINMDVEDLSWAVLDRDQTTTSQAYALNIAGSRYFVEHAPITDPDDLDRRLRSGELSLAVEIPP 647
Cdd:NF033858 559 TFALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPP 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  648 NFGRDLKRGSDPAIGVWIDGAMPTRANTVLGYVQGLHTSYLADLSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPAVI 727
Cdd:NF033858 639 GFGRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLARERGGAAAASPATIETRYRYNPDFKSLPAMVPAVI 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  728 PLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKGSFLALTIGA 807
Cdd:NF033858 719 PLLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGA 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  808 FLYVVTSTGLGLFLSTFMRSQIAAVFGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGAFSKSLGLS 887
Cdd:NF033858 799 LLYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFA 878
                        890       900
                 ....*....|....*....|....*...
gi 15600424  888 DLWAYYLPLAASIVVLTLLSVACLKKQE 915
Cdd:NF033858 879 DLWPSFLALAAFIPVLLGLSVLLLKKQE 906
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
275-506 3.82e-100

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 312.38  E-value: 3.82e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:COG1131   1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:COG1131  81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglpTLEATFI 506
Cdd:COG1131 161 GLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR----LLEDVFL 228
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
10-253 8.68e-96

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 300.83  E-value: 8.68e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMP 89
Cdd:COG1131   2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYVP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG1131  80 QEP--ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTgtqsLESAFIALL 248
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAA--EGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL----LEDVFLELT 231

                ....*
gi 15600424 249 PESKR 253
Cdd:COG1131 232 GEEAR 236
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
8-492 1.10e-93

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: 305.29  E-value: 1.10e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   8 VASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---ARKMQDGEIRVLDGDMRDRRHRRAvC 82
Cdd:COG1123   4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR-G 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  83 PRIAYMPQGLGKNLYPtLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:COG1123  83 RRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQELRERtgTQSLE 241
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQR-ERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA--PQALA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 242 SAfiallpesKRAGHHRLVIPPRPQsegAPRIAIEAEGLTCRF-----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTT 316
Cdd:COG1123 239 AV--------PRLGAARGRAAPAAA---AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTL 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 317 MKMLTGLLPASEGTCALFGQPVDASDMAT----RRRVGYMSQ--AFSLYAELSVRQNLVLHARLFH-LPADGIPARVGEM 389
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAEL 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 390 LRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVT-IFIsTHFMN 467
Cdd:COG1123 388 LERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFI-SHDLA 466
                       490       500
                ....*....|....*....|....*.
gi 15600424 468 EAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG1123 467 VVRYiADRVAVMYDGRIVEDGPTEEV 492
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
275-506 7.15e-73

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: 239.76  E-value: 7.15e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:COG4555   2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:COG4555  82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLEATFI 506
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFV 233
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
275-483 3.68e-72

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: 234.98  E-value: 3.68e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03230   1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLvlharlfhlpadgiparvgemlrrfdlekvadelpnDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03230  81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03230 125 GLDPESRREFWELLREL-KKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
275-492 9.86e-72

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: 235.73  E-value: 9.86e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03265   1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03265  81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
274-502 2.59e-70

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 235.00  E-value: 2.59e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmatRRRVGYMS 353
Cdd:COG4152   1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:COG4152  78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 434 SGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLE 502
Cdd:COG4152 158 SGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
11-252 1.59e-67

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: 225.12  E-value: 1.59e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRavcpRIAYM 88
Cdd:COG4555   4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARR----QIGVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 PQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:COG4555  80 PDERG--LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAER-FDWLVAMDDGKVLATGTPQELRERTGTQSLESAFIAL 247
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKK--EGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235

                ....*
gi 15600424 248 LPESK 252
Cdd:COG4555 236 IGSEE 240
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
275-492 4.83e-66

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


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 220.45  E-value: 4.83e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD--FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYM 352
Cdd:cd03263   1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03263  81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 433 TSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
10-222 4.28e-62

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: 207.64  E-value: 4.28e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMP 89
Cdd:cd03230   2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYLP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTLSVFENVdffgrlfghdkaererriadllqstglapfaerpagKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03230  80 EEPS--LYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWLVAMDDGKV 222
Cdd:cd03230 122 PTSGLDPESRREFWELLRELK--KEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
10-232 2.58e-58

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


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 198.88  E-value: 2.58e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAY 87
Cdd:cd03263   2 QIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLGY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03263  80 CPQF--DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGR---SIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQELK 220
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
275-485 3.85e-58

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: 198.27  E-value: 3.85e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAsdmATRRRVGYMSQ 354
Cdd:cd03269   1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYLPE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03269  78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLA 485
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
10-483 7.15e-56

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 201.40  E-value: 7.15e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHrravcPR----- 84
Cdd:COG1129   6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-LDGEPVRFRS-----PRdaqaa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  85 -IAYMPQGLgkNLYPTLSVFENVdFFGRLFGH----DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:COG1129  80 gIAIIHQEL--NLVPNLSVAENI-FLGREPRRggliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 160 HDPDLLILDEPTTgvdPLSRN---QFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER- 234
Cdd:COG1129 157 RDARVLILDEPTA---SLTEReveRLFRIIRRLKA--QGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAELTEDe 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 235 -----TGtQSLESAFiallpeskraghhrlviPPRPQSEGAPriAIEAEGLTCRfgdfVAVDHVSFRIERGEIFGFLGSN 309
Cdd:COG1129 232 lvrlmVG-RELEDLF-----------------PKRAAAPGEV--VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLV 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 310 GCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGYMS---QAFSLYAELSVRQNLVL-----HARLFHLPA 379
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSprDAIRAGIAYVPedrKGEGLVLDLSIRENITLasldrLSRGGLLDR 367
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 380 DGIPARVGEMLRRFDLeKVADElpnDLPL-----GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRR 454
Cdd:COG1129 368 RRERALAEEYIKRLRI-KTPSP---EQPVgnlsgGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE 443
                       490       500       510
                ....*....|....*....|....*....|
gi 15600424 455 DGVTIFISTHfMNEAQR-CDRISLMHAGKV 483
Cdd:COG1129 444 GKAVIVISSE-LPELLGlSDRILVMREGRI 472
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
270-492 1.28e-55

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: 192.12  E-value: 1.28e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD----MAT 345
Cdd:COG1127   1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelYEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHAR-LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:COG1127  81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
17-248 4.65e-55

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 192.99  E-value: 4.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMPQGlgKNL 96
Cdd:TIGR01188   2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--REPRKVRRSIGIVPQY--ASV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    97 YPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:TIGR01188  78 DEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424   177 LSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAFIALL 248
Cdd:TIGR01188 158 RTRRAIWDYIRALK--EEGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQ 228
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
275-496 4.04e-54

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: 187.54  E-value: 4.04e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYM 352
Cdd:COG1122   1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 -----SQAFslyaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:COG1122  81 fqnpdDQLF----APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQR 496
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
10-241 6.33e-54

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 189.55  E-value: 6.33e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRavcpRIAYMP 89
Cdd:COG4152   3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRR----RIGYLP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG4152  78 EERG--LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLE 241
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAA--KGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
17-232 1.58e-53

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: 185.65  E-value: 1.58e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMPQGLgkNL 96
Cdd:cd03265   9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIVFQDL--SV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  97 YPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:cd03265  85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 177 LSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:cd03265 165 QTRAHVWEYIEKLKE-EFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEELK 220
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
10-231 2.49e-53

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: 185.61  E-value: 2.49e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYM 88
Cdd:COG1122   2 ELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-DGKDITKKNLRELRRKVGLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 PQglgknlYP-----TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:COG1122  81 FQ------NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWLVAMDDGKVLATGTPQEL 231
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLN--KEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
265-502 3.56e-53

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 188.89  E-value: 3.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  265 PQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA 344
Cdd:PRK13536  32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  345 TRRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  425 EILILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQR-GLPTLE 502
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEHiGCQVIE 270
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
271-491 1.21e-52

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 184.47  E-value: 1.21e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 271 PRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMATRRRVG 350
Cdd:COG0411   1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI--TGLPPHRIAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 Y-MSQAF---SLYAELSVRQNLVL--HAR--------LFHLPA-----DGIPARVGEMLRRFDLEKVADELPNDLPLGIR 411
Cdd:COG0411  79 LgIARTFqnpRLFPELTVLENVLVaaHARlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 412 QRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPD 490
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238

                .
gi 15600424 491 E 491
Cdd:COG0411 239 E 239
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
10-226 5.80e-52

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: 180.85  E-value: 5.80e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPaNRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrDRRHRRAVCPRIAYMP 89
Cdd:cd03264   2 QLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQPQKLRRRIGYLP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03264  79 QEFG--VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDR---IVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
275-486 6.51e-52

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: 181.03  E-value: 6.51e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVG 350
Cdd:cd03266   2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03266  82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 431 EPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYE 217
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
275-486 9.29e-52

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: 180.11  E-value: 9.29e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDaSDMATRRRVGYMSQ 354
Cdd:cd03268   1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFhlpadGIP-ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:cd03268  80 APGFYPNLTARENLRLLARLL-----GIRkKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600424 434 SGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03268 155 NGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKvADRIGIINKGKLIEE 207
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
274-493 1.55e-50

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 180.39  E-value: 1.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMS 353
Cdd:PRK13537   7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:PRK13537  87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  434 SGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
275-486 7.75e-50

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: 175.07  E-value: 7.75e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGeIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03264   1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03264  80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELSrrDGVTIFISTHFMNE-AQRCDRISLMHAGKVLAS 486
Cdd:cd03264 160 GLDPEERIRFRNLLSELG--EDRIVILSTHIVEDvESLCNQVAVLNKGKLVFE 210
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
10-483 1.71e-49

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: 183.73  E-value: 1.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLAGARKMQDGEIRvLDG-DMR--DRRHR 78
Cdd:COG4172   8 SVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIL-FDGqDLLglSEREL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  79 RAVC-PRIAYMPQ----------GLGKNLYPTLSVFEnvdffgrlfGHDKAERERRIADLLQSTGLaPFAERPAGK---- 143
Cdd:COG4172  87 RRIRgNRIAMIFQepmtslnplhTIGKQIAEVLRLHR---------GLSGAAARARALELLERVGI-PDPERRLDAyphq 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 144 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQR-ELGMALLLITHDLGVVRRFaDRVAVMRQGEI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 223 LATGTPQELRERTG---TQSLesafIALLPEskraghhrlvIPPRPQSEGAPRIaIEAEGLTCRF-----------GDFV 288
Cdd:COG4172 236 VEQGPTAELFAAPQhpyTRKL----LAAEPR----------GDPRPVPPDAPPL-LEARDLKVWFpikrglfrrtvGHVK 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGTCALFGQPVDA---SDM-ATRRRVgymsQA-F-----SL 358
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGlsrRALrPLRRRM----QVvFqdpfgSL 375
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 359 YAELSVRQ----NLVLHARlfHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:COG4172 376 SPRMTVGQiiaeGLRVHGP--GLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVT-IFIStH------FMneaqrCDRISLMHAGKV 483
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAyLFIS-HdlavvrAL-----AHRVMVMKDGKV 504
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
274-492 2.59e-49

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 178.37  E-value: 2.59e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMAT-RRRVGYM 352
Cdd:COG3842   5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPPeKRNVGMV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG3842  83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTPEEI 223
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
10-231 3.85e-49

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: 174.46  E-value: 3.85e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRIAYMP 89
Cdd:COG1120   3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS-RRELARRIAYVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLgkNLYPTLSVFENVdFFGR-----LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:COG1120  82 QEP--PAPFGLTVRELV-ALGRyphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 165 LILDEPTTGVDPlsRNQFwELIGRIR--AGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:COG1120 159 LLLDEPTSHLDL--AHQL-EVLELLRrlARERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
YadH COG0842
ABC-type multidrug transport system, permease component [Defense mechanisms];
722-916 7.27e-49

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


Pssm-ID: 440604 [Multi-domain]  Cd Length: 200  Bit Score: 171.92  E-value: 7.27e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 722 MVPAVIPLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKG-SF 800
Cdd:COG0842   5 LVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGlSL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 801 LALTIGAFLYVVTSTGLGLFLSTFMRSQIAAVfGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGAF 880
Cdd:COG0842  85 LLLLLVLLLFALAFSGLGLLISTLARSQEQAS-AISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALF 163
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15600424 881 SKSLGLSDLWAYYLPLAASIVVLTLLSVACLKKQED 916
Cdd:COG0842 164 LGGAGLADVWPSLLVLLAFAVVLLALALRLFRRRLR 199
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
11-483 8.33e-49

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 181.42  E-value: 8.33e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRdrrhrravcprIAYMPQ 90
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR-----------IGYLPQ 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  91 GLgkNLYPTLSVFENV-DFFGRL---------------FGHDKAER----------------ERRIADLLQSTGLAPF-A 137
Cdd:COG0488  69 EP--PLDDDLTVLDTVlDGDAELraleaeleeleaklaEPDEDLERlaelqeefealggweaEARAEEILSGLGFPEEdL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 138 ERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfWeLIGRIRaGREGmSVLVAT--------------- 202
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--W-LEEFLK-NYPG-TVLVVShdryfldrvatrile 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 203 --------------AYMEE-AERFDWLVAMDD--GKVLAtgtpQEL--------RERTGTQ--SLESAFIALLPESK--R 253
Cdd:COG0488 222 ldrgkltlypgnysAYLEQrAERLEQEAAAYAkqQKKIA----KEEefirrfraKARKAKQaqSRIKALEKLEREEPprR 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 254 AGHHRLVIPPRPQSegaPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL 333
Cdd:COG0488 298 DKTVEIRFPPPERL---GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 334 fGQPVdasdmatrrRVGYMSQAF-SLYAELSVRQNLVLHARlfhlpaDGIPARVGEMLRRF-----DLEKVAdelpNDLP 407
Cdd:COG0488 375 -GETV---------KIGYFDQHQeELDPDKTVLDELRDGAP------GGTEQEVRGYLGRFlfsgdDAFKPV----GVLS 434
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 408 LGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARdgfwELMVE-LSRRDGVTIFIS--THFMNEAqrCDRISLMHAGKV 483
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL----EALEEaLDDFPGTVLLVShdRYFLDRV--ATRILEFEDGGV 507
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
275-494 5.32e-48

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: 170.70  E-value: 5.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGyMSQ 354
Cdd:cd03219   1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-IGR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AF---SLYAELSVRQNLVL--HARLFHLPADG--------IPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVI 421
Cdd:cd03219  80 TFqipRLFPELTVLENVMVaaQARTGSGLLLArarreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 422 HKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
275-494 5.44e-48

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: 170.76  E-value: 5.44e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD----ASDMATRRRVG 350
Cdd:cd03261   1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03261  81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
10-221 7.94e-48

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: 169.18  E-value: 7.94e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRIAY 87
Cdd:cd03225   1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS-LKELRRKVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQglgknlYP-----TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03225  80 VFQ------NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGK 221
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLK--AEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
275-485 9.15e-48

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: 169.24  E-value: 9.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdASDMATRRRVGYMSQ 354
Cdd:cd03259   1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03259  80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLA 485
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
274-505 1.02e-47

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: 170.61  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMATR---RRVG 350
Cdd:COG1120   1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRelaRRIA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQnLVLHARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1120  79 YVPQEPPAPFGLTVRE-LVALGRYPHLGLFGRPsaedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglPTLEAT 504
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLTP---ELLEEV 234

                .
gi 15600424 505 F 505
Cdd:COG1120 235 Y 235
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
10-230 2.03e-47

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 169.50  E-value: 2.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcprIAYMP 89
Cdd:COG1121   8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGYVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGKNLYPTLSVFENV----DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:COG1121  82 QRAEVDWDFPITVRDVVlmgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWLVAMDDGkVLATGTPQE 230
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELR--REGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPEE 224
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
275-483 4.06e-47

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: 167.67  E-value: 4.06e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT----- 345
Cdd:cd03255   1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:cd03255  81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
276-482 5.39e-47

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: 166.87  E-value: 5.39e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDF--VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYM 352
Cdd:cd03225   1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVGLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 -----SQAFslyaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:cd03225  81 fqnpdDQFF----GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGK 482
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
10-226 1.33e-46

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: 165.92  E-value: 1.33e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRavcpRIAYMP 89
Cdd:cd03269   2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARN----RIGYLP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03269  77 EERG--LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELA--RAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
275-477 3.42e-46

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: 164.57  E-value: 3.42e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:COG4133   3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGipARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:COG4133  83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQRCDRISL 477
Cdd:COG4133 161 ALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARVLDL 202
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
270-481 1.64e-45

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 164.49  E-value: 1.64e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAsdmaT 345
Cdd:COG1116   3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----P 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1116  79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAG 481
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSAR 215
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
11-495 5.69e-45

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: 170.37  E-value: 5.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVL---------------------- 68
Cdd:TIGR03269   3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIyhvalcekcgyverpskvgepc 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    69 ---DGDMR---------DRRHRRAVCPRIAYMPQGLGKnLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPF 136
Cdd:TIGR03269  83 pvcGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   137 AERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATAYMEEAERF-DWLV 215
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNAL-EEAVKASGISMVLTSHWPEVIEDLsDKAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   216 AMDDGKVLATGTPQELRERtgtqslesaFIALLPESKRAghhrlvippRPQSEGAPriAIEAEGLTCRF-----GDFVAV 290
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAV---------FMEGVSEVEKE---------CEVEVGEP--IIKVRNVSKRYisvdrGVVKAV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-TCALFGQpvDASDMATR---------RRVGYMSQAFSLYA 360
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGeVNVRVGD--EWVDMTKPgpdgrgrakRYIGILHQEYDLYP 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   361 ELSVRQNLVlHARLFHLPADGIPARVGEMLRR--FDLEK---VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:TIGR03269 379 HRTVLDNLT-EAIGLELPDELARMKAVITLKMvgFDEEKaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424   436 VDPVARDGFWELMVELSRRDGVTIFISTH---FMNEAqrCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHdmdFVLDV--CDRAALMRDGKIVKIGDPEEIVEE 518
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
275-494 7.62e-45

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: 162.08  E-value: 7.62e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD-MATRRRVGYM 352
Cdd:cd03295   1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpVELRRKIGYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLE--KVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03295  81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 431 EPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
274-485 8.14e-45

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 161.36  E-value: 8.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMAT- 345
Cdd:COG1136   4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELARl 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 -RRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:COG1136  84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLA 485
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
274-505 1.11e-44

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 161.41  E-value: 1.11e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmatRRRVGYMS 353
Cdd:COG1121   6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAE--LSVRQnLVLHARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:COG1121  82 QRAEVDWDfpITVRD-VVLMGRYGRRGLFRRPsradrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMhAGKVLASDTPDELVRQrglPTLEATF 505
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLTP---ENLSRAY 235
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
10-202 4.11e-44

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: 158.41  E-value: 4.11e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhrRAVCPRIAYMP 89
Cdd:COG4133   4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR--EDYRRRLAYLG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERerRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG4133  82 HADG--LKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
                       170       180       190
                ....*....|....*....|....*....|...
gi 15600424 170 PTTGVDPLSRNQFWELIgRIRAGREGMsVLVAT 202
Cdd:COG4133 158 PFTALDAAGVALLAELI-AAHLARGGA-VLLTT 188
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
10-234 4.30e-44

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 161.90  E-value: 4.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR-RHRRAvcpRIAYM 88
Cdd:PRK13537   9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRaRHARQ---RVGVV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   89 PQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK13537  86 PQF--DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  169 EPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLA--RGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIES 228
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
275-485 9.80e-44

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: 158.02  E-value: 9.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAsdmaTRRRVG 350
Cdd:cd03293   1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03293  77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 431 EPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHA--GKVLA 485
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVA 214
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
10-233 2.74e-43

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: 157.45  E-value: 2.74e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPRIAY 87
Cdd:COG1127   7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRRRIGM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLGknLYPTLSVFENVDFFGRLFGH-DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:COG1127  87 LFQGGA--LFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRE 233
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRD-ELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
274-494 3.65e-43

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 164.81  E-value: 3.65e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGY 351
Cdd:COG3845   5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSprDAIALGIGM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVL---HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:COG3845  85 VHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV-----LASDTPDELVR 494
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAiADRVTVLRRGKVvgtvdTAETSEEELAE 235
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
10-232 5.17e-43

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 157.12  E-value: 5.17e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAvcpRiaym 88
Cdd:COG0411   6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIA---R---- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 pQGLGK-----NLYPTLSVFENV-------------DFFGRLFGHDKAERE--RRIADLLQSTGLAPFAERPAGKLSGGM 148
Cdd:COG0411  79 -LGIARtfqnpRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEREarERAEELLERVGLADRADEPAGNLSYGQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 149 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVL--------VatayMEEAerfDWLVAMDDG 220
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDER-GITILliehdmdlV----MGLA---DRIVVLDFG 229
                       250
                ....*....|..
gi 15600424 221 KVLATGTPQELR 232
Cdd:COG0411 230 RVIAEGTPAEVR 241
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
275-482 1.72e-42

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: 152.73  E-value: 1.72e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT---RRRVGY 351
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVlharlfhlpadgiparvgemlrrfdlekvadelpndLPL--GIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03229  81 VFQDFALFPHLTVLENIA------------------------------------LGLsgGQQQRVALARALAMDPDVLLL 124
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGK 482
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
272-495 1.95e-42

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 157.56  E-value: 1.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 272 RIAIEAEGLTCRFGDFV--------AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFG-QPVdasd 342
Cdd:COG4586  12 RVYEKEPGLKGALKGLFrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPF---- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 343 matRRRVGY-------MSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLS 415
Cdd:COG4586  88 ---KRRKEFarrigvvFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 416 LAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244

                .
gi 15600424 495 Q 495
Cdd:COG4586 245 R 245
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
11-226 2.09e-42

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: 153.83  E-value: 2.09e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRavcpRIAYMP 89
Cdd:cd03259   3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpERR----NIGMVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03259  79 QDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03259 157 PLSALDAKLREELREELKELQR-ELGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
10-226 2.61e-42

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: 153.46  E-value: 2.61e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcprIAYMP 89
Cdd:cd03235   1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGKNLYPTLSVFENV----DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03235  75 QRRSIDRDFPISVRDVVlmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWlVAMDDGKVLATG 226
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELR--REGMTILVVTHDLGLVLEyFDR-VLLLNRTVVASG 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-208 2.92e-42

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 155.25  E-value: 2.92e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   1 MTAGGSGVaSLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrDRR 76
Cdd:COG1116   1 MSAAAPAL-ELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV------DGK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  77 HRRAVCPRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCC 156
Cdd:COG1116  74 PVTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQ-ETGKTVLFVTHDVDEA 202
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
274-495 4.35e-42

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 157.54  E-value: 4.35e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMATRRR-VGYM 352
Cdd:COG3839   3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRnIAMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG3839  81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 433 TSGVDPVARdgfWELMVELS---RRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG3839 161 LSNLDAKLR---VEMRAEIKrlhRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEELYDR 224
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
10-496 4.41e-42

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 161.35  E-value: 4.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdmRDRRHRRavcPRIAyMP 89
Cdd:COG3845   7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DG--KPVRIRS---PRDA-IA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGK-----NLYPTLSVFENV------DFFGRLfghDKAERERRIADLLQSTGLA--PfaERPAGKLSGGMKQKLGLCC 156
Cdd:COG3845  80 LGIGMvhqhfMLVPNLTVAENIvlglepTKGGRL---DRKAARARIRELSERYGLDvdP--DAKVEDLSVGEQQRVEILK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQElrerT 235
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAA--EGKSIIFITHKLREVMAIaDRVTVLRRGKVVGTVDTAE----T 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 236 GTQSLESAFIallpeskraGHH-RLVIPPRPQSEGAPRiaIEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGK 313
Cdd:COG3845 229 SEEELAELMV---------GREvLLRVEKAPAEPGEVV--LEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQ 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 314 STTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYMS---QAFSLYAELSVRQNLVLH-------ARLFHLPADG 381
Cdd:COG3845 298 SELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgVAYIPedrLGRGLVPDMSVAENLILGryrrppfSRGGFLDRKA 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 382 IPARVGEMLRRFDLeKVADElpnDLPlgIR-------QRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRR 454
Cdd:COG3845 378 IRAFAEELIEEFDV-RTPGP---DTP--ARslsggnqQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RD 450
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....
gi 15600424 455 DGVTI-FISTHfMNEAQR-CDRISLMHAGKVLASDTPDELVRQR 496
Cdd:COG3845 451 AGAAVlLISED-LDEILAlSDRIAVMYEGRIVGEVPAAEATREE 493
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
10-232 5.44e-42

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: 153.36  E-value: 5.44e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAVcpriaym 88
Cdd:cd03219   2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIAR------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 pQGLGK-----NLYPTLSVFENV----------DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLG 153
Cdd:cd03219  75 -LGIGRtfqipRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVA----TAYMEEAERfdwLVAMDDGKVLATGTPQ 229
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELR--ERGITVLLVehdmDVVMSLADR---VTVLDQGRVIAEGTPD 228

                ...
gi 15600424 230 ELR 232
Cdd:cd03219 229 EVR 231
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
275-493 8.21e-42

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: 152.70  E-value: 8.21e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYM 352
Cdd:cd03218   1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03218  81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELV 493
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIA 221
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
10-234 2.40e-41

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 155.64  E-value: 2.40e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG-DMRDRR-HRRavcpRIAY 87
Cdd:COG3842   7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-LDGrDVTGLPpEKR----NVGM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:COG3842  82 VFQDYA--LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQR-ELGITFIYVTHDQEEALALaDRIAVMNDGRIEQVGTPEEIYER 226
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
10-222 2.47e-41

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: 151.10  E-value: 2.47e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-----RDRRH-RR 79
Cdd:cd03255   2 ELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklseKELAAfRR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  80 AvcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:cd03255  82 R---HIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 160 HDPDLLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLREL-NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
11-241 2.68e-41

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 154.99  E-value: 2.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhrRAVCPRIAYMPQ 90
Cdd:PRK13536  44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARARIGVVPQ 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:PRK13536 122 F--DNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  171 TTGVDPLSRNQFWEligRIRA-GREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL-RERTGTQSLE 241
Cdd:PRK13536 200 TTGLDPHARHLIWE---RLRSlLARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALiDEHIGCQVIE 270
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
23-226 2.98e-41

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: 150.98  E-value: 2.98e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdMRDRRHRRAVCPRIAYMPQGLGknLYPTLSV 102
Cdd:cd03266  20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DG-FDVVKEPAEARRRLGFVSDSTG--LYDRLTA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQF 182
Cdd:cd03266  96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15600424 183 WELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03266 176 REFIRQLRA--LGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
275-492 3.66e-41

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: 150.79  E-value: 3.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA-----SEGTCALFGQPVDASDM---ATR 346
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVdvlELR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAeLSVRQNLVLHARLfH--LPADGIPARVGEMLRRFDL-EKVADEL-PNDLPLGIRQRLSLAVAVIH 422
Cdd:cd03260  81 RRVGMVFQKPNPFP-GSIYDNVAYGLRL-HgiKLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARALAN 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 423 KPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDEL 492
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
275-495 4.49e-41

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 154.53  E-value: 4.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDaSDMATR-RRVGYMS 353
Cdd:COG1118   3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPReRRVGFVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:COG1118  82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDR 224
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
276-487 7.37e-41

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: 149.61  E-value: 7.37e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdasdMATRRRVGYMSQA 355
Cdd:cd03235   1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKRIGYVPQR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 356 FSL--YAELSVRQnLVLHARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:cd03235  77 RSIdrDFPISVRD-VVLMGLYGHKGLFRRLskadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMhAGKVLASD 487
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
274-494 8.69e-41

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: 150.34  E-value: 8.69e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFG----DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DASDMATRRR 348
Cdd:COG1124   1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQ--AFSLYAELSVRQNLVLHARLFHLPAdgIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1124  81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
275-495 2.45e-40

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: 148.54  E-value: 2.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmATRRRVGYMSQ 354
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-PHKRPVNTVFQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03300  80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEIYEE 221
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
274-495 4.14e-40

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: 155.83  E-value: 4.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPVDASDMATR-R 347
Cdd:COG1123   4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 348 RVGYMSQ-AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:COG1123  84 RIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA 233
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
275-483 5.97e-40

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 147.12  E-value: 5.97e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF-GDFVAVDHVSFRIERGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMA-TRRR 348
Cdd:COG2884   2 IRFENVSKRYpGGREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIPyLRRR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:COG2884  81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTH---FMNEAQRcdRISLMHAGKV 483
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHdleLVDRMPK--RVLELEDGRL 215
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
10-232 1.05e-39

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: 146.88  E-value: 1.05e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHRRavcp 83
Cdd:cd03261   2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaelYRLRR---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  84 RIAYMPQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADL-LQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03261  78 RMGMLFQSGA--LFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKK-ELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELR 225
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
10-208 1.12e-39

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: 146.46  E-value: 1.12e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHrravcPRI 85
Cdd:cd03293   2 EVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV-DGEPVTGPG-----PDR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 AYMPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03293  76 GYVFQQ--DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWR-ETGKTVLLVTHDIDEA 195
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
275-492 2.25e-39

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: 145.80  E-value: 2.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD----ASDMATR 346
Cdd:cd03258   2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:cd03258  82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
274-492 2.46e-39

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: 145.94  E-value: 2.46e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMATRRR-VGYM 352
Cdd:cd03296   2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERnVGFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQN----LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:cd03296  80 FQHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGTPDEV 224
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
271-494 2.73e-39

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 152.87  E-value: 2.73e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 271 PRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRR 348
Cdd:COG1129   1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprDAQAAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQAFSLYAELSVRQNLVLHarlfHLPADG-------IPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVI 421
Cdd:COG1129  81 IAIIHQELNLVPNLSVAENIFLG----REPRRGglidwraMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 422 HKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTI-FIStHFMNEAQR-CDRISLMHAGKVLASD-----TPDELVR 494
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIiYIS-HRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
10-224 4.47e-39

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 144.80  E-value: 4.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD---GDMRDR---RHRR 79
Cdd:COG1136   6 ELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERelaRLRR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  80 AvcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:COG1136  86 R---HIGFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 160 HDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLA 224
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNR-ELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
285-494 6.97e-39

glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 148.46  E-value: 6.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-----TRRRVGYMSQAFSLY 359
Cdd:TIGR01186   4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVelrevRRKKIGMVFQQFALF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   360 AELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPV 439
Cdd:TIGR01186  84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424   440 ARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVR 494
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIgDRIVIMKAGEIVQVGTPDEILR 219
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
283-487 7.97e-39

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: 144.40  E-value: 7.97e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQ-PVDASDmATRRRVGY-MSQAFSLYA 360
Cdd:cd03267  30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRK-KFLRRIGVvFGQKTQLWW 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15600424 441 RDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASD 487
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDiEALARRVLVIDKGRLLYDG 236
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
11-222 1.37e-38

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 143.27  E-value: 1.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRavcprIAYMP 89
Cdd:COG2884   4 FENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE-----IPYLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLG------KnLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:COG2884  79 RRIGvvfqdfR-LLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDW-LVAMDDGKV 222
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN--RRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
276-486 1.44e-38

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: 141.80  E-value: 1.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATR-RRVGYMSQ 354
Cdd:cd03214   1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELaRKIAYVPQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AfslyaelsvrqnlvlharlfhlpadgiparvgemLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03214  81 A----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
10-226 1.46e-38

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: 142.74  E-value: 1.46e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAvcpRIAYMP 89
Cdd:cd03268   2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR---RIGALI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTLSVFENVDFFGRLFGhdkaERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03268  79 EAPG--FYPNLTARENLRLLARLLG----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRD--QGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
10-226 1.89e-38

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: 141.42  E-value: 1.89e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:cd03214   1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-LDGKDLASLSPKELARKIAYVP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QglgknlyptlsvfenvdffgrlfghdkaererriadLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03214  80 Q------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 170 PTTGVDPlsRNQFwELIGRIR--AGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03214 124 PTSHLDI--AHQI-ELLELLRrlARERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
276-482 2.85e-38

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: 140.07  E-value: 2.85e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQ 354
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElRRRIGYVPQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 afslyaeLSVrqnlvlharlfhlpadgiparvGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd00267  81 -------LSG----------------------GQ----------------------RQRVALARALLLNPDLLLLDEPTS 109
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15600424 435 GVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGK 482
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
275-483 2.87e-38

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 141.88  E-value: 2.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMS 353
Cdd:COG4619   1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAElSVRQNLVLHARLFHLPADgiPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG4619  81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
10-233 4.87e-38

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: 141.80  E-value: 4.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAvcpR--IA 86
Cdd:cd03224   2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERA---RagIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  87 YMPQglGKNLYPTLSVFENVdffgRL--FGHDKAERERRIADLLQS-TGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03224  79 YVPE--GRRIFPELTVEENL----LLgaYARRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLV----ATAYMEEAERFdwlVAMDDGKVLATGTPQELRE 233
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELR--DEGVTILLveqnARFALEIADRA---YVLERGRVVLEGTAAELLA 221
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
10-233 6.57e-38

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 141.66  E-value: 6.57e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAvcpR--IA 86
Cdd:COG0410   5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIA---RlgIG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  87 YMPQGlgKNLYPTLSVFENVDFfGRLFGHDKAERERRIADLLQst-gLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:COG0410  82 YVPEG--RRIFPSLTVEENLLL-GAYARRDRAEVRADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLV----ATAYMEEAERFdwlVAMDDGKVLATGTPQELRE 233
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLN--REGVTILLveqnARFALEIADRA---YVLERGRIVLEGTAAELLA 225
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
275-493 7.23e-38

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 141.71  E-value: 7.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYM 352
Cdd:COG1137   4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGYL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG1137  84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEIL 224
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
260-492 1.19e-37

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 145.36  E-value: 1.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  260 VIP-PRPQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpv 338
Cdd:PRK11607   4 AIPrPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  339 DASDMATRRR-VGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA 417
Cdd:PRK11607  82 DLSHVPPYQRpINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  418 VAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
578-908 1.56e-37

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 144.07  E-value: 1.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   578 MFIIGYGINmDVEDLSWAVLDRDQTTTSQAYALNIAGSRYFVEHAPITDPDDLDRRLRSGELSLAVEIPPNFGRDLKRGS 657
Cdd:pfam12698  19 GLIFSNAVN-DPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLLKGE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   658 DPAIGVWIDGAMPTRANTVLGYVQGLHTSYLA-DLSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPaVIPLLLIMIPA 736
Cdd:pfam12698  98 SATVTVYINSSNLLVSKLILNALQSLLQQLNAsALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIILIGA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   737 MLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFrVPLKGSFLALtIGAFLYVVTSTG 816
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIG-IPFGNLGLLL-LLFLLYGLAYIA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   817 LGLFLSTFMRSQIAAVFGVAIATMIPAIQFSGLIhPVSSLEGAAAWIGKLYPTSHFLVVSRgAFSKSLGLSDLWAYYLPL 896
Cdd:pfam12698 255 LGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLF-PLEDPPSFLQWIFSIIPFFSPIDGLL-RLIYGDSLWEIAPSLIIL 332
                         330
                  ....*....|..
gi 15600424   897 AASIVVLTLLSV 908
Cdd:pfam12698 333 LLFAVVLLLLAL 344
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
11-231 1.86e-37

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: 140.78  E-value: 1.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHR--RAVCPRIAY 87
Cdd:cd03256   3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQIGM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLgkNLYPTLSVFENVdFFGRLFGH----------DKAERERRIAdLLQSTGLAPFAERPAGKLSGGMKQKLGLCCA 157
Cdd:cd03256  83 IFQQF--NLIERLSVLENV-LSGRLGRRstwrslfglfPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRI-NREEGITVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
275-483 1.96e-37

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: 140.33  E-value: 1.96e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMATRR 347
Cdd:cd03257   2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 348 R-VGYMSQ--AFSLYAELSVRQnLVLHARLFHLPADG---IPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAV 420
Cdd:cd03257  82 KeIQMVFQdpMSSLNPRMTIGE-QIAEPLRIHGKLSKkeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 421 IHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
283-495 2.00e-37

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: 141.63  E-value: 2.00e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-----RRRVGYMSQAFS 357
Cdd:cd03294  33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVFQSFA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 438 PVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVRQ 495
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTN 251
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
24-172 4.37e-37

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: 136.24  E-value: 4.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM--RDRRHRRAvcpRIAYMPQGLgkNLYPTLS 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRK---EIGYVFQDP--QLFPRLT 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424   102 VFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:pfam00005  76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
10-234 5.29e-37

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 142.90  E-value: 5.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGdmRDRRHRRAVCPRIAYMP 89
Cdd:COG3839   5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-IGG--RDVTDLPPKDRNIAMVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG3839  82 QSYA--LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRnqfWELIGRIRA--GREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:COG3839 160 PLSNLDAKLR---VEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLaDRIAVMNDGRIQQVGTPEELYDR 224
GldA_ABC_ATP TIGR03522
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ...
14-244 2.36e-36

gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.


Pssm-ID: 132561 [Multi-domain]  Cd Length: 301  Bit Score: 139.52  E-value: 2.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    14 VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMPQGlg 93
Cdd:TIGR03522   8 LTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVL--QNPKEVQRNIGYLPEH-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    94 KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 173
Cdd:TIGR03522  84 NPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTG 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424   174 VDPlsrNQFWELIGRIRAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAF 244
Cdd:TIGR03522 164 LDP---NQLVEIRNVIKNIGKDKTIILSTHIMQEVEAIcDRVIIINKGKIVADKKLDELSAANKKQVIEVEF 232
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
277-493 3.12e-36

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 137.02  E-value: 3.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   277 AEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYMSQ 354
Cdd:TIGR04406   4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYLPQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   355 AFSLYAELSVRQNL--VLHARlFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:TIGR04406  84 EASIFRKLTVEENImaVLEIR-KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424   433 TSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:TIGR04406 163 FAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDiCDRAYIISDGKVLAEGTPAEIV 223
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
275-492 3.59e-36

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: 136.41  E-value: 3.59e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD--ASDMATRRRVGYM 352
Cdd:cd03224   1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglPPHERARAGIGYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHArlFHLPADGIPARVGEMLRRF-DLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDE 431
Cdd:cd03224  81 PEGRRIFPELTVEENLLLGA--YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 432 PTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
290-434 9.72e-36

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: 132.39  E-value: 9.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPL----GIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
10-221 1.38e-35

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: 132.37  E-value: 1.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD---GDMRDRRHRRavcpRIA 86
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiAKLPLEELRR----RIG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  87 YMPQglgknlyptlsvfenvdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:cd00267  77 YVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGK 221
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELA--EEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
275-486 1.71e-35

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: 132.17  E-value: 1.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGYM 352
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASprDARRAGIAMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQafslyaelsvrqnlvlharlfhlpadgiparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03216  81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 433 TSGVDPVARDGFWELMVELsRRDGVT-IFIStHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03216 110 TAALTPAEVERLFKVIRRL-RAQGVAvIFIS-HRLDEVFEiADRVTVLRDGRVVGT 163
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
10-483 3.62e-35

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 141.08  E-value: 3.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK09700   7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QGLgkNLYPTLSVFENVdFFGRL-----FGH---DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK09700  87 QEL--SVIDELTVLENL-YIGRHltkkvCGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  162 PDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE------LRER 234
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLR--KEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDvsnddiVRLM 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  235 TGtQSLESAFIALLPESKRAGHhrlvipprpqsegapRIAIEAEGLTCRfgDFVAVDHVSFRIERGEIFGFLGSNGCGKS 314
Cdd:PRK09700 242 VG-RELQNRFNAMKENVSNLAH---------------ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRT 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  315 TTMKMLTGLLPASEGTCALFGQ------PVDA--SDMA----TRRRVGYmsqafslYAELSVRQNLvlhARLFHLPADGI 382
Cdd:PRK09700 304 ELMNCLFGVDKRAGGEIRLNGKdisprsPLDAvkKGMAyiteSRRDNGF-------FPNFSIAQNM---AISRSLKDGGY 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  383 PARVGeMLRRFDLEKVADELPNDLPL--------------GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:PRK09700 374 KGAMG-LFHEVDEQRTAENQRELLALkchsvnqnitelsgGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM 452
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15600424  449 VELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK09700 453 RQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
10-236 5.21e-35

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: 141.43  E-value: 5.21e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAvcpRIA 86
Cdd:COG4988 338 ELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdlDPASWRR---QIA 414
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  87 YMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAER-PAG----------KLSGGMKQKL 152
Cdd:COG4988 415 WVPQN------PYLfagTIRENL-----RLGRPDASDEE-LEAALEAAGLDEFVAAlPDGldtplgeggrGLSGGQAQRL 482
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELR 232
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR---TVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559

                ....
gi 15600424 233 ERTG 236
Cdd:COG4988 560 AKNG 563
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
276-483 6.97e-35

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: 132.00  E-value: 6.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFV-AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMatRRRVGYMSQ 354
Cdd:cd03226   1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 --AFSLYAElSVRQNLVLHARlfhlPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03226  79 dvDYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600424 433 TSGVDPVARDGFWELMVELSRRdGVTIFISTH---FMneAQRCDRISLMHAGKV 483
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHdyeFL--AKVCDRVLLLANGAI 204
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
275-483 1.37e-34

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 131.61  E-value: 1.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDM-ATRRRVGYMS 353
Cdd:cd03301   1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLpPKDRDIAMVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:cd03301  79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
10-235 2.69e-34

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: 131.85  E-value: 2.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGE----TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRI 85
Cdd:COG1124   3 EVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR-RKAFRRRV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 AYMPQglgknlYPTLSV--FENVDffgRLFG-----HDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCA 157
Cdd:COG1124  82 QMVFQ------DPYASLhpRHTVD---RILAeplriHGLPDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERT 235
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLRE-ERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAGP 230
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
10-242 2.71e-34

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: 131.65  E-value: 2.71e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR---RHRRavcpRI 85
Cdd:cd03295   2 EFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvELRR----KI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 AYMPQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP--FAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03295  78 GYVIQQIG--LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLE 241
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQ--QElGKTIVFVTHDIDEAFRLaDRIAIMKNGEIVQVGTPDEILRSPANDFVA 233

                .
gi 15600424 242 S 242
Cdd:cd03295 234 E 234
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
11-500 4.75e-34

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: 137.65  E-value: 4.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARK--MQDGEIRVLDGDMRDRRHRRAVCPRIAYM 88
Cdd:TIGR02633   4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIVII 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    89 PQGLgkNLYPTLSVFENVdFFGRLFGH-----DKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:TIGR02633  84 HQEL--TLVPELSVAENI-FLGNEITLpggrmAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   163 DLLILDEPTTGvdpLSRNQFWELIGRIR-AGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRE-RTGTQS 239
Cdd:TIGR02633 161 RLLILDEPSSS---LTEKETEILLDIIRdLKAHGVACVYISHKLNEVKAVcDTICVIRDGQHVATKDMSTMSEdDIITMM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   240 LESAFIALLPEskraghhrlvippRPQSEGapRIAIEAEGLTCRFGD---FVAVDHVSFRIERGEIFGFLGSNGCGKSTT 316
Cdd:TIGR02633 238 VGREITSLYPH-------------EPHEIG--DVILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTEL 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   317 MKMLTGLLP-ASEGTCALFGQPVDASDMAT------------RRRVGYMSQafslyaeLSVRQNLVL-----HARLFHLP 378
Cdd:TIGR02633 303 VQALFGAYPgKFEGNVFINGKPVDIRNPAQairagiamvpedRKRHGIVPI-------LGVGKNITLsvlksFCFKMRID 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   379 ADGIPARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGV 457
Cdd:TIGR02633 376 AAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVA 455
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 15600424   458 TIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGLPT 500
Cdd:TIGR02633 456 IIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAA 498
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
10-231 8.56e-34

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: 130.01  E-value: 8.56e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETR----AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-----RDRRHRRA 80
Cdd:cd03258   3 ELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgKELRKARR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  81 vcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:cd03258  83 ---RIGMIFQHF--NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVA-MDDGKVLATGTPQEL 231
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINR-ELGLTIVLITHEMEVVKRICDRVAvMEKGEVVEEGTVEEV 228
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
11-221 1.22e-33

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: 127.30  E-value: 1.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-MRDRRHRRAVCPRIAYMP 89
Cdd:cd03229   3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGMVF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLgkNLYPTLSVFENVDFfgrlfghdkaererriadllqstglapfaerpagKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03229  83 QDF--ALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGK 221
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQA-QLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
10-226 2.19e-33

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: 128.39  E-value: 2.19e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM--RDRRHRRAVCP 83
Cdd:cd03257   3 EVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIRRK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  84 RIAYMPQGLGKNLYPTLSVFENVD--FFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:cd03257  83 EIQMVFQDPMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALAL 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVAT------AYMeeAERfdwLVAMDDGKVLATG 226
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEEL-GLTLLFIThdlgvvAKI--ADR---VAVMYAGKIVEEG 228
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
275-483 2.22e-33

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: 128.03  E-value: 2.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---MATRRRVGY 351
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkniNELRQKVGM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVLHAR-LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03262  81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600424 431 EPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
10-234 4.76e-33

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 131.04  E-value: 4.76e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-------DMRDRRhrravc 82
Cdd:COG1118   4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGrdlftnlPPRERR------ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  83 prIAYMPQglgkN--LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:COG1118  77 --VGFVFQ----HyaLFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFV-THDQEEALELaDRVVVMNQGRIEQVGTPDEVYDR 224
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
245-498 5.64e-33

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: 136.50  E-value: 5.64e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 245 IALLPESKRAGHHRLvipPRPQSEGApriaIEAEGLTCRFGDFV--AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTG 322
Cdd:COG2274 451 ILDLPPEREEGRSKL---SLPRLKGD----IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 323 LLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQNLvlhaRLFHLPADgiPARVGEMLRRFDLEKVADE 401
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASlRRQIGVVLQDVFLFSG-TIRENI----TLGDPDAT--DEEIIEAARLAGLHDFIEA 596
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 402 LPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQ 470
Cdd:COG2274 597 LPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR 674
                       250       260
                ....*....|....*....|....*...
gi 15600424 471 RCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:COG2274 675 LADRIIVLDKGRIVEDGTHEELLARKGL 702
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
275-492 7.37e-33

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: 127.30  E-value: 7.37e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV----DASDMATRRRV 349
Cdd:cd03256   1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQAFSLYAELSVRQNlVLHARLFHLP-----------ADGIPARvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAV 418
Cdd:cd03256  81 GMIFQQFNLIERLSVLEN-VLSGRLGRRStwrslfglfpkEEKQRAL--AALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
10-483 8.62e-33

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 133.50  E-value: 8.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK11288   6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QGLgkNLYPTLSVFENVdFFGRL---FGH-DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK11288  86 QEL--HLVPEMTVAENL-YLGQLphkGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  166 ILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKvlatgtpqelrertgtqslesaF 244
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRA--EGRVILYVSHRMEEIFALcDAITVFKDGR----------------------Y 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  245 IALLPESKRAGHHRLV-------------IPPRPQSEgaprIAIEAEGLTcrfGDFVAVDhVSFRIERGEIFGFLGSNGC 311
Cdd:PRK11288 219 VATFDDMAQVDRDQLVqamvgreigdiygYRPRPLGE----VRLRLDGLK---GPGLREP-ISFSVRAGEIVGLFGLVGA 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  312 GKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYM-----SQAFSLYAELSVRQNLVLHARLFHLPADGI--PA 384
Cdd:PRK11288 291 GRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGIIPVHSVADNINISARRHHLRAGCLinNR 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  385 RVGEMLRRF-DLEKV----ADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdGVTI 459
Cdd:PRK11288 371 WEAENADRFiRSLNIktpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAV 449
                        490       500
                 ....*....|....*....|....*
gi 15600424  460 -FISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK11288 450 lFVSSDLPEVLGVADRIVVMREGRI 474
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
275-492 9.88e-33

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 129.81  E-value: 9.88e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDM-ATR 346
Cdd:COG1135   2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELrAAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:COG1135  82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDV 228
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
289-489 1.05e-32

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 137.84  E-value: 1.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 15600424    449 veLSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTP 489
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
274-505 1.21e-32

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: 127.12  E-value: 1.21e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-TCALFGQPVDASDMAT-RRRVGY 351
Cdd:COG1119   3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElRKRIGL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLY--AELSVRqNLVLHAR-----LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:COG1119  83 VSPALQLRfpRDETVL-DVVLSGFfdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVRQrglPTLEA 503
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS---ENLSE 238

                ..
gi 15600424 504 TF 505
Cdd:COG1119 239 AF 240
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
8-231 1.48e-32

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: 126.74  E-value: 1.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG-ARKMQDGEIRVLD-----GDMRDRRhrrav 81
Cdd:COG1119   3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGerrggEDVWELR----- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  82 cPRIAYMPQGLGKNLYPTLSVFENV--DFFG--RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCA 157
Cdd:COG1119  78 -KRIGLVSPALQLRFPRDETVLDVVlsGFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQEL 231
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKL-AAEGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEV 230
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
10-236 4.39e-32

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: 133.81  E-value: 4.39e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG-DMR--DRRHRRAvcpR 84
Cdd:COG2274 475 ELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-DGiDLRqiDPASLRR---Q 550
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  85 IAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAER-PAG----------KLSGGMKQ 150
Cdd:COG2274 551 IGVVLQD------VFLfsgTIRENI-----TLGDPDATDEE-IIEAARLAGLHDFIEAlPMGydtvvgeggsNLSGGQRQ 618
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR---TVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEE 695

                ....*.
gi 15600424 231 LRERTG 236
Cdd:COG2274 696 LLARKG 701
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
15-230 4.40e-32

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 125.51  E-value: 4.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   15 SLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR---DRRHRRavcpRIAYMPQG 91
Cdd:PRK11231   9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlsSRQLAR----RLALLPQH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   92 LgknLYPT-LSVFENV--------DFFGRLFGHDKAererRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK11231  85 H---LTPEgITVRELVaygrspwlSLWGRLSAEDNA----RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE 230
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNT--QGKTVVTVLHDLNQASRYcDHLVVLANGHVMAQGTPEE 224
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
10-231 5.53e-32

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: 124.60  E-value: 5.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ-----DGEIRVLDGDMRDRRHRRAVCPR 84
Cdd:cd03260   2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELRR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  85 IAYM----PqglgkNLYPtLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLAPFAERP--AGKLSGGMKQKLGLCCA 157
Cdd:cd03260  82 RVGMvfqkP-----NPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARA 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAEL---KKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
270-497 6.37e-32

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: 131.80  E-value: 6.37e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RR 347
Cdd:COG4988 332 AGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRR 411
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 348 RVGYMSQAFSLYAElSVRQNLvlhaRLFHLPADgiPARVGEMLRRFDLEKVADELPNDL--PL---------GIRQRLSL 416
Cdd:COG4988 412 QIAWVPQNPYLFAG-TIRENL----RLGRPDAS--DEELEAALEAAGLDEFVAALPDGLdtPLgeggrglsgGQAQRLAL 484
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 417 AVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562

                .
gi 15600424 497 G 497
Cdd:COG4988 563 G 563
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
10-234 6.74e-32

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: 124.27  E-value: 6.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD----RRHRRAVCPRI 85
Cdd:cd03300   2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphKRPVNTVFQNY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 AympqglgknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03300  82 A---------LFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQK-ELGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEIYEE 221
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
10-208 6.99e-32

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 125.36  E-value: 6.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGdmrdrrhrRAVcpri 85
Cdd:COG4525   5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT-LDG--------VPV---- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 aympQGLGKN---------LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCC 156
Cdd:COG4525  72 ----TGPGADrgvvfqkdaLLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQ-RTGKGVFLITHSVEEA 198
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
10-222 9.35e-32

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: 123.14  E-value: 9.35e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAvcpRIAYM 88
Cdd:cd03226   1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-LNGKPIKAKERRK---SIGYV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 PQGLGKNLYpTLSVFENVdffgRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:cd03226  77 MQDVDYQLF-TDSVREEL----LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAA--QGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
275-495 1.08e-31

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 125.13  E-value: 1.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDF--VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD-ASDMATRRRVGY 351
Cdd:PRK13635   6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQVGM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 MSQ-AFSLYAELSVRQNLVlharlFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK13635  86 VFQnPDNQFVGATVQDDVA-----FGLENIGVPreemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
289-482 1.08e-31

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: 121.72  E-value: 1.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03228  17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAYVPQDPFLFSG-TIREN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LvlharlfhlpadgiparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:cd03228  96 I-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15600424 448 MveLSRRDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:cd03228 139 L--RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
260-497 1.56e-31

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: 130.66  E-value: 1.56e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 260 VIPPRPQSEGAPRIAIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQP 337
Cdd:COG4987 319 VTEPAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 338 VDASDMAT-RRRVGYMSQAFSLYAElSVRQNLVLhARlfhlpADGIPARVGEMLRRFDLEKVADELPN--DLPLGI---- 410
Cdd:COG4987 399 LRDLDEDDlRRRIAVVPQRPHLFDT-TLRENLRL-AR-----PDATDEELWAALERVGLGDWLAALPDglDTWLGEggrr 471
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 411 -----RQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVtIFIsTHFMNEAQRCDRISLMHAGKVLA 485
Cdd:COG4987 472 lsggeRRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV-LLI-THRLAGLERMDRILVLEDGRIVE 549
                       250
                ....*....|..
gi 15600424 486 SDTPDELVRQRG 497
Cdd:COG4987 550 QGTHEELLAQNG 561
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
12-209 1.71e-31

gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.


Pssm-ID: 163452 [Multi-domain]  Cd Length: 223  Bit Score: 122.89  E-value: 1.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMPqg 91
Cdd:TIGR03740   4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI-IFDGHPWTRKDLHKIGSLIESPP-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    92 lgknLYPTLSVFENVDFFGRLFGHDkaerERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:TIGR03740  81 ----LYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15600424   172 TGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAE 209
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFP--EQGITVILSSHILSEVQ 188
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
10-221 1.91e-31

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: 120.95  E-value: 1.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGET--RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAvcpRI 85
Cdd:cd03228   2 EFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdlDLESLRK---NI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 AYMPQGlgknlyPTL---SVFENVdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDP 162
Cdd:cd03228  79 AYVPQD------PFLfsgTIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGK 221
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGK---TVIVIAHRLSTIRDADRIIVLDDGR 171
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
9-238 2.24e-31

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 125.58  E-value: 2.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   9 ASLRG-VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDgdMRDRRHRRAVCPRIAY 87
Cdd:COG4586  22 GALKGlFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRRKEFARRIGV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 -MPQglgKN-LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:COG4586 100 vFGQ---RSqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQ 238
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNR-ERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPY 249
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
288-495 3.05e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 124.04  E-value: 3.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMAT----RRRVGYMSQA--FSLYAE 361
Cdd:PRK13633  24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENlwdiRNKAGMVFQNpdNQIVAT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  362 LsVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK13633 102 I-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15600424  442 DGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
283-495 3.61e-31

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 122.50  E-value: 3.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCalfgqpvdasdmatrRRVGYMSQAFSL---- 358
Cdd:COG1134  35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV---------------EVNGRVSALLELgagf 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 359 YAELSVRQNLVLHARLFHLPADgiparvgEMLRRFDleKVAD--ELPN--DLPL-----GIRQRLSLAVAVIHKPEILIL 429
Cdd:COG1134 100 HPELTGRENIYLNGRLLGLSRK-------EIDEKFD--EIVEfaELGDfiDQPVktyssGMRARLAFAVATAVDPDILLV 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 430 DEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
5-236 9.65e-31

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: 128.35  E-value: 9.65e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   5 GSGVASLRGVSLRY-GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRA 80
Cdd:COG4987 330 GGPSLELEDVSFRYpGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRR 409
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  81 vcpRIAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAErERRIADLLQSTGLAPFAER-PAG----------KLSG 146
Cdd:COG4987 410 ---RIAVVPQR------PHLfdtTLRENL-----RLARPDAT-DEELWAALERVGLGDWLAAlPDGldtwlgeggrRLSG 474
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 147 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATG 226
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR---TVLLITHRLAGLERMDRILVLEDGRIVEQG 551
                       250
                ....*....|
gi 15600424 227 TPQELRERTG 236
Cdd:COG4987 552 THEELLAQNG 561
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
3-483 1.05e-30

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 127.47  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    3 AGGSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrDRRHRRAVC 82
Cdd:PRK15439   6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI------GGNPCARLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   83 PRIAY------MPQGlgKNLYPTLSVFENVdffgrLFGHDK-AERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK15439  80 PAKAHqlgiylVPQE--PLLFPNLSVKENI-----LFGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEIL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  156 CALIHDPDLLILDEPTTGVDPLSRNQfweLIGRIRAGR-EGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRE 233
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETER---LFSRIRELLaQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADLST 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  234 RTGTQSLESAFIAL-LPESKR-----AGHHRLvipprpQSEGAPRIAIE---AEGltcrfgdFVavdHVSFRIERGEIFG 304
Cdd:PRK15439 230 DDIIQAITPAAREKsLSASQKlwlelPGNRRQ------QAAGAPVLTVEdltGEG-------FR---NISLEVRAGEILG 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  305 FLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVG--YMS---QAFSLYAELSVRQNLVlhARLFHLPA 379
Cdd:PRK15439 294 LAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLAWNVC--ALTHNRRG 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  380 DGI-PARVGEMLRRF---------DLEKVADELPNdlplGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:PRK15439 372 FWIkPARENAVLERYrralnikfnHAEQAARTLSG----GNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIR 447
                        490       500       510
                 ....*....|....*....|....*....|....
gi 15600424  450 ELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK15439 448 SIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
266-492 1.21e-30

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 121.68  E-value: 1.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 266 QSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKML---TGLLPAS--EGTCALFGQPVDA 340
Cdd:COG1117   3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGArvEGEILLDGEDIYD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 341 SDM---ATRRRVGYMSQ---AFSlyaeLSVRQNLVLHARLFHLPADG-IPARVGEMLRRFDL-EKVADEL---PNDLPLG 409
Cdd:COG1117  83 PDVdvvELRRRVGMVFQkpnPFP----KSIYDNVAYGLRLHGIKSKSeLDEIVEESLRKAALwDEVKDRLkksALGLSGG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 410 IRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQRC-DRISLMHAGKVLASDT 488
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVsDYTAFFYLGELVEFGP 236

                ....
gi 15600424 489 PDEL 492
Cdd:COG1117 237 TEQI 240
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
10-235 1.40e-30

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 120.87  E-value: 1.40e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-RDRRHRRAVCPRIAYM 88
Cdd:COG1126   3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtDSKKDINKLRRKVGMV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 PQGLgkNLYPTLSVFENVdFFG--RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:COG1126  83 FQQF--NLFPHLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 167 LDEPTTGVDPlsrnqfwELIGRI-----RAGREGMSVLVATAYMEEAER-FDWLVAMDDGKVLATGTPQEL-----RERT 235
Cdd:COG1126 160 FDEPTSALDP-------ELVGEVldvmrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFfenpqHERT 232
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
273-491 1.44e-30

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 121.42  E-value: 1.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  273 IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDMATRRRV 349
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  350 gyMSQAFSLYAELSVRQnLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA-V-----AVIH 422
Cdd:PRK13548  81 --LPQHSSLSFPFTVEE-VVAMGRAPHgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVlaqlwEPDG 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  423 KPEILILDEPTSGVDP--------VARdgfwelmvELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDE 491
Cdd:PRK13548 158 PPRWLLLDEPTSALDLahqhhvlrLAR--------QLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAE 227
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
10-260 1.50e-30

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 123.65  E-value: 1.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHRR 79
Cdd:COG1135   3 ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserelRAARR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  80 avcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAER-PAgKLSGGMKQKLGLCCAL 158
Cdd:COG1135  83 ----KIGMIFQHF--NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAyPS-QLSGGQKQRVGIARAL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEE----AERfdwlVA-MDDGKVLATGTPQEL-- 231
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINR-ELGLTIVLITHEMDVvrriCDR----VAvLENGRIVEQGPVLDVfa 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15600424 232 --RERTGTQSLESAFIALLPES------KRAGHHRLV 260
Cdd:COG1135 231 npQSELTRRFLPTVLNDELPEEllarlrEAAGGGRLV 267
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
275-505 1.75e-30

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 120.99  E-value: 1.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA---SDMATRRRVgy 351
Cdd:COG4559   2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspWELARRRAV-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQnLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA--VAVIHKPE--- 425
Cdd:COG4559  80 LPQHSSLAFPFTVEE-VVALGRAPHgSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAQLWEPVdgg 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 --ILILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMN-EAQRCDRISLMHAGKVLASDTPDELVRQrglPTLE 502
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVLTD---ELLE 234

                ...
gi 15600424 503 ATF 505
Cdd:COG4559 235 RVY 237
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
17-231 3.15e-30

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: 120.83  E-value: 3.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGD----MRDRRHRRAVCPRIAYMPQGL 92
Cdd:cd03294  33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV-LIDGQdiaaMSRKELRELRRKKISMVFQSF 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  93 GknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:cd03294 112 A--LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 173 GVDPLSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFI-THDLDEALRLgDRIAIMKDGRLVQVGTPEEI 248
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
10-222 3.60e-30

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 118.77  E-value: 3.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDR----RHRRavcpRI 85
Cdd:COG4619   2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-LDGKPLSAmpppEWRR----QV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 AYMPQglgknlYPTL---SVFENVDFfGRLFGHDKAERERrIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:COG4619  77 AYVPQ------EPALwggTVRDNLPF-PFQLRERKFDRER-ALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQ 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLA-EEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
10-231 4.83e-30

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: 119.18  E-value: 4.83e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-RDRRHRRAvcpR--IA 86
Cdd:cd03218   2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKRA---RlgIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  87 YMPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:cd03218  79 YLPQE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVL------------VATAYMeeaerfdwlvaMDDGKVLATGTPQEL 231
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKD--RGIGVLitdhnvretlsiTDRAYI-----------IYEGKVLAEGTPEEI 220
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
306-492 5.50e-30

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 121.45  E-value: 5.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   306 LGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMATRRR-VGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPA 384
Cdd:TIGR01187   2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDG--EDVTNVPPHLRhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   385 RVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTH 464
Cdd:TIGR01187  80 RVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTH 159
                         170       180
                  ....*....|....*....|....*....
gi 15600424   465 FMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:TIGR01187 160 DQEEAmTMSDRIAIMRKGKIAQIGTPEEI 188
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-241 5.78e-30

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 122.15  E-value: 5.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    1 MTAGGSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVgkssllallAGARKMQDGEIRVLDGDMRDRR---- 76
Cdd:NF000106   6 ISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---------A**RGALPAHV*GPDAGRRPWRf*tw 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   77 --HRRAVCPRIA-YMPQGLGKNlyPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLG 153
Cdd:NF000106  77 caNRRALRRTIG*HRPVR*GRR--ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV--RDGATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELK 232

                 ....*....
gi 15600424  233 ERTGTQSLE 241
Cdd:NF000106 233 TKVGGRTLQ 241
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
12-237 8.46e-30

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: 118.60  E-value: 8.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-----RVLDGDMRDRrhrravcpRIA 86
Cdd:cd03296   6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggeDATDVPVQER--------NVG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  87 YMPQGLGknLYPTLSVFENVDfFG-----RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:cd03296  78 FVFQHYA--LFRHMTVFDNVA-FGlrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGT 237
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
cbiO PRK13637
energy-coupling factor transporter ATPase;
288-502 1.23e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 119.38  E-value: 1.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFG-----QPVDASDMatRRRVGYMSQ--AFSLYA 360
Cdd:PRK13637  21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDI--RKKVGLVFQypEYQLFE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  361 ElSVRQNLVLHARLFHLPADGIPARVGEMLR--RFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK13637  99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  439 VARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQrgLPTLE 502
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPREVFKE--VETLE 240
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
275-495 1.43e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 119.03  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDMATRRRVG 350
Cdd:PRK13639   2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQA--FSLYAElSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK13639  82 IVFQNpdDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD 227
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
26-226 2.41e-29

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: 116.24  E-value: 2.41e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  26 DVSLEIPANRmVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-------HRRavcpRIAYMPQGLGknLYP 98
Cdd:cd03297  16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlppQQR----KIGLVFQQYA--LFP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  99 TLSVFENVDFfgRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:cd03297  89 HLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15600424 179 RNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03297 167 RLQLLPELKQIKK-NLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
283-487 3.43e-29

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: 115.86  E-value: 3.43e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAvdHVSFRIErGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-----TRRRVGYMSQAFS 357
Cdd:cd03297   9 RLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppQQRKIGLVFQQYA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNLVLHARLFHLPADGIpaRVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03297  86 LFPHLNVRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 438 PVARDgfwELMVELSRR----DGVTIFIsTHFMNEAQR-CDRISLMHAGKVLASD 487
Cdd:cd03297 164 RALRL---QLLPELKQIkknlNIPVIFV-THDLSEAEYlADRIVVMEDGRLQYIG 214
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
15-277 3.55e-29

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: 119.83  E-value: 3.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    15 SLRYGETRAvdDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG----DMRDRR----HRRavcpRIA 86
Cdd:TIGR02142   6 SKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-VLNGrtlfDSRKGIflppEKR----RIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    87 YMPQGlgKNLYPTLSVFENVDF-FGRLFGHDKAERERRIADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:TIGR02142  79 YVFQE--ARLFPHLSVRGNLRYgMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAF 244
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHA-EFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWASPDLPWLARED 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 15600424   245 IALLPESKRAGHH-------------RLVIPPRPQSEGAP-RIAIEA 277
Cdd:TIGR02142 233 QGSLIEGVVAEHDqhygltalrlgggHLWVPENLGPTGARlRLRVPA 279
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
10-226 3.95e-29

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: 116.66  E-value: 3.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLR-YGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR--HRRavcpRIA 86
Cdd:cd03267  22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRkkFLR----RIG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  87 YMpQGLGKNLYPTLSVFENVDFFGRLFGHDKAE---RERRIADLLQstgLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03267  98 VV-FGQKTQLWWDLPVIDSFYLLAAIYDLPPARfkkRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRER-GTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
275-464 4.04e-29

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: 115.97  E-value: 4.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DASDMAT---RRRV 349
Cdd:cd03292   1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIpylRRKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03292  81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRdGVTIFISTH 464
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATH 194
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
11-231 5.30e-29

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 119.44  E-value: 5.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRDRR-HRRAVCprIAYM 88
Cdd:PRK11432   9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FIDGeDVTHRSiQQRDIC--MVFQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   89 PQGLgknlYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK11432  86 SYAL----FPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  169 EPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATayMEEAERF---DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK11432 162 EPLSNLDANLRRSMREKI-RELQQQFNITSLYVT--HDQSEAFavsDTVIVMNKGKIMQIGSPQEL 224
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
275-491 5.81e-29

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 119.67  E-value: 5.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDM-ATRRRVGYMS 353
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVpAENRHVNTVF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:PRK09452  93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  434 SGVDPVARDgfwELMVE---LSRRDGVT-IFIsTHFMNEA-QRCDRISLMHAGKVLASDTPDE 491
Cdd:PRK09452 173 SALDYKLRK---QMQNElkaLQRKLGITfVFV-THDQEEAlTMSDRIVVMRDGRIEQDGTPRE 231
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
275-483 8.81e-29

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: 117.85  E-value: 8.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGTCALFGQPV---DASDMA 344
Cdd:COG0444   2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklSEKELR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 345 TRR--RVGYMSQ-AF-SLYAELSVRQ----NLVLHarlFHLPADGIPARVGEMLRRFDL---EKVADELPNDLPLGIRQR 413
Cdd:COG0444  82 KIRgrEIQMIFQdPMtSLNPVMTVGDqiaePLRIH---GGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVT-IFIsTHFMNE-AQRCDRISLMHAGKV 483
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAiLFI-THDLGVvAEIADRVAVMYAGRI 229
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
10-231 1.09e-28

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 115.13  E-value: 1.09e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGD------MrdrrHRRAvcp 83
Cdd:COG1137   5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF-LDGEdithlpM----HKRA--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  84 R--IAYMPQ------GLgknlyptlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:COG1137  77 RlgIGYLPQeasifrKL--------TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVA------------TAYMeeaerfdwlvaMDDGKVL 223
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE--RGIGVLITdhnvretlgicdRAYI-----------ISEGKVL 215

                ....*...
gi 15600424 224 ATGTPQEL 231
Cdd:COG1137 216 AEGTPEEI 223
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
262-498 1.34e-28

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 121.81  E-value: 1.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 262 PPRPQSEGAPRIAIEAEGLTcrF---GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV 338
Cdd:COG1132 327 PPGAVPLPPVRGEIEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 339 DASDMAT-RRRVGYMSQAFSLYAElSVRQNLvlhaRLFHLPADgiPARVGEMLRRFDLEKVADELPN--DLPLGI----- 410
Cdd:COG1132 405 RDLTLESlRRQIGVVPQDTFLFSG-TIRENI----RYGRPDAT--DEEVEEAAKAAQAHEFIEALPDgyDTVVGErgvnl 477
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 411 ----RQRLSLAVAVIHKPEILILDEPTSGVDPVA----RDGFWELMvelsrrDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:COG1132 478 sggqRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLM------KGRTTIVIAHRLSTIRNADRILVLDDGR 551
                       250
                ....*....|....*.
gi 15600424 483 VLASDTPDELVRQRGL 498
Cdd:COG1132 552 IVEQGTHEELLARGGL 567
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
22-483 1.43e-28

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 120.88  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQGLgkNLYPTLS 101
Cdd:PRK10762  18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQEL--NLIPQLT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  102 VFENVdFFGR----LFGHDKAERERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK10762  96 IAENI-FLGRefvnRFGRIDWKKMYAEADkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  177 LSRNQFWELIGRIRAgrEGMSVLVATAYMEEA-ERFDWLVAMDDGKVLAtgtpqelrERTGTQSLESAFIALLpeskrAG 255
Cdd:PRK10762 175 TETESLFRVIRELKS--QGRGIVYISHRLKEIfEICDDVTVFRDGQFIA--------EREVADLTEDSLIEMM-----VG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  256 hhrlvippRPQSEGAPRIAI-------EAEGLTcrfGDfvAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASE 328
Cdd:PRK10762 240 --------RKLEDQYPRLDKapgevrlKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  329 GTCALFGQPVDASDMATRRRVG--YMSQ---AFSLYAELSVRQNLVLHArLFHLPADGIPAR-------VGEMLRRFDLE 396
Cdd:PRK10762 307 GYVTLDGHEVVTRSPQDGLANGivYISEdrkRDGLVLGMSVKENMSLTA-LRYFSRAGGSLKhadeqqaVSDFIRLFNIK 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  397 KVA-DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDR 474
Cdd:PRK10762 386 TPSmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVlGMSDR 464

                 ....*....
gi 15600424  475 ISLMHAGKV 483
Cdd:PRK10762 465 ILVMHEGRI 473
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
275-496 1.47e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 116.10  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFV-AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---MATRRRVG 350
Cdd:PRK13636   6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLRESVG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YM-----SQAFSLyaelSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK13636  86 MVfqdpdNQLFSA----SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
11-231 1.94e-28

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 114.47  E-value: 1.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAvdDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAVcpriAYMP 89
Cdd:COG3840   4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAERPV----SMLF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGlgKNLYPTLSVFENVDFfG-----RLfghDKAERERrIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:COG3840  78 QE--NNLFPHLTVAQNIGL-GlrpglKL---TAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDEL-CRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAAL 217
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
19-462 1.96e-28

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 120.97  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   19 GETR-AVDDVSLEIPANRMVGLIGPDGVGKS----SLLALL-AGARKMQDGEIR-----VLDGDMRDRRHRRAvcPRIAY 87
Cdd:PRK15134  19 QTVRtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRfhgesLLHASEQTLRGVRG--NKIAM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQ----------GLGKNLYPTLSVFenvdffgRLFGHDKAERErrIADLLQSTGLAPFAERPAG---KLSGGMKQKLGL 154
Cdd:PRK15134  97 IFQepmvslnplhTLEKQLYEVLSLH-------RGMRREAARGE--ILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLatgtpqelr 232
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQ--QElNMGLLFITHNLSIVRKLaDRVAVMQNGRCV--------- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  233 ERTGTQSLESA----FIALLPESKRAGHhrlvipPRPQSEGAPRIaIEAEGLTCRF-----------GDFVAVDHVSFRI 297
Cdd:PRK15134 237 EQNRAATLFSApthpYTQKLLNSEPSGD------PVPLPEPASPL-LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  298 ERGEIFGFLGSNGCGKSTTMKMLTGLLpASEGTCALFGQPVDASD----MATRRRVGYMSQ--AFSLYAELSVRQ----N 367
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqlLPVRHRIQVVFQdpNSSLNPRLNVLQiieeG 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  368 LVLHARlfHLPADGIPARVGEMLRRFDLEKVA-DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:PRK15134 389 LRVHQP--TLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA 466
                        490
                 ....*....|....*..
gi 15600424  447 LMVELSRRDGVT-IFIS 462
Cdd:PRK15134 467 LLKSLQQKHQLAyLFIS 483
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
275-495 2.00e-28

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 115.09  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD--ASDMATRRRVGYM 352
Cdd:PRK11300   6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  353 SQAFSLYAELSVRQNLV----------LHARLFHLPA------DGIpARVGEMLRRFDLEKVADELPNDLPLGIRQRLSL 416
Cdd:PRK11300  86 FQHVRLFREMTVIENLLvaqhqqlktgLFSGLLKTPAfrraesEAL-DRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  417 AVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDElVRQ 495
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE-IRN 243
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
11-240 2.34e-28

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 114.42  E-value: 2.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP- 89
Cdd:PRK09493   4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QGLgkNLYPTLSVFENVdFFG--RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK09493  84 QQF--YLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  168 DEPTTGVDPLSRNqfwELIGRIRA-GREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSL 240
Cdd:PRK09493 161 DEPTSALDPELRH---EVLKVMQDlAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
275-491 4.34e-28

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: 113.58  E-value: 4.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVaVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMA-TRRRVGYMS 353
Cdd:cd03299   1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG--KDITNLPpEKRDISYVP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:cd03299  78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDE 491
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
8-437 7.02e-28

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: 119.27  E-value: 7.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     8 VASLRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIA 86
Cdd:TIGR03719   4 IYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG------------IKVG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    87 YMPQGlgKNLYPTLSVFENV--------DFFGRL------FG-----HDK-AERERRIADLLQSTGL------------- 133
Cdd:TIGR03719  72 YLPQE--PQLDPTKTVRENVeegvaeikDALDRFneisakYAepdadFDKlAAEQAELQEIIDAADAwdldsqleiamda 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   134 --APFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfWelIGRIRAGREGMSVLV---------AT 202
Cdd:TIGR03719 150 lrCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA--W--LERHLQEYPGTVVAVthdryfldnVA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   203 AYMEEAER----------FDWLVAMDdgKVLATGTPQEL-RERTGTQSLE-----------------SAFIALLPES--K 252
Cdd:TIGR03719 226 GWILELDRgrgipwegnySSWLEQKQ--KRLEQEEKEESaRQKTLKRELEwvrqspkgrqakskarlARYEELLSQEfqK 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   253 RAGHHRLVIPPrpqsegAPR---IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG 329
Cdd:TIGR03719 304 RNETAEIYIPP------GPRlgdKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   330 TCALfGQPVdasdmatrrRVGYMSQAfslyaelsvRQNLVLHARLFHLPADG----------IPAR--VGemlrRF---- 393
Cdd:TIGR03719 378 TIEI-GETV---------KLAYVDQS---------RDALDPNKTVWEEISGGldiiklgkreIPSRayVG----RFnfkg 434
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 15600424   394 -DLEKVADELPNdlplGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:TIGR03719 435 sDQQKKVGQLSG----GERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
11-202 1.18e-27

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: 111.73  E-value: 1.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRavcprIAYMP 89
Cdd:cd03292   3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA-----IPYLR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLG-----KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:cd03292  78 RKIGvvfqdFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVAT 202
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINK--AGTTVVVAT 193
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
275-503 1.51e-27

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 111.77  E-value: 1.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAvdHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQ 354
Cdd:COG3840   2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSMLFQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQN--LVLHARLfHLPADGIpARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG3840  79 ENNLFPHLTVAQNigLGLRPGL-KLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLEA 503
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
17-464 2.40e-27

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 117.04  E-value: 2.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLlallagARKMQdGEIRVLDGDMRDRRHRravCPRIAY------MPQ 90
Cdd:PRK10938  12 RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSAL------ARALA-GELPLLSGERQSQFSH---ITRLSFeqlqklVSD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GLGKNLYPTLSVFEnvDFFGR------LFGHDKAERERRIADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK10938  82 EWQRNNTDMLSPGE--DDTGRttaeiiQDEVKDPARCEQLAQQF---GITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMS-VLVATAYMEEAERFDWLVAMDDGKVLATGTPQELrertgtqsLESA 243
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQ--SGITlVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI--------LQQA 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  244 FIALLPESKRAGHHRLVIPPRPQ-----SEGAPRiaIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMK 318
Cdd:PRK10938 227 LVAQLAHSEQLEGVQLPEPDEPSarhalPANEPR--IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  319 MLTGLLPAS-EGTCALFGqpvdasdmatRRR------------VGYMSQAFSL-Y-AELSVRqNLVLHA-----RLFHLP 378
Cdd:PRK10938 305 LITGDHPQGySNDLTLFG----------RRRgsgetiwdikkhIGYVSSSLHLdYrVSTSVR-NVILSGffdsiGIYQAV 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  379 ADGIPARVGEMLRRFDLEK-VADELPNDLPLGiRQRLSLAV-AVIHKPEILILDEPTSGVDPVARD---GFWELMVelsr 453
Cdd:PRK10938 374 SDRQQKLAQQWLDILGIDKrTADAPFHSLSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLI---- 448
                        490
                 ....*....|...
gi 15600424  454 RDGVT--IFISTH 464
Cdd:PRK10938 449 SEGETqlLFVSHH 461
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
26-277 2.61e-27

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: 114.43  E-value: 2.61e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP---RIAYMPQGlgKNLYPTLSV 102
Cdd:COG4148  17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhrrRIGYVFQE--ARLFPHLSV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 103 FENVdffgrLFGHDKAERERR------IADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:COG4148  95 RGNL-----LYGRKRAPRAERrisfdeVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 177 LSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAFIA--LLpESKR 253
Cdd:COG4148 167 ARKAEILPYLERLRD-ELDIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAgsVL-EATV 244
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15600424 254 AGHH-------------RLVIPPRPQSEGAP-RIAIEA 277
Cdd:COG4148 245 AAHDpdygltrlalgggRLWVPRLDLPPGTRvRVRIRA 282
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
10-222 3.12e-27

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: 110.31  E-value: 3.12e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRavcprIAYMP 89
Cdd:cd03262   2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-DGLKLTDDKKN-----INELR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGK-----NLYPTLSVFENVDFFGR-LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03262  76 QKVGMvfqqfNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 164 LLILDEPTTGVDPlsrnqfwELIGRI-----RAGREGMSVLVATAYMEEA-ERFDWLVAMDDGKV 222
Cdd:cd03262 156 VMLFDEPTSALDP-------ELVGEVldvmkDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
12-231 3.63e-27

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 110.83  E-value: 3.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR-RHRRAvcpR--IAYM 88
Cdd:TIGR04406   5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpMHERA---RlgIGYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    89 PQGlgKNLYPTLSVFENV----DFFGRLfghDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:TIGR04406  82 PQE--ASIFRKLTVEENImavlEIRKDL---DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424   165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEE----AERfDWLVAmdDGKVLATGTPQEL 231
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDIKKIIKHLKE--RGIGVLITDHNVREtldiCDR-AYIIS--DGKVLAEGTPAEI 222
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
7-226 3.99e-27

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 110.37  E-value: 3.99e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   7 GVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG------DMRDRRHR 78
Cdd:cd03245   1 GRIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL-LDGtdirqlDPADLRRN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  79 ravcprIAYMPQGlgknlyPTL---SVFENVDFfGRLFGHDkaERERRIADLlqsTGLAPFAER-PAG----------KL 144
Cdd:cd03245  80 ------IGYVPQD------VTLfygTLRDNITL-GAPLADD--ERILRAAEL---AGVTDFVNKhPNGldlqigergrGL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 145 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFwelIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLA 224
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218

                ..
gi 15600424 225 TG 226
Cdd:cd03245 219 DG 220
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
12-230 4.42e-27

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 111.40  E-value: 4.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD-----RRHRRAVcpria 86
Cdd:PRK13548   6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaeLARRRAV----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   87 yMPQglgknlYPTLSvF----ENVDFFGRL-FGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI-- 159
Cdd:PRK13548  81 -LPQ------HSSLS-FpftvEEVVAMGRApHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  160 ----HDPDLLILDEPTTGVDPlsRNQFWEL-IGRIRAGREGMSVLV-------ATAYmeeAERfdwLVAMDDGKVLATGT 227
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDL--AHQHHVLrLARQLAHERGLAVIVvlhdlnlAARY---ADR---IVLLHQGRLVADGT 224

                 ...
gi 15600424  228 PQE 230
Cdd:PRK13548 225 PAE 227
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
11-226 4.63e-27

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 109.65  E-value: 4.63e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR--HRravcpRIAYM 88
Cdd:cd03301   3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkDR-----DIAMV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 PQGLGknLYPTLSVFENVDFFGRLFGHDKAE---RERRIADLLQSTGLapfAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03301  78 FQNYA--LYPHMTVYDNIAFGLKLRKVPKDEideRVREVAELLQIEHL---LDRKPKQLSGGQRQRVALGRAIVREPKVF 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQ-RLGTTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
275-495 5.97e-27

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 113.28  E-value: 5.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMaTRRRVGYMSQ 354
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI-QQRDICMVFQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK11432  86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQ 227
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
8-484 6.19e-27

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 117.26  E-value: 6.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRGVSLRYGETR----AVDDVSLEIPANRMVGLIGPDGVGKS----SLLALL--AGARKMQDGEI------RVLD-G 70
Cdd:PRK10261  12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLlrrrsrQVIElS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   71 DMRDRRHRRAVCPRIAYMPQGLGKNLYPTLSVFENVDFFGRL---FGHDKAERE-RRIADLLQSTGLAPFAERPAGKLSG 146
Cdd:PRK10261  92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLhqgASREEAMVEaKRMLDQVRIPEAQTILSRYPHQLSG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  147 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATAYMEE-AERFDWLVAMDDGKVLAT 225
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI-KVLQKEMSMGVIFITHDMGVvAEIADRVLVMYQGEAVET 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  226 GTPQELRERTG---TQSLESAfIALLPESKRAGHHR---LVIPPRPQS-----------EGAPriAIEAEGLTCRFG--- 285
Cdd:PRK10261 251 GSVEQIFHAPQhpyTRALLAA-VPQLGAMKGLDYPRrfpLISLEHPAKqeppieqdtvvDGEP--ILQVRNLVTRFPlrs 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  286 --------DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDM-ATRRRVGYMS 353
Cdd:PRK10261 328 gllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLqALRRDIQFIF 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  354 QafSLYAELSVRQNL---VLHARLFH--LPADGIPARVGEMLRRFDLE-KVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK10261 408 Q--DPYASLDPRQTVgdsIMEPLRVHglLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  428 ILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCD-RISLMHAGKVL 484
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIShRVAVMYLGQIV 543
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
289-481 7.11e-27

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 118.96  E-value: 7.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
                          170       180       190
                   ....*....|....*....|....*....|....
gi 15600424    449 VELSrRDGVTIFISTHFMNEAQR-CDRISLMHAG 481
Cdd:TIGR01257 2114 VSII-REGRAVVLTSHSMEECEAlCTRLAIMVKG 2146
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
11-234 1.25e-26

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: 109.35  E-value: 1.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRaVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG--------DMRDrrhrravc 82
Cdd:cd03299   3 VENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL-LNGkditnlppEKRD-------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  83 prIAYMPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03299  73 --ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRK-EFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKK 220
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
275-494 1.39e-26

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 114.88  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGYM 352
Cdd:PRK09700   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhkLAAQLGIGII 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  353 SQAFSLYAELSVRQNLVLhARLFHLPADGIP--------ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK09700  86 YQELSVIDELTVLENLYI-GRHLTKKVCGVNiidwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  425 EILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASD-----TPDELVR 494
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSNDDIVR 239
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
11-226 1.53e-26

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: 108.35  E-value: 1.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAvdDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGdmRDRRHRRAVCPRIAYMPQ 90
Cdd:cd03298   3 LDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-LING--VDVTAAPPADRPVSMLFQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  91 GlgKNLYPTLSVFENVDFfGRLFG-HDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03298  78 E--NNLFAHLTVEQNVGL-GLSPGlKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAER-FDWLVAMDDGKVLATG 226
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAET-KMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
273-493 2.03e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 109.70  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  273 IAIEAEGLTCRFGDFV--AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRV 349
Cdd:PRK13632   6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  350 GYMSQ---------------AFSLyaelsvrQNLvlharlfHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRL 414
Cdd:PRK13632  86 GIIFQnpdnqfigatveddiAFGL-------ENK-------KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  415 SLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFIS-THFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDL-RKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
267-502 2.22e-26

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 111.75  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  267 SEGApRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTtmkmltGLLPASEGTCALFGQPVD-----AS 341
Cdd:NF000106   7 SNGA-RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHV*GPDAGRRPWRf*twcAN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  342 DMATRRRVG-YMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAV 420
Cdd:NF000106  80 RRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  421 IHKPEILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELVRQRGLP 499
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGGR 238

                 ...
gi 15600424  500 TLE 502
Cdd:NF000106 239 TLQ 241
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
282-487 2.28e-26

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 108.00  E-value: 2.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 282 CRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATrrrvgymsqafSLYAE 361
Cdd:cd03220  30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----------GFNPE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 LSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVAdelpnDLPL-----GIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03220  99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-----DLPVktyssGMKARLAFAIATALEPDILLIDEVLAVG 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 437 DPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASD 487
Cdd:cd03220 174 DAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
275-483 2.40e-26

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 111.43  E-value: 2.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDM-ATR 346
Cdd:PRK11153   2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELrKAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  347 RRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK11153  82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
17-212 2.63e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.93  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrhrravcpRIAYMPQGLGKNL 96
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA------------RVAYVPQRSEVPD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   97 YPTLSVFENVD--FFGR--LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:NF040873  69 SLPLTVRDLVAmgRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15600424  173 GVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERFD 212
Cdd:NF040873 149 GLDAESRERIIALLAEEHA--RGATVVVVTHDLELVRRAD 186
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
277-493 4.60e-26

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 107.67  E-value: 4.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  277 AEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpVDASDMA-------TRRRV 349
Cdd:PRK10895   6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII-----IDDEDISllplharARRGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  350 GYMSQAFSLYAELSVRQNL--VLHARLfHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK10895  81 GYLPQEASIFRRLSVYDNLmaVLQIRD-DLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  428 ILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEIL 225
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
274-505 5.98e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 108.28  E-value: 5.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFV-AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRVGY 351
Cdd:PRK13647   4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 M-----SQAFSLyaelSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK13647  84 VfqdpdDQVFSS----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  427 LILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMN-EAQRCDRISLMHAGKVLASDTP-----DELVRQRGL-- 498
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKslltdEDIVEQAGLrl 238

                 ....*..
gi 15600424  499 PTLEATF 505
Cdd:PRK13647 239 PLVAQIF 245
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
11-208 6.03e-26

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 107.86  E-value: 6.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVcpriAYMPQ 90
Cdd:PRK11248   4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV----VFQNE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GLgknlYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:PRK11248  80 GL----LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15600424  171 TTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQ-ETGKQVLLITHDIEEA 192
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
283-502 9.44e-26

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: 109.82  E-value: 9.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   283 RFGDFvAVDhVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-----ATRRRVGYMSQAFS 357
Cdd:TIGR02142   8 RLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiflpPEKRRIGYVFQEAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   358 LYAELSVRQNLVlHARLFHLPADGI--PARVGEMLrrfDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:TIGR02142  86 LFPHLSVRGNLR-YGMKRARPSERRisFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424   436 VDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLE 502
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
11-496 1.71e-25

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 111.56  E-value: 1.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGA--RKMQDGEIRVLDGDMRDRRHRRAVCPRIAYM 88
Cdd:PRK13549   8 MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAGIAII 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   89 PQGLgkNLYPTLSVFENVdFFGRLFGH----DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK13549  88 HQEL--ALVKELSVLENI-FLGNEITPggimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  165 LILDEPTTgvdPLSRNQFWELIGRIRAGREGMsvlVATAYM-----EEAERFDWLVAMDDGKVLATGTPQELRE-RTGTQ 238
Cdd:PRK13549 165 LILDEPTA---SLTESETAVLLDIIRDLKAHG---IACIYIshklnEVKAISDTICVIRDGRHIGTRPAAGMTEdDIITM 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  239 SLESAFIALLPEskraghhrlvippRPQSEGapRIAIEAEGLTCRfgDFV-----AVDHVSFRIERGEIFGFLGSNGCGK 313
Cdd:PRK13549 239 MVGRELTALYPR-------------EPHTIG--EVILEVRNLTAW--DPVnphikRVDDVSFSLRRGEILGIAGLVGAGR 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  314 STTMKMLTGLLP-ASEGTCALFGQPVD--ASDMATRRRVGYMSQ---AFSLYAELSVRQNLVL-----HARLFHLPADGI 382
Cdd:PRK13549 302 TELVQCLFGAYPgRWEGEIFIDGKPVKirNPQQAIAQGIAMVPEdrkRDGIVPVMGVGKNITLaaldrFTGGSRIDDAAE 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  383 PARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFI 461
Cdd:PRK13549 382 LKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15600424  462 STHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:PRK13549 462 SSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
11-236 2.00e-25

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 112.18  E-value: 2.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG-DMRD------RRHrravc 82
Cdd:COG1132 342 FENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-DGvDIRDltleslRRQ----- 415
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  83 prIAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERErRIADLLQSTGLAPFAER-PAG----------KLSGGM 148
Cdd:COG1132 416 --IGVVPQD------TFLfsgTIRENI-----RYGRPDATDE-EVEEAAKAAQAHEFIEAlPDGydtvvgergvNLSGGQ 481
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 149 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegMSVLVA----TaymeeAERFDWLVAMDDGKVLA 224
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAhrlsT-----IRNADRILVLDDGRIVE 554
                       250
                ....*....|..
gi 15600424 225 TGTPQELRERTG 236
Cdd:COG1132 555 QGTHEELLARGG 566
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
274-484 2.00e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 106.46  E-value: 2.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGTCALFGQPVDASDM---AT 345
Cdd:PRK14267   4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVdpiEV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  346 RRRVGYMSQAFSLYAELSVRQNLVLHARLFHL--PADGIPARVGEMLRRFDL-EKVADEL---PNDLPLGIRQRLSLAVA 419
Cdd:PRK14267  84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARA 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  420 VIHKPEILILDEPTSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARvSDYVAFLYLGKLI 227
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
10-199 2.46e-25

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: 107.83  E-value: 2.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLAGARKMqDGEIRvLDG----DMRDRRH 77
Cdd:COG0444   3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKStlarAILGLLPPPGIT-SGEIL-FDGedllKLSEKEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  78 RRAVCPRIAYMPQGLGKNLYPTLSVFENVDFFGRLFGH-DKAERERRIADLLQSTGLaPFAERPAGK----LSGGMKQKL 152
Cdd:COG0444  81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGL-PDPERRLDRypheLSGGMRQRV 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVL 199
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQR-ELGLAIL 205
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
275-483 3.45e-25

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 104.74  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   275 IEAEGLTCRF--GDF--VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA---SDMATRR 347
Cdd:TIGR02211   2 LKCENLGKRYqeGKLdtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssNERAKLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   348 --RVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:TIGR02211  82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424   426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
23-237 4.04e-25

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 113.18  E-value: 4.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR----RHRRAVCPRiaympqglGKNLYP 98
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavRQSLGMCPQ--------HNILFH 1016
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     99 TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    179 RNQFWELIGRIRAGRegmSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGT 237
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGR---TIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNCFGT 1153
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
8-210 4.90e-25

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 105.12  E-value: 4.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-------ALLAGARkmQDGEIRVLDGDMRDRR---- 76
Cdd:COG1117  11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR--VEGEILLDGEDIYDPDvdvv 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  77 -HRRavcpRIAYMPQglgK-NLYPTlSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLapFAE------RPAGKLSGG 147
Cdd:COG1117  89 eLRR----RVGMVFQ---KpNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAAL--WDEvkdrlkKSALGLSGG 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 148 MKQKLglcC---ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAER 210
Cdd:COG1117 159 QQQRL---CiarALAVEPEVLLMDEPTSALDPISTAKIEELILEL---KKDYTIVIVTHNMQQAAR 218
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
288-493 6.89e-25

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 108.20  E-value: 6.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMAT-------RRRVGYMSQAFSLYA 360
Cdd:PRK10070  42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDaelrevrRKKIAMVFQSFALMP 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  361 ELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:PRK10070 120 HMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15600424  441 RDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELV 493
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
289-485 7.02e-25

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 103.82  E-value: 7.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03245  19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlRRNIGYVPQDVTLFYG-TLRDN 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVlharLFHLPADGipARVGEMLRRFDLEKVADELPNDLPL-----------GIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03245  98 IT----LGAPLADD--ERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTSAM 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15600424 437 DPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLA 485
Cdd:cd03245 172 DMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
10-231 8.29e-25

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 105.10  E-value: 8.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGET--RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRH----RRAVcp 83
Cdd:PRK13635   7 RVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEETvwdvRRQV-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   84 riaympqGLgknlyptlsVFENVD--FFGRLFGHDKA--------ERE---RRIADLLQSTGLAPFAERPAGKLSGGMKQ 150
Cdd:PRK13635  84 -------GM---------VFQNPDnqFVGATVQDDVAfglenigvPREemvERVDQALRQVGMEDFLNREPHRLSGGQKQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKE-QKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226

                 .
gi 15600424  231 L 231
Cdd:PRK13635 227 I 227
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
275-498 1.01e-24

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: 103.72  E-value: 1.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFG--DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpVDASDMAT------R 346
Cdd:cd03252   1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-----VDGHDLALadpawlR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAElSVRQNLVLharlfhlpADGIPA--RVGEMLRRFDLEKVADELPN-----------DLPLGIRQR 413
Cdd:cd03252  76 RQVGVVLQENVLFNR-SIRDNIAL--------ADPGMSmeRVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSrrDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224

                ....*
gi 15600424 494 RQRGL 498
Cdd:cd03252 225 AENGL 229
cbiO PRK13642
energy-coupling factor transporter ATPase;
275-492 1.08e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 104.79  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRF---GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVG 350
Cdd:PRK13642   5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlRRKIG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQ-AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:PRK13642  85 MVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
295-492 1.14e-24

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 103.39  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   295 FRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmatRRRVGYMSQ--AFSLYAELSVRQnLVLHA 372
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQrhEFAWDFPISVAH-TVMSG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   373 R-----LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:TIGR03771  76 RtghigWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 15600424   448 MVELSrRDGVTIFISTHFMNEA-QRCDRISLMHaGKVLASDTPDEL 492
Cdd:TIGR03771 156 FIELA-GAGTAILMTTHDLAQAmATCDRVVLLN-GRVIADGTPQQL 199
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
10-217 1.17e-24

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: 109.30  E-value: 1.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    10 SLRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAvcpRIA 86
Cdd:TIGR02857 323 EFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRD---QIA 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    87 YMPQglgknlYPTL---SVFENVdffgRLFGHDKAERErrIADLLQSTGLAPF-AERPAG----------KLSGGMKQKL 152
Cdd:TIGR02857 400 WVPQ------HPFLfagTIAENI----RLARPDASDAE--IREALERAGLDEFvAALPQGldtpigeggaGLSGGQAQRL 467
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424   153 GLCCALIHDPDLLILDEPTTGVDPLSRNqfwELIGRIRAGREGMSVLVATAYMEEAERFDWLVAM 217
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEA---EVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
289-497 1.19e-24

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 103.46  E-value: 1.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03254  18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIGVVLQDTFLFSG-TIMEN 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LvlhaRLFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03254  97 I----RLGRPNAT--DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 437 DPVA----RDGFWELMvelsrrDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:cd03254 171 DTETekliQEALEKLM------KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
8-222 1.44e-24

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: 101.74  E-value: 1.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   8 VASLRGVSLRygetRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAY 87
Cdd:cd03215   4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MP---QGLGknLYPTLSVFENVdFFGRLfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDL 164
Cdd:cd03215  80 VPedrKREG--LVLDLSVAENI-ALSSL-------------------------------LSGGNQQKVVLARWLARDPRV 125
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELAD--AGKAVLLISSELDELLGLcDRILVMYEGRI 182
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
16-226 1.45e-24

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 103.00  E-value: 1.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  16 LRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrdrrhRRAVCPRIaympqGLGKN 95
Cdd:cd03220  30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------RGRVSSLL-----GLGGG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  96 LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:cd03220  95 FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 176 PLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03220 175 AAFQEKCQRRLRELLKQ--GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
11-280 1.73e-24

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 103.60  E-value: 1.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcprIAYMPQ 90
Cdd:PRK11247  15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------TRLMFQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GlgKNLYPTLSVFENVDFfgRLFGHDKAERERriadLLQSTGLAPFA-ERPAGkLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK11247  89 D--ARLLPWKKVIDNVGL--GLKGQWRDAALQ----ALAAVGLADRAnEWPAA-LSGGQKQRVALARALIHRPGLLLLDE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  170 PTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAerfdwlVAMDDgKVlatgtpqelrertgtqslesafiaLLP 249
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESL-WQQHGFTVLLVTHDVSEA------VAMAD-RV------------------------LLI 207
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15600424  250 ESKRAGHHRLVIPPRPQSEGAPRIA-IEAEGL 280
Cdd:PRK11247 208 EEGKIGLDLTVDLPRPRRRGSARLAeLEAEVL 239
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
21-234 1.95e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 104.05  E-value: 1.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLdGDMRDRRHRRAVCPRIAYMPQGLGKNLYpTL 100
Cdd:PRK13647  18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GREVNAENEKWVRSKVGLVFQDPDDQVF-SS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  101 SVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRN 180
Cdd:PRK13647  96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  181 QFWELIGRIRagREGMSVLVATAYME-EAERFDWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK13647 176 TLMEILDRLH--NQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
275-505 2.09e-24

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 106.85  E-value: 2.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMS 353
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAaSRRVASVP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  354 QAFSLYAELSVRQnLVLHARLFHL-------PADgiPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK09536  84 QDTSLSFEFDVRQ-VVEMGRTPHRsrfdtwtETD--RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  427 LILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglPTLEATF 505
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA---DTLRAAF 236
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
275-498 2.33e-24

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 103.17  E-value: 2.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMS 353
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  354 QAFSLYAELSVRQnLVLHARLFHLP-----ADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK11231  83 QHHLTPEGITVRE-LVAYGRSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGLL 231
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
8-234 2.61e-24

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 105.80  E-value: 2.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRD----RRHRRAVC 82
Cdd:PRK09452  14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDGqDITHvpaeNRHVNTVF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   83 PRIAympqglgknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK09452  93 QSYA---------LFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  163 DLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQ--RKlGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGTPREIYEE 235
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
280-501 2.66e-24

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: 105.57  E-value: 2.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 280 LTCRFGDFvAVDhVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQP-VDAS---DMAT-RRRVGYMSQ 354
Cdd:COG4148   7 FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSArgiFLPPhRRRIGYVFQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLvLHARlfhlpadgipARVGEMLRRFDLEKVADEL---------PNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG4148  85 EARLFPHLSVRGNL-LYGR----------KRAPRAERRISFDEVVELLgighlldrrPATLSGGERQRVAIGRALLSSPR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 ILILDEPTSGVDPVARDgfwELMVELSR-RD--GVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTL 501
Cdd:COG4148 154 LLLMDEPLAALDLARKA---EILPYLERlRDelDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
274-469 3.16e-24

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 103.02  E-value: 3.16e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFV----AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmATRrrv 349
Cdd:COG4525   3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-ADR--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:COG4525  79 GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA 469
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
262-478 3.60e-24

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: 107.76  E-value: 3.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   262 PPRPQSEGAPRIAIEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA 340
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   341 SDMAT-RRRVGYMSQAFSLYAElSVRQNlVLHARlfhlpADGIPARVGEMLRRFDLekvaDELPNDLPLGI--------- 410
Cdd:TIGR02857 389 ADADSwRDQIAWVPQHPFLFAG-TIAEN-IRLAR-----PDASDAEIREALERAGL----DEFVAALPQGLdtpigegga 457
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424   411 ------RQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLM 478
Cdd:TIGR02857 458 glsggqAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
275-498 3.97e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 103.34  E-value: 3.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYM 352
Cdd:PRK13652   4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  353 -----SQAFSLyaelSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK13652  84 fqnpdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  428 ILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
283-478 6.50e-24

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 100.00  E-value: 6.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpvdasdMATRRRVGYMSQAFSLYAEL 362
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR----------RAGGARVAYVPQRSEVPDSL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  363 --SVRQNLVL----HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:NF040873  71 plTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15600424  437 DPVARDGFWELMVELsRRDGVTIFISTHFMNEAQRCDRISLM 478
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
10-231 7.37e-24

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 101.70  E-value: 7.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRIAYMP 89
Cdd:COG4604   3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP-SRELAKRLAILR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGKNLypTLSVFENVdFFGRlFGHDK----AERERRIADLLQSTGLAPFAERPAGKLSGGMKQKlglccALI-----H 160
Cdd:COG4604  82 QENHINS--RLTVRELV-AFGR-FPYSKgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQR-----AFIamvlaQ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 161 DPDLLILDEPTTGVDPL-SRnqfwELIGRIR-AGRE-GMSVLV-------ATAYMeeaerfDWLVAMDDGKVLATGTPQE 230
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKhSV----QMMKLLRrLADElGKTVVIvlhdinfASCYA------DHIVAMKDGRVVAQGTPEE 222

                .
gi 15600424 231 L 231
Cdd:COG4604 223 I 223
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
289-492 7.94e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 102.14  E-value: 7.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRVGYMSQ-AFSLYAELSVRQ 366
Cdd:PRK13648  24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVFQnPDNQFVGSIVKY 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  367 NLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15600424  447 LMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
11-231 1.11e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 101.14  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ-----DGEIrVLDG------DMRDRRHRR 79
Cdd:PRK14247   6 IRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEV-YLDGqdifkmDVIELRRRV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   80 AVCPRIAympqglgkNLYPTLSVFENVDFFGRL--FGHDKAERERRIADLLQSTGL-APFAER---PAGKLSGGMKQKLG 153
Cdd:PRK14247  85 QMVFQIP--------NPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLC 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLEL---KKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
20-231 1.18e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 101.70  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQGLGKNLYPT 99
Cdd:PRK13633  22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVAT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  100 LsVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR 179
Cdd:PRK13633 102 I-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600424  180 NQFWELIGRIRaGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13633 181 REVVNTIKELN-KKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
12-236 1.41e-23

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 100.38  E-value: 1.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  12 RGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRDRRhRRAVCPRIAYMP 89
Cdd:cd03254   6 ENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGiDIRDIS-RKSLRSMIGVVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGknLYPTlSVFENVDFfgrlfGHDKAERERrIADLLQSTGLAPFAER----------PAGK-LSGGMKQKLGLCCAL 158
Cdd:cd03254  84 QDTF--LFSG-TIMENIRL-----GRPNATDEE-VIEAAKEAGAHDFIMKlpngydtvlgENGGnLSQGERQLLAIARAM 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGR---TSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
293-488 1.57e-23

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 100.28  E-value: 1.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATR-----RRVGYMSQAFSLYAELSVRQN 367
Cdd:PRK11629  28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALEN 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  368 LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15600424  448 MVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDT 488
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
10-202 2.12e-23

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: 98.58  E-value: 2.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM---RDRRHRRavcprIA 86
Cdd:TIGR01189   2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHEN-----IL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    87 YMpqGLGKNLYPTLSVFENVDFFGRLFGHDkaerERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:TIGR01189  77 YL--GHLPGLKPELSALENLHFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 15600424   167 LDEPTTGVDPLSRNQFWELIgRIRAGREGMsVLVAT 202
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLL-RAHLARGGI-VLLTT 184
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
10-244 2.31e-23

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 103.77  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK09536   5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV-AGDDVEALSARAASRRVASVP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QglGKNLYPTLSVFENVDF-----FGRLFGHDKAEReRRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK09536  84 Q--DTSLSFEFDVRQVVEMgrtphRSRFDTWTETDR-AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  165 LILDEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELrerTGTQSLESA 243
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRL--VDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADV---LTADTLRAA 235

                 .
gi 15600424  244 F 244
Cdd:PRK09536 236 F 236
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
13-231 3.00e-23

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 102.47  E-value: 3.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   13 GVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-----RDRrhrravcpRIAY 87
Cdd:PRK10851   7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlhaRDR--------KVGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQGLGknLYPTLSVFENVDF----FGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK10851  79 VFQHYA--LFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  164 LLILDEPTTGVDPLSRNqfwELIGRIRAGREGM---SVLVaTAYMEEA-ERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10851 157 ILLLDEPFGALDAQVRK---ELRRWLRQLHEELkftSVFV-THDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
cbiO PRK13637
energy-coupling factor transporter ATPase;
20-230 3.49e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 100.51  E-value: 3.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHR-RAVCPRIAYMPQglgknlYP 98
Cdd:PRK13637  19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQ------YP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   99 TLSVFE-----NVDFFGRLFGHDKAERERRIADLLQSTGLA--PFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK13637  93 EYQLFEetiekDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  172 TGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE 230
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHK-EYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
275-464 3.96e-23

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 98.41  E-value: 3.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATrrRVGYMSQ 354
Cdd:PRK13539   3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--ACHYLGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  355 AFSLYAELSVRQNLVLHARLFhlpaDGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA-VAVIHKPeILILDEPT 433
Cdd:PRK13539  81 RNAMKPALTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALArLLVSNRP-IWILDEPT 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15600424  434 SGVDPVARDGFWELMVELSRRDGvTIFISTH 464
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGG-IVIAATH 185
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
11-230 4.33e-23

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 99.39  E-value: 4.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdmrdrrhrravcpRIAyMPQ 90
Cdd:COG1134  29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NG-------------RVS-ALL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  91 GLGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:COG1134  94 ELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 171 TTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE 230
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELR--ESGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
10-231 7.64e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 101.26  E-value: 7.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDrrhrraVCPriayMP 89
Cdd:PRK11000   5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND------VPP----AE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QGLGK-----NLYPTLSVFENVDFFGRLFGHDKAERERRI---ADLLQstgLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK11000  75 RGVGMvfqsyALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHK-RLGRTMIYVTHDQVEAMTLaDKIVVLDAGRVAQVGKPLEL 221
cbiO PRK13643
energy-coupling factor transporter ATPase;
21-231 7.90e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 99.81  E-value: 7.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP---RIAYMPQGLGKNLY 97
Cdd:PRK13643  19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkKVGVVFQFPESQLF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   98 PTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK13643  99 EE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  177 LSRNQFWELIGRIRagREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13643 178 KARIEMMQLFESIH--QSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDV 231
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
265-471 9.52e-23

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 98.70  E-value: 9.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  265 PQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMK---MLTGLLPA--SEGTCALFGQPVD 339
Cdd:PRK14243   1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  340 ASDM---ATRRRVGYMSQAFSLYAElSVRQNLVLHARLFHLPADgIPARVGEMLRRFDL-EKVADEL-PNDLPL--GIRQ 412
Cdd:PRK14243  81 APDVdpvEVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGD-MDELVERSLRQAALwDEVKDKLkQSGLSLsgGQQQ 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  413 RLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQR 471
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
272-483 1.01e-22

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: 96.35  E-value: 1.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 272 RIAIEAEGLTCRfgdfVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRV 349
Cdd:cd03215   2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprDAIRAGI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMS---QAFSLYAELSVRQNLVLHARLfhlpaDGiparvgemlrrfdlekvadelpndlplGIRQRLSLAVAVIHKPEI 426
Cdd:cd03215  78 AYVPedrKREGLVLDLSVAENIALSSLL-----SG---------------------------GNQQKVVLARWLARDPRV 125
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHfMNEAQR-CDRISLMHAGKV 483
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE-LDELLGlCDRILVMYEGRI 182
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
290-489 1.37e-22

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: 97.54  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmATRRRVGYmsQAFSLYAELSVRQNLV 369
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP--GPDRMVVF--QNYSLLPWLTVRENIA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   370 L--HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:TIGR01184  77 LavDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15600424   448 MVELSRRDGVTIFISTHFMNEAQ-RCDRISLM------HAGKVLASDTP 489
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLtngpaaNIGQILEVPFP 205
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
10-236 1.80e-22

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: 97.30  E-value: 1.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHrrav 81
Cdd:cd03251   2 EFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytlaslRRQ---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  82 cprIAYMPQGLgkNLYPTlSVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAER-PAG----------KLSGGMKQ 150
Cdd:cd03251  78 ---IGLVSQDV--FLFND-TVAENI-----AYGRPGATREE-VEEAARAANAHEFIMElPEGydtvigergvKLSGGQRQ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR---TTFVIAHRLSTIENADRIVVLEDGKIVERGTHEE 222

                ....*.
gi 15600424 231 LRERTG 236
Cdd:cd03251 223 LLAQGG 228
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
293-484 1.96e-22

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: 96.96  E-value: 1.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLP---ASEGTCALFGQPVDASDMatRRRVGYMSQAFSLYAELSVRQNL- 368
Cdd:cd03234  26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQF--QKCVAYVRQDDILLPGLTVRETLt 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 -VLHARLFHLPADGIPARVGE--MLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW 445
Cdd:cd03234 104 yTAILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15600424 446 ELMVELSRRdGVTIFISTH------FmneaQRCDRISLMHAGKVL 484
Cdd:cd03234 184 STLSQLARR-NRIVILTIHqprsdlF----RLFDRILLLSSGEIV 223
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
10-250 2.00e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 98.14  E-value: 2.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYG--ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHrravcprIAY 87
Cdd:PRK13632   9 KVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK-IDGITISKEN-------LKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQGLGknlyptlSVFENVD--FFGRL------FG-----HDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGL 154
Cdd:PRK13632  81 IRKKIG-------IIFQNPDnqFIGATveddiaFGlenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREgMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL--- 231
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRK-KTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIlnn 232
                        250
                 ....*....|....*....
gi 15600424  232 RERTGTQSLESAFIALLPE 250
Cdd:PRK13632 233 KEILEKAKIDSPFIYKLSK 251
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
289-483 2.04e-22

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 99.42  E-value: 2.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDM-ATRRRVGYMSQafSLYAELSV 364
Cdd:COG4608  33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELrPLRRRMQMVFQ--DPYASLNP 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 365 RQN--------LVLHaRLfhLPADGIPARVGEMLRRFDLEK-VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:COG4608 111 RMTvgdiiaepLRIH-GL--ASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 436 VDPVARDGFWELMVELSRRDGVT-IFIS------THFmneaqrCDRISLMHAGKV 483
Cdd:COG4608 188 LDVSIQAQVLNLLEDLQDELGLTyLFIShdlsvvRHI------SDRVAVMYLGKI 236
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
12-202 2.08e-22

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 96.10  E-value: 2.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcPRIAYmpqg 91
Cdd:PRK13539   6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA----EACHY---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   92 LG-KN-LYPTLSVFENVDFFGRLFGhdkaERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK13539  78 LGhRNaMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15600424  170 PTTGVDPLSRNQFWELIgRIRAGREGMsVLVAT 202
Cdd:PRK13539 154 PTAALDAAAVALFAELI-RAHLAQGGI-VIAAT 184
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
289-505 2.53e-22

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 97.55  E-value: 2.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIE-------------RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMSQ 354
Cdd:PRK10575  13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  355 AFSLYAELSVRQnLVLHARlfhLPADGIPARVGEMLRR--------FDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK10575  93 QLPAAEGMTVRE-LVAIGR---YPWHGALGRFGAADREkveeaislVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglPTLEATF 505
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRG---ETLEQIY 245
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
289-505 2.58e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 98.17  E-value: 2.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-----RRRVGYM-----SQAFsl 358
Cdd:PRK13634  22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplRKKVGIVfqfpeHQLF-- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  359 yaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK13634 100 --EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  438 PVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR--------QRGLPT-------L 501
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAdpdeleaiGLDLPEtvkfkraL 257

                 ....
gi 15600424  502 EATF 505
Cdd:PRK13634 258 EEKF 261
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
10-232 2.66e-22

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 97.37  E-value: 2.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGdmrdrrHRRAVCP--RIAY 87
Cdd:PRK11300   7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL-LRG------QHIEGLPghQIAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MpqGLGKN-----LYPTLSVFENV----------DFFGRLF---GHDKAERE--RRIADLLQSTGLAPFAERPAGKLSGG 147
Cdd:PRK11300  80 M--GVVRTfqhvrLFREMTVIENLlvaqhqqlktGLFSGLLktpAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  148 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLV----ATAYMEEAERfdwLVAMDDGKV 222
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELR--NEhNVTVLLiehdMKLVMGISDR---IYVVNQGTP 232
                        250
                 ....*....|
gi 15600424  223 LATGTPQELR 232
Cdd:PRK11300 233 LANGTPEEIR 242
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
10-225 3.25e-22

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: 94.03  E-value: 3.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRhrravCPRIAymp 89
Cdd:cd03216   2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGKEVSFA-----SPRDA--- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 qglgknlyptlsvfenvdffgrlfghdkaeRERRIADLLQstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03216  73 ------------------------------RRAGIAMVYQ--------------LSVGERQMVEIARALARNARLLILDE 108
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLAT 225
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRA--QGVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
21-231 3.40e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 97.46  E-value: 3.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDmrdrrhrravcpRIAYMPQGLGKNLYPTL 100
Cdd:PRK13639  15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGE------------PIKYDKKSLLEVRKTVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  101 SVFENVD------------FFGRL-FGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK13639  82 IVFQNPDdqlfaptveedvAFGPLnLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  168 DEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDL--NKEGITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
273-495 3.94e-22

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 99.00  E-value: 3.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  273 IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMATR-RRVGY 351
Cdd:PRK10851   1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARdRKVGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 MSQAFSLYAELSVRQNLVLHARLfhLP------ADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK10851  79 VFQHYALFRHMTVFDNIAFGLTV--LPrrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWRE 227
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
275-486 3.97e-22

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: 101.05  E-value: 3.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMATRRRVG-- 350
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGiv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   351 YMSQAFSLYAELSVRQNLVLHARLFH----LPADGIPARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIHKPE 425
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424   426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFIStHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAvCDTICVIRDGQHVAT 222
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
10-226 4.97e-22

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 96.10  E-value: 4.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK11614   7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QglGKNLYPTLSVFENVDFFGrlFGHDKAERERRIADLLqstGLAP-FAERP---AGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK11614  87 E--GRRVFSRMTVEENLAMGG--FFAERDQFQERIKWVY---ELFPrLHERRiqrAGTMSGGEQQMLAIGRALMSQPRLL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  166 ILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAerfdwLVAMDDGKVLATG 226
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLRE--QGMTIFLVEQNANQA-----LKLADRGYVLENG 213
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
11-235 5.01e-22

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 96.76  E-value: 5.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGD---MRDRRHRRAVCPRIAY 87
Cdd:PRK11831  10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGEnipAMSRSRLYTVRKRMSM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQglGKNLYPTLSVFENVDFFGRlfghdkaERERRIADLLQST--------GLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:PRK11831  89 LFQ--SGALFTDMNVFDNVAYPLR-------EHTQLPAPLLHSTvmmkleavGLRGAAKLMPSELSGGMARRAALARAIA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  160 HDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERT 235
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
275-493 5.09e-22

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 95.93  E-value: 5.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDMATRRRVGY 351
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 MSQAFSLYAELSVRQNLV---LHARLFHLPADGIPARvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK09493  82 VFQQFYLFPHLTALENVMfgpLRVRGASKEEAEKQAR--ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELV 493
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
253-495 5.18e-22

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: 101.36  E-value: 5.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 253 RAGHHRL-----VIPPRPQSEG--APRIAIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGL 323
Cdd:COG4618 302 RQAYRRLnellaAVPAEPERMPlpRPKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV 381
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 324 LPASEGTCALFGQPVDASDMATR-RRVGYMSQAFSLYAElSVRQNLvlhARLfhlpADGIPARVGEMLRRFDLEKVADEL 402
Cdd:COG4618 382 WPPTAGSVRLDGADLSQWDREELgRHIGYLPQDVELFDG-TIAENI---ARF----GDADPEKVVAAAKLAGVHEMILRL 453
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 403 PN--DLPLGI---------RQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR 471
Cdd:COG4618 454 PDgyDTRIGEggarlsggqRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA 532
                       250       260
                ....*....|....*....|....
gi 15600424 472 CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDEVLAR 556
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
23-245 5.21e-22

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 99.14  E-value: 5.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGdmRDRRHRRAVCPRIAYMPQGLGknLYPTLSV 102
Cdd:PRK11607  34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDG--VDLSHVPPYQRPINMMFQSYA--LFPHMTV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQF 182
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  183 -WELIGRIRagREGMSVLVATAYMEEAERFDWLVA-MDDGKVLATGTPQELRERTGTQsLESAFI 245
Cdd:PRK11607 189 qLEVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAiMNRGKFVQIGEPEEIYEHPTTR-YSAEFI 250
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
292-485 5.57e-22

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: 95.25  E-value: 5.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELSVRQN--LV 369
Cdd:cd03298  16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQENNLFAHLTVEQNvgLG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 LHARLFHLPADgiPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:cd03298  95 LSPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15600424 450 ELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLA 485
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAA 209
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
3-231 6.05e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 96.74  E-value: 6.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    3 AGGSGVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-----RVLDGDMRDR 75
Cdd:PRK13648   2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   76 RHRRAVcpriaympqglgknlyptlsVFENVD--FFGRLFGHDKA-----------ERERRIADLLQSTGLAPFAERPAG 142
Cdd:PRK13648  82 RKHIGI--------------------VFQNPDnqFVGSIVKYDVAfglenhavpydEMHRRVSEALKQVDMLERADYEPN 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  143 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREgMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHN-ITIISITHDLSEAMEADHVIVMNKGTV 220

                 ....*....
gi 15600424  223 LATGTPQEL 231
Cdd:PRK13648 221 YKEGTPTEI 229
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
274-484 6.42e-22

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 95.85  E-value: 6.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL------FGQPVDASDMAT-R 346
Cdd:PRK11124   2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAIRElR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  347 RRVGYMSQAFSLYAELSVRQNLVlHA--RLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK11124  82 RNVGMVFQQYNLWPHLTVQQNLI-EApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  425 EILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
10-230 1.11e-21

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 94.09  E-value: 1.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ---DGEIRvLDGDMRDRR--HRRavcpR 84
Cdd:COG4136   3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVL-LNGRRLTALpaEQR----R 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  85 IAYMPQ-GLgknLYPTLSVFENVdffgrLFG----HDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:COG4136  78 IGILFQdDL---LFPHLSVGENL-----AFAlpptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 160 HDPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATAYMEEAErfdwlvamDDGKVLATGTPQE 230
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFV-FEQIRQRGIPALLVTHDEEDAP--------AAGRVLDLGNWQH 211
cbiO PRK13650
energy-coupling factor transporter ATPase;
290-492 1.15e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 95.95  E-value: 1.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYMSQ-AFSLYAELSVRQN 367
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQnPDNQFVGATVEDD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  368 LVlharlFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARD 442
Cdd:PRK13650 103 VA-----FGLENKGIPheemkERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15600424  443 GFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
cbiO PRK13640
energy-coupling factor transporter ATPase;
289-492 1.19e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 96.02  E-value: 1.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGTCALFGQPVDASDM-ATRRRVGYMSQ-AFSLYAELS 363
Cdd:PRK13640  22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIREKVGIVFQnPDNQFVGAT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLVlharlFHLPADGIPAR-----VGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK13640 102 VGDDVA-----FGLENRAVPRPemikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15600424  439 VARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
23-250 1.26e-21

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 101.63  E-value: 1.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV----LDGDMRDRRHRRAVCPRIAYMPQglgknlyp 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagksILTNISDVHQNMGYCPQFDAIDD-------- 2025
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     99 TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:TIGR01257 2026 LLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424    179 RNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTG-----TQSLESAFIALLPE 250
Cdd:TIGR01257 2106 RRMLWNTIVSII--REGRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSKFGdgyivTMKIKSPKDDLLPD 2181
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
293-474 1.27e-21

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 94.46  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATR-----RRVGYMSQAFSLYAELSVRQN 367
Cdd:PRK10584  29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALEN 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  368 LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
                        170       180
                 ....*....|....*....|....*..
gi 15600424  448 MVELSRRDGVTIFISTHFMNEAQRCDR 474
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAARCDR 215
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
20-231 1.51e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 95.86  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDMRDRRHRRAvcpriaympqglgKNL--- 96
Cdd:PRK13634  19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITAGKKN-------------KKLkpl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   97 ---------YPTLSVFENV---DF-FGRL-FGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK13634  84 rkkvgivfqFPEHQLFEETvekDIcFGPMnFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAME 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHK-EKGLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
10-226 1.52e-21

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: 92.76  E-value: 1.52e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGE--TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGdmrdrrhrravcpriaY 87
Cdd:cd03247   2 SINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDG----------------V 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLGKNLYPTLSVFENVDFfgrLFGhdkaererriADLLQSTGLapfaerpagKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03247  65 PVSDLEKALSSLISVLNQRPY---LFD----------TTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLL 122
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAERFDWLVAMDDGKVLATG 226
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEV---LKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
275-483 1.68e-21

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: 92.66  E-value: 1.68e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVA--VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGY 351
Cdd:cd03246   1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHVGY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAElSVRQNLvlharlfhlpadgiparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDE 431
Cdd:cd03246  81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600424 432 PTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
275-484 1.70e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 94.98  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL-----PASEGTCALFGQPVDASDMAT-RRR 348
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIElRRR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  349 VGYMSQAFSLYAELSVRQNLVLHARLFHLPADG--IPARVGEMLRRFDL-EKVADEL---PNDLPLGIRQRLSLAVAVIH 422
Cdd:PRK14247  84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkeLQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAF 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  423 KPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQRC-DRISLMHAGKVL 484
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIV 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
293-484 2.12e-21

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: 93.00  E-value: 2.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGTCALFGQPVDASDMatRRRVGYMSQAFSLYAELSVRQNLVL 370
Cdd:cd03213  28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTLTVRETLMF 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 371 HARLfhlpaDGIPArvGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTSGVDPV-ARDgfweLMV 449
Cdd:cd03213 106 AAKL-----RGLSG--GE----------------------RKRVSIALELVSNPSLLFLDEPTSGLDSSsALQ----VMS 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15600424 450 ELSR--RDGVTIFISTH------FmneaQRCDRISLMHAGKVL 484
Cdd:cd03213 153 LLRRlaDTGRTIICSIHqpsseiF----ELFDKLLLLSQGRVI 191
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
283-482 2.14e-21

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 93.63  E-value: 2.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMSQAFSLYAE 361
Cdd:PRK10247  16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  362 lSVRQNLVLHARLFHLPADgiPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:PRK10247  96 -TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15600424  441 RDGFWELMVELSRRDGVTIFISTHFMNEAQRCDR-ISLM-HAGK 482
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKvITLQpHAGE 216
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
10-231 2.23e-21

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 94.85  E-value: 2.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK10575  13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSSKAFARKVAYLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QGLgknlyPT---LSVFENVDFfGRL-----FGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK10575  92 QQL-----PAaegMTVRELVAI-GRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQER-GLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL 235
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
6-231 2.98e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 94.91  E-value: 2.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    6 SGVASLRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPR 84
Cdd:PRK13636   3 DYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMKLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   85 --IAYMPQGLGKNLYpTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK13636  82 esVGMVFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  163 DLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
cbiO PRK13641
energy-coupling factor transporter ATPase;
270-492 3.68e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 94.90  E-value: 3.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  270 APRIAIEAEGLtcrfgdfvavDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD-----MA 344
Cdd:PRK13641  13 SPGTPMEKKGL----------DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  345 TRRRVGYMSQafslYAELSVRQNLVLH-----ARLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAV 418
Cdd:PRK13641  83 LRKKVSLVFQ----FPEAQLFENTVLKdvefgPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAG 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
11-227 4.05e-21

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 95.64  E-value: 4.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdmRD---------RRH 77
Cdd:PRK11153   4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV-DG--QDltalsekelRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   78 RRavcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAER-PAgKLSGGMKQKLGLCC 156
Cdd:PRK11153  81 RR----QIGMIFQHF--NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRyPA-QLSGGQKQRVAIAR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATGT 227
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDIN--RElGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
8-437 6.26e-21

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 97.88  E-value: 6.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIA 86
Cdd:PRK11819   6 IYTMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG------------IKVG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   87 YMPQGlgKNLYPTLSVFENV--------DFFGRL------FGHDKA------ERERRIADLLQSTGLA------------ 134
Cdd:PRK11819  74 YLPQE--PQLDPEKTVRENVeegvaevkAALDRFneiyaaYAEPDAdfdalaAEQGELQEIIDAADAWdldsqleiamda 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  135 ---PFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfW-EligRIRAGREGMSVLV---------A 201
Cdd:PRK11819 152 lrcPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA--WlE---QFLHDYPGTVVAVthdryfldnV 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  202 TAYMEEAER----------FDWLVAMDdgKVLATGTPQEL-RERTGTQSLE-----------------SAFIALLPES-- 251
Cdd:PRK11819 227 AGWILELDRgrgipwegnySSWLEQKA--KRLAQEEKQEAaRQKALKRELEwvrqspkarqakskarlARYEELLSEEyq 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  252 KRAGHHRLVIPPrpqsegAPR---IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASE 328
Cdd:PRK11819 305 KRNETNEIFIPP------GPRlgdKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDS 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  329 GTCALfGQPVdasdmatrrRVGYMSQAfslyaelsvRQNLVLHARLFHLPADG----------IPAR--VGemlrRF--- 393
Cdd:PRK11819 379 GTIKI-GETV---------KLAYVDQS---------RDALDPNKTVWEEISGGldiikvgnreIPSRayVG----RFnfk 435
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15600424  394 --DLEKVADELPNdlplGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK11819 436 ggDQQKKVGVLSG----GERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
10-222 6.36e-21

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: 90.74  E-value: 6.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRA--VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCPRIAY 87
Cdd:cd03246   2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-LDGADISQWDPNELGDHVGY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLgkNLYPTlSVFENVdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03246  81 LPQDD--ELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAA--GATRIVIAHRPETLASADRILVLEDGRV 173
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
8-171 6.51e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 97.44  E-value: 6.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvldgdmrdRRHRRAvcpRIAY 87
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---------KLGETV---KIGY 382
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLgKNLYPTLSVFENVdffgRLFGHDKAERERRiaDLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:COG0488 383 FDQHQ-EELDPDKTVLDEL----RDGAPGGTEQEVR--GYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455

                ....*
gi 15600424 167 LDEPT 171
Cdd:COG0488 456 LDEPT 460
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
275-474 8.89e-21

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: 91.40  E-value: 8.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03231   1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLvlhaRLFHlpADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03231  81 APGIKTTLSVLENL----RFWH--ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDR 474
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAR 194
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
8-231 1.01e-20

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 93.13  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRG--VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRI 85
Cdd:PRK10253   5 VARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARRI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   86 AYMPQGLGKnlyPTLSVFENVDFFGR-----LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:PRK10253  84 GLLAQNATT---PGDITVQELVARGRyphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  161 DPDLLILDEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAY-MEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSEL--NREKGYTLAAVLHdLNQACRYaSHLIALREGKIVAQGAPKEI 231
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
286-486 1.01e-20

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: 90.45  E-value: 1.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAElSVR 365
Cdd:cd03247  14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 QNLvlharlfhlpadGIPARVGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW 445
Cdd:cd03247  93 NNL------------GRRFSGGE----------------------RQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15600424 446 ELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLAS 486
Cdd:cd03247 139 SLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
cbiO PRK13646
energy-coupling factor transporter ATPase;
286-495 1.05e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 93.31  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-----DASDMATRRRVGYM-----SQA 355
Cdd:PRK13646  19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKRIGMVfqfpeSQL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  356 FslyaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEK-VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK13646  99 F----EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKD 236
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
288-498 1.25e-20

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 92.30  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  288 VAVDH----VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGTCALFGQPV---DASDMATRRrvGYMSQAFSLYA 360
Cdd:PRK03695   6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeawSAAELARHR--AYLSQQQTPPF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  361 ELSVRQNLVLHaRLFHLPADGIPARVGEMLRRFDLEkvaDELP---NDLPLGIRQRLSLAVAV--IHkPEI------LIL 429
Cdd:PRK03695  83 AMPVFQYLTLH-QPDKTRTEAVASALNEVAEALGLD---DKLGrsvNQLSGGEWQRVRLAAVVlqVW-PDInpagqlLLL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  430 DEPTSGVDpVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK03695 158 DEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
cbiO PRK13640
energy-coupling factor transporter ATPase;
10-235 1.41e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 92.94  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---------ARKMQDGeIRVLDGDMRDRRHR 78
Cdd:PRK13640   7 EFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpnSKITVDG-ITLTAKTVWDIREK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   79 RAVcpriaympqglgknlyptlsVFENVD--FFGRLFGHDKA-----------ERERRIADLLQSTGLAPFAERPAGKLS 145
Cdd:PRK13640  86 VGI--------------------VFQNPDnqFVGATVGDDVAfglenravprpEMIKIVRDVLADVGMLDYIDSEPANLS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  146 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKK-KNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
                        250
                 ....*....|
gi 15600424  226 GTPQELRERT 235
Cdd:PRK13640 225 GSPVEIFSKV 234
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
20-231 1.54e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 93.76  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDMRDRRHRRAVCPRIAYMPQGLG--KNLY 97
Cdd:PRK13631  38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKnfKELR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   98 PTLS-VFENVDF------------FGRL-FGHDKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK13631 116 RRVSmVFQFPEYqlfkdtiekdimFGPVaLGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  163 DLLILDEPTTGVDPLSRNQFWELIgrIRAGREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLI--LDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
cbiO PRK13644
energy-coupling factor transporter ATPase;
289-504 1.72e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 92.36  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMA----TRRRVGYMSQ-AFSLYAELS 363
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSklqgIRKLVGIVFQnPETQFVGRT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:PRK13644  95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  444 FWELMVELSRRdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGLPTLEAT 504
Cdd:PRK13644 175 VLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLT 234
cbiO PRK13644
energy-coupling factor transporter ATPase;
11-262 2.02e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 92.36  E-value: 2.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYmp 89
Cdd:PRK13644   4 LENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 qglgknlyptlsVFEN--VDFFGRLFGHDKA-----------ERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCC 156
Cdd:PRK13644  82 ------------VFQNpeTQFVGRTVEEDLAfgpenlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH--EKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
                        250       260
                 ....*....|....*....|....*.
gi 15600424  237 TQSLESAFIALLPESKRAGHHRLVIP 262
Cdd:PRK13644 228 LQTLGLTPPSLIELAENLKMHGVVIP 253
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
10-227 2.05e-20

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 91.23  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDG--DMRDRRHRRAvcprIAY 87
Cdd:COG4161   4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKA----IRL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLGK-----NLYPTLSVFEN-VDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:COG4161  80 LRQKVGMvfqqyNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGT 227
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIREL--SQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQGD 224
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
263-464 2.25e-20

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: 95.89  E-value: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   263 PRPQSEGAPRIAIEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DA 340
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSL 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   341 SDMATRRRVGYMSQAFSLYAElSVRQNLVLhARlfhlpADGIPARVGEMLRRFDLEKVADELPNDLPL-----------G 409
Cdd:TIGR02868 403 DQDEVRRRVSVCAQDAHLFDT-TVRENLRL-AR-----PDATDEELWAALERVGLADWLRALPDGLDTvlgeggarlsgG 475
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424   410 IRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMveLSRRDGVTIFISTH 464
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITH 528
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
258-492 2.80e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 92.99  E-value: 2.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  258 RLVIPPRPQSEGaprIAIEAEGLTCRFGD-----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCA 332
Cdd:PRK13631   8 KKLKVPNPLSDD---IILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  333 L----FGQPVDASDMAT-------------RRRVGYMSQafslYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDL 395
Cdd:PRK13631  85 VgdiyIGDKKNNHELITnpyskkiknfkelRRRVSMVFQ----FPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  396 EKVA------DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVElSRRDGVTIFISTHFM-NE 468
Cdd:PRK13631 161 NKMGlddsylERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMeHV 239
                        250       260
                 ....*....|....*....|....
gi 15600424  469 AQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEI 263
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
7-236 3.14e-20

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 95.55  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     7 GVASLRGVSLRYG--ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDmrDRRHRRAVCPR 84
Cdd:TIGR02203 329 GDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-LLDGH--DLADYTLASLR 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    85 --IAYMPQGLgknlypTL---SVFENVDFfGRLFGHDKAERERRIADL-LQS------TGLAPFAERPAGKLSGGMKQKL 152
Cdd:TIGR02203 406 rqVALVSQDV------VLfndTIANNIAY-GRTEQADRAEIERALAAAyAQDfvdklpLGLDTPIGENGVLLSGGQRQRL 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERfdwLVAMDDGKVLATGTPQELR 232
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADR---IVVMDDGRIVERGTHNELL 555

                  ....
gi 15600424   233 ERTG 236
Cdd:TIGR02203 556 ARNG 559
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
17-231 3.27e-20

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 93.94  E-value: 3.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI--------RVLDGDMRDRRHRRavcprIAYM 88
Cdd:PRK10070  37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiaKISDAELREVRRKK-----IAMV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   89 PQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK10070 112 FQSFA--LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  169 EPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
293-496 4.59e-20

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 94.86  E-value: 4.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRrvgymsQAFSlyaelSVRQNLVLHA 372
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLFS-----AVFSDFHLFD 419
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 373 RLFHLPADGIPARVGEMLRRFDLE-KVA---DELPN-DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW-E 446
Cdd:COG4615 420 RLLGLDGEADPARARELLERLELDhKVSvedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYtE 499
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600424 447 LMVELsRRDGVTIFISTH----FmneaQRCDRISLMHAGKvLASDTPDELVRQR 496
Cdd:COG4615 500 LLPEL-KARGKTVIAISHddryF----DLADRVLKMDYGK-LVELTGPAALAAS 547
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
10-221 4.76e-20

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: 89.07  E-value: 4.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETR-----AVDDVSLEIPANRMVGLIGPDGVGKSSLL-ALLagarkmqdGEIRVLDGdmrdrrhRRAVCP 83
Cdd:cd03250   2 SVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLsALL--------GELEKLSG-------SVSVPG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  84 RIAYMPQglgknlYPTL---SVFENVdffgrLFGHDkaERERRIADLLQSTGLAP-FAERPAG----------KLSGGMK 149
Cdd:cd03250  67 SIAYVSQ------EPWIqngTIRENI-----LFGKP--FDEERYEKVIKACALEPdLEILPDGdlteigekgiNLSGGQK 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 150 QKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWE--LIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGK 221
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK---TRILVTHQLQLLPHADQIVVLDNGR 204
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
274-469 5.16e-20

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 90.53  E-value: 5.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmATRrrvGYMS 353
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER---GVVF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:PRK11248  77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15600424  434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA 469
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
275-493 5.45e-20

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 90.82  E-value: 5.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMS 353
Cdd:PRK10253   8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  354 QAFSLYAELSVrQNLVLHARLFHLPA-----DGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK10253  88 QNATTPGDITV-QELVARGRYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
293-493 5.54e-20

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 95.11  E-value: 5.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPVDASDMatRRRVGYMSQAFSLYAELSVRQNLV 369
Cdd:TIGR00955  44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLM 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   370 LHARLF---HLPADGIPARVGEMLRRFDLEKVADEL---PND---LPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:TIGR00955 122 FQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424   441 RDGFWELMVELSRRdGVTIFISTH---------FmneaqrcDRISLMHAGKVLASDTPDELV 493
Cdd:TIGR00955 202 AYSVVQVLKGLAQK-GKTIICTIHqpsselfelF-------DKIILMAEGRVAYLGSPDQAV 255
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
10-231 5.87e-20

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 94.89  E-value: 5.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG----DMRDRRHRRAVC- 82
Cdd:PRK11160 340 TLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL-LNGqpiaDYSEAALRQAISv 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   83 --PRIAYMPQGLGKNLyptlsvfenvdffgrLFGHDKAERERrIADLLQSTGLAPFAERPAG----------KLSGGMKQ 150
Cdd:PRK11160 419 vsQRVHLFSATLRDNL---------------LLAAPNASDEA-LIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQR 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK---TVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559

                 .
gi 15600424  231 L 231
Cdd:PRK11160 560 L 560
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
275-492 7.11e-20

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 94.23  E-value: 7.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMATRRRVG-- 350
Cdd:PRK13549   6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAGia 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQAFSLYAELSVRQNLVLHARLFH---LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK13549  86 IIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  428 ILDEPTSGVDPVARDGFWELMVELSRRDGVTIFIStHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAHGIACIYIS-HKLNEVKAiSDTICVIRDGRHIGTRPAAGM 230
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
290-483 7.17e-20

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 90.52  E-value: 7.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMATRRRVGYMSQAFSLYA---ELS 363
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQDSISAvnpRKT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLVLHAR-LFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15600424  442 DGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQI 230
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
275-493 7.28e-20

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: 94.10  E-value: 7.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGL------------------------------- 323
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverpskvge 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   324 -LPASEGTCAL----FGQPVDASDMATRRRVGYMSQ-AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEK 397
Cdd:TIGR03269  81 pCPVCGGTLEPeevdFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   398 VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRIS 476
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEViEDLSDKAI 240
                         250
                  ....*....|....*..
gi 15600424   477 LMHAGKVLASDTPDELV 493
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVV 257
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
10-227 7.77e-20

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 89.69  E-value: 7.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDG--DMRDRRHRRAvcprIAY 87
Cdd:PRK11124   4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKA----IRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   88 MPQGLGK-----NLYPTLSVFEN-VDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK11124  80 LRRNVGMvfqqyNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGT 227
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAE--TGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGD 224
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
11-202 9.60e-20

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: 93.96  E-value: 9.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    11 LRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-TLDGVPVSSLDQDEVRRRVSVCA 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    90 QGlgKNLYPTlSVFENVdffgRLFGHDKAERErrIADLLQSTGLAPF-AERPAG----------KLSGGMKQKLGLCCAL 158
Cdd:TIGR02868 416 QD--AHLFDT-TVRENL----RLARPDATDEE--LWAALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARAL 486
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 15600424   159 IHDPDLLILDEPTTGVDPLSRNqfwELIGRIRAGREGMSVLVAT 202
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETAD---ELLEDLLAALSGRTVVLIT 527
cbiO PRK13646
energy-coupling factor transporter ATPase;
20-231 1.12e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 90.22  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR---RHRRAVCPRIAYMPQglgknl 96
Cdd:PRK13646  19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdKYIRPVRKRIGMVFQ------ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   97 YPTLSVFEN-----VDFFGRLFGHDKAERERRIADLLQSTG-------LAPFaerpagKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK13646  93 FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGfsrdvmsQSPF------QMSGGQMRKIAIVSILAMNPDI 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  165 LILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQT-DENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKEL 233
cbiO PRK13650
energy-coupling factor transporter ATPase;
11-234 1.27e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 90.18  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYG---ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMR------DRRHRrav 81
Cdd:PRK13650   7 VKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLLteenvwDIRHK--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   82 cprIAYMPQGlGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK13650  83 ---IGMVFQN-PDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  162 PDLLILDEPTTGVDPLSRnqfWELIGRIRAGRE--GMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK13650 159 PKIIILDEATSMLDPEGR---LELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
cbiO PRK13649
energy-coupling factor transporter ATPase;
293-495 1.50e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 89.80  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-----ATRRRVGYMSQafslYAELSVRQN 367
Cdd:PRK13649  26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikQIRKKVGLVFQ----FPESQLFEE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  368 LVLHARLFHLPADGIPARVGEMLRRFDL------EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLalvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  442 DGFWELMVELsRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13649 182 KELMTLFKKL-HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQD 235
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
14-248 1.62e-19

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 89.56  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   14 VSLRYGETrAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVcpriAYMPQGLG 93
Cdd:PRK15056  14 VTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLV----AYVPQSEE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   94 KNL-YPTLsvFENVDFFGRlFGH------DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:PRK15056  89 VDWsFPVL--VEDVVMMGR-YGHmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  167 LDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPqelrERTGT-QSLESAFI 245
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRD--EGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPT----ETTFTaENLELAFS 239

                 ...
gi 15600424  246 ALL 248
Cdd:PRK15056 240 GVL 242
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
19-231 1.73e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 89.48  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMPQGLGKNLYP 98
Cdd:PRK13652  15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-RGEPITKENIREVRKFVGLVFQNPDDQIFS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   99 TlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:PRK13652  94 P-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15600424  179 RNQFWELIGRIrAGREGMSVLVATAYME-EAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13652 173 VKELIDFLNDL-PETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1-230 1.74e-19

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: 88.26  E-value: 1.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   1 MTAGGSGVASLRGVSLRYGETRAV----DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV-------LD 69
Cdd:COG4181   1 MSSSSAPIIELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfaLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  70 GDMRDRRHRRavcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAerERRIADLLQSTGLapfAER----PAGkLS 145
Cdd:COG4181  81 EDARARLRAR----HVGFVFQSF--QLLPTLTALENVMLPLELAGRRDA--RARARALLERVGL---GHRldhyPAQ-LS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 146 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNR-ERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227

                ....*
gi 15600424 226 GTPQE 230
Cdd:COG4181 228 TAATA 232
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
289-498 1.79e-19

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: 88.44  E-value: 1.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03251  17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlRRQIGLVSQDVFLFND-TVAEN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 lVLHARLfhlpaDGIPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03251  96 -IAYGRP-----GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 437 DPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:cd03251 170 DTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
35-437 2.49e-19

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 92.95  E-value: 2.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   35 RMVGLIGPDGVGKSSLLALLAGA------------------------------RKMQDGEIRVldgdmrdrrhrrAVCPR 84
Cdd:PRK13409 100 KVTGILGPNGIGKTTAVKILSGElipnlgdyeeepswdevlkrfrgtelqnyfKKLYNGEIKV------------VHKPQ 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   85 -IAYMPQGL-GKnlypTLSVFENVDffgrlfghdkaerERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK13409 168 yVDLIPKVFkGK----VRELLKKVD-------------ERGKLDeVVERLGLENILDRDISELSGGELQRVAIAAALLRD 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  162 PDLLILDEPTTGVDplsrnqfwelIG-RIRAGR------EGMSVLV-----ATaymeeaerFDWLVamdDGKVLATGTPq 229
Cdd:PRK13409 231 ADFYFFDEPTSYLD----------IRqRLNVARlirelaEGKYVLVvehdlAV--------LDYLA---DNVHIAYGEP- 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  230 elrertgtqsleSAF-IALLPESKRAG-HHRL-------------------VIPPRPQSEGapRIAIEAEGLTCRFGDF- 287
Cdd:PRK13409 289 ------------GAYgVVSKPKGVRVGiNEYLkgylpeenmrirpepiefeERPPRDESER--ETLVEYPDLTKKLGDFs 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  288 VAVDHVSfrIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGtcalfgqpvdasDMATRRRVGYMSQAFSLYAELSVRQN 367
Cdd:PRK13409 355 LEVEGGE--IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG------------EVDPELKISYKPQYIKPDYDGTVEDL 420
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  368 LvlharlfhlpaDGIPARVG------EMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK13409 421 L-----------RSITDDLGssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
13-243 2.99e-19

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.91  E-value: 2.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   13 GVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRD--RRHRRAVCPRIAYMPQ 90
Cdd:PRK13638   6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDysKRGLLALRQQVATVFQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GLGKNLYPTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:PRK13638  85 DPEQQIFYT-DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  171 TTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQELRERtgTQSLESA 243
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVA--QGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFAC--TEAMEQA 233
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
275-484 3.07e-19

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 88.53  E-value: 3.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGTCALFGQPVD-----ASDM-AT 345
Cdd:PRK09984   5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIrKS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  346 RRRVGYMSQAFSLYAELSVRQNLVLHA--------RLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA 417
Cdd:PRK09984  85 RANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  418 VAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVF 232
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
290-464 3.17e-19

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 87.15  E-value: 3.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELSVRQ 366
Cdd:COG4136  17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRIGILFQDDLLFPHLSVGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 367 NLvlharLFHLPAdGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:COG4136  96 NL-----AFALPP-TIGraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
                       170       180
                ....*....|....*....|...
gi 15600424 442 DGFWELMVELSRRDGVTIFISTH 464
Cdd:COG4136 170 AQFREFVFEQIRQRGIPALLVTH 192
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
11-483 3.29e-19

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 92.10  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQ 90
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GLgkNLYPTLSVFENVdFFGR-----LF-GHDKAERE-RRIADLLqSTGLAPfaERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK10982  81 EL--NLVLQRSVMDNM-WLGRyptkgMFvDQDKMYRDtKAIFDEL-DIDIDP--RAKVATLSVSQMQMIEIAKAFSYNAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATgtpQELRERTGTQsles 242
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLK--ERGCGIVYISHKMEEIFQLcDEITILRDGQWIAT---QPLAGLTMDK---- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  243 aFIALLpeSKRAGHHRLviPPRPQSEGapRIAIEAEGLTCRfgDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTG 322
Cdd:PRK10982 226 -IIAMM--VGRSLTQRF--PDKENKPG--EVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  323 LLPASEGTCALFGQPVDASD----------MAT--RRRVGymsqafsLYAELSVRQNLVLHARLFHLPADGIPARvGEMl 390
Cdd:PRK10982 297 IREKSAGTITLHGKKINNHNaneainhgfaLVTeeRRSTG-------IYAYLDIGFNSLISNIRNYKNKVGLLDN-SRM- 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  391 rRFDLEKVADEL----PN------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIF 460
Cdd:PRK10982 368 -KSDTQWVIDSMrvktPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
                        490       500
                 ....*....|....*....|...
gi 15600424  461 ISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK10982 447 ISSEMPELLGITDRILVMSNGLV 469
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
275-492 3.46e-19

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 88.22  E-value: 3.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRfGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA----SEGTCALFGQPVDASDMATRRRVG 350
Cdd:PRK10418   5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIAT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQAFSLYAELsvrQNLVLHARLfHLPADGIPARVGEMLRRF------DLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK10418  84 IMQNPRSAFNPL---HTMHTHARE-TCLALGKPADDATLTAALeavgleNAARVLKLYPFEMSGGMLQRMMIALALLCEA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDEL 492
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
275-464 5.06e-19

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: 86.26  E-value: 5.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   355 AFSLYAELSVRQNLVLHARlFHLPADGIPArvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:TIGR01189  81 LPGLKPELSALENLHFWAA-IHGGAQRTIE---DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
                         170       180       190
                  ....*....|....*....|....*....|
gi 15600424   435 GVDPVARDGFWELMVELSRRDGVTIfISTH 464
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVL-LTTH 185
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
292-471 5.48e-19

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 86.94  E-value: 5.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELSVRQN--LV 369
Cdd:PRK10771  17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQENNLFSHLTVAQNigLG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  370 LHARLfHLPADGiPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:PRK10771  96 LNPGL-KLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
                        170       180
                 ....*....|....*....|..
gi 15600424  450 ELSRRDGVTIFISTHFMNEAQR 471
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAAR 195
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
28-437 5.53e-19

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: 91.77  E-value: 5.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  28 SLEIP-ANRMVGLIGPDGVGKSSLLALLAGA------------------------------RKMQDGEIRVldgdmrdrr 76
Cdd:COG1245  92 GLPVPkKGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswdevlkrfrgtelqdyfKKLANGEIKV--------- 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  77 hrravcpriAYMPQ----------GLGKNLyptlsvFENVDFFGRLfghdkaereRRIADLLqstGLAPFAERPAGKLSG 146
Cdd:COG1245 163 ---------AHKPQyvdlipkvfkGTVREL------LEKVDERGKL---------DELAEKL---GLENILDRDISELSG 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 147 GMKQKLGLCCALIHDPDLLILDEPTTGVDplsrnqfwelIG-RIRAGR-------EGMSVLV-----ATaymeeaerFDW 213
Cdd:COG1245 216 GELQRVAIAAALLRDADFYFFDEPSSYLD----------IYqRLNVARlirelaeEGKYVLVvehdlAI--------LDY 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 214 LVamdDGKVLATGTPqelrertgtqsleSAF-IALLPESKRAG-HHRL-------------------VIPPRPQSEGAPr 272
Cdd:COG1245 278 LA---DYVHILYGEP-------------GVYgVVSKPKSVRVGiNQYLdgylpeenvrirdepiefeVHAPRREKEEET- 340
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 273 iAIEAEGLTCRFGDF-VAVDhvSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGtcalfgqpvdasDMATRRRVGY 351
Cdd:COG1245 341 -LVEYPDLTKSYGGFsLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG------------EVDEDLKISY 405
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLvlharlfhlpADGIPARVG------EMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1245 406 KPQYISPDYDGTVEEFL----------RSANTDDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
                       490
                ....*....|..
gi 15600424 426 ILILDEPTSGVD 437
Cdd:COG1245 476 LYLLDEPSAHLD 487
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
22-226 9.07e-19

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: 86.17  E-value: 9.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---ARKMQDGEIrVLDGDmrdRRHRRAVCPRIAYMPQGlgKNLYP 98
Cdd:cd03234  21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQI-LFNGQ---PRKPDQFQKCVAYVRQD--DILLP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  99 TLSVFENVDFFGRLFGH---DKAERERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 174
Cdd:cd03234  95 GLTVRETLTYTAILRLPrksSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 175 DPLSRNQFWELIGRIraGREGMSVLVaTAYMEEAE---RFDWLVAMDDGKVLATG 226
Cdd:cd03234 175 DSFTALNLVSTLSQL--ARRNRIVIL-TIHQPRSDlfrLFDRILLLSSGEIVYSG 226
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
2-210 9.17e-19

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 87.14  E-value: 9.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    2 TAGGSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLA-------LLAGARKmqDGEIRVLDGDMRD 74
Cdd:PRK14243   4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   75 RR-HRRAVCPRIAYMPQglGKNLYPTlSVFENVDFFGRLFGH-----DKAERERRIA-------DLLQSTGLApfaerpa 141
Cdd:PRK14243  82 PDvDPVEVRRRIGMVFQ--KPNPFPK-SIYDNIAYGARINGYkgdmdELVERSLRQAalwdevkDKLKQSGLS------- 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  142 gkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAER 210
Cdd:PRK14243 152 --LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL---KEQYTIIIVTHNMQQAAR 215
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
291-498 1.17e-18

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: 86.05  E-value: 1.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMA---TRRRVGYMSQAFSLYAeLSVRQN 367
Cdd:cd03249  20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDLNlrwLRSQIGLVSQEPVLFD-GTIAEN 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVLharlfhlpadGIPARVGEMLRRFDLEKVADELPNDLPLGI---------------RQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03249  97 IRY----------GKPDATDEEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlsggqKQRIAIARALLRNPKILLLDEA 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 433 TSGVDPVArdgfwELMVE--LSR-RDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:cd03249 167 TSALDAES-----EKLVQeaLDRaMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
26-231 1.18e-18

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 90.88  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGaRKMQDGEI---RVLDGDMRDRRHRRAVCpriAYMPQGlgKNLYPTLSV 102
Cdd:TIGR00955  43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGVKGsgsVLLNGMPIDAKEMRAIS---AYVQQD--DLFIPTLTV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   103 FENVDFFGRLFGHD---KAERERRIADLLQSTGLAPFAERPAGK------LSGGMKQKLGLCCALIHDPDLLILDEPTTG 173
Cdd:TIGR00955 117 REHLMFQAHLRMPRrvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424   174 VDPLSRNQFWELIGRIraGREGMSVLV------ATAYmeeaERFDWLVAMDDGKVLATGTPQEL 231
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGL--AQKGKTIICtihqpsSELF----ELFDKIILMAEGRVAYLGSPDQA 254
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
278-503 1.58e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 86.27  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  278 EGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRrrvgYMSQAFS 357
Cdd:PRK11247  16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR----LMFQDAR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  358 LYAELSVRQNLVLHARLFHLPAdgipARvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK11247  92 LLPWKKVIDNVGLGLKGQWRDA----AL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  438 PVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKV---LASDTPDElvRQRG---LPTLEA 503
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIgldLTVDLPRP--RRRGsarLAELEA 236
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
18-231 1.85e-18

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 85.72  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   18 YGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR----DRRHRRAvcprIAYMPQglG 93
Cdd:PRK10895  13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRG----IGYLPQ--E 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   94 KNLYPTLSVFENVDFFGRLFGHDKAE-RERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:PRK10895  87 ASIFRRLSVYDNLMAVLQIRDDLSAEqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  173 GVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEA----ERfDWLVAmdDGKVLATGTPQEL 231
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLR--DSGLGVLITDHNVRETlavcER-AYIVS--QGHLIAHGTPTEI 224
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
17-231 1.94e-18

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 86.18  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR------------DRRHRRAVCPR 84
Cdd:PRK10619  14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQLRLLRTR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   85 IAYMPQGLgkNLYPTLSVFENV-DFFGRLFGHDKAERERRIADLLQSTGLApfaERPAGK----LSGGMKQKLGLCCALI 159
Cdd:PRK10619  94 LTMVFQHF--NLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGID---ERAQGKypvhLSGGQQQRVSIARALA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  160 HDPDLLILDEPTTGVDPlsrnqfwELIGRI-----RAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10619 169 MEPEVLLFDEPTSALDP-------ELVGEVlrimqQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQL 239
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
24-220 2.28e-18

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: 85.21  E-value: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRrhrravcPRIAYMPQGLGKNLYPTLSVF 103
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI-LEGKQITE-------PGPDRMVVFQNYSLLPWLTVR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   104 ENVDFFGRLFGHDKAERERR--IADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQ 181
Cdd:TIGR01184  73 ENIALAVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15600424   182 FWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDG 220
Cdd:TIGR01184 153 LQEELMQI-WEEHRVTVLMVTHDVDEALLLsDRVVMLTNG 191
cbiO PRK13645
energy-coupling factor transporter ATPase;
11-231 2.46e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 86.60  E-value: 2.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYG-----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD----GDMRDRRHRRAV 81
Cdd:PRK13645   9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   82 CPRIAYMPQglgknlYPTLSVFENV---DF-FGRL-FGHDKAERERRIADLLQSTGLA-PFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK13645  89 RKEIGLVFQ------FPEYQLFQETiekDIaFGPVnLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALA 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNK-EYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSPFEI 238
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
288-483 3.38e-18

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 85.52  E-value: 3.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMATRRRVGYMSQAF-------SlyA 360
Cdd:COG1101  20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLPEYKRAKYIGRVFqdpmmgtA--P 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVL-----HARLFHLpadGIP----ARVGEMLRRFDLekvadELPNDL--PLGI-----RQRLSLAVAVIHKP 424
Cdd:COG1101  96 SMTIEENLALayrrgKRRGLRR---GLTkkrrELFRELLATLGL-----GLENRLdtKVGLlsggqRQALSLLMATLTKP 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKV 483
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
cbiO PRK13649
energy-coupling factor transporter ATPase;
10-231 3.63e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 85.57  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYG-----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP- 83
Cdd:PRK13649   4 NLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQi 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   84 --RIAYMPQGLGKNLYPTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:PRK13649  84 rkKVGLVFQFPESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAM 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLH--QSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDI 232
cbiO PRK13645
energy-coupling factor transporter ATPase;
286-492 4.05e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 85.83  E-value: 4.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL--FGQPVDASDMAT----RRRVGYMSQ--AFS 357
Cdd:PRK13645  23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANLKKIKEvkrlRKEIGLVFQfpEYQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  358 LYAElSVRQNLVLHArlFHLPADGIPA--RVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK13645 103 LFQE-TIEKDIAFGP--VNLGENKQEAykKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
10-236 4.05e-18

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: 84.46  E-value: 4.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYG--ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMR--DRRHRRAvcpR 84
Cdd:cd03252   2 TFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGhDLAlaDPAWLRR---Q 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  85 IAYMPQglgKNLYPTLSVFENVDFfgrlfgHDKAERERRIADLLQSTGLAPF------------AERPAGkLSGGMKQKL 152
Cdd:cd03252  78 VGVVLQ---ENVLFNRSIRDNIAL------ADPGMSMERVIEAAKLAGAHDFiselpegydtivGEQGAG-LSGGQRQRI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELR 232
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR---TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224

                ....
gi 15600424 233 ERTG 236
Cdd:cd03252 225 AENG 228
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
24-266 4.08e-18

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: 85.24  E-value: 4.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPRIAYMPQGLGKNLYPTLS 101
Cdd:TIGR02769  27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   102 VFENV-DFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR 179
Cdd:TIGR02769 107 VRQIIgEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   180 NQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLatgtpqELRERTGTQSLESAFIALLPESkraghhr 258
Cdd:TIGR02769 187 AVILELLRKLQQ-AFGTAYLFITHDLRLVQSFcQRVAVMDKGQIV------EECDVAQLLSFKHPAGRNLQSA------- 252

                  ....*...
gi 15600424   259 lVIPPRPQ 266
Cdd:TIGR02769 253 -VLPEHPV 259
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
294-483 4.25e-18

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 83.76  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   294 SFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdMATRRRVGYMSQAFSLYAELSVRQNLVLHAR 373
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-APYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   374 lfhlPADGIPA----RVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:TIGR01277  97 ----PGLKLNAeqqeKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15600424   450 ELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
289-492 4.60e-18

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 86.30  E-value: 4.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDM------ATRRRVGYMSQ--AFSLYA 360
Cdd:PRK15079  36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK--DLLGMkddewrAVRSDIQMIFQdpLASLNP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  361 ELSVRQNLVLHARLFH--LPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK15079 114 RMTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  438 PVARDGFWELMVELSRRDGVT-IFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSlIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
11-236 4.69e-18

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: 84.20  E-value: 4.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHrravcp 83
Cdd:cd03253   3 FENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtldslRRA------ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  84 rIAYMPQGLgkNLYPTlSVFENVDFfGRLFGHD----KAERERRIADLLQSTglaPFA------ERpaG-KLSGGMKQKL 152
Cdd:cd03253  77 -IGVVPQDT--VLFND-TIGYNIRY-GRPDATDeeviEAAKAAQIHDKIMRF---PDGydtivgER--GlKLSGGEKQRV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELR 232
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR---TTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223

                ....
gi 15600424 233 ERTG 236
Cdd:cd03253 224 AKGG 227
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
284-492 5.51e-18

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 87.01  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  284 FGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELS 363
Cdd:PRK11000  13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERGVGMVFQSYALYPHLS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARdg 443
Cdd:PRK11000  92 VAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR-- 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15600424  444 fWELMVELSR---RDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK11000 170 -VQMRIEISRlhkRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
279-498 6.44e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 84.67  E-value: 6.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  279 GLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---MATRRRVGYMSQA 355
Cdd:PRK13638   6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVFQD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  356 FS---LYAELSvrQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:PRK13638  86 PEqqiFYTDID--SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  433 TSGVDPVARdgfwELMVELSRR---DGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTP------DELVRQRGL 498
Cdd:PRK13638 164 TAGLDPAGR----TQMIAIIRRivaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPgevfacTEAMEQAGL 235
cbiO PRK13641
energy-coupling factor transporter ATPase;
20-231 7.77e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 84.88  E-value: 7.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD-------GDMRDRRHRRAVCPRIAYMPQGL 92
Cdd:PRK13641  19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetGNKNLKKLRKKVSLVFQFPEAQL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   93 GKNlyptlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK13641  99 FEN-----TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  172 TGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQ--KAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
275-482 9.80e-18

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: 80.57  E-value: 9.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALfGQPVdasdmatrrRVGYMSQ 354
Cdd:cd03221   1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTV---------KIGYFEQ 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 afslyaeLSvrqnlvlharlfhlpadGiparvGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03221  71 -------LS-----------------G-----GE----------------------KMRLALAKLLLENPNLLLLDEPTN 99
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15600424 435 GVDPVARDgfWeLMVELSRRDGVTIFIS--THFMNEAqrCDRISLMHAGK 482
Cdd:cd03221 100 HLDLESIE--A-LEEALKEYPGTVILVShdRYFLDQV--ATKIIELEDGK 144
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
6-190 1.01e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 83.62  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    6 SGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmrdrrhrRAVCPRI 85
Cdd:PRK09544   2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   86 AYMPQGLgkNLYPTLSVfeNVDFFGRLfghDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK09544  70 GYVPQKL--YLDTTLPL--TVNRFLRL---RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
                        170       180
                 ....*....|....*....|....*
gi 15600424  166 ILDEPTTGVDPLSRNQFWELIGRIR 190
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLR 167
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
293-482 1.09e-17

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: 82.52  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpvdasdmatrrRVGYMSQ-AFSLYAelSVRQNLvlh 371
Cdd:cd03250  24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQePWIQNG--TIRENI--- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 372 arLFHLPADgiPARVGEMLRRFDLEKVADELPN-DLPL----GI------RQRLSLAVAVIHKPEILILDEPTSGVDP-V 439
Cdd:cd03250  87 --LFGKPFD--EERYEKVIKACALEPDLEILPDgDLTEigekGInlsggqKQRISLARAVYSDADIYLLDDPLSAVDAhV 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15600424 440 ARDGFWELMVELsRRDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:cd03250 163 GRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1-231 1.51e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 83.56  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    1 MTAGGSG--VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDM----RD 74
Cdd:PRK14246   1 MEAGKSAedVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV-DGKVlyfgKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   75 RRHRRAVCPRIAYMPQGLGKNLYPTLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGL-APFAER---PAGKLSGGMK 149
Cdd:PRK14246  80 IFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  150 QKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQ 229
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237

                 ..
gi 15600424  230 EL 231
Cdd:PRK14246 238 EI 239
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
24-223 1.54e-17

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: 81.83  E-value: 1.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ--DGEIRVlDGDMRDRRHRRAvcpRIAYMPQGLgkNLYPTLS 101
Cdd:cd03213  25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLI-NGRPLDKRSFRK---IIGYVPQDD--ILHPTLT 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 VFENVDFfgrlfghdkaererriADLLQStglapfaerpagkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQ 181
Cdd:cd03213  99 VRETLMF----------------AAKLRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15600424 182 FWELIGRIR-AGREGMSVLVATAYmEEAERFDWLVAMDDGKVL 223
Cdd:cd03213 150 VMSLLRRLAdTGRTIICSIHQPSS-EIFELFDKLLLLSQGRVI 191
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
289-484 1.64e-17

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 83.69  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRR---RVGYMSQAFSLYAELSVR 365
Cdd:PRK15112  28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqriRMIFQDPSTSLNPRQRIS 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  366 QNLVLHARL-FHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:PRK15112 108 QILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15600424  444 FWELMVELSRRDGVT-IFISTHFMNEAQRCDRISLMHAGKVL 484
Cdd:PRK15112 188 LINLMLELQEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVV 229
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
5-235 1.65e-17

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: 86.78  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     5 GSGVASLRGVSLRY-----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDG----DMRDR 75
Cdd:TIGR03269 276 GEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKP 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    76 R--HRRAVCPRIAYMPQGLGknLYPTLSVFENV-DFFGRLFGHDKAERERRIAdlLQSTGlapFAERPA--------GKL 144
Cdd:TIGR03269 356 GpdGRGRAKRYIGILHQEYD--LYPHRTVLDNLtEAIGLELPDELARMKAVIT--LKMVG---FDEEKAeeildkypDEL 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   145 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLA 224
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
                         250
                  ....*....|..
gi 15600424   225 TGTPQE-LRERT 235
Cdd:TIGR03269 509 IGDPEEiVEELT 520
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
17-222 1.99e-17

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 82.56  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   17 RYGE----TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAvcpRIAYMPQGL 92
Cdd:PRK11629  14 RYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLSSAA---KAELRNQKL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   93 G-----KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK11629  90 GfiyqfHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  168 DEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNR-LQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
283-502 2.30e-17

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 82.71  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-------------DASDMAT-RRR 348
Cdd:PRK10619  14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLlRTR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  349 VGYMSQAFSLYAELSVRQNlVLHA--RLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK10619  94 LTMVFQHFNLWSHMTVLEN-VMEApiQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  426 ILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVRQRGLPTLE 502
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
cbiO PRK13643
energy-coupling factor transporter ATPase;
289-495 2.58e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 83.63  E-value: 2.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-----TRRRVGYMSQafslYAELS 363
Cdd:PRK13643  21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQ----FPESQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVA------DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK13643  97 LFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGladefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  438 PVARDGFWELMvELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13643 177 PKARIEMMQLF-ESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQE 234
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
265-492 2.75e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 85.87  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  265 PQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA 344
Cdd:PRK15439   2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  345 TRRRVG-YM-SQAFSLYAELSVRQNLvlharLFHLPADGIP-ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVI 421
Cdd:PRK15439  82 KAHQLGiYLvPQEPLLFPNLSVKENI-----LFGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  422 HKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
27-199 2.75e-17

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: 81.39  E-value: 2.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV---LDGDMRDRRHRRavCPRIAYMPqglgkNLYPTLSVF 103
Cdd:cd03231  19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggPLDFQRDSIARG--LLYLGHAP-----GIKTTLSVL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 104 ENVDFFGRLFGHDKAErerriaDLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFW 183
Cdd:cd03231  92 ENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
                       170
                ....*....|....*.
gi 15600424 184 ELIgRIRAGREGMSVL 199
Cdd:cd03231 166 EAM-AGHCARGGMVVL 180
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
20-222 3.15e-17

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 82.44  E-value: 3.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-RDRRHRRAvcPRIAYMPQGLGKNLYP 98
Cdd:COG1101  18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRA--KYIGRVFQDPMMGTAP 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  99 TLSVFENV-------DFFGRLFGHDKAERERrIADLLQSTGLApFAER---PAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:COG1101  96 SMTIEENLalayrrgKRRGLRRGLTKKRREL-FRELLATLGLG-LENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLD 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:COG1101 174 EHTAALDPKTAALVLELTEKI-VEENNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
10-437 3.17e-17

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 86.54  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHR----RAVCPRI 85
Cdd:PRK11147   5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIVARLQqdppRNVEGTV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   86 -AYMPQGL---GKNL--YPTLSvfenvdffgRLFGHDKAER--------------------ERRIADLLQSTGLAPfaER 139
Cdd:PRK11147  84 yDFVAEGIeeqAEYLkrYHDIS---------HLVETDPSEKnlnelaklqeqldhhnlwqlENRINEVLAQLGLDP--DA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  140 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfW------ELIGRI------RAGREGMS---------V 198
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIE--WlegflkTFQGSIifishdRSFIRNMAtrivdldrgK 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  199 LVA-----TAYM---EEAER--------FDWLVAMD---------------DGKVLA-TGTPQELRERTGTQSleSAFIA 246
Cdd:PRK11147 231 LVSypgnyDQYLlekEEALRveelqnaeFDRKLAQEevwirqgikarrtrnEGRVRAlKALRRERSERREVMG--TAKMQ 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  247 lLPESKRAGhhrlvipprpqsegapRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA 326
Cdd:PRK11147 309 -VEEASRSG----------------KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQA 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  327 SEGT--CalfgqpvdasdmATRRRVGYMSQ-AFSLYAELSVRQNLvlharlfhlpAD--------GIPARVGEMLRRFDL 395
Cdd:PRK11147 372 DSGRihC------------GTKLEVAYFDQhRAELDPEKTVMDNL----------AEgkqevmvnGRPRHVLGYLQDFLF 429
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 15600424  396 E-KVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK11147 430 HpKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
275-482 3.51e-17

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 85.79  E-value: 3.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGD--FvAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVgyM 352
Cdd:PRK10522 323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL--F 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  353 SQAFS---LYAELSVRQNlvlharlfhLPADgiPARVGEMLRRFDLE---KVADELPNDLPL--GIRQRLSLAVAVIHKP 424
Cdd:PRK10522 400 SAVFTdfhLFDQLLGPEG---------KPAN--PALVEKWLERLKMAhklELEDGRISNLKLskGQKKRLALLLALAEER 468
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
291-495 4.49e-17

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 85.93  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMATRRR--VGYMSQAFSLYAELSVR 365
Cdd:PRK10535  25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatlDADALAQLRRehFGFIFQRYHLLSHLTAA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  366 QNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDgfw 445
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE--- 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600424  446 ELMVELS--RRDGVTIFISTHFMNEAQRCDRISLMHAGKVLaSDTPDELVRQ 495
Cdd:PRK10535 182 EVMAILHqlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV-RNPPAQEKVN 232
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
275-489 5.90e-17

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 80.53  E-value: 5.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFV--AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGY 351
Cdd:cd03369   7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAElSVRQNLvlharlfhlpadgiparvgEMLRRFDLEKVADELP-----NDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:cd03369  87 IPQDPTLFSG-TIRSNL-------------------DPFDEYSDEEIYGALRvseggLNLSQGQRQLLCLARALLKRPRV 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 427 LILDEPTSGVDpVARDGfweLMVELSRRD--GVTIFISTHFMNEAQRCDRISLMHAGKVLASDTP 489
Cdd:cd03369 147 LVLDEATASID-YATDA---LIQKTIREEftNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
13-255 6.27e-17

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 81.66  E-value: 6.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   13 GVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPRIAYMPQ 90
Cdd:PRK10419  17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKAFRRDIQMVFQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GLGKNLYPTLSVFENVDFFGR-LFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK10419  97 DSISAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  169 EPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVA-MDDGKVL---ATGTPQELRERTGtQSLESAF 244
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQ-QFGTACLFITHDLRLVERFCQRVMvMDNGQIVetqPVGDKLTFSSPAG-RVLQNAV 254
                        250
                 ....*....|.
gi 15600424  245 IALLPESKRAG 255
Cdd:PRK10419 255 LPAFPVRRRTT 265
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
10-181 6.40e-17

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: 78.26  E-value: 6.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIAYMP 89
Cdd:cd03221   2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYFE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QglgknlyptlsvfenvdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03221  70 Q-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
                       170
                ....*....|..
gi 15600424 170 PTTGVDPLSRNQ 181
Cdd:cd03221  97 PTNHLDLESIEA 108
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
14-231 9.84e-17

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 81.21  E-value: 9.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   14 VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---ARKMQDGEIRVL------DGDM-RDRRHRRAvcp 83
Cdd:PRK09984  10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLgrtvqrEGRLaRDIRKSRA--- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   84 RIAYMPQGLgkNLYPTLSVFENV--------DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK09984  87 NTGYIFQQF--NLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYALRYcERIVALRQGHVFYDGSSQQF 240
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
10-170 9.85e-17

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 82.97  E-value: 9.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-----RVLDGDMRDRRhrravcp 83
Cdd:PRK11650   5 KLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrVVNELEPADRD------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   84 rIAYMPQglgkN--LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK11650  78 -IAMVFQ----NyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152

                 ....*....
gi 15600424  162 PDLLILDEP 170
Cdd:PRK11650 153 PAVFLFDEP 161
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
11-237 1.04e-16

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: 80.28  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  11 LRGVSLRY---GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRD---RRHRRavcp 83
Cdd:cd03249   3 FKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-LLDGvDIRDlnlRWLRS---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  84 RIAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERERRIADLLQSTGLAPFAERPAG----------KLSGGMKQ 150
Cdd:cd03249  78 QIGLVSQE------PVLfdgTIAENI-----RYGKPDATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsQLSGGQKQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR---TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE 223

                ....*..
gi 15600424 231 LRERTGT 237
Cdd:cd03249 224 LMAQKGV 230
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
293-495 1.18e-16

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 84.32  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQNLvlh 371
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfGKHIGYLPQDVELFPG-TVAENI--- 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   372 ARlFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:TIGR01842 413 AR-FGENAD--PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEG 489
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424   441 RDGFWELMVELSRRDGVTIFIsTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:TIGR01842 490 EQALANAIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
275-483 1.83e-16

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: 83.58  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTC---ALF-GQPVDASDMATR 346
Cdd:COG4172   7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPsgsILFdGQDLLGLSEREL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRV--GYMSQAF-----SLYAELSV-RQ---NLVLHARlfhLPADGIPARVGEMLRRF---DLEKVADELPNDLPLGIRQ 412
Cdd:COG4172  87 RRIrgNRIAMIFqepmtSLNPLHTIgKQiaeVLRLHRG---LSGAAARARALELLERVgipDPERRLDAYPHQLSGGQRQ 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 413 RLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTI-FIsTHFMNEAQR-CDRISLMHAGKV 483
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALlLI-THDLGVVRRfADRVAVMRQGEI 235
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
275-498 1.96e-16

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 83.61  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   275 IEAEGLTCRFG--DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DASDMATRRRVGY 351
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQVAL 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   352 MSQAFSLYAElSVRQNlVLHARlfhlPADGIPARVGEMLRRFDLEKVADELPN--DLPLGI---------RQRLSLAVAV 420
Cdd:TIGR02203 411 VSQDVVLFND-TIANN-IAYGR----TEQADRAEIERALAAAYAQDFVDKLPLglDTPIGEngvllsggqRQRLAIARAL 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   421 IHKPEILILDEPTSGVDP----VARDGFWELMvelsrrDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:TIGR02203 485 LKDAPILILDEATSALDNeserLVQAALERLM------QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558

                  ..
gi 15600424   497 GL 498
Cdd:TIGR02203 559 GL 560
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
11-210 3.23e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 79.70  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQdGEIRVlDGDM---------------RDR 75
Cdd:PRK14258  10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRV-EGRVeffnqniyerrvnlnRLR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   76 RHRRAVCPRiaympqglgKNLYPtLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLAPFAE----RPAGKLSGGMKQ 150
Cdd:PRK14258  88 RQVSMVHPK---------PNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQ 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAER 210
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRL-RSELTMVIVSHNLHQVSR 216
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
293-498 3.28e-16

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: 78.81  E-value: 3.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSL----------YAE 361
Cdd:cd03253  20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVVPQDTVLfndtigynirYGR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 LSVRQNLV--------LHARLFHLPaDGIPARVGEM-LRrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03253 100 PDATDEEVieaakaaqIHDKIMRFP-DGYDTIVGERgLK--------------LSGGEKQRVAIARAILKNPPILLLDEA 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDgVTIFIsTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGR-TTIVI-AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
286-492 3.35e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 79.32  E-value: 3.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLP------ASEGTCALFGQPVDASD-MATRRRVGYMSQAFSL 358
Cdd:PRK14246  22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDaIKLRKEVGMVFQQPNP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  359 YAELSVRQNLVlharlFHLPADGIPAR------VGEMLRRFDLEK-VADEL---PNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK14246 102 FPHLSIYDNIA-----YPLKSHGIKEKreikkiVEECLRKVGLWKeVYDRLnspASQLSGGQQQRLTIARALALKPKVLL 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
270-497 3.54e-16

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 82.95  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  270 APRIAIEAEGLTCRFGD--FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATR 346
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALR 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  347 RRVGYMSQAFSLYAElSVRQNLVLHArlfhlpADGIPARVGEMLRRFDLEKVADelpNDLPL------GIRQ-------R 413
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDNLLLAA------PNASDEALIEVLQQVGLEKLLE---DDKGLnawlgeGGRQlsggeqrR 483
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561

                 ....
gi 15600424  494 RQRG 497
Cdd:PRK11160 562 AQQG 565
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
289-462 4.04e-16

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 80.39  E-value: 4.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT----RRRVGYMSQafSLYAELSV 364
Cdd:PRK11308  30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllRQKIQIVFQ--NPYGSLNP 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  365 RQN--------LVLHARlfhLPADGIPARVGEMLRRFDLE-KVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:PRK11308 108 RKKvgqileepLLINTS---LSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
                        170       180
                 ....*....|....*....|....*...
gi 15600424  436 VDPVARDGFWELMVELSRRDGVT-IFIS 462
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSyVFIS 212
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
22-175 4.65e-16

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 80.55  E-value: 4.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR-----VLDGDMRDRRHRRavcPRIAYM---PQGlg 93
Cdd:COG4608  32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdITGLSGRELRPLR---RRMQMVfqdPYA-- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  94 kNLYPTLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:COG4608 107 -SLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185

                ....
gi 15600424 172 TGVD 175
Cdd:COG4608 186 SALD 189
GguA NF040905
sugar ABC transporter ATP-binding protein;
276-482 6.11e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.76  E-value: 6.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMATRRRVGY-- 351
Cdd:NF040905   3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIvi 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 MSQAFSLYAELSVRQNLVL---HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:NF040905  83 IHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELsRRDGVT-IFIStHFMNE-AQRCDRISLMHAGK 482
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLEL-KAQGITsIIIS-HKLNEiRRVADSITVLRDGR 216
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
279-495 7.08e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 81.50  E-value: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  279 GLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDmATRRRVGYMSQA 355
Cdd:PRK11288   9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTA-ALAAGVAIIYQE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  356 FSLYAELSVRQNLVLHarlfHLPADG-------IPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK11288  88 LHLVPEMTVAENLYLG----QLPHKGgivnrrlLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV------LASDTPDELVRQ 495
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFAlCDAITVFKDGRYvatfddMAQVDRDQLVQA 236
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
275-464 1.30e-15

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 76.38  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:PRK13538   2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  355 AFSLYAELSVRQNLVLHARLFHLPADgipARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK13538  82 QPGIKTELTALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 15600424  435 GVDPVARDGFWELMVELSRRDGVTIFiSTH 464
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVIL-TTH 187
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
27-263 1.35e-15

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 77.57  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQdGEIRVLDGDMRD------RRHRravcpriAYMPQglgkNLYPT- 99
Cdd:COG4138  15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDwsaaelARHR-------AYLSQ----QQSPPf 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 -LSVFENVDFFGRLfGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCAL--IH---DPD--LLILDEPT 171
Cdd:COG4138  83 aMPVFQYLALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptiNPEgqLLLLDEPM 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 172 TGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-D--WLvaMDDGKVLATGTPQE-LRERTGTQSLESAFIAL 247
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQ--QGITVVMSSHDLNHTLRHaDrvWL--LKQGKLVASGETAEvMTPENLSEVFGVKFRRL 237
                       250
                ....*....|....*.
gi 15600424 248 lpeskRAGHHRLVIPP 263
Cdd:COG4138 238 -----EVEGHRWLIPT 248
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
289-464 1.64e-15

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 76.45  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMAT------RRRVGYMSQAFSLYAEL 362
Cdd:PRK10908  17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DITRLKNrevpflRRQIGMIFQDHHLLMDR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  363 SVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARD 442
Cdd:PRK10908  95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
                        170       180
                 ....*....|....*....|..
gi 15600424  443 GFWELMVELSRRdGVTIFISTH 464
Cdd:PRK10908 175 GILRLFEEFNRV-GVTVLMATH 195
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
12-233 1.98e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 77.19  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-------ALLAGARkmQDGEIR-----VLDGDMRDRRHRR 79
Cdd:PRK14267   8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllELNEEAR--VEGEVRlfgrnIYSPDVDPIEVRR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   80 AVCPRIAYmpqglgKNLYPTLSVFENVDFFGRLFG--HDKAERERRIADLLQSTGL-APFAER---PAGKLSGGMKQKLG 153
Cdd:PRK14267  86 EVGMVFQY------PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRE 233
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
289-486 2.10e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 77.62  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmATRRRVGYMSQ------AFSLYAEL 362
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA--LQKNLVAYVPQseevdwSFPVLVED 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  363 SVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARD 442
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15600424  443 GFWELMVELsRRDGVTIFISTHFMNEAQR-CDrISLMHAGKVLAS 486
Cdd:PRK15056 180 RIISLLREL-RDEGKTMLVSTHNLGSVTEfCD-YTVMVKGTVLAS 222
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
275-495 2.15e-15

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 77.50  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD----MATRRRVG 350
Cdd:PRK11831   8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlYTVRKRMS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQAFSLYAELSVRQNLVLHARLF-HLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:PRK11831  88 MLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL-------VRQ 495
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALqanpdprVRQ 241
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
274-471 2.62e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 77.00  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGTCALFGQPVDASDMAT--- 345
Cdd:PRK14258   7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLnrl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  346 RRRVGYMSQAFSLYAeLSVRQNLVLHARLF----HLPADGIparVGEMLRRFDLekvADELPN-------DLPLGIRQRL 414
Cdd:PRK14258  87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDI---VESALKDADL---WDEIKHkihksalDLSGGQQQRL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  415 SLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR 471
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
289-497 2.93e-15

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: 80.17  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlRQFINYLPQEPYIFSG-SILEN 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   368 LVLHARLfhlpadgiPARVGEMLRRFDLEKVADELPNdLPLGI---------------RQRLSLAVAVIHKPEILILDEP 432
Cdd:TIGR01193 568 LLLGAKE--------NVSQDEIWAACEIAEIKDDIEN-MPLGYqtelseegssisggqKQRIALARALLTDSKVLILDES 638
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424   433 TSGVDPVARDGFWELMVELsrRDGVTIFIStHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNL--QDKTIIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
7-228 3.62e-15

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C 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-resistance 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: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 75.61  E-value: 3.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   7 GVASLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSL-LALLagaR--KMQDGEIRVlDG------DMRDR 75
Cdd:cd03244   1 GDIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALF---RlvELSSGSILI-DGvdiskiGLHDL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  76 RHRRAVCPRIAYMPQGlgknlyptlSVFENVDFFGRlfgHDKAErerrIADLLQSTGLAPFAERPAGKL----------- 144
Cdd:cd03244  77 RSRISIIPQDPVLFSG---------TIRSNLDPFGE---YSDEE----LWQALERVGLKEFVESLPGGLdtvveeggenl 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 145 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVAtaymeeAER------FDWLVAMD 218
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC---TVLTI------AHRldtiidSDRILVLD 211
                       250
                ....*....|
gi 15600424 219 DGKVLATGTP 228
Cdd:cd03244 212 KGRVVEFDSP 221
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
24-243 4.09e-15

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: 79.10  E-value: 4.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ-DGEIrVLDGDMRDRRH-RRAVCPRIAYMPQ----------- 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNV-FINGKPVDIRNpAQAIRAGIAMVPEdrkrhgivpil 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    91 GLGKNLypTLSVFENVDFFGRLfghDKAERERRIADLLQSTGLAPFA-ERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:TIGR02633 355 GVGKNI--TLSVLKSFCFKMRI---DAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424   170 PTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELrerTGTQSLESA 243
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQL--AQEGVAIIVVSSELAEVLGLsDRVLVIGEGKLKGDFVNHAL---TQEQVLAAA 499
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
21-236 7.93e-15

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 78.73  E-value: 7.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQdGEIRVLDGDMRD------RRHrravcprIAYmpqgLGK 94
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELREldpeswRKH-------LSW----VGQ 430
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   95 NlyPTL---SVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAERP-----------AGKLSGGMKQKLGLCCALIH 160
Cdd:PRK11174 431 N--PQLphgTLRDNV-----LLGNPDASDEQ-LQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARALLQ 502
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ---TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG 575
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
293-483 8.48e-15

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: 74.43  E-value: 8.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRVGYMSQAFSLYAElSVRQNLVLH 371
Cdd:cd03248  33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLVGQEPVLFAR-SLQDNIAYG 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 372 arLFHLPADGIPAR---------VGEMLRRFDLEkvADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVArd 442
Cdd:cd03248 112 --LQSCSFECVKEAaqkahahsfISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES-- 185
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15600424 443 gfwELMVELSRRDGV---TIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:cd03248 186 ---EQQVQQALYDWPerrTVLVIAHRLSTVERADQILVLDGGRI 226
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
275-493 9.06e-15

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 74.92  E-value: 9.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMAT----RRRVG 350
Cdd:PRK11614   6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK--DITDWQTakimREAVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQAFSLYAELSVRQNLVLharlfhlpaDGIPARVGEMLRRfdLEKVADELP----------NDLPLGIRQRLSLAVAV 420
Cdd:PRK11614  84 IVPEGRRVFSRMTVEENLAM---------GGFFAERDQFQER--IKWVYELFPrlherriqraGTMSGGEQQMLAIGRAL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  421 IHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
7-222 9.32e-15

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: 74.43  E-value: 9.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   7 GVASLRGVSLRY---GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG---DMRDRRHRRA 80
Cdd:cd03248  10 GIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGkpiSQYEHKYLHS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  81 VCPRIAYMPQGLGKnlyptlSVFENVDF------FGRLF-GHDKAERERRIADLLQstGLAPFAERPAGKLSGGMKQKLG 153
Cdd:cd03248  89 KVSLVGQEPVLFAR------SLQDNIAYglqscsFECVKeAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVA 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELigrIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQA---LYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
277-486 1.05e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 74.96  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  277 AEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcALF----GQPVDASDM--ATRRRVG 350
Cdd:PRK11701   9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE-VHYrmrdGQLRDLYALseAERRRLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQAFslyaelsVRQNlvlharlfhlPADGIP------ARVGEML-----RRFD---------LEKVA------DELPN 404
Cdd:PRK11701  88 RTEWGF-------VHQH----------PRDGLRmqvsagGNIGERLmavgaRHYGdiratagdwLERVEidaariDDLPT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  405 DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQ-RCDRISLMHAGKV 483
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGRV 230

                 ...
gi 15600424  484 LAS 486
Cdd:PRK11701 231 VES 233
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
27-234 1.18e-14

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 74.79  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQGLGK-----NLYPTLS 101
Cdd:PRK11264  22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLRQHVGFvfqnfNLFPHRT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  102 VFENVdFFGRLF--GHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsr 179
Cdd:PRK11264 102 VLENI-IEGPVIvkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP--- 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  180 nqfwELIGR----IRA-GREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATG-------TPQELRER 234
Cdd:PRK11264 178 ----ELVGEvlntIRQlAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGpakalfaDPQQPRTR 241
cbiO PRK13642
energy-coupling factor transporter ATPase;
20-231 1.20e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 75.13  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMPQGlGKNLYPT 99
Cdd:PRK13642  19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRRKIGMVFQN-PDNQFVG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  100 LSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR 179
Cdd:PRK13642  97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600424  180 NQFWELIGRIRaGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13642 177 QEIMRVIHEIK-EKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
275-489 1.21e-14

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C 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-resistance 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: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 74.07  E-value: 1.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD--FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMAT---RRRV 349
Cdd:cd03244   3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--VDISKIGLhdlRSRI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQ---AFSlyaeLSVRQNLvlhaRLFHLPADgipARVGEMLRRFDLEKVADELPNDLPL-----------GIRQRLS 415
Cdd:cd03244  81 SIIPQdpvLFS----GTIRSNL----DPFGEYSD---EELWQALERVGLKEFVESLPGGLDTvveeggenlsvGQRQLLC 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 416 LAVAVIHKPEILILDEPTSGVDPvARDgfwELMVEL--SRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTP 489
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDP-ETD---ALIQKTirEAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
285-495 1.82e-14

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 75.71  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCA--LFGQPVDASDMATRRRVGYMSQAFSLyael 362
Cdd:COG4170  18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTAdrFRWNGIDLLKLSPRERRKIIGREIAM---- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 363 sVRQN----LVLHARLFHLPADGIPA----------------RVGEMLRRF---DLEKVADELPNDLPLGIRQRLSLAVA 419
Cdd:COG4170  94 -IFQEpsscLDPSAKIGDQLIEAIPSwtfkgkwwqrfkwrkkRAIELLHRVgikDHKDIMNSYPHELTEGECQKVMIAMA 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 420 VIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTI-FISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIlLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
289-486 2.07e-14

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 76.69  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD--ASDMATRRRVGYMSQAFSLYAELSVRQ 366
Cdd:PRK10982  13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMVHQELNLVLQRSVMD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  367 NLVLHarlfHLPADGIPARVGEMLRrfDLEKVADEL-----PND----LPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK10982  93 NMWLG----RYPTKGMFVDQDKMYR--DTKAIFDELdididPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15600424  438 PVARDGFWELMVELSRRDGVTIFIStHFMNEA-QRCDRISLMHAGKVLAS 486
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIfQLCDEITILRDGQWIAT 215
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
11-238 2.49e-14

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 77.07  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV-------LDGD----MRdR 75
Cdd:PRK10535   7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqdvatLDADalaqLR-R 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   76 RHRRAVCPRIaympqglgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK10535  86 EHFGFIFQRY---------HLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERT 235
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVA 234

                 ...
gi 15600424  236 GTQ 238
Cdd:PRK10535 235 GGT 237
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
14-236 2.54e-14

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: 77.09  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    14 VSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMPQGl 92
Cdd:TIGR01193 479 VSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI-LLNGFSLKDIDRHTLRQFINYLPQE- 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    93 gknlyPTL---SVFENVdffgrLFG------HDKAERERRIADLLQ-----STGLAPFAERPAGKLSGGMKQKLGLCCAL 158
Cdd:TIGR01193 557 -----PYIfsgSILENL-----LLGakenvsQDEIWAACEIAEIKDdienmPLGYQTELSEEGSSISGGQKQRIALARAL 626
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424   159 IHDPDLLILDEPTTGVDPLSRNQfweLIGRIRAGREGMSVLVATAyMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKK---IVNNLLNLQDKTIIFVAHR-LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
10-230 2.79e-14

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: 76.71  E-value: 2.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRY-GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCPRIAY 87
Cdd:COG4618 332 SVENLTVVPpGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-LDGADLSQWDREELGRHIGY 410
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  88 MPQGLGknLYPTlSVFENVdffGRLfghDKAERERRIA--------DLLQS------TGLAPFAERpagkLSGGMKQKLG 153
Cdd:COG4618 411 LPQDVE--LFDG-TIAENI---ARF---GDADPEKVVAaaklagvhEMILRlpdgydTRIGEGGAR----LSGGQRQRIG 477
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVAT---AYMEEAerfDWLVAMDDGKVLATGTPQE 230
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA--RGATVVVIThrpSLLAAV---DKLLVLRDGRVQAFGPRDE 552
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
23-243 3.14e-14

nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 73.17  E-value: 3.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    23 AVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLAGARKMQDGEIRVLDGDMRDRRHR-RAVC-----PRIAYMP-QG 91
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSltclAILGLLPPGLTQTSGEILLDGRPLLPLSIRgRHIAtimqnPRTAFNPlFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    92 LGKNLYPTLsvfenvdffgRLFGHDKAERERRIADLLQSTGLAPFAE---RPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:TIGR02770  81 MGNHAIETL----------RSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIAD 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424   169 EPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQELRER---TGTQSLESA 243
Cdd:TIGR02770 151 EPTTDLDVVNQARVLKLLRELRQ-LFGTGILLITHDLGVvARIADEVAVMDDGRIVERGTVKEIFYNpkhETTRKLLSA 228
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
294-498 3.22e-14

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 77.07  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   294 SFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD-MATRRRVGYMSQAFSLYAElSVRQNLVLHa 372
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhHYLHRQVALVGQEPVLFSG-SVRENIAYG- 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   373 rLFHLPADGIPAR---------VGEMLRRFDLEkvADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:TIGR00958 579 -LTDTPDEEIMAAakaanahdfIMEFPNGYDTE--VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15600424   444 FWELMVELSRrdgvTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:TIGR00958 656 LQESRSRASR----TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
275-464 3.43e-14

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 73.22  E-value: 3.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvdasdmatrRRVGYMSQ 354
Cdd:PRK09544   5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------LRIGYVPQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  355 AFSLYAELSVRQNLVLHARLFHLPADGIPArvgemLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK09544  75 KLYLDTTLPLTVNRFLRLRPGTKKEDILPA-----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
                        170       180       190
                 ....*....|....*....|....*....|
gi 15600424  435 GVDPVARDGFWELMVELSRRDGVTIFISTH 464
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
28-231 4.08e-14

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 72.69  E-value: 4.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   28 SLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrHRRAVCPR--IAYMPQGlgKNLYPTLSVFEN 105
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRrpVSMLFQE--NNLFSHLTVAQN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  106 VDFfG-----RLfghdKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRN 180
Cdd:PRK10771  92 IGL-GlnpglKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600424  181 QFWELIGRIRAGREgMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10771 167 EMLTLVSQVCQERQ-LTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDEL 217
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
274-484 5.13e-14

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 72.86  E-value: 5.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---------MA 344
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkgliRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  345 TRRRVGYMSQAFSLYAELSVRQNLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHK 423
Cdd:PRK11264  83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKgEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  424 PEILILDEPTSGVDPvardgfwELMVEL---------SRRdgvTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK11264 163 PEVILFDEPTSALDP-------ELVGEVlntirqlaqEKR---TMVIVTHEMSFARDvADRAIFMDQGRIV 223
NosY COG1277
ABC-type transport system involved in multi-copper enzyme maturation, permease component ...
726-841 6.10e-14

ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440888 [Multi-domain]  Cd Length: 201  Bit Score: 71.38  E-value: 6.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 726 VIPLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLK------GS 799
Cdd:COG1277  56 LLSLLLPLLAPALGMDAISGERESGTLELLLTLPISRWEIVLGKFLGALLVLLLALLITFLLALLLGLLLFGspppdlGA 135
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15600424 800 FLALTIGAFLYVVTSTGLGLFLSTFMRSQIAAvFGVAIATMI 841
Cdd:COG1277 136 ILGFYLGLLLLGLAFLAIGLFISALTRNQIVA-AILAIALWL 176
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
16-483 9.02e-14

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 75.21  E-value: 9.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   16 LRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR------------------------VLDGD 71
Cdd:PRK10636   9 IRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawvnqetpalpqpaleyVIDGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   72 mrdrRHRRAVCPRIAYMPQGLGKNLYPTLSvfenvdffGRLFGHDKAERERRIADLLQSTGLA-PFAERPAGKLSGGMKQ 150
Cdd:PRK10636  89 ----REYRQLEAQLHDANERNDGHAIATIH--------GKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  151 KLGLCCALIHDPDLLILDEPTTGVDpLSRNQFWEligRIRAGREGMSVLVAtaymeeAERfDWLVAMDDgKVLATgTPQE 230
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLD-LDAVIWLE---KWLKSYQGTLILIS------HDR-DFLDPIVD-KIIHI-EQQS 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  231 LRERTGT-----------------------------QSLESAFIALLPESKRAGHH-------RLVIPPR---P------ 265
Cdd:PRK10636 224 LFEYTGNyssfevqratrlaqqqamyesqqervahlQSYIDRFRAKATKAKQAQSRikmlermELIAPAHvdnPfhfsfr 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  266 QSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALfgqpvdasdmAT 345
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AK 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  346 RRRVGYMSQ---AFsLYAELSVRQNLvlhARLfhlpadgIPARVGEMLRR------FDLEKVADElPNDLPLGIRQRLSL 416
Cdd:PRK10636 374 GIKLGYFAQhqlEF-LRADESPLQHL---ARL-------APQELEQKLRDylggfgFQGDKVTEE-TRRFSGGEKARLVL 441
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  417 AVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsrrDGVTIFIS--THFMNEAQrcDRISLMHAGKV 483
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVShdRHLLRSTT--DDLYLVHDGKV 505
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
20-230 9.56e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 73.20  E-value: 9.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL----ALL---AGA-----------RKMQDGEIRVLDGDMRDRRHRR-- 79
Cdd:PRK13651  19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnALLlpdTGTiewifkdeknkKKTKEKEKVLEKLVIQKTRFKKik 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   80 ---AVCPRIAYMPQGLGKNLYPTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK13651  99 kikEIRRRVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALA 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQE 230
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN--KQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYD 251
ABC2_membrane_2 pfam12679
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
729-915 1.31e-13

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family.


Pssm-ID: 403774 [Multi-domain]  Cd Length: 281  Bit Score: 72.43  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   729 LLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKGS--------- 799
Cdd:pfam12679  76 FLIPVIAALLGADAIAGERERGTIELLLSLPVSRSEILLGKFIGRLAIGLILAVALLAGVLLALAITLALGdpldlgdll 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   800 FLALTIGAFLYVVTSTGLGLFLSTFMRSQ---IAAVFGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLY----PTSHF 872
Cdd:pfam12679 156 LLVAASVLLALALVFLSIGLLLSSVARSTrtaAAIALGLFFVLAILWPIVLYGLAELLAGPAPPQELLDFLlflnPTSPY 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15600424   873 LVVSRGAFSKSLGLSDL--WAYYLPLAASIVVLTLLSVACLKKQE 915
Cdd:pfam12679 236 NTLLSTILAGSDLSLYGstATNLLILLAWIAVPLALAYVLFKRKD 280
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
285-506 1.35e-13

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 73.34  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDasDMATRRRVGYMS-QAFSLYAELS 363
Cdd:PRK11650  15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN--ELEPADRDIAMVfQNYALYPHMS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpvARdg 443
Cdd:PRK11650  93 VRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD--AK-- 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  444 fweLMV-------ELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDElVRQRGLPTLEATFI 506
Cdd:PRK11650 169 ---LRVqmrleiqRLHRRLKTTSLYVTHDQVEAMTlADRVVVMNGGVAEQIGTPVE-VYEKPASTFVASFI 235
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
19-237 1.37e-13

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 75.37  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvldgdmrdrrhrrAVCPRIAYMPQglgKNLYP 98
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------HMKGSVAYVPQ---QAWIQ 711
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     99 TLSVFENVdffgrLFGHdkAERERRIADLLQSTGLAPFAE-RPAG----------KLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:TIGR00957  712 NDSLRENI-----LFGK--ALNEKYYQQVLEACALLPDLEiLPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLF 784
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424    168 DEPTTGVDP-LSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGT 237
Cdd:TIGR00957  785 DDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILV-THGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA 854
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
6-236 1.98e-13

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 74.23  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    6 SGVASLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG-DMRD---RRHRRA 80
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-DGtDIRTvtrASLRRN 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   81 vcprIAYMPQGLGknLYpTLSVFENVdffgRLFGHDKAERERRIA-------DLL--QSTGLAPFAERPAGKLSGGMKQK 151
Cdd:PRK13657 411 ----IAVVFQDAG--LF-NRSIEDNI----RVGRPDATDEEMRAAaeraqahDFIerKPDGYDTVVGERGRQLSGGERQR 479
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  152 LGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERfdwLVAMDDGKVLATGTPQEL 231
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADR---ILVFDNGRVVESGSFDEL 556

                 ....*
gi 15600424  232 RERTG 236
Cdd:PRK13657 557 VARGG 561
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
23-191 2.29e-13

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: 70.54  E-value: 2.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-------------MRDRRHR--------RAV 81
Cdd:COG4778  26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspreiLALRRRTigyvsqflRVI 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  82 cPRIaympqglgknlyPTLSVFENVdffGRLFGHDKAERERRIADLLQSTGLApfaER----PAGKLSGGMKQKLGLCCA 157
Cdd:COG4778 106 -PRV------------SALDVVAEP---LLERGVDREEARARARELLARLNLP---ERlwdlPPATFSGGEQQRVNIARG 166
                       170       180       190
                ....*....|....*....|....*....|....
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRA 191
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKA 200
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
27-255 3.16e-13

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 73.02  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRD-RRHRRAVCPRIAYMPQGLGKN-LYPTLSVFE 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY-LDGKPIDiRSPRDAIRAGIMLCPEDRKAEgIIPVHSVAD 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  105 NVDF-------FGRLFGHDKAERE---RRIADLLQSTglaPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 174
Cdd:PRK11288 351 NINIsarrhhlRAGCLINNRWEAEnadRFIRSLNIKT---PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  175 DPLSRNQFWELIGRIRAGreGMSVLVATAYMEE----AERfdwLVAMDDGKVLAtgtpqelrERTGTQSLESAFIAL-LP 249
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ--GVAVLFVSSDLPEvlgvADR---IVVMREGRIAG--------ELAREQATERQALSLaLP 494

                 ....*.
gi 15600424  250 ESKRAG 255
Cdd:PRK11288 495 RTSAAV 500
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
19-199 3.29e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 69.45  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRH--RRAVCpriaYMPQGLGknL 96
Cdd:PRK13538  12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyHQDLL----YLGHQPG--I 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   97 YPTLSVFENVDFFGRLfgHDKAERERrIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK13538  86 KTELTALENLRFYQRL--HGPGDDEA-LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
                        170       180
                 ....*....|....*....|...
gi 15600424  177 LSRNQFWELIGRiRAGREGMSVL 199
Cdd:PRK13538 163 QGVARLEALLAQ-HAEQGGMVIL 184
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
289-485 3.62e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 73.11  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD-----ASDMATrrrVGYMSQAFSLYAELS 363
Cdd:PRK10762  19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkSSQEAG---IGIIHQELNLIPQLT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLVLhARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK10762  96 IAENIFL-GREFVNRFGRIDwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15600424  439 VARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLA 485
Cdd:PRK10762 175 TETESLFRVIREL-KSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIA 221
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
285-484 3.67e-13

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 71.68  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPV-DASDMATRR-RVGYMSQAF--- 356
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlNLPEKELNKlRAEQISMIFqdp 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  357 --SLYAELSVRQNLV----LHARLFHLPAdgiparVGEMLRRFDLEKVADE------LPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK09473 107 mtSLNPYMRVGEQLMevlmLHKGMSKAEA------FEESVRMLDAVKMPEArkrmkmYPHEFSGGMRQRVMIAMALLCRP 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424  425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQRCDRISLMHAGKVL 484
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
ABC2_membrane pfam01061
ABC-2 type transporter;
729-879 3.77e-13

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 69.22  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   729 LLLIMIPAMLTALGVVREKELGSITNLYVTPV-TRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPL-KGSFLALTIG 806
Cdd:pfam01061  53 SILFNAFSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPsAGRFFLFLLV 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424   807 AFLYVVTSTGLGLFLSTFMRSQIAAVFgVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGA 879
Cdd:pfam01061 133 LLLTALAASSLGLFISALAPSFEDASQ-LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
289-497 4.69e-13

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 73.07  E-value: 4.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDM---ATRRRVGYMSQAFSLYAElSVR 365
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTVtraSLRRNIAVVFQDAGLFNR-SIE 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  366 QNLVL------HARLfhLPADGIPARVGEMLRRFD-LEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK13657 427 DNIRVgrpdatDEEM--RAAAERAQAHDFIERKPDgYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  439 VARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:PRK13657 505 ETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
10-236 5.71e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 72.70  E-value: 5.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAvcpriaym 88
Cdd:PRK10522 324 ELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAEQPED-------- 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   89 pqglgknlYPTL--SVFENVDFFGRLFGHDKAERERRIADL-LQSTGLAPFAERPAG-----KLSGGMKQKLGLCCALIH 160
Cdd:PRK10522 395 --------YRKLfsAVFTDFHLFDQLLGPEGKPANPALVEKwLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAE 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  161 DPDLLILDEPTTGVDPLSRNQFW-ELIGRIRAgrEGMSVLVAT---AYMEEAERfdwLVAMDDGkvlatgtpqELRERTG 236
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYqVLLPLLQE--MGKTIFAIShddHYFIHADR---LLEMRNG---------QLSELTG 532
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
27-175 6.91e-13

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 69.04  E-value: 6.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPR-IAYMPQGLgkNLYPTLSVF 103
Cdd:PRK10584  29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAKLRAKhVGFVFQSF--MLIPTLNAL 106
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  104 ENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK10584 107 ENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
27-244 9.60e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 69.19  E-value: 9.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGArKMQDGEIRVLDGDMRDRRHRRAVCPRiAYMPQglGKNLYPTLSVFENV 106
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR-AYLSQ--QQTPPFAMPVFQYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  107 DffgrLFGHDKA---ERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH-DPD------LLILDEPTTGVDP 176
Cdd:PRK03695  91 T----LHQPDKTrteAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDinpagqLLLLDEPMNSLDV 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  177 LSRNQFWELIGRIraGREGMSVLVAT----AYMEEAERFdWLVAmdDGKVLATGTPQE-LRERTGTQSLESAF 244
Cdd:PRK03695 167 AQQAALDRLLSEL--CQQGIAVVMSShdlnHTLRHADRV-WLLK--QGKLLASGRRDEvLTPENLAQVFGVNF 234
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
273-498 1.14e-12

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 71.80  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  273 IAIEAEGLT-CRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGTCALFGQPVDASDMAT-RRRVG 350
Cdd:PRK11174 348 VTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESwRKHLS 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  351 YMSQAFSLYAElSVRQNLVLHArlfhlpADGIPARVGEMLRRFDLEKVADELPN--DLPLGIR---------QRLSLAVA 419
Cdd:PRK11174 427 WVGQNPQLPHG-TLRDNVLLGN------PDASDEQLQQALENAWVSEFLPLLPQglDTPIGDQaaglsvgqaQRLALARA 499
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424  420 VIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
278-494 1.59e-12

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 69.77  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  278 EGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGTCALFGQPVDASDMATRRR--- 348
Cdd:PRK11022   7 DKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRVMAEKLEFNGQDLQRISEKERrnl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  349 ----VGYMSQ------------AFSLYAELSVRQ---NLVLHARLFHLPAD-GIParvgemlrrfDLEKVADELPNDLPL 408
Cdd:PRK11022  87 vgaeVAMIFQdpmtslnpcytvGFQIMEAIKVHQggnKKTRRQRAIDLLNQvGIP----------DPASRLDVYPHQLSG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  409 GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQRCDRISLMHAGKVLASD 487
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETG 236

                 ....*..
gi 15600424  488 TPDELVR 494
Cdd:PRK11022 237 KAHDIFR 243
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
5-175 1.62e-12

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 71.29  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    5 GSGVASLRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCP 83
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR-LDGRPLSSLSHSVLRQ 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   84 RIAYMPQGlgknlyPTL---SVFENVDfFGRLFGhdkaerERRIADLLQSTGLAPFAER-PAG----------KLSGGMK 149
Cdd:PRK10790 416 GVAMVQQD------PVVladTFLANVT-LGRDIS------EEQVWQALETVQLAELARSlPDGlytplgeqgnNLSVGQK 482
                        170       180
                 ....*....|....*....|....*.
gi 15600424  150 QKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANID 508
PLN03232 PLN03232
ABC transporter C family member; Provisional
264-497 1.69e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 71.93  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   264 RPQSEGAPRIAIEAEGLTCRF-GDFVAVDH-VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAS 341
Cdd:PLN03232 1224 RPVSGWPSRGSIKFEDVHLRYrPGLPPVLHgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF 1303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   342 DMATRRRV-GYMSQAFSLYAElSVRQNLVLHARlfHLPADGIPA----RVGEMLRR--FDLEKVADELPNDLPLGIRQRL 414
Cdd:PLN03232 1304 GLTDLRRVlSIIPQSPVLFSG-TVRFNIDPFSE--HNDADLWEAleraHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLL 1380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   415 SLAVAVIHKPEILILDEPTSGVDpVARDGFWELMVELSRRDgVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVR 494
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVD-VRTDSLIQRTIREEFKS-CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458

                  ...
gi 15600424   495 QRG 497
Cdd:PLN03232 1459 RDT 1461
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
8-210 2.85e-12

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 67.88  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLagaRKMQDGEIRV-LDGDMRDRRHRrAVCPR-- 84
Cdd:PRK14239   5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI---NRMNDLNPEVtITGSIVYNGHN-IYSPRtd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   85 -------IAYMPQGlgKNLYPtLSVFENVDFFGRLFG-HDKA------ERERRIA-------DLLQSTGLApfaerpagk 143
Cdd:PRK14239  81 tvdlrkeIGMVFQQ--PNPFP-MSIYENVVYGLRLKGiKDKQvldeavEKSLKGAsiwdevkDRLHDSALG--------- 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  144 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAER 210
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL---KDDYTMLLVTRSMQQASR 212
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
10-186 2.93e-12

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 70.22  E-value: 2.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRA-VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrhRRAVCPRIAYM 88
Cdd:COG4178 364 ALEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA------RVLFLPQRPYL 437
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 PQG-----LgknLYPtlsvfenvdffgrlfGHDKAERERRIADLLQSTGLAPFAERP------AGKLSGGMKQKLGLCCA 157
Cdd:COG4178 438 PLGtlreaL---LYP---------------ATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARL 499
                       170       180
                ....*....|....*....|....*....
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELI 186
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLL 528
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
290-492 3.68e-12

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 69.73  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGTCALFGQPVDASDMATRRRV--GYMSQAF-----S 357
Cdd:PRK15134  25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgNKIAMIFqepmvS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  358 LYAELSVRQNL--VLharLFHLPADGIPARvGEMLR---RFDLEKVADEL---PNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:PRK15134 105 LNPLHTLEKQLyeVL---SLHRGMRREAAR-GEILNcldRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIA 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
287-484 3.82e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 68.19  E-value: 3.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  287 FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALF-------GQPVDASDMAT-------------- 345
Cdd:PRK13651  20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkKKTKEKEKVLEklviqktrfkkikk 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  346 ----RRRVGYMSQaFSLYA--ELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAV 418
Cdd:PRK13651 100 ikeiRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAG 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEA-QRCDRISLMHAGKVL 484
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVlEWTKRTIFFKDGKII 244
GguA NF040905
sugar ABC transporter ATP-binding protein;
11-483 5.15e-12

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.43  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG--ARKMQDGEIrVLDG------DMRDRRHRravc 82
Cdd:NF040905   4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyPHGSYEGEI-LFDGevcrfkDIRDSEAL---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   83 pRIAYMPQGLGknLYPTLSVFENVdFFGRLFGH----DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCAL 158
Cdd:NF040905  79 -GIVIIHQELA--LIPYLSIAENI-FLGNERAKrgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  159 IHDPDLLILDEPTTGV-DPLSRNqFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATgtpqeLRERTG 236
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAA-LLDLLLELKA--QGITSIIISHKLNEIRRVaDSITVLRDGRTIET-----LDCRAD 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  237 TQSlESAFIALLpeSKRAGHHRLviPPRpqsegAPRI---AIEAEGLTCR---FGDFVAVDHVSFRIERGEIFGFLGSNG 310
Cdd:NF040905 227 EVT-EDRIIRGM--VGRDLEDRY--PER-----TPKIgevVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMG 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  311 CGKsTTMKMltGLLPAS-----EGTCALFGQPVDASDM--ATRRRVGYMSQ---AFSLYAELSVRQNLVLhARLFHLPAD 380
Cdd:NF040905 297 AGR-TELAM--SVFGRSygrniSGTVFKDGKEVDVSTVsdAIDAGLAYVTEdrkGYGLNLIDDIKRNITL-ANLGKVSRR 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  381 GIPARVGEMlrrfdleKVADELPNDLPL---GIRQ---RLS--------LAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:NF040905 373 GVIDENEEI-------KVAEEYRKKMNIktpSVFQkvgNLSggnqqkvvLSKWLFTDPDVLILDEPTRGIDVGAKYEIYT 445
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 15600424  447 LMVELSRRDGVTIFISTHfMNEA-QRCDRISLMHAGKV 483
Cdd:NF040905 446 IINELAAEGKGVIVISSE-LPELlGMCDRIYVMNEGRI 482
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
263-462 6.82e-12

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 69.07  E-value: 6.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 263 PRPQSEGAPRI------AIEAEGLTCRFGDF-VAVDHVSFRIERGEifGFL--GSNGCGKSTTMKMLTGLLPASEGTCAL 333
Cdd:COG4178 345 ADALPEAASRIetsedgALALEDLTLRTPDGrPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR 422
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 334 fgqPVDASDMatrrrvgYMSQafSLYAEL-SVRQNLvlharLFHLPADGIP-ARVGEMLRRFDLEKVADEL------PND 405
Cdd:COG4178 423 ---PAGARVL-------FLPQ--RPYLPLgTLREAL-----LYPATAEAFSdAELREALEAVGLGHLAERLdeeadwDQV 485
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 406 LPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVElsRRDGVTIfIS 462
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTV-IS 539
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
10-233 7.20e-12

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: 65.24  E-value: 7.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG--ARKMQDGEIRvLDG----DMR-DRRHRRavc 82
Cdd:cd03217   2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEIL-FKGeditDLPpEERARL--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  83 priaympqGLgknlypTLSVFENVDFFGRlfghdkaererRIADLLQSTGLapfaerpagKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03217  78 --------GI------FLAFQYPPEIPGV-----------KNADFLRYVNE---------GFSGGEKKRNEILQLLLLEP 123
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAE--RFDWLVAMDDGKVLATGTPQELRE 233
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLR--EEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALE 194
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
289-493 1.31e-11

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 66.75  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCA--LFGQPVDASDMATRRR---VGY-MSQAFS----- 357
Cdd:PRK15093  22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTAdrMRFDDIDLLRLSPRERrklVGHnVSMIFQepqsc 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  358 LYAELSVRQNLVlharlfhlpaDGIPA----------------RVGEMLRRF---DLEKVADELPNDLPLGIRQRLSLAV 418
Cdd:PRK15093 102 LDPSERVGRQLM----------QNIPGwtykgrwwqrfgwrkrRAIELLHRVgikDHKDAMRSFPYELTEGECQKVMIAI 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424  419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMlSQWADKINVLYCGQTVETAPSKELV 247
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
284-464 1.33e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 64.59  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  284 FGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELS 363
Cdd:PRK13540  11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  364 VRQNLvlharLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:PRK13540  91 LRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
                        170       180
                 ....*....|....*....|.
gi 15600424  444 FWElMVELSRRDGVTIFISTH 464
Cdd:PRK13540 166 IIT-KIQEHRAKGGAVLLTSH 185
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
23-231 1.39e-11

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 65.97  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD-----GDMRDRRHrravcpRIAYMPQGLGKNLY 97
Cdd:PRK15112  28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfGDYSYRSQ------RIRMIFQDPSTSLN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   98 PTLSVFENVDFFGRL-FGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK15112 102 PRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  176 PLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK15112 182 MSMRSQLINLMLELQE-KQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADV 237
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
22-266 1.90e-11

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 66.30  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   22 RAVDDVSLEIPANRMVGLIGPDGVGKS-SLLALLA----GARKMQDGeirvLDGDMRD------RRHRRAVCPRIAYMPQ 90
Cdd:PRK11022  21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGlidyPGRVMAEK----LEFNGQDlqriseKERRNLVGAEVAMIFQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   91 GLGKNLYPTLSV-FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAER----PAgKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK11022  97 DPMTSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvyPH-QLSGGMSQRVMIAMAIACRPKLL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYME-EAERFDWLVAMDDGKVLATGTPQELReRTGTQSLESAF 244
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQ-KENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHDIF-RAPRHPYTQAL 253
                        250       260       270
                 ....*....|....*....|....*....|
gi 15600424  245 IALLPESKrAGHHRL-----VIP---PRPQ 266
Cdd:PRK11022 254 LRALPEFA-QDKARLaslpgVVPgkyDRPN 282
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
275-495 2.62e-11

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: 63.70  E-value: 2.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLlPASE---GTCALFGQPVDASDMATRRRVG- 350
Cdd:cd03217   1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvteGEILFKGEDITDLPPEERARLGi 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSqafslyaelsvrqnlvlharlFHLPADgIPA-RVGEMLRrfdlekvadELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03217  80 FLA---------------------FQYPPE-IPGvKNADFLR---------YVNEGFSGGEKKRNEILQLLLLEPDLAIL 128
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 430 DEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHF--MNEAQRCDRISLMHAGKVLASDtPDELVRQ 495
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYqrLLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
265-494 3.28e-11

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 67.19  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  265 PQSEGAP-RIAIEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalfgqpVD 339
Cdd:PRK10261   2 PHSDELDaRDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGL-------VQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  340 ASDMATRRR------VGYMSQA------------------FSLYAELSVRQNLV----LHARLFHLPADGIPARVGEMLR 391
Cdd:PRK10261  75 CDKMLLRRRsrqvieLSEQSAAqmrhvrgadmamifqepmTSLNPVFTVGEQIAesirLHQGASREEAMVEAKRMLDQVR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  392 RFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQ 470
Cdd:PRK10261 155 IPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAE 234
                        250       260
                 ....*....|....*....|....
gi 15600424  471 RCDRISLMHAGKVLASDTPDELVR 494
Cdd:PRK10261 235 IADRVLVMYQGEAVETGSVEQIFH 258
PLN03130 PLN03130
ABC transporter C family member; Provisional
292-493 4.06e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 67.46  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpVDASDMAT------RRRVGYMSQAFSLYAElSVR 365
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-----IDGCDISKfglmdlRKVLGIIPQAPVLFSG-TVR 1330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   366 QNLVLHARlfHLPADGIP----ARVGEMLRR--FDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpV 439
Cdd:PLN03130 1331 FNLDPFNE--HNDADLWEslerAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-V 1407
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424   440 ARDGfweLMVELSRRD--GVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PLN03130 1408 RTDA---LIQKTIREEfkSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
24-247 5.54e-11

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 63.95  E-value: 5.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   24 VDDVSLEIPANRMVGLIGPDGVGKS-SLLALL----AGARKMQdGEIRvLDG------DMRDRrHRRAVC--PRIAYMP- 89
Cdd:PRK10418  19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTA-GRVL-LDGkpvapcALRGR-KIATIMqnPRSAFNPl 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QGLGKNLYPTLSVFenvdffgrlfghDKAERERRIADLLQSTGLAP---FAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:PRK10418  96 HTMHTHARETCLAL------------GKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  167 LDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTG---TQSLES 242
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKR-ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKhavTRSLVS 242

                 ....*
gi 15600424  243 AFIAL 247
Cdd:PRK10418 243 AHLAL 247
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
274-492 5.64e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 64.35  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-----TCALFGQPV-DASD-MATR 346
Cdd:PRK14271  21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDvLEFR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  347 RRVGYMSQAFSLYAeLSVRQNLVLHARLFHL-PADGIPARVGEMLRRFDL-EKVADEL---PNDLPLGIRQRLSLAVAVI 421
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLA 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  422 HKPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
PLN03211 PLN03211
ABC transporter G-25; Provisional
300-464 5.67e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 66.44  E-value: 5.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  300 GEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMatrRRVGYMSQAFSLYAELSVRQNLVLHArLFHL 377
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL---KRTGFVTQDDILYPHLTVRETLVFCS-LLRL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  378 P-----------ADGIPARVGemLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:PLN03211 170 PksltkqekilvAESVISELG--LTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
                        170
                 ....*....|....*...
gi 15600424  447 LMVELSRRdGVTIFISTH 464
Cdd:PLN03211 248 TLGSLAQK-GKTIVTSMH 264
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
7-228 7.38e-11

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 62.81  E-value: 7.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   7 GVASLRGVSLRYGE--TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD---RRHRRav 81
Cdd:cd03369   5 GEIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiplEDLRS-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  82 cpRIAYMPQGlgknlyPTL---SVFENVDFFGRLfghdkAERERRIADLLQSTGLapfaerpagKLSGGMKQKLGLCCAL 158
Cdd:cd03369  83 --SLTIIPQD------PTLfsgTIRSNLDPFDEY-----SDEEIYGALRVSEGGL---------NLSQGQRQLLCLARAL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRnqfwELIGR-IRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTP 228
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATD----ALIQKtIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
NatB COG1668
ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ...
578-908 7.40e-11

ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 441274 [Multi-domain]  Cd Length: 402  Bit Score: 65.32  E-value: 7.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 578 MFIIGYGINMDVEDLSWAVLDRDQTTTSQAYALNIAGSryFVEHAPITDPDDLDRRLRSGELSLAVEIPPNFGRDlkrgS 657
Cdd:COG1668  37 GLGMLFMSGNDDEPLKVAVVDESGAPALAEALKEAAVN--FEVVPEVADEEEAEAAVEDGEIDAVLVIPEDFSLE----N 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 658 DPAIGVWIDGAMPTRANTVL-GYVQGLHTSYLAD---LSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPAVIPLLL-- 731
Cdd:COG1668 111 PATVELYSDSSPDSSAVSRLeSALSQALLALRLAalgLDPEQLQALLAPVSVETVDLSKASPEEGAGYILGYLLPFLLym 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 732 -IMIPAMLTALGVVREKELGSITNLyVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFR------------VPLKG 798
Cdd:COG1668 191 fIFTYGSMIADSVAEEKESRTLEIL-LSSVSPRQLLLGKILGIGLVGLTQALLWLVGGLIGLLlasglglsalsgLNLSP 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 799 SFLALTI-----GAFLYVVTSTGLGLFLSTFMRSQiAAVFGVAIATMIPA-IQFSGLIHPVSSLEGAAAWIgklyP-TSH 871
Cdd:COG1668 270 GLLLLFLlffllGYLLYAALFAALGALASSFKEAQ-QYLSPLTLLLMIPFfVAMFVLSNPDGPLATVLSLI----PfTSP 344
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15600424 872 FLVVSRGAFSkSLGLSDLWAYYLPLAASIVVLTLLSV 908
Cdd:COG1668 345 ILMPLRLALG-EVPWWEILLSLALLLATAVLLLWLAA 380
hmuV PRK13547
heme ABC transporter ATP-binding protein;
288-494 8.09e-11

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 63.69  E-value: 8.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--------EGTCALFGQP---VDASDMATRRRVgyMSQAF 356
Cdd:PRK13547  15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlaaIDAPRLARLRAV--LPQAA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  357 SLYAELSVRQnLVLHARLFHLPADGIPAR-----VGEMLRRFDLEKVADELPNDLPLGIRQRLSLA--VAVIHK------ 423
Cdd:PRK13547  93 QPAFAFSARE-IVLLGRYPHARRAGALTHrdgeiAWQALALAGATALVGRDVTTLSGGELARVQFArvLAQLWPphdaaq 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  424 -PEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:PRK13547 172 pPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLT 244
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
264-438 9.10e-11

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 62.56  E-value: 9.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  264 RPQSEGAPRIAieAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM 343
Cdd:PRK13543   3 EPLHTAPPLLA--AHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  344 AtrRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIParvGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHK 423
Cdd:PRK13543  81 S--RFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
                        170
                 ....*....|....*
gi 15600424  424 PEILILDEPTSGVDP 438
Cdd:PRK13543 156 APLWLLDEPYANLDL 170
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
275-484 9.45e-11

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 63.26  E-value: 9.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLT---GLLPASEGTCA-------LFGQPVDASDMa 344
Cdd:PRK14239   6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEVTITGSivynghnIYSPRTDTVDL- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  345 tRRRVGYMSQAFSLYAeLSVRQNLVLHARLfhlpaDGIP------ARVGEMLRRFDL-EKVADELpNDLPLGI----RQR 413
Cdd:PRK14239  85 -RKEIGMVFQQPNPFP-MSIYENVVYGLRL-----KGIKdkqvldEAVEKSLKGASIwDEVKDRL-HDSALGLsggqQQR 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLI 226
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
5-175 9.91e-11

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: 65.34  E-value: 9.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     5 GSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDmrdrrhrrAVcpR 84
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GE--------TV--K 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    85 IAYMPQGLgKNLYPTLSVFE------------NVDFFGR----LFGHDKAERERRIadllqstglapfaerpaGKLSGGM 148
Cdd:TIGR03719 387 LAYVDQSR-DALDPNKTVWEeisggldiiklgKREIPSRayvgRFNFKGSDQQKKV-----------------GQLSGGE 448
                         170       180
                  ....*....|....*....|....*..
gi 15600424   149 KQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD 475
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
8-223 1.03e-10

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 62.67  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQD--GEIRVLDGDmrdrrhrravcpri 85
Cdd:COG2401  30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPvaGCVDVPDNQ-------------- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  86 aympqglgknLYPTLSVFENVDFFGRLfgHDKAErerriadLLQSTGL--APFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:COG2401  96 ----------FGREASLIDAIGRKGDF--KDAVE-------LLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPK 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 164 LLILDEPTTGVDP-----LSRNqfwelIGRIrAGREGMSVLVATAYME--EAERFDWLVAMDDGKVL 223
Cdd:COG2401 157 LLVIDEFCSHLDRqtakrVARN-----LQKL-ARRAGITLVVATHHYDviDDLQPDLLIFVGYGGVP 217
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
291-481 1.07e-10

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 61.88  E-value: 1.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASdmaTRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:cd03232  24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKN---FQRSTGYVEQQDVHSPNLTVREAL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 VLHArlfhlpadgiparvgeMLRRFDLEKvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTSGVDPVARdgfWELM 448
Cdd:cd03232 101 RFSA----------------LLRGLSVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAA---YNIV 148
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15600424 449 VELSR--RDGVTIFISTHFMNEA--QRCDRISLMHAG 481
Cdd:cd03232 149 RFLKKlaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
289-483 1.62e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 64.53  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalfgqpVDASDMATRRRVGYmsqafSLYAELSVRQNL 368
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-------VDIKGSAALIAISS-----GLNGQLTGIENI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15600424  449 VELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK13545 187 NEF-KEQGKTIFFISHSLSQVKSfCTKALWLHYGQV 221
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
26-226 2.04e-10

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 63.35  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP---RIAYMPQGlgKNLYPTLSV 102
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPekrRIGYVFQD--ARLFPHYKV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  103 FENVdffgrLFGHDKAERER--RIADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDpLSRN 180
Cdd:PRK11144  94 RGNL-----RYGMAKSMVAQfdKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRK 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15600424  181 QfwELIGRI-RAGRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:PRK11144 165 R--ELLPYLeRLAREiNIPILYVSHSLDEILRLaDRVVVLEQGKVKAFG 211
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
23-169 2.20e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 64.14  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrdrrhrRAVCPRIAympqgLGKNLYPTLSV 102
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIA-----ISSGLNGQLTG 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
285-437 2.77e-10

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 64.36  E-value: 2.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKML-----TGLLpaSEGTCALFGQPVDASdmaTRRRVGYMSQAFSLY 359
Cdd:TIGR00956  774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSS---FQRSIGYVQQQDLHL 848
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    360 AELSVRQNLVLHARLfHLPADgIPAR-----VGEMLRRFDLEKVADELPNDLPLGI----RQRLSLAVAVIHKPEILI-L 429
Cdd:TIGR00956  849 PTSTVRESLRFSAYL-RQPKS-VSKSekmeyVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfL 926

                   ....*...
gi 15600424    430 DEPTSGVD 437
Cdd:TIGR00956  927 DEPTSGLD 934
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
264-497 3.24e-10

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 63.97  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  264 RPQSEGapRIAIEAEGLTCRfGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SD 342
Cdd:PRK10790 334 RPLQSG--RIDIDNVSFAYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSH 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  343 MATRRRVGYMSQ-----AFSLYA---------ELSVRQNL--VLHARLFHLPADGIPARVGEMlrrfdlekvadelPNDL 406
Cdd:PRK10790 411 SVLRQGVAMVQQdpvvlADTFLAnvtlgrdisEEQVWQALetVQLAELARSLPDGLYTPLGEQ-------------GNNL 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  407 PLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQRCDRISLMHAGKVLAS 486
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVEADTILVLHRGQAVEQ 555
                        250
                 ....*....|.
gi 15600424  487 DTPDELVRQRG 497
Cdd:PRK10790 556 GTHQQLLAAQG 566
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
7-236 3.33e-10

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 63.88  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    7 GVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRDRRHRravcp 83
Cdd:PRK11176 340 GDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI-LLDGhDLRDYTLA----- 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   84 riaympqglgkNLYPTLS-VFENVDFF------------GRLFGHDKAERERRIA---DLLQS--TGLAPFAERPAGKLS 145
Cdd:PRK11176 414 -----------SLRNQVAlVSQNVHLFndtianniayarTEQYSREQIEEAARMAyamDFINKmdNGLDTVIGENGVLLS 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  146 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR---TSLVIAHRLSTIEKADEILVVEDGEIVER 559
                        250
                 ....*....|.
gi 15600424  226 GTPQELRERTG 236
Cdd:PRK11176 560 GTHAELLAQNG 570
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
185-498 3.51e-10

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 64.20  E-value: 3.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    185 LIGR--IRAGREGMSV---LVATAYMeeaerfDWLVAMDDGKVLATGTPQELRERTGTQSlESAFIallpeskraghhrl 259
Cdd:TIGR00957 1211 VISRhsLSAGLVGLSVsysLQVTFYL------NWLVRMSSEMETNIVAVERLKEYSETEK-EAPWQ-------------- 1269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    260 VIPPRPQSEGAPRIAIEAEGLTCRFG---DFVaVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGq 336
Cdd:TIGR00957 1270 IQETAPPSGWPPRGRVEFRNYCLRYRedlDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG- 1347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    337 pVDASDMAT---RRRVGYMSQ--------------AFSLYAELSVRQNLVL-HARLFhlpADGIPARvgemlrrfdLEKV 398
Cdd:TIGR00957 1348 -LNIAKIGLhdlRFKITIIPQdpvlfsgslrmnldPFSQYSDEEVWWALELaHLKTF---VSALPDK---------LDHE 1414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    399 ADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpVARDGFWELMVElSRRDGVTIFISTHFMNEAQRCDRISLM 478
Cdd:TIGR00957 1415 CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD-LETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDYTRVIVL 1492
                          330       340
                   ....*....|....*....|
gi 15600424    479 HAGKVLASDTPDELVRQRGL 498
Cdd:TIGR00957 1493 DKGEVAEFGAPSNLLQQRGI 1512
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
26-236 4.23e-10

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 63.59  E-value: 4.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRD------RRHRRAVcpriAYMPQGLGKnlyp 98
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-LLDGvPLVQydhhylHRQVALV----GQEPVLFSG---- 569
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    99 tlSVFENVdffgrLFGHDKAERERRIADLLQSTGLAPFAERPAG----------KLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:TIGR00958 570 --SVRENI-----AYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsQLSGGQKQRIAIARALVRKPRVLILD 642
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424   169 EPTTGVDPLSRNQFWELigrirAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:TIGR00958 643 EATSALDAECEQLLQES-----RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
18-202 4.72e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 59.96  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   18 YGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMrdRRHRRAVCPRIAYMPQGLGKNly 97
Cdd:PRK13540  11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHRSGIN-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   98 PTLSVFENVdffgrLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 177
Cdd:PRK13540  87 PYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
                        170       180
                 ....*....|....*....|....*.
gi 15600424  178 SrnqFWELIGRIRAGR-EGMSVLVAT 202
Cdd:PRK13540 162 S---LLTIITKIQEHRaKGGAVLLTS 184
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
14-231 6.09e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 61.27  E-value: 6.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   14 VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLagaRKMQD--------GEIRVLDGDMRDRRHRRAVCPRI 85
Cdd:PRK14271  27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL---NRMNDkvsgyrysGDVLLGGRSIFNYRDVLEFRRRV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   86 AYMPQGlgKNLYPtLSVFENVdfFGRLFGHDKAERE--RRIADL-LQSTGL----------APFaerpagKLSGGMKQKL 152
Cdd:PRK14271 104 GMLFQR--PNPFP-MSIMDNV--LAGVRAHKLVPRKefRGVAQArLTEVGLwdavkdrlsdSPF------RLSGGQQQLL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELigrIRAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF---IRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQL 249
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
275-467 8.02e-10

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 62.22  E-value: 8.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALfgqpvDASDmatrrRVGYMSQ 354
Cdd:PRK15064   2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-----DPNE-----RLGKLRQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  355 AFSLYAELSVRQNLVL-HA----------RLFHLP----ADGIpaRVGEMLRRF------DLEKVADELPndLPLGI--- 410
Cdd:PRK15064  72 DQFAFEEFTVLDTVIMgHTelwevkqerdRIYALPemseEDGM--KVADLEVKFaemdgyTAEARAGELL--LGVGIpee 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  411 -------------RQRLSLAVAVIHKPEILILDEPTSGVD-PVARdgfWeLMVELSRRDGVTIFIS--THFMN 467
Cdd:PRK15064 148 qhyglmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLDiNTIR---W-LEDVLNERNSTMIIIShdRHFLN 216
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
22-175 9.16e-10

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 61.26  E-value: 9.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRH--RRAVCPRIAYMPQGLGKNLYPT 99
Cdd:PRK15079  35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSDIQMIFQDPLASLNPR 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  100 LSVFENV-----DFFGRLfghDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 173
Cdd:PRK15079 115 MTIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191

                 ..
gi 15600424  174 VD 175
Cdd:PRK15079 192 LD 193
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
256-464 1.07e-09

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 59.59  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 256 HHRLVIPPRPQSegapRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfg 335
Cdd:COG2401  16 VYSSVLDLSERV----AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC--- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 336 qpVDASDMatrrrvgymsqafSLYAELSVRQNlVLHARLFHLpADGIPARVG-----EMLRRFdlekvaDELPNdlplGI 410
Cdd:COG2401  89 --VDVPDN-------------QFGREASLIDA-IGRKGDFKD-AVELLNAVGlsdavLWLRRF------KELST----GQ 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 411 RQRLSLAVAVIHKPEILILDEPTSGVDP-----VARDgfwelMVELSRRDGVTIFISTH 464
Cdd:COG2401 142 KFRFRLALLLAERPKLLVIDEFCSHLDRqtakrVARN-----LQKLARRAGITLVVATH 195
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
14-202 1.17e-09

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 59.50  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   14 VSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRavcprIAYMPQGL 92
Cdd:PRK10908   7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE-----VPFLRRQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   93 G-----KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK10908  82 GmifqdHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15600424  168 DEPTTGVDplsrNQFWELIGRI--RAGREGMSVLVAT 202
Cdd:PRK10908 162 DEPTGNLD----DALSEGILRLfeEFNRVGVTVLMAT 194
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
23-169 1.30e-09

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 59.83  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRdrrhrravcprIAYMPQGLGKNLyptlSV 102
Cdd:PRK13546  39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-RNGEVS-----------VIAISAGLSGQL----TG 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
302-487 1.34e-09

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 61.04  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  302 IFGFLGSngcGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-----RRRVGYMSQAFSLYAELSVRQNLvlharlfh 376
Cdd:PRK11144  29 IFGRSGA---GKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQDARLFPHYKVRGNL-------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  377 lpadgipaRVG---EMLRRFD-------LEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD-PVARdgfw 445
Cdd:PRK11144  98 --------RYGmakSMVAQFDkivallgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR---- 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15600424  446 ELMV---ELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASD 487
Cdd:PRK11144 166 ELLPyleRLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
11-202 1.45e-09

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 59.34  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGD----MRDRRHRRAVcpriA 86
Cdd:PRK10247  10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LFEGEdistLKPEIYRQQV----S 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   87 YMPQGlgknlyPTL---SVFENVdFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK10247  85 YCAQT------PTLfgdTVYDNL-IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15600424  164 LLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVAT 202
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRY-VREQNIAVLWVT 195
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
25-175 1.79e-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: 59.34  E-value: 1.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  25 DDVSLEIPA-----NRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLdgdmrdrrhrravCPRIAYMPQGLgKNLYPT 99
Cdd:cd03237  11 GEFTLEVEGgsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-------------LDTVSYKPQYI-KADYEG 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 100 lsvfeNVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:cd03237  77 -----TVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
297-437 3.12e-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: 58.57  E-value: 3.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 297 IERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvdasdmatrrRVGYMSQAFSLYAELSVRQNLVlharlfh 376
Cdd:cd03237  22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-----------TVSYKPQYIKADYEGTVRDLLS------- 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 377 lpadGIPARVG-------EMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03237  84 ----SITKDFYthpyfktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
10-175 3.60e-09

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 58.40  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI--RVLDGDMRD------RRHRRAV 81
Cdd:PRK11701   8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLRDlyalseAERRRLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   82 CPRIAYMPQGLGKNLYPTLSVFENVdffG-RLF--GHDKAERERRIA-DLLQSTGLAP--FAERPAgKLSGGMKQKLGLC 155
Cdd:PRK11701  88 RTEWGFVHQHPRDGLRMQVSAGGNI---GeRLMavGARHYGDIRATAgDWLERVEIDAarIDDLPT-TFSGGMQQRLQIA 163
                        170       180
                 ....*....|....*....|
gi 15600424  156 CALIHDPDLLILDEPTTGVD 175
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLD 183
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
289-497 4.28e-09

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 60.11  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYMSQAFSLYAElSVRQN 367
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdSWRSRLAVVSQTPFLFSD-TVANN 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  368 LVL-------------------HARLFHLPaDGIPARVGE---MLRRfdlekvadelpndlplGIRQRLSLAVAVIHKPE 425
Cdd:PRK10789 409 IALgrpdatqqeiehvarlasvHDDILRLP-QGYDTEVGErgvMLSG----------------GQKQRISIARALLLNAE 471
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424  426 ILILDEPTSGVDPVARdgfWELMVELSR-RDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:PRK10789 472 ILILDDALSAVDGRTE---HQILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
290-462 5.41e-09

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: 56.01  E-value: 5.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCalfgqpvdasDMATRRRVGYMSQAfSLYAELSVRQNLV 369
Cdd:cd03223  17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLLFLPQR-PYLPLGTLREQLI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 LharlfhlPADGIparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:cd03223  86 Y-------PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
                       170
                ....*....|...
gi 15600424 450 ELSrrdgvTIFIS 462
Cdd:cd03223 136 ELG-----ITVIS 143
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
26-228 5.81e-09

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: 58.01  E-value: 5.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  26 DVSLEIPANRMVGLIGPDGVGKSSL--------LALLAGARKMQDGE------------IRVLDGDMRDRRHR------- 78
Cdd:cd03271  13 NIDVDIPLGVLTCVTGVSGSGKSSLindtlypaLARRLHLKKEQPGNhdrieglehidkVIVIDQSPIGRTPRsnpatyt 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  79 ------RA----VCPRIAYMPQGL-----GKNLYPTL--SVFENVDFFgrlfghDKAERERRIADLLQSTGLAPFA-ERP 140
Cdd:cd03271  93 gvfdeiRElfceVCKGKRYNRETLevrykGKSIADVLdmTVEEALEFF------ENIPKIARKLQTLCDVGLGYIKlGQP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 141 AGKLSGGMKQKLGLCCALiHDPD----LLILDEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLVA 216
Cdd:cd03271 167 ATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDK--GNTVVVIEHNLDVIKCADWIID 243
                       250
                ....*....|....*...
gi 15600424 217 M------DDGKVLATGTP 228
Cdd:cd03271 244 LgpeggdGGGQVVASGTP 261
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
5-171 6.44e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 59.36  E-value: 6.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    5 GSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDmrdrrhrrAVcpR 84
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--GE--------TV--K 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   85 IAYMPQGLGkNLYPTLSVFENV-DffgrlfGHD-----KAERERRiadllqsTGLAPFA------ERPAGKLSGGMKQKL 152
Cdd:PRK11819 389 LAYVDQSRD-ALDPNKTVWEEIsG------GLDiikvgNREIPSR-------AYVGRFNfkggdqQKKVGVLSGGERNRL 454
                        170
                 ....*....|....*....
gi 15600424  153 GLCCALIHDPDLLILDEPT 171
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPT 473
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
293-481 9.38e-09

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 59.54  E-value: 9.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpvdasdmatrrRVGYMSQaFSLYAELSVRQNLvlha 372
Cdd:TIGR01271  445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQ-TSWIMPGTIKDNI---- 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    373 rLFHLPADGIpaRVGEMLRRFDLEKVADELPN--DLPL---------GIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:TIGR01271  508 -IFGLSYDEY--RYTSVIKACQLEEDIALFPEkdKTVLgeggitlsgGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 15600424    442 DGFWE-----LMVELSRrdgvtiFISTHFMNEAQRCDRISLMHAG 481
Cdd:TIGR01271  585 KEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
21-171 1.01e-08

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: 59.03  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  21 TRAVDDVSLEIPANRM-----VGLIGPDGVGKSSLLALLAGARKMQDGEIrvlDGDMRdrrhrravcprIAYMPQglgkn 95
Cdd:COG1245 348 TKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK-----------ISYKPQ----- 408
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  96 lYPTLSVFENVDFFgrLFGHDKAERERRI--ADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:COG1245 409 -YISPDYDGTVEEF--LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
19-199 1.02e-08

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 57.99  E-value: 1.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARK---------MQDGEIRVLDGDMRDRRhrRAVCPRIAYMP 89
Cdd:COG4170  18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrFRWNGIDLLKLSPRERR--KIIGREIAMIF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  90 QGLGKNLYPTLSVFENV------DFFGRLFGHDKAERERRIADLLQSTGLA---------PFaerpagKLSGGMKQKLGL 154
Cdd:COG4170  96 QEPSSCLDPSAKIGDQLieaipsWTFKGKWWQRFKWRKKRAIELLHRVGIKdhkdimnsyPH------ELTEGECQKVMI 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15600424 155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVL 199
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQ-GTSIL 213
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
22-175 1.06e-08

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 58.05  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR-----VLDGDMRDRRHRR------------AVCPR 84
Cdd:PRK11308  29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdLLKADPEAQKLLRqkiqivfqnpygSLNPR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   85 iaympQGLGKNLYPTLSVfeNVDFfgrlfghDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK11308 109 -----KKVGQILEEPLLI--NTSL-------SAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPD 174
                        170
                 ....*....|..
gi 15600424  164 LLILDEPTTGVD 175
Cdd:PRK11308 175 VVVADEPVSALD 186
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
10-226 1.43e-08

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK 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 complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 56.76  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD--------MRDRRHRRAV 81
Cdd:TIGR02323   5 QVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSEAERRRLM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    82 CPRIAYMPQGLGKNLYPTLSVFENV-----DFFGRLFGHDKAERErriaDLLQSTGLAP--FAERPAgKLSGGMKQKLGL 154
Cdd:TIGR02323  85 RTEWGFVHQNPRDGLRMRVSAGANIgerlmAIGARHYGNIRATAQ----DWLEEVEIDPtrIDDLPR-AFSGGMQQRLQI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424   155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLV--RDlGLAVIIVTHDLGVARLLaQRLLVMQQGRVVESG 231
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
21-248 1.52e-08

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 58.77  E-value: 1.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmrdRRHRRAVCPRIAY-MPQGLGKNLypt 99
Cdd:TIGR01271  439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--------HSGRISFSPQTSWiMPGTIKDNI--- 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    100 lsvfenvdffgrLFGHDKAE-RERRIADLLQ-STGLAPFAER---PAGK----LSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:TIGR01271  508 ------------IFGLSYDEyRYTSVIKACQlEEDIALFPEKdktVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    171 TTGVDPLSRNQFWE------LIGRIRagregmsvLVATAYMEEAERFDWLVAMDDGKVLATGTPQELrertgtQSLESAF 244
Cdd:TIGR01271  576 FTHLDVVTEKEIFEsclcklMSNKTR--------ILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL------QAKRPDF 641

                   ....
gi 15600424    245 IALL 248
Cdd:TIGR01271  642 SSLL 645
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
6-175 1.83e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 58.04  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    6 SG--VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV---LDgdmrdrrhrra 80
Cdd:PRK11147 315 SGkiVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtkLE----------- 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   81 vcprIAYMPQgLGKNLYPTLSVFENVdffgrlfGHDKAE-----RERRIADLLQSTGLAPF-AERPAGKLSGGMKQKLGL 154
Cdd:PRK11147 384 ----VAYFDQ-HRAELDPEKTVMDNL-------AEGKQEvmvngRPRHVLGYLQDFLFHPKrAMTPVKALSGGERNRLLL 451
                        170       180
                 ....*....|....*....|.
gi 15600424  155 CCALIHDPDLLILDEPTTGVD 175
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD 472
PLN03130 PLN03130
ABC transporter C family member; Provisional
258-492 1.91e-08

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 58.60  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   258 RLVIPPRPQSEGAPRIAIeaegltcRFGDFV--------AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA-SE 328
Cdd:PLN03130  600 RVLLPNPPLEPGLPAISI-------KNGYFSwdskaerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSD 672
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   329 GTCALfgqpvdasdmatRRRVGYMSQAfSLYAELSVRQNLvlharLFHLPADgiPARVGEMLRRFDLEKVADELPN---- 404
Cdd:PLN03130  673 ASVVI------------RGTVAYVPQV-SWIFNATVRDNI-----LFGSPFD--PERYERAIDVTALQHDLDLLPGgdlt 732
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   405 -------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP-VARDGFWE-LMVELSRRDGVTIFISTHFMNeaqRCDRI 475
Cdd:PLN03130  733 eigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKcIKDELRGKTRVLVTNQLHFLS---QVDRI 809
                         250
                  ....*....|....*..
gi 15600424   476 SLMHAGKVLASDTPDEL 492
Cdd:PLN03130  810 ILVHEGMIKEEGTYEEL 826
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
5-220 2.07e-08

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: 55.80  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   5 GSGVASLRGVSLRygetravddvsleIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-------RVLDGDMRDRRH 77
Cdd:cd03290  11 GSGLATLSNINIR-------------IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkneSEPSFEATRSRN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  78 RRAVcpriAYMPQglgKNLYPTLSVFENVDfFGRLFGHDKAERERRIADLLQSTGLAPFAERP-----AGKLSGGMKQKL 152
Cdd:cd03290  78 RYSV----AYAAQ---KPWLLNATVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRI 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVD-PLSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERFDWLVAMDDG 220
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLV-THKLQYLPHADWIIAMKDG 217
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
286-483 2.14e-08

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 56.36  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvdasdmatrrrVGYMSQAFSLYAELSVR 365
Cdd:PRK13546  36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------------VSVIAISAGLSGQLTGI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  366 QNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW 445
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15600424  446 ELMVELSRRDGvTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK13546 184 DKIYEFKEQNK-TIFFVSHNLGQVRQfCTKIAWIEGGKL 221
PLN03232 PLN03232
ABC transporter C family member; Provisional
6-237 2.30e-08

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 58.45  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     6 SGVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-----MRDRRHR 78
Cdd:PLN03232 1232 RGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfgLTDLRRV 1311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    79 RAVCPRIAYMPQGlgknlyptlSVFENVDFFGRLFGHD--KAERERRIADLLQSTGLAPFAERPAG--KLSGGMKQKLGL 154
Cdd:PLN03232 1312 LSIIPQSPVLFSG---------TVRFNIDPFSEHNDADlwEALERAHIKDVIDRNPFGLDAEVSEGgeNFSVGQRQLLSL 1382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   155 CCALIHDPDLLILDEPTTGVDPLSRNqfweLIGR-IRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRE 233
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDS----LIQRtIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458

                  ....
gi 15600424   234 RTGT 237
Cdd:PLN03232 1459 RDTS 1462
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
278-498 2.68e-08

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 58.00  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    278 EGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLpASEGTCALFGQPVDASDMAT-RRRVGYMSQ 354
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTwRKAFGVIPQ 1299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    355 AFSLYAElSVRQNLVLHARLfhlpADGIPARVGEmlrRFDLEKVADELPNDLPL-----------GIRQRLSLAVAVIHK 423
Cdd:TIGR01271 1300 KVFIFSG-TFRKNLDPYEQW----SDEEIWKVAE---EVGLKSVIEQFPDKLDFvlvdggyvlsnGHKQLMCLARSILSK 1371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    424 PEILILDEPTSGVDPVArdgfwelmVELSRR------DGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVT--------LQIIRKtlkqsfSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS 1443

                   .
gi 15600424    498 L 498
Cdd:TIGR01271 1444 L 1444
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
30-171 2.80e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.51  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   30 EIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvlDGDmrdrrhrravcPRIAYMPQglgknlYPTLSVFENVDFF 109
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPE-----------LKISYKPQ------YIKPDYDGTVEDL 420
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424  110 grLfghdkaereRRIADLLQST----------GLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK13409 421 --L---------RSITDDLGSSyykseiikplQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
10-222 5.18e-08

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 54.19  E-value: 5.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRA----VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ---DGEIRV--LDGDMRDRRHRRa 80
Cdd:cd03233   5 SWRNISFTTGKGRSkipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYngIPYKEFAEKYPG- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  81 vcpRIAYMPQglGKNLYPTLSVFENVDFFGRLFGHDKAErerriadllqstglapfaerpagKLSGGMKQKLGLCCALIH 160
Cdd:cd03233  84 ---EIIYVSE--EDVHFPTLTVRETLDFALRCKGNEFVR-----------------------GISGGERKRVSIAEALVS 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVAT--AYMEEAERFDWLVAMDDGKV 222
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCI-RTMADVLKTTTFVSLyqASDEIYDLFDKVLVLYEGRQ 198
PTZ00243 PTZ00243
ABC transporter; Provisional
26-255 6.63e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 56.71  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvldgdMRDRrhrravcpRIAYMPQglgKNLYPTLSVFEN 105
Cdd:PTZ00243  678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAER--------SIAYVPQ---QAWIMNATVRGN 740
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   106 VDFFgrlfghdKAERERRIADLLQSTGL-APFAERPAG----------KLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 174
Cdd:PTZ00243  741 ILFF-------DEEDAARLADAVRVSQLeADLAQLGGGleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   175 DPLSRNQFWE--LIGRIRagreGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRErtgtQSLESAFIALLPESK 252
Cdd:PTZ00243  814 DAHVGERVVEecFLGALA----GKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR----TSLYATLAAELKENK 885

                  ...
gi 15600424   253 RAG 255
Cdd:PTZ00243  886 DSK 888
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
272-437 7.00e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.05  E-value: 7.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  272 RIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalfgqpVDASDMAtrrRVGY 351
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKWSENA---NIGY 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 MSQafSLYAELSVRQNLVLHARLFHLPADG---IPARVGEMLrrF---DLEKVADELPNdlplGIRQRLSLAVAVIHKPE 425
Cdd:PRK15064 387 YAQ--DHAYDFENDLTLFDWMSQWRQEGDDeqaVRGTLGRLL--FsqdDIKKSVKVLSG----GEKGRMLFGKLMMQKPN 458
                        170
                 ....*....|..
gi 15600424  426 ILILDEPTSGVD 437
Cdd:PRK15064 459 VLVMDEPTNHMD 470
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
41-176 7.52e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 54.08  E-value: 7.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   41 GPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMPqglgkNLYPTLSVFENVDFFGRLFGHdkaeR 120
Cdd:PRK13543  44 GDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLP-----GLKADLSTLENLHFLCGLHGR----R 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  121 ERRI-ADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK13543 114 AKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
10-186 7.61e-08

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: 52.93  E-value: 7.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  10 SLRGVSLRYGETRA-VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmRDRRHRRAVCPRIAYM 88
Cdd:cd03223   2 ELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG------MPEGEDLLFLPQRPYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  89 PQGlgknlypTLsvfenvdffgrlfghdkaeRERRIadllqstglapfaeRPAGK-LSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03223  76 PLG-------TL-------------------REQLI--------------YPWDDvLSGGEQQRLAFARLLLHKPKFVFL 115
                       170
                ....*....|....*....
gi 15600424 168 DEPTTGVDPLSRNQFWELI 186
Cdd:cd03223 116 DEATSALDEESEDRLYQLL 134
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
293-496 8.52e-08

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 54.86  E-value: 8.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpvdasdmatrrRVGYMSQaFSLYAELSVRQNLVlha 372
Cdd:cd03291  56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQ-FSWIMPGTIKENII--- 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 373 rlFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:cd03291 120 --FGVSYD--EYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 442 DGFWE-----LMVELSRrdgvtiFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:cd03291 196 KEIFEscvckLMANKTR------ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
288-464 8.68e-08

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 55.91  E-value: 8.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGT------CALFGQPvdasdmatrrRVGYMSQAfslyae 361
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRltkpakGKLFYVP----------QRPYMTLG------ 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   362 lSVRQNLVLharlfhlpadgiPARVGEMLRR----FDLEKVADELPND------------------LPLGIRQRLSLAVA 419
Cdd:TIGR00954 530 -TLRDQIIY------------PDSSEDMKRRglsdKDLEQILDNVQLThilereggwsavqdwmdvLSGGEKQRIAMARL 596
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15600424   420 VIHKPEILILDEPTSGVDPVARDGfwelMVELSRRDGVTIFISTH 464
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGY----MYRLCREFGITLFSVSH 637
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
261-497 1.06e-07

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 56.11  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    261 IPPRPQSEGAPR-IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvd 339
Cdd:TIGR00957  624 IERRTIKPGEGNsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--- 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    340 asdmatrrrVGYMSQAfSLYAELSVRQNLVLHARLFH------LPADGIPARVgEMLRRFDLEKVADELPNdLPLGIRQR 413
Cdd:TIGR00957  701 ---------VAYVPQQ-AWIQNDSLRENILFGKALNEkyyqqvLEACALLPDL-EILPSGDRTEIGEKGVN-LSGGQKQR 768
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    414 LSLAVAVIHKPEILILDEPTSGVDP-VARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:TIGR00957  769 VSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL 848

                   ....*
gi 15600424    493 VRQRG 497
Cdd:TIGR00957  849 LQRDG 853
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
280-437 1.50e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 55.18  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  280 LTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFG--------QPVDASDMATRRRVGY 351
Cdd:PRK10636   7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEYVID 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  352 MSQAF-SLYAELSV--RQN-----LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIH 422
Cdd:PRK10636  87 GDREYrQLEAQLHDanERNdghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALIC 166
                        170
                 ....*....|....*
gi 15600424  423 KPEILILDEPTSGVD 437
Cdd:PRK10636 167 RSDLLLLDEPTNHLD 181
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
14-175 1.60e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 55.18  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   14 VSLRYGETRAVDDVSLE-IPANRmVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIAYMPQGL 92
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNlVPGSR-IGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG------------IKLGYFAQHQ 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   93 GKNLYPTLSVFENVdffGRLfghDKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK10636 385 LEFLRADESPLQHL---ARL---APQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458

                 ....
gi 15600424  172 TGVD 175
Cdd:PRK10636 459 NHLD 462
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
275-498 1.65e-07

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 53.70  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLpASEGTCALFGQPVDASDMAT-RRRVGY 351
Cdd:cd03289   3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKwRKAFGV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAElSVRQNLVLHARLfhlpADGIPARVGEmlrRFDLEKVADELPNDLPL-----------GIRQRLSLAVAV 420
Cdd:cd03289  82 IPQKVFIFSG-TFRKNLDPYGKW----SDEEIWKVAE---EVGLKSVIEQFPGQLDFvlvdggcvlshGHKQLMCLARSV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 421 IHKPEILILDEPTSGVDPVArdgfwelmVELSRR------DGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT--------YQVIRKtlkqafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225

                ....
gi 15600424 495 QRGL 498
Cdd:cd03289 226 EKSH 229
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
26-248 1.84e-07

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 53.71  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmrdRRHRRAVCPRIAYMPQGlgknlyptlSVFEN 105
Cdd:cd03291  55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------HSGRISFSSQFSWIMPG---------TIKEN 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 106 VdffgrLFGHDKAE-RERRIADLLQ-STGLAPFAER---PAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:cd03291 118 I-----IFGVSYDEyRYKSVVKACQlEEDITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 177 LSRNQFWE-LIGRIRAGRegMSVLVaTAYMEEAERFDWLVAMDDGKVLATGTPQELrertgtQSLESAFIALL 248
Cdd:cd03291 193 FTEKEIFEsCVCKLMANK--TRILV-TSKMEHLKKADKILILHEGSSYFYGTFSEL------QSLRPDFSSKL 256
hmuV PRK13547
heme ABC transporter ATP-binding protein;
22-231 2.68e-07

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 52.91  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG--ARKMQDGEIRV-----LDGD-MRDRRHRRAVCPRiAYMPQGlG 93
Cdd:PRK13547  15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVtgdvtLNGEpLAAIDAPRLARLR-AVLPQA-A 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   94 KNLYPtLSVFENVdFFGRlFGHDK-----AERERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCAL--------- 158
Cdd:PRK13547  93 QPAFA-FSAREIV-LLGR-YPHARragalTHRDGEIAWqALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424  159 IHDPDLLILDEPTTGVDPLSRNQFWELIGRI-RAGREGMSVLVATAYMeEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNL-AARHADRIAMLADGAIVAHGAPADV 242
PLN03232 PLN03232
ABC transporter C family member; Provisional
26-231 2.85e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 54.60  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrhrravcprIAYMPQglgKNLYPTLSVFEN 105
Cdd:PLN03232  635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS-------------VAYVPQ---VSWIFNATVREN 698
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   106 VdffgrLFGHD-KAERERRIA---------DLLQSTGLAPFAERPAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PLN03232  699 I-----LFGSDfESERYWRAIdvtalqhdlDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424   176 PLSRNQFWEliGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PLN03232  773 AHVAHQVFD--SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
6-236 3.34e-07

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 54.57  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424      6 SGVASLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG------DMRDRRH 77
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGlniakiGLHDLRF 1360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     78 RRAVCPRIAYMPQGlgknlyptlSVFENVDFFGRLfghdkaeRERRIADLLQSTGLAPF-AERPAG----------KLSG 146
Cdd:TIGR00957 1361 KITIIPQDPVLFSG---------SLRMNLDPFSQY-------SDEEVWWALELAHLKTFvSALPDKldhecaeggeNLSV 1424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    147 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfweLI-GRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDN----LIqSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
                          250
                   ....*....|.
gi 15600424    226 GTPQELRERTG 236
Cdd:TIGR00957 1501 GAPSNLLQQRG 1511
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
284-462 5.84e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.42  E-value: 5.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  284 FGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEgtcalfGQPVDASDMATRRR--------------- 348
Cdd:PRK11147  13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDD------GRIIYEQDLIVARLqqdpprnvegtvydf 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  349 ----VGYMSQAFSLYAELSVR-------QNL----VLHARLFHLPADGIPARVGEMLRRFDLEkvADELPNDLPLGIRQR 413
Cdd:PRK11147  87 vaegIEEQAEYLKRYHDISHLvetdpseKNLnelaKLQEQLDHHNLWQLENRINEVLAQLGLD--PDAALSSLSGGWLRK 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15600424  414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSrrdGVTIFIS 462
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---GSIIFIS 210
PLN03130 PLN03130
ABC transporter C family member; Provisional
19-231 6.48e-07

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 53.59  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-ALLAGARKMQDGEIrVLDGdmrdrrhrravcpRIAYMPQglgKNLY 97
Cdd:PLN03130  628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASV-VIRG-------------TVAYVPQ---VSWI 690
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    98 PTLSVFENVdFFGRLFGHDKAERERRIA------DLLQSTGLAPFAERPAgKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PLN03130  691 FNATVRDNI-LFGSPFDPERYERAIDVTalqhdlDLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPL 768
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424   172 TGVDPLSRNQFW------ELIGRIRagregmsVLVaTAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PLN03130  769 SALDAHVGRQVFdkcikdELRGKTR-------VLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
23-243 7.44e-07

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 52.79  E-value: 7.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR--HRRAvcpRIAYMPQglgknlYPTL 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRS---RLAVVSQ------TPFL 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  101 ---SVFENVdffgrLFGHDKA-----ERERRIA----DLLQstgLAPFAERPAGK----LSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK10789 401 fsdTVANNI-----ALGRPDAtqqeiEHVARLAsvhdDILR---LPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEI 472
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  165 LILDEPTTGVDPLSRNQfweLIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG-------T 237
Cdd:PRK10789 473 LILDDALSAVDGRTEHQ---ILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGwyrdmyrY 549

                 ....*.
gi 15600424  238 QSLESA 243
Cdd:PRK10789 550 QQLEAA 555
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
292-464 1.27e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 49.87  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  292 HVSFRIERGEIFG----FL--------GSNGCGKSTTMKMLTGLLPASEGTcaLFGQPVDASDMAtRRRVGYMSQAFSLY 359
Cdd:PRK13541   6 QLQFNIEQKNLFDlsitFLpsaityikGANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNINNIA-KPYCTYIGHNLGLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  360 AELSVRQNLVLHARLFHlPADGIPARVgemlRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPV 439
Cdd:PRK13541  83 LEMTVFENLKFWSEIYN-SAETLYAAI----HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
                        170       180
                 ....*....|....*....|....*
gi 15600424  440 ARDGFWELMVELSRRDGVtIFISTH 464
Cdd:PRK13541 158 NRDLLNNLIVMKANSGGI-VLLSSH 181
PLN03232 PLN03232
ABC transporter C family member; Provisional
238-494 2.19e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 51.90  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   238 QSLESAFIAllpeskragHHRLVIPPRPQSEGAPRIAIEAegltcrfGDFV--------AVDHVSFRIERGEIFGFLGSN 309
Cdd:PLN03232  589 QRIEELLLS---------EERILAQNPPLQPGAPAISIKN-------GYFSwdsktskpTLSDINLEIPVGSLVAIVGGT 652
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   310 GCGKSTTMKMLTGLLPASEGTCALFgqpvdasdmatRRRVGYMSQAFSLYaELSVRQNLvlharLFHlpADGIPARVGEM 389
Cdd:PLN03232  653 GEGKTSLISAMLGELSHAETSSVVI-----------RGSVAYVPQVSWIF-NATVRENI-----LFG--SDFESERYWRA 713
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   390 LRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP-VARDGFWELMV-ELSRRDG 456
Cdd:PLN03232  714 IDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKdELKGKTR 793
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 15600424   457 VTIFISTHFMNEAqrcDRISLMHAGKVLASDTPDELVR 494
Cdd:PLN03232  794 VLVTNQLHFLPLM---DRIILVSEGMIKEEGTFAELSK 828
PLN03211 PLN03211
ABC transporter G-25; Provisional
36-175 2.72e-06

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 51.03  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   36 MVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLdgdMRDRRHRRAVCPRIAYMPQGlgKNLYPTLSVFENVDFFG--RLF 113
Cdd:PLN03211  96 ILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIL---ANNRKPTKQILKRTGFVTQD--DILYPHLTVRETLVFCSllRLP 170
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424  114 GHDKAERERRIAD-LLQSTGLAPFAERPAGK-----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PLN03211 171 KSLTKQEKILVAEsVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
PLN03073 PLN03073
ABC transporter F family; Provisional
109-437 2.76e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.40  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  109 FGRLFGHDKAERERRIADLLQSTGLAPFAERPAGK-LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRNQFW---- 183
Cdd:PLN03073 309 YKRLELIDAYTAEARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWlety 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  184 -----ELIGRIRAGREGMSVLVATAYMEEAER-------FDWLVAMDDGKVLATGTPQELRERtgTQSLESAFI------ 245
Cdd:PLN03073 387 llkwpKTFIVVSHAREFLNTVVTDILHLHGQKlvtykgdYDTFERTREEQLKNQQKAFESNER--SRSHMQAFIdkfryn 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  246 ---ALLPESK-----RAGHHRLVIP--------PRPQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSN 309
Cdd:PLN03073 465 akrASLVQSRikaldRLGHVDAVVNdpdykfefPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPN 544
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  310 GCGKSTTMKMLTGLLPASEGTC--------ALFGQ-PVDASDMATRRRVgYMSQAFSLYAELSVRQnlvlharlfHLPAD 380
Cdd:PLN03073 545 GIGKSTILKLISGELQPSSGTVfrsakvrmAVFSQhHVDGLDLSSNPLL-YMMRCFPGVPEQKLRA---------HLGSF 614
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  381 GIPArvgemlrrfdleKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PLN03073 615 GVTG------------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
24-176 2.87e-06

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 51.29  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrDRRHRRAVCPRIAYMPQGLGKN--LYPTlS 101
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK------PAKGKLFYVPQRPYMTLGTLRDqiIYPD-S 540
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   102 VFenvDFFgrlfghDKAERERRIADLLQSTGLAPFAERPAG---------KLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:TIGR00954 541 SE---DMK------RRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611

                  ....
gi 15600424   173 GVDP 176
Cdd:TIGR00954 612 AVSV 615
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
81-231 3.18e-06

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: 51.17  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    81 VCPRIAYMPQGL-----GKNLYPTL--SVFENVDFFgrlfghDKAERERRIADLLQSTGLA--PFAeRPAGKLSGGMKQK 151
Cdd:TIGR00630 765 VCKGKRYNRETLevkykGKNIADVLdmTVEEAYEFF------EAVPSISRKLQTLCDVGLGyiRLG-QPATTLSGGEAQR 837
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   152 LGLCCALIHD---PDLLILDEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLV------AMDDGKV 222
Cdd:TIGR00630 838 IKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK--GNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTV 915

                  ....*....
gi 15600424   223 LATGTPQEL 231
Cdd:TIGR00630 916 VASGTPEEV 924
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
286-481 4.25e-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: 4.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-----TCALFGQPVDASDMATRRRVGYMSQAfSLYA 360
Cdd:cd03290  13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsNKNESEPSFEATRSRNRYSVAYAAQK-PWLL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVlharlFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03290  92 NATVEENIT-----FGSPFN--KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600424 430 DEPTSGVDPVARDGFW-ELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAG 481
Cdd:cd03290 165 DDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
290-437 6.01e-06

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 48.03  E-value: 6.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQ 366
Cdd:cd03233  23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 367 NLVLHARLfhlpadgipaRVGEMLRRFDlekvadelpndlpLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03233 103 TLDFALRC----------KGNEFVRGIS-------------GGERKRVSIAEALVSRASVLCWDNSTRGLD 150
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
19-189 6.64e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 49.03  E-value: 6.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---------ARKMQDGEIRVLDGDMRDRRhrRAVCPRIAYMP 89
Cdd:PRK15093  18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtADRMRFDDIDLLRLSPRERR--KLVGHNVSMIF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   90 QGLGKNLYPTLSVFENV-------DFFGRLFGHDKAeRERRIADLLQSTGLA---------PFaerpagKLSGGMKQKLG 153
Cdd:PRK15093  96 QEPQSCLDPSERVGRQLmqnipgwTYKGRWWQRFGW-RKRRAIELLHRVGIKdhkdamrsfPY------ELTEGECQKVM 168
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15600424  154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRI 189
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRL 204
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
26-233 7.71e-06

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 50.11  E-value: 7.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     26 DVSLEIPANRMVGLIGPDGVGKSSLLALLA----GARKMQDGEIRvLDG----DMRdrRHRRAvcpRIAYMPQGlgKNLY 97
Cdd:TIGR00956   79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVIT-YDGitpeEIK--KHYRG---DVVYNAET--DVHF 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     98 PTLSVFENVDFFGRL-------FGHDKAERERRIADLLQST-GLAPFAERPAGK-----LSGGMKQKLGLCCALIHDPDL 164
Cdd:TIGR00956  151 PHLTVGETLDFAARCktpqnrpDGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKI 230
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424    165 LILDEPTTGVDPLSRNQFweligrIRAGREGMSVLVATAYM------EEA-ERFDWLVAMDDGKVLATGTPQELRE 233
Cdd:TIGR00956  231 QCWDNATRGLDSATALEF------IRALKTSANILDTTPLVaiyqcsQDAyELFDKVIVLYEGYQIYFGPADKAKQ 300
PLN03140 PLN03140
ABC transporter G family member; Provisional
300-440 8.04e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 49.84  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   300 GEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMAtrRRVGYMSQAFSLYAELSVRQNLVLHARLfHL 377
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFA--RISGYCEQNDIHSPQVTVRESLIYSAFL-RL 982
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424   378 PADGIPAR----VGEMLRRFDLEKVADE---LPNDLPLGI--RQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:PLN03140  983 PKEVSKEEkmmfVDEVMELVELDNLKDAivgLPGVTGLSTeqRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
7-266 1.05e-05

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 48.31  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   7 GVASLRGVSLRYGE--TRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-ALLagarKM--QDGEIRVlDG----DMRDRRH 77
Cdd:cd03289   1 GQMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLsAFL----RLlnTEGDIQI-DGvswnSVPLQKW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  78 RRA--VCPRIAYMPQG-LGKNLYPtlsvfenvdffgrlFGHDKAERERRIADllqSTGLAPFAERPAGKL---------- 144
Cdd:cd03289  76 RKAfgVIPQKVFIFSGtFRKNLDP--------------YGKWSDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcv 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 145 -SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSrnqfWELIGR-IRAGREGMSVLVATAYME---EAERFdwlVAMDD 219
Cdd:cd03289 139 lSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT----YQVIRKtLKQAFADCTVILSEHRIEamlECQRF---LVIEE 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15600424 220 GKVLATGTPQELRERTGT--QSLESA-FIALLPESKRAGHHRlviPPRPQ 266
Cdd:cd03289 212 NKVRQYDSIQKLLNEKSHfkQAISPSdRLKLFPRRNSSKSKR---KPRPQ 258
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
20-226 1.53e-05

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 48.70  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG---DMRDRRHRRAVCPRIAYMPQGLGKNL 96
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI-IFNGqriDTLSPGKLQALRRDIQFIFQDPYASL 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   97 YPTL----SVFENVDFFGRLFGHDKAereRRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK10261 415 DPRQtvgdSIMEPLRVHGLLPGKAAA---ARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424  172 TGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERFDWLVA-MDDGKVLATG 226
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQ--RDfGIAYLFISHDMAVVERISHRVAvMYLGQIVEIG 546
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
19-175 1.58e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 48.18  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   19 GETRAVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLA------GARKMQDGEIRvldgDMRDRRHRRAVCPRIAYM 88
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangrigGSATFNGREIL----NLPEKELNKLRAEQISMI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   89 PQGLGKNLYPTLSVFENVDFFGRLF-GHDKAERERRIADLLQSTGLaPFAERPAG----KLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK09473 103 FQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKM-PEARKRMKmyphEFSGGMRQRVMIAMALLCRPK 181
                        170
                 ....*....|..
gi 15600424  164 LLILDEPTTGVD 175
Cdd:PRK09473 182 LLIADEPTTALD 193
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
22-226 1.78e-05

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: 46.16  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLalLAGARKmqdgeirvldgdmrdrrhrrAVCPRIAYMPQGLGKNlyPTLs 101
Cdd:cd03238   9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA--------------------SGKARLISFLPKFSRN--KLI- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 vfenvdFFGRLfghdkaereRRIADLlqstGLAPFA-ERPAGKLSGGMKQKLGLCCALIHDPD--LLILDEPTTGVDPLS 178
Cdd:cd03238  64 ------FIDQL---------QFLIDV----GLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600424 179 RNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAM------DDGKVLATG 226
Cdd:cd03238 125 INQLLEVIKGLI--DLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
PLN03130 PLN03130
ABC transporter C family member; Provisional
6-231 2.53e-05

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 48.20  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     6 SGVASLRGVSLRY-GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-----MRDRRHR 78
Cdd:PLN03130 1235 SGSIKFEDVVLRYrPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfgLMDLRKV 1314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    79 RAVCPRIAYMPQGlgknlyptlSVFENVDFFGRlfgHDKAE----RER-RIADLLQSTGLAPFAERPAG--KLSGGMKQK 151
Cdd:PLN03130 1315 LGIIPQAPVLFSG---------TVRFNLDPFNE---HNDADlwesLERaHLKDVIRRNSLGLDAEVSEAgeNFSVGQRQL 1382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   152 LGLCCALIHDPDLLILDEPTTGVDPLSRnqfwELIGR-IRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVRTD----ALIQKtIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPEN 1458

                  .
gi 15600424   231 L 231
Cdd:PLN03130 1459 L 1459
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
7-178 2.84e-05

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 47.98  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424      7 GVASLRGVSLRYGET-RAV-DDVSLEIPANRMVGLIGPDGVGKSSLL-ALLAGARkmQDGEIRVlDG------DMRDRRH 77
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAgRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLsALLRLLS--TEGEIQI-DGvswnsvTLQTWRK 1292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     78 RRAVCPRIAYMPQG-LGKNLYPtlsvfenvdffgrlfgHDKAERER--RIADllqSTGLAPFAERPAGK----------- 143
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGtFRKNLDP----------------YEQWSDEEiwKVAE---EVGLKSVIEQFPDKldfvlvdggyv 1353
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 15600424    144 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
294-437 4.07e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 47.47  E-value: 4.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 294 SFRI------ERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalFGQPVDASDMATRRRVGYMSQAFSLYAELSVR-- 365
Cdd:COG1245  87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSGELKPNLGD---YDEEPSWDEVLKRFRGTELQDYFKKLANGEIKva 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 ---QNLVLHARLFhlpaDGipaRVGEMLRRFDLEKVADELPNDLPLG------IR-------QRLSLAVAVIHKPEILIL 429
Cdd:COG1245 164 hkpQYVDLIPKVF----KG---TVRELLEKVDERGKLDELAEKLGLEnildrdISelsggelQRVAIAAALLRDADFYFF 236

                ....*...
gi 15600424 430 DEPTSGVD 437
Cdd:COG1245 237 DEPSSYLD 244
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
293-437 4.45e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 47.72  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcALFGQPVDASDMAT---RRRVGYMSQAFSLYAElSVRQNLV 369
Cdd:PTZ00265  404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGD-IIINDSHNLKDINLkwwRSKIGVVSQDPLLFSN-SIKNNIK 481
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   370 --------LHARLFHLPADGIPARVGEMLRRFDLEKVADE---------------------------------------- 401
Cdd:PTZ00265  482 yslyslkdLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDlndmsnttdsneliemrknyqtikdsevvdvskkvlihdf 561
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 15600424   402 ---LPND-----------LPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PTZ00265  562 vsaLPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
143-217 4.87e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 44.66  E-value: 4.87e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 143 KLSGGMKQKLGLCCALIH----DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLVAM 217
Cdd:cd03227  77 QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELAELADKLIHI 153
PTZ00243 PTZ00243
ABC transporter; Provisional
260-496 5.57e-05

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 47.08  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   260 VIPPRPQSEGAPRI----AIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL 333
Cdd:PTZ00243 1290 VIEPASPTSAAPHPvqagSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV 1369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   334 FGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNL--VLHARlfhlpadgiPARVGEMLRRFDL-EKVADELP------- 403
Cdd:PTZ00243 1370 NGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdpFLEAS---------SAEVWAALELVGLrERVASESEgidsrvl 1440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   404 ---NDLPLGIRQRLSLAVAVIHKPEILIL-DEPTSGVDPvARDGFWELMVeLSRRDGVTIFISTHFMNEAQRCDRISLMH 479
Cdd:PTZ00243 1441 eggSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDP-ALDRQIQATV-MSAFSAYTVITIAHRLHTVAQYDKIIVMD 1518
                         250
                  ....*....|....*..
gi 15600424   480 AGKVLASDTPDELVRQR 496
Cdd:PTZ00243 1519 HGAVAEMGSPRELVMNR 1535
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
20-186 7.57e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 44.48  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHrravcPRIAYMPQGLGKNLypT 99
Cdd:PRK13541  12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-----PYCTYIGHNLGLKL--E 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  100 LSVFENVDFFGRLFGH----DKAERERRIADLLqstglapfaERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK13541  85 MTVFENLKFWSEIYNSaetlYAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
                        170
                 ....*....|.
gi 15600424  176 PLSRNQFWELI 186
Cdd:PRK13541 156 KENRDLLNNLI 166
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
141-201 8.47e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 46.56  E-value: 8.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424   141 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVA 201
Cdd:PTZ00265  577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
292-496 9.48e-05

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 45.28  E-value: 9.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQNLVL 370
Cdd:cd03288  39 HVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSIILQDPILFSG-SIRFNLDP 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 371 HARLfhlpadgIPARVGEMLRRFDLEKVADELPNDL-----------PLGIRQRLSLAVAVIHKPEILILDEPTSGVDPV 439
Cdd:cd03288 118 ECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 440 ARDGFWE-LMVELSRRDGVTIfisTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:cd03288 191 TENILQKvVMTAFADRTVVTI---AHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
100-231 1.41e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 45.79  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   100 LSVFENVDFfgrlfGHDKAERE--RR------IADLLQS------TGLAPFAErpagKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PTZ00265 1310 MSIYENIKF-----GKEDATREdvKRackfaaIDEFIESlpnkydTNVGPYGK----SLSGGQKQRIAIARALLREPKIL 1380
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424   166 ILDEPTTGVDPLSRNQFWELIGRIRaGREGMSVLVATAYMEEAERFDWLVAMDDGK-----VLATGTPQEL 231
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIK-DKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEEL 1450
ABC-2_lan_permease-like cd21809
lantibiotic immunity ABC transporter permease (also called ABC-2 transporter permease) subunit ...
722-913 1.89e-04

lantibiotic immunity ABC transporter permease (also called ABC-2 transporter permease) subunit and similar proteins; This subfamily contains lantibiotic ABC transporter permease subunits which are highly hydrophobic, integral membrane proteins, and part of the bacitracin ABC transport system that confers resistance to the Gram-positive bacteria in which this system operates, particularly to type-A lantibiotics. Lantibiotics are small peptides, produced by Gram-positive bacteria, which are ribosomally-synthesized as pre-peptides and act by disrupting membrane integrity. Genes encoding the lantibiotic ABC transporter subunits are highly organized in operons containing all the genes required for maturation, transport, immunity, and synthesis. For example, in Lactococcus lactis, the lantibiotic nisin is active against other Gram-positive bacteria via various modes of actions; however, its self-protection against the pore-forming nisin is mediated by the ABC transporter composed of NisF, NisE and NisG; the NisG permease subunit transports nisin to the surface and expels it from the membrane. This family includes mostly uncharacterized transport permease subunits that transport lantibiotics to the surface and expel them from the membrane.


Pssm-ID: 409634  Cd Length: 235  Bit Score: 44.11  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 722 MVPAVIPLLLIMIPAMLTALgVVR-EKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLV--LAIVVFRVPLKG 798
Cdd:cd21809  50 VVLFYGLLFLPLLIGILASL-VCRiEHKNNGWKQLLALPVSRTQIYLAKFLVVLLLLALTQLLFLGaiILGGLLLGFGGP 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 799 SFLALTIGAFLYVVTST----GLGLFLSTFMRSQIAAVFGVAIATMIpaiqfsGLIhpvssleGAAAWIGKLYPTSHFLV 874
Cdd:cd21809 129 IPWLLILKSVLLGWIASlpliALQLWLSLRFKSFAAPLGIGILTLPA------GLI-------ANSSKLGPFYPWAYPIL 195
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15600424 875 VSRGAFSKSLGLSDLWAYYLPLAASIVVLTLLSVACLKK 913
Cdd:cd21809 196 AMLPGSGDGAFNVSLELFLIVSLGSFILFLLIGLRHFKR 234
PTZ00243 PTZ00243
ABC transporter; Provisional
293-483 1.90e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 45.54  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGtcalfgqpvdasDMATRRRVGYM-SQAFSLYAelSVRQNLvlh 371
Cdd:PTZ00243  679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG------------RVWAERSIAYVpQQAWIMNA--TVRGNI--- 741
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   372 arLFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpvA 440
Cdd:PTZ00243  742 --LFFDEED--AARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALD--A 815
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 15600424   441 RDGfwELMVE---LSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PTZ00243  816 HVG--ERVVEecfLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
299-464 3.55e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.98  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    299 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFgqpvdasdmatrrrvgymsqafslyaelsvrqnlvlharlfhlp 378
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    379 aDGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAviHKPEILILDEPTSGVDPVARDGFWELMV-----ELSR 453
Cdd:smart00382  37 -DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK--LKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKS 113
                          170
                   ....*....|.
gi 15600424    454 RDGVTIFISTH 464
Cdd:smart00382 114 EKNLTVILTTN 124
PTZ00243 PTZ00243
ABC transporter; Provisional
12-260 5.34e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 44.00  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    12 RGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgDMRD------RRHRRavcp 83
Cdd:PTZ00243 1312 EGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV---NGREigayglRELRR---- 1384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    84 RIAYMPQGlgknlyPTL---SVFENVDFFgrlfghdkaeRERRIADLLQSTGLAPFAERPAGK--------LSGGMKQKL 152
Cdd:PTZ00243 1385 QFSMIPQD------PVLfdgTVRQNVDPF----------LEASSAEVWAALELVGLRERVASEsegidsrvLEGGSNYSV 1448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   153 G----LCCA---LIHDPDLLILDEPTTGVDP-LSRnqfweligRIRAgrEGMSVLVATAYMEEAER------FDWLVAMD 218
Cdd:PTZ00243 1449 GqrqlMCMAralLKKGSGFILMDEATANIDPaLDR--------QIQA--TVMSAFSAYTVITIAHRlhtvaqYDKIIVMD 1518
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 15600424   219 DGKVLATGTPQELRERtgTQSLESAFIALLPESKRAGHHRLV 260
Cdd:PTZ00243 1519 HGAVAEMGSPRELVMN--RQSIFHSMVEALGRSEAKRFLQLV 1558
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
409-493 5.50e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 43.86  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   409 GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMH-----AGKV 483
Cdd:PTZ00265 1362 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNnpdrtGSFV 1441
                          90
                  ....*....|
gi 15600424   484 LASDTPDELV 493
Cdd:PTZ00265 1442 QAHGTHEELL 1451
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
139-231 9.16e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 43.28  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   139 RPAGKLSGGMKQKLGLCCALIH---DPDLLILDEPTTGvdpLSRNQFWELIGRIRA-GREGMSVLVATAYMEEAERFDWL 214
Cdd:PRK00635  805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTG---LHTHDIKALIYVLQSlTHQGHTVVIIEHNMHVVKVADYV 881
                          90       100
                  ....*....|....*....|...
gi 15600424   215 VAMD------DGKVLATGTPQEL 231
Cdd:PRK00635  882 LELGpeggnlGGYLLASCSPEEL 904
ABC2_membrane_4 pfam12730
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
726-832 1.74e-03

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 403819  Cd Length: 179  Bit Score: 40.26  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   726 VIPLLLIMIPAMLtalgVVREKELGSITNLYVTPVTRLEFLVGKqlpYVAMGMINFLLMLVLAIVVFRVPLKGSFLALTI 805
Cdd:pfam12730  59 LLPIILGIIASYL----FFREYDNDTLKNLLTIPVSRRKLLFAK---LIVLLLLSVLFMLVTFLITVLFGLLSGFVGFSW 131
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15600424   806 GAFLYVV---TSTGLGLF--------LSTFMRSQIAAV 832
Cdd:pfam12730 132 GLILYLLkkcLEIGLLVFfavlpiiaLALLFKGYVLPV 169
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
294-465 2.15e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 41.54  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  294 SFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL-FGQPVDASDMATRRRVgymSQAFS-----LYAE------ 361
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSqFSHITRLSFEQLQKLV---SDEWQrnntdMLSPgeddtg 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424  362 LSVRQNLVLHARlfhlpadgIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK10938 100 RTTAEIIQDEVK--------DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
                        170       180
                 ....*....|....*....|....
gi 15600424  442 DGFWELMVELSRRDGVTIFISTHF 465
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRF 195
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
99-233 2.62e-03

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: 41.54  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424    99 TLSVFENVDFFGRLfghDKAERERRIADL-----------LQSTGLAPFA-ERPAGKLSGGMKQKLGLC----CALIHdp 162
Cdd:TIGR00630 435 ELSIREAHEFFNQL---TLTPEEKKIAEEvlkeirerlgfLIDVGLDYLSlSRAAGTLSGGEAQRIRLAtqigSGLTG-- 509
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424   163 DLLILDEPTTGVDPlSRNQfwELIGRIRAGRE-GMSVLVATAYMEEAERFDWLVAM------DDGKVLATGTPQELRE 233
Cdd:TIGR00630 510 VLYVLDEPSIGLHQ-RDNR--RLINTLKRLRDlGNTLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILA 584
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
19-175 2.66e-03

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 41.63  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     19 GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ--DGEIRVLDGDMRDRRHRRavcpRIAYMPQglgKN 95
Cdd:TIGR00956  773 KEKRVIlNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGviTGGDRLVNGRPLDSSFQR----SIGYVQQ---QD 845
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424     96 LY-PTLSVFENVDF--FGRLFGH-DKAERERRIADLLQSTGLAPFAERPAGKLSGGM----KQKLGLCCALIHDPDLLI- 166
Cdd:TIGR00956  846 LHlPTSTVRESLRFsaYLRQPKSvSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLf 925

                   ....*....
gi 15600424    167 LDEPTTGVD 175
Cdd:TIGR00956  926 LDEPTSGLD 934
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
400-503 3.48e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 41.35  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424   400 DELPNDLPL-----GIRQRLSLA---VAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR 471
Cdd:PRK00635  799 DYLPLGRPLsslsgGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKV 877
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15600424   472 CDRISLM------HAGKVLASDTPDELVrQRGLPTLEA 503
Cdd:PRK00635  878 ADYVLELgpeggnLGGYLLASCSPEELI-HLHTPTAKA 914
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
33-79 3.98e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.06  E-value: 3.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15600424    33 ANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmRDR---RHRR 79
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKLG--RGRhttTHVE 152
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
275-358 4.05e-03

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 39.09  E-value: 4.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFvavdHVSFR---IERGEIFGFLGSNGCGKSTTMKMLTGLLpasegtcalfgQPVDASDMATRRRVGY 351
Cdd:cd03222   1 QLYPDCVKRYGVF----FLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQL-----------IPNGDNDEWDGITPVY 65

                ....*..
gi 15600424 352 MSQAFSL 358
Cdd:cd03222  66 KPQYIDL 72
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
33-66 4.10e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 39.69  E-value: 4.10e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 15600424  33 ANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR 66
Cdd:cd01854  84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
 
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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