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Conserved domains on  [gi|516735053|ref|WP_018073908|]
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choline ABC transporter ATP-binding protein [Rhizobium ruizarguesonis]

Protein Classification

choline ABC transporter ATP-binding protein( domain architecture ID 11496814)

choline ABC transporter ATP-binding protein is the ATP-binding subunit of a three-component transporter system, belonging to the family of proline and glycine-betaine transporters

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ABC_choXWV_ATP TIGR03415
choline ABC transporter, ATP-binding protein; Members of this protein family are the ...
4-344 0e+00

choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]


:

Pssm-ID: 188317 [Multi-domain]  Cd Length: 382  Bit Score: 592.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    4 VSFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:TIGR03415   1 IRFKNVDIVFGDQPDEALALLDQGKTREEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   84 VAVSTTTGPVNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:TIGR03415  81 VLVKDGDGSVDVANCDAATLRRLRTHRVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES 243
Cdd:TIGR03415 161 KPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  244 GRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQS--------------------------GLGQTAAGMSVS 297
Cdd:TIGR03415 241 GRIIQHGTPEEIVLNPANDYVADFVAHTNPLNVLTARDLMRPlttlekvdgewcvskrydtwlktadkQVRRAAAGLPVA 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053  298 ATA---------------RAATPLIDILDALARQPGSIGIVENGAIVGTISAQDIVAGLTRH 344
Cdd:TIGR03415 321 AWAaeqevesleklptviNPDTPMRDVLAARHRTGGAILLVENGRIVGVIGDQNIYHALLGH 382
 
Name Accession Description Interval E-value
ABC_choXWV_ATP TIGR03415
choline ABC transporter, ATP-binding protein; Members of this protein family are the ...
4-344 0e+00

choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 188317 [Multi-domain]  Cd Length: 382  Bit Score: 592.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    4 VSFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:TIGR03415   1 IRFKNVDIVFGDQPDEALALLDQGKTREEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   84 VAVSTTTGPVNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:TIGR03415  81 VLVKDGDGSVDVANCDAATLRRLRTHRVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES 243
Cdd:TIGR03415 161 KPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  244 GRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQS--------------------------GLGQTAAGMSVS 297
Cdd:TIGR03415 241 GRIIQHGTPEEIVLNPANDYVADFVAHTNPLNVLTARDLMRPlttlekvdgewcvskrydtwlktadkQVRRAAAGLPVA 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053  298 ATA---------------RAATPLIDILDALARQPGSIGIVENGAIVGTISAQDIVAGLTRH 344
Cdd:TIGR03415 321 AWAaeqevesleklptviNPDTPMRDVLAARHRTGGAILLVENGRIVGVIGDQNIYHALLGH 382
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
1-342 0e+00

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 531.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG4175    1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAVSTttgpVNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:COG4175   81 AGEVLIDG----EDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAI 240
Cdd:COG4175  157 EDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 241 MESGRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQ--SGLGQTAAGMSVS--------------------- 297
Cdd:COG4175  237 MKDGRIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRppEAVVSEKDGPRVAlrrmreegisslyvvdrdrrl 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 298 ---------------------------ATARAATPLIDILDALARQPGSIGIV-ENGAIVGTISAQDIVAGLT 342
Cdd:COG4175  317 lgvvtaddaleavkgekdleeilltdvPTVSPDTPLRDLLPLVAESPYPLAVVdEDGRLLGVISRGSLLAALA 389
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
4-275 2.58e-134

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: 383.53  E-value: 2.58e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03294    1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVSTTtgPVNpySCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:cd03294   81 VLIDGQ--DIA--AMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES 243
Cdd:cd03294  157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 516735053 244 GRIIQCGTPHDIVKNPADQYVADFVQNLNPIN 275
Cdd:cd03294  237 GRLVQVGTPEEILTNPANDYVREFFRGVDRAK 268
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
8-287 3.16e-84

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 260.74  E-value: 3.16e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   8 NVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS 87
Cdd:PRK10070   9 NLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  88 TttgpVNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNE 167
Cdd:PRK10070  89 G----VDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 168 LSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 516735053 248 QCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQSGL 287
Cdd:PRK10070 245 QVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTP 284
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
45-196 2.16e-38

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: 133.93  E-value: 2.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpySCNAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:pfam00005   3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ-------DLTDDERKSLRKE-IGYVFQDPQLFPRL 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053  125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKV----NELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:pfam00005  75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
43-231 5.17e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 100.00  E-value: 5.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyscnakalrdlrthTVSMVFQQFALlP 122
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-------------------RVAYVPQRSEV-P 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WR---TVAENVGFGL----ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:NF040873  68 DSlplTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 516735053 196 SALDPLIRTRLqDELLEFQRRLKKTILFVSHDLDEA 231
Cdd:NF040873 148 TGLDAESRERI-IALLAEEHARGATVVVVTHDLELV 182
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
43-257 4.25e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 79.40  E-value: 4.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVsttTG-PVNPyscnakalRDLRT-HTVSMVFQQFAL 120
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL---FGqPVDA--------GDIATrRRVGYMSQAFSL 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENvgfgLEL-A---GMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:NF033858 351 YGELTVRQN----LELhArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 197 ALDPLIRTRLQDELLEFQRRLKKTIlFVS-HDLDEAFRIgNRIAIMESGRIIQCGTPHDIVK 257
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREDGVTI-FIStHFMNEAERC-DRISLMHAGRVLASDTPAALVA 486
GguA NF040905
sugar ABC transporter ATP-binding protein;
40-248 3.62e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 76.37  E-value: 3.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP--------VVRGDVavstttgpvnpysCNAKALRDLRTHTV 111
Cdd:NF040905  14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeiLFDGEV-------------CRFKDIRDSEALGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 112 SMVFQQFALLPWRTVAENVGFGLELA--GM---PEAERKLRvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:NF040905  81 VIIHQELALIPYLSIAENIFLGNERAkrGVidwNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILfVSHDLDEAFRIGNRIAIMESGRIIQ 248
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRTIE 219
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
130-250 2.29e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 67.07  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 130 VGFGLELAgmpEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDE 209
Cdd:NF000106 110 IGR*LDLS---RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 516735053 210 LLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:NF000106 187 VRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
38-255 2.00e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 58.98  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLL------RAV-NGLAPVVRGDVAvstttgpvnpyscNAKALRDLRTHT 110
Cdd:NF033858  12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIqQGRVEVLGGDMA-------------DARHRRAVCPRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 111 VSMVfQQFA--LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPI 188
Cdd:NF033858  79 AYMP-QGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 189 LLMDEPFSALDPLIRTR---LQDELLefQRRLKKTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDI 255
Cdd:NF033858 158 LILDEPTTGVDPLSRRQfweLIDRIR--AERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
53-248 5.82e-06

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: 45.44  E-value: 5.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    53 GEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpYSCNAKALRdlrthtvsmvfqqfallpwrtvaenvgf 132
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-----------IYIDGEDIL---------------------------- 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   133 glelagmpeaerklrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDE--- 209
Cdd:smart00382  43 -----------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 516735053   210 --LLEFQRRLKKTILFVSHDLDEafrIGNRIAIMESGRIIQ 248
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKD---LGPALLRRRFDRRIV 143
GguA NF040905
sugar ABC transporter ATP-binding protein;
164-247 2.49e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.77  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPfsaldplirTRLQD-----ELLEFQRRLK---KTILFVSHDLDEAFRIG 235
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEP---------TRGIDvgakyEIYTIINELAaegKGVIVISSELPELLGMC 471
                         90
                 ....*....|..
gi 516735053 236 NRIAIMESGRII 247
Cdd:NF040905 472 DRIYVMNEGRIT 483
 
Name Accession Description Interval E-value
ABC_choXWV_ATP TIGR03415
choline ABC transporter, ATP-binding protein; Members of this protein family are the ...
4-344 0e+00

choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 188317 [Multi-domain]  Cd Length: 382  Bit Score: 592.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    4 VSFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:TIGR03415   1 IRFKNVDIVFGDQPDEALALLDQGKTREEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   84 VAVSTTTGPVNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:TIGR03415  81 VLVKDGDGSVDVANCDAATLRRLRTHRVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES 243
Cdd:TIGR03415 161 KPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  244 GRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQS--------------------------GLGQTAAGMSVS 297
Cdd:TIGR03415 241 GRIIQHGTPEEIVLNPANDYVADFVAHTNPLNVLTARDLMRPlttlekvdgewcvskrydtwlktadkQVRRAAAGLPVA 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053  298 ATA---------------RAATPLIDILDALARQPGSIGIVENGAIVGTISAQDIVAGLTRH 344
Cdd:TIGR03415 321 AWAaeqevesleklptviNPDTPMRDVLAARHRTGGAILLVENGRIVGVIGDQNIYHALLGH 382
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
1-342 0e+00

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 531.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG4175    1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAVSTttgpVNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:COG4175   81 AGEVLIDG----EDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAI 240
Cdd:COG4175  157 EDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 241 MESGRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQ--SGLGQTAAGMSVS--------------------- 297
Cdd:COG4175  237 MKDGRIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRppEAVVSEKDGPRVAlrrmreegisslyvvdrdrrl 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 298 ---------------------------ATARAATPLIDILDALARQPGSIGIV-ENGAIVGTISAQDIVAGLT 342
Cdd:COG4175  317 lgvvtaddaleavkgekdleeilltdvPTVSPDTPLRDLLPLVAESPYPLAVVdEDGRLLGVISRGSLLAALA 389
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
4-275 2.58e-134

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: 383.53  E-value: 2.58e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03294    1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVSTTtgPVNpySCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:cd03294   81 VLIDGQ--DIA--AMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES 243
Cdd:cd03294  157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 516735053 244 GRIIQCGTPHDIVKNPADQYVADFVQNLNPIN 275
Cdd:cd03294  237 GRLVQVGTPEEILTNPANDYVREFFRGVDRAK 268
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
43-341 5.31e-96

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 287.37  E-value: 5.31e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV---STTTgpVNPYscnakALRdlRthtvSM--VFQQ 117
Cdd:COG1125   18 VDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIdgeDIRD--LDPV-----ELR--R----RIgyVIQQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL--TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:COG1125   85 IGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV---QNLN 272
Cdd:COG1125  165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVgadRGLR 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 273 PINMLTAADVMQSGLgqtaagmsvsATARAATPLIDILDALARQPGSIGIV--ENGAIVGTISAQDIVAGL 341
Cdd:COG1125  245 RLSLLRVEDLMLPEP----------PTVSPDASLREALSLMLERGVDWLLVvdEDGRPLGWLTLEDLLRAL 305
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
36-284 1.60e-90

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: 275.58  E-value: 1.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   36 ATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYSCNAKALRDLRTHTVSMVF 115
Cdd:TIGR01186   2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDG----ENIMKQSPVELREVRRKKIGMVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  116 QQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:TIGR01186  78 QQFALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQNLNPIN 275
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQ 237

                  ....*....
gi 516735053  276 MLTAADVMQ 284
Cdd:TIGR01186 238 VFDAERIAQ 246
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-305 1.92e-90

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 274.67  E-value: 1.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDrpetalamvdqgksrdeigaatglVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG3842    3 MPALELENVSKRYGD------------------------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAVstttgpvnpyscNAKALRDLRTHT--VSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:COG3842   59 SGRILL------------DGRDVTGLPPEKrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLE 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRI 238
Cdd:COG3842  127 GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRI 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 239 AIMESGRIIQCGTPHDIVKNPADQYVADFVqnlNPINMLTAADVMQSGLGQTAAGMSVSATARAATP 305
Cdd:COG3842  207 AVMNDGRIEQVGTPEEIYERPATRFVADFI---GEANLLPGTVLGDEGGGVRTGGRTLEVPADAGLA 270
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-247 1.43e-85

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 259.25  E-value: 1.43e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPETALAmvdqgksrdeigaatglvlgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG1116    5 APALELRGVSKRFPTGGGGVTA--------------------LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAV--STTTGPvnpyscnakalrdlrTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:COG1116   65 SGEVLVdgKPVTGP---------------GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLA 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRI 238
Cdd:COG1116  130 GFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRV 209
                        250
                 ....*....|.
gi 516735053 239 AIMES--GRII 247
Cdd:COG1116  210 VVLSArpGRIV 220
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
8-287 3.16e-84

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 260.74  E-value: 3.16e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   8 NVSIIFGDRPETALAMVDQGKSRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS 87
Cdd:PRK10070   9 NLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  88 TttgpVNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNE 167
Cdd:PRK10070  89 G----VDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 168 LSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 516735053 248 QCGTPHDIVKNPADQYVADFVQNLNPINMLTAADVMQSGL 287
Cdd:PRK10070 245 QVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTP 284
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
38-250 8.42e-81

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: 245.12  E-value: 8.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnPYSCNAKALRDlrthtVSMVFQQ 117
Cdd:cd03259   11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-----DVTGVPPERRN-----IGMVFQD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03259   81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03259  161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-322 2.28e-80

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 248.83  E-value: 2.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPetalamvdqgksrdeigaatglvlGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG3839    1 MASLELENVSKSYGGVE------------------------ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVA----VSTTTGPVNpyscnakalRDlrthtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVN 156
Cdd:COG3839   57 SGEILiggrDVTDLPPKD---------RN-----IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLG 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 157 LTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGN 236
Cdd:COG3839  123 LEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLAD 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 237 RIAIMESGRIIQCGTPHDIVKNPADQYVADFVQNlNPINMLTaADVMQSGLgqTAAGMSVsataraatPLIDILDALARQ 316
Cdd:COG3839  203 RIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGS-PPMNLLP-GTVEGGGV--RLGGVRL--------PLPAALAAAAGG 270

                 ....*.
gi 516735053 317 PGSIGI 322
Cdd:COG3839  271 EVTLGI 276
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
43-269 5.84e-80

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: 244.13  E-value: 5.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPVnpyscnakalrDLRTHtVSMVFQQF 118
Cdd:cd03295   17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgediREQDPV-----------ELRRK-IGYVIQQI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL--TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:cd03295   85 GLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:cd03295  165 ALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
34-248 1.29e-78

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: 240.07  E-value: 1.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyscnakalrdlRTHTVSM 113
Cdd:cd03293   11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--PVTG-----------PGPDRGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03293   78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES--GRIIQ 248
Cdd:cd03293  158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
43-268 2.20e-73

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 230.80  E-value: 2.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvnpyscnakalRDLRTHT------VSMVFQ 116
Cdd:COG1118   18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---------------RDLFTNLpprerrVGFVFQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:COG1118   83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:COG1118  163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
41-268 4.25e-70

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: 218.65  E-value: 4.25e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  41 LGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHT--VSMVFQQF 118
Cdd:cd03300   14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL------------DGKDITNLPPHKrpVNTVFQNY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03300   82 ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:cd03300  162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
30-272 4.91e-66

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 212.20  E-value: 4.91e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   30 RDEIGAATGLvlgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS---TTTGPVnpyscnakALRDL 106
Cdd:TIGR03265  11 RKRFGAFTAL----KDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGgrdITRLPP--------QKRDY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  107 rthtvSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:TIGR03265  79 -----GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVAD 266
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVAD 233

                  ....*.
gi 516735053  267 FVQNLN 272
Cdd:TIGR03265 234 FVGEVN 239
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
3-268 6.86e-66

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: 207.91  E-value: 6.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   3 AVSFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG 82
Cdd:COG1127    5 MIEVRNLTKSFGDRV----------------------VL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  83 DVAVstttGPVNPYSCNAKALRDLRTHtVSMVFQQFALLPWRTVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWA 161
Cdd:COG1127   61 EILV----DGQDITGLSEKELYELRRR-IGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 162 GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPlIRTRLQDEL-LEFQRRLKKTILFVSHDLDEAFRIGNRIAI 240
Cdd:COG1127  136 DKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELiRELRDELGLTSVVVTHDLDSAFAIADRVAV 214
                        250       260
                 ....*....|....*....|....*...
gi 516735053 241 MESGRIIQCGTPHDIVKNPaDQYVADFV 268
Cdd:COG1127  215 LADGKIIAEGTPEELLASD-DPWVRQFL 241
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
4-259 2.33e-62

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: 198.57  E-value: 2.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPETALAmvdqgksrdeigaatglvlgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03258    2 IELKNVSKVFGDTGGKVTA--------------------LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVSTTtgpvNPYSCNAKALRDLRTHtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGR 163
Cdd:cd03258   62 VLVDGT----DLTLLSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES 243
Cdd:cd03258  137 YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
                        250
                 ....*....|....*.
gi 516735053 244 GRIIQCGTPHDIVKNP 259
Cdd:cd03258  217 GEVVEEGTVEEVFANP 232
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
34-269 2.33e-62

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 202.23  E-value: 2.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS---TTTgpvnpysCNAKALRDLRtHT 110
Cdd:COG1135   12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdLTA-------LSERELRAAR-RK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 111 VSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILL 190
Cdd:COG1135   84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 191 MDEPFSALDP------LirtrlqdELL-EFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:COG1135  164 CDEATSALDPettrsiL-------DLLkDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSEL 236

                 ....*.
gi 516735053 264 VADFVQ 269
Cdd:COG1135  237 TRRFLP 242
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-248 1.01e-60

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 195.47  E-value: 1.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPETALAMvdqgksrdeigaatglvlgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG4525    1 MSMLTVRHVSVRYPGGGQPQPAL--------------------QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAVS--TTTGPvnpyscnaKALRdlrthtvSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:COG4525   61 SGEITLDgvPVTGP--------GADR-------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRI 238
Cdd:COG4525  126 DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRL 205
                        250
                 ....*....|..
gi 516735053 239 AIMES--GRIIQ 248
Cdd:COG4525  206 VVMSPgpGRIVE 217
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
45-259 2.61e-60

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: 193.32  E-value: 2.61e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYSCNAKALRDLRTHtVSMVFQQ-----FA 119
Cdd:COG1122   19 DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-------DGKDITKKNLRELRRK-VGLVFQNpddqlFA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG1122   91 ----PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 200 PLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:COG1122  167 PRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
43-263 3.02e-60

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: 201.67  E-value: 3.02e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYSCNAKALRDLRTHtVSMVFQ--QFAL 120
Cdd:COG1123  281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF----DGKDLTKLSRRSLRELRRR-VQMVFQdpYSSL 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENVGFGLELAG-MPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:COG1123  356 NPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:COG1123  436 DVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
43-255 1.27e-59

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 191.82  E-value: 1.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGpVNPYSCNAKALRDlrthtVSMVFQQFALLP 122
Cdd:COG1131   16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL---G-EDVARDPAEVRRR-----IGYVPQEPALYP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:COG1131   87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 203 RTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:COG1131  167 RRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
4-267 1.46e-59

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: 191.56  E-value: 1.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03261    1 IELRGLTKSFGGRT----------------------VL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVSTttgpVNPYSCNAKALRDLRTHtVSMVFQQFALLPWRTVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWAG 162
Cdd:cd03261   57 VLIDG----EDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAED 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 163 RKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIME 242
Cdd:cd03261  132 LYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLY 211
                        250       260
                 ....*....|....*....|....*
gi 516735053 243 SGRIIQCGTPHDIvKNPADQYVADF 267
Cdd:cd03261  212 DGKIVAEGTPEEL-RASDDPLVRQF 235
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
45-246 4.92e-59

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: 189.62  E-value: 4.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYSCNAKALRDLRTHTVSMVFQQFALLPWR 124
Cdd:cd03255   22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT----DISKLSEKELAAFRRRHIGFVFQSFNLLPDL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03255   98 TALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGK 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 516735053 205 RLQDELLEFQRRLKKTILFVSHDLDEAfRIGNRIAIMESGRI 246
Cdd:cd03255  178 EVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
58-278 5.07e-59

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: 193.09  E-value: 5.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   58 LMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYscnakalrdLRThtVSMVFQQFALLPWRTVAENVGFGLEL 136
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDgEDVTNVPPH---------LRH--INMVFQSYALFPHMTVEENVAFGLKM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  137 AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRR 216
Cdd:TIGR01187  70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053  217 LKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQNLNPINMLT 278
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATV 211
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
45-272 1.21e-58

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 193.63  E-value: 1.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvnpyscnakalRDLrTHT------VSMVFQQF 118
Cdd:PRK09452  32 NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG---------------QDI-THVpaenrhVNTVFQSY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK09452  96 ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQNLN 272
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEIN 249
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
45-247 5.55e-58

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 187.17  E-value: 5.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYSCNAKALRDLRTHTVSMVFQQFALLPWR 124
Cdd:COG1136   26 GVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI----DGQDISSLSERELARLRRRHIGFVFQFFNLLPEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:COG1136  102 TALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGE 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 516735053 205 RLQDELLEFQRRLKKTILFVSHDLdEAFRIGNRIAIMESGRII 247
Cdd:COG1136  182 EVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
38-250 1.32e-57

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: 185.92  E-value: 1.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPvnpyscnakALRDlrthtVSM 113
Cdd:cd03301   11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPP---------KDRD-----IAM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03301   77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03301  157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
43-272 6.50e-57

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 189.28  E-value: 6.50e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYScnakalrdlrtHTVSMVFQQFALL 121
Cdd:PRK11607  35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQ-----------RPINMMFQSYALF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQNLN 272
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
45-245 1.39e-56

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: 182.00  E-value: 1.39e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAKALRDlrthTVSMVFQQFALLPWR 124
Cdd:cd03229   18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE--DLTDLEDELPPLRR----RIGMVFQDFALFPHL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLelagmpeaerklrvgeqlelvnltkwagrkvnelSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03229   92 TVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 516735053 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGR 245
Cdd:cd03229  138 EVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
45-268 4.05e-56

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: 182.92  E-value: 4.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGpvnpyscnakALRDLRTHTVSMVFQQFALLPWR 124
Cdd:cd03296   20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----------TDVPVQERNVGFVFQHYALFRHM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLEL----AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:cd03296   90 TVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:cd03296  170 KVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
45-268 5.95e-55

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: 179.84  E-value: 5.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpySCNAKALRDL--RTHTVSMVFQQFALLP 122
Cdd:cd03299   17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI------------LLNGKDITNLppEKRDISYVPQNYALFP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:cd03299   85 HMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:cd03299  165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
47-269 5.34e-54

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 177.49  E-value: 5.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnPYSCNAKALRDLRTHtVSMVFQQFALLPWRTV 126
Cdd:COG1126   21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE-----DLTDSKKDINKLRRK-VGMVFQQFNLFPHLTV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGFGLELA-GMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPlirtR 205
Cdd:COG1126   95 LENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----E 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 206 LQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:COG1126  171 LVGEVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
34-269 9.05e-54

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 180.00  E-value: 9.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYSCNAKALRDLRtHTVSM 113
Cdd:PRK11153  12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV----DGQDLTALSEKELRKAR-RQIGM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK11153  87 IFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 194 PFSALDPLIrTRLQDELL-EFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK11153 167 ATSALDPAT-TRSILELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
45-267 9.81e-54

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 180.30  E-value: 9.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG-------DVAVSTTTGpvnpyscnakalRDlrthtVSMVFQQ 117
Cdd:PRK11432  24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgeDVTHRSIQQ------------RD-----ICMVFQS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:PRK11432  87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADF 267
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
43-250 1.96e-53

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: 175.77  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnaKALRDLRTHTVSMVFQ--QFAL 120
Cdd:cd03257   21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK--DLLKLS---RRLRKIRRKEIQMVFQdpMSSL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENVGFGLELAGMP--EAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03257   96 NPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSA 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03257  176 LDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
5-245 3.84e-53

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: 174.19  E-value: 3.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   5 SFNNVSIIFGDRPETALamvdqgksrDEIgaatglvlgvadaSLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV 84
Cdd:cd03225    1 ELKNLSFSYPDGARPAL---------DDI-------------SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  85 AVstttgpvNPYSCNAKALRDLRTHtVSMVFQ----QFALLpwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:cd03225   59 LV-------DGKDLTKLSLKELRRK-VGLVFQnpddQFFGP---TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAI 240
Cdd:cd03225  128 RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIV 206

                 ....*
gi 516735053 241 MESGR 245
Cdd:cd03225  207 LEDGK 211
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
45-272 2.80e-52

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 176.43  E-value: 2.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLApvvrgdvavSTTTGPVNPYSCNAKAL--RDLRthtVSMVFQQFALLP 122
Cdd:PRK10851  20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE---------HQTSGHIRFHGTDVSRLhaRDRK---VGFVFQHYALFR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELagMPEAER------KLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK10851  88 HMTVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQNLN 272
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVN 241
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
46-267 1.07e-51

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 171.09  E-value: 1.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  46 ASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPvnpyscnakALRdlrthTVSMVFQQFALL 121
Cdd:COG3840   18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdlTALPP---------AER-----PVSMLFQENNLF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:COG3840   84 PHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADF 267
Cdd:COG3840  164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
33-260 1.28e-51

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: 178.94  E-value: 1.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  33 IGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP---VVRGDVAVSTTTgpvnpyscNAKALRDLRTH 109
Cdd:COG1123   12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRD--------LLELSEALRGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 110 TVSMVFQQF--ALLPWrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAP 187
Cdd:COG1123   84 RIGMVFQDPmtQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 188 ILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:COG1123  163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
43-269 3.47e-51

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: 170.37  E-value: 3.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPyscnaKALRDLRtHTVSMVFQQF--AL 120
Cdd:COG1124   21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR--PVTR-----RRRKAFR-RRVQMVFQDPyaSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENVGFGLELAGMPEAERklRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG1124   93 HPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:COG1124  171 VSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELLA 240
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
45-250 9.47e-50

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: 165.55  E-value: 9.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEgEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnPYSCNAKALrDLRTHT--VSMVFQQFALLP 122
Cdd:cd03297   16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-----VLFDSRKKI-NLPPQQrkIGLVFQQYALFP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLElaGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:cd03297   89 HLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 516735053 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03297  167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
45-269 1.66e-49

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 166.04  E-value: 1.66e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS--TTTGPvnpyscnAKALRDLRTHTvSMVFQQFALLP 122
Cdd:PRK09493  19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDP-------KVDERLIRQEA-GMVFQQFYLFP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPl 201
Cdd:PRK09493  91 HLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP- 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 202 irtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK09493 170 ---ELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQ 237
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
40-255 2.25e-49

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 165.62  E-value: 2.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYSCNAKALRDLRTHtVSMVFQQFA 119
Cdd:COG3638   16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV----DGQDVTALRGRALRRLRRR-IGMIFQQFN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENVgfgleLAGM--------------PEAERkLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATG 185
Cdd:COG3638   91 LVPRLSVLTNV-----LAGRlgrtstwrsllglfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQE 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:COG3638  165 PKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
45-255 1.88e-48

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: 163.12  E-value: 1.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:cd03256   19 DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLK--GKALRQLRRQ-IGMIFQQFNLIERL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGL--------ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:cd03256   94 SVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVA 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 197 ALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:cd03256  174 SLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
45-246 1.12e-47

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: 160.39  E-value: 1.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnPYSCNAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:cd03262   18 GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGL-----KLTDDKKNINELRQK-VGMVFQQFNLFPHL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPlir 203
Cdd:cd03262   92 TVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP--- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 516735053 204 tRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:cd03262  169 -ELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
47-329 1.58e-47

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 164.25  E-value: 1.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVN---PyscnakALRDlrthtVSMVFQQFALLPW 123
Cdd:PRK11650  24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR--VVNeleP------ADRD-----IAMVFQNYALYPH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 RTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIR 203
Cdd:PRK11650  91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 204 TRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQNlNPINMLtAADVM 283
Cdd:PRK11650 171 VQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGS-PAMNLL-DGRVS 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 516735053 284 QSGLGQTAAGMSVSATARAATPLIDILDALARQPGSIGIVENGAIV 329
Cdd:PRK11650 249 ADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEGGV 294
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
43-256 2.76e-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: 160.59  E-value: 2.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTH----TVSMVFQQF 118
Cdd:COG1120   17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL------------DGRDLASLSRRelarRIAYVPQEP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALlPWR-TVAENVGFG----LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG1120   85 PA-PFGlTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 194 PFSALDPlirtRLQDELLEFQRRL----KKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIV 256
Cdd:COG1120  164 PTSHLDL----AHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
38-255 3.41e-47

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: 160.02  E-value: 3.41e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYSCNAKALRDLrthtvSMVFQQ 117
Cdd:COG4555   12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG----EDVRKEPREARRQI-----GVLPDE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4555   83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 198 LDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:COG4555  163 LDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-268 3.50e-47

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 163.66  E-value: 3.50e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDrpetalamvdqgksrdeigaatglVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:PRK11000   1 MASVTLRNVTKAYGD------------------------VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAVstttgpvnpyscNAKALRDL--RTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:PRK11000  57 SGDLFI------------GEKRMNDVppAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLA 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRI 238
Cdd:PRK11000 125 HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKI 204
                        250       260       270
                 ....*....|....*....|....*....|
gi 516735053 239 AIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK11000 205 VVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
43-260 1.29e-46

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: 160.60  E-value: 1.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP---VVRGDVAVstttGPVNPYSCNAKALRDLRTHTVSMVFQ--Q 117
Cdd:COG0444   21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILF----DGEDLLKLSEKELRKIRGREIQMIFQdpM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKWAGRKVN---ELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG0444   97 TSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLIADE 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:COG0444  177 PTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
44-231 3.16e-46

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 157.94  E-value: 3.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  44 ADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV--STTTGPvnpyscnaKALRdlrthtvSMVFQQFALL 121
Cdd:PRK11248  18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGP--------GAER-------GVVFQNEGLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK11248  83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
                        170       180       190
                 ....*....|....*....|....*....|
gi 516735053 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEA 231
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDIEEA 192
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
4-247 3.75e-46

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 156.37  E-value: 3.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPEtALAmvdqgksrdeigaatglvlgvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:COG2884    2 IRFENVSKRYPGGRE-ALS----------------------DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQ 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVstttgpvnpyscNAKALRDLRTHTVS-------MVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVN 156
Cdd:COG2884   59 VLV------------NGQDLSRLKRREIPylrrrigVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVG 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 157 LTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGN 236
Cdd:COG2884  127 LSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPK 205
                        250
                 ....*....|.
gi 516735053 237 RIAIMESGRII 247
Cdd:COG2884  206 RVLELEDGRLV 216
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
45-244 1.21e-45

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: 155.70  E-value: 1.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPVNpyscnakalrdlrthtvSMVFQQFAL 120
Cdd:TIGR01184   3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkqiTEPGPDR-----------------MVVFQNYSL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  121 LPWRTVAENVGFGLE--LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:TIGR01184  66 LPWLTVRENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 516735053  199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESG 244
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
45-255 1.49e-45

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: 155.03  E-value: 1.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavSTTTGPVNPYSCNAKALRD----LRThTVSMVFQQFAL 120
Cdd:cd03260   18 DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG----APDEGEVLLDGKDIYDLDVdvleLRR-RVGMVFQKPNP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLTKWAGRKVN--ELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03260   93 FP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 198 LDPlIRTRLQDELLefqRRLKK--TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:cd03260  172 LDP-ISTAKIEELI---AELKKeyTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
45-259 1.67e-44

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


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 154.15  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYSCNAKALRDLRtHTVSMVFQQ-----FA 119
Cdd:TIGR04521  23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTI----DGRDITAKKKKKLKDLR-KKVGLVFQFpehqlFE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:TIGR04521  98 ----ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053  199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
45-260 3.01e-44

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: 155.64  E-value: 3.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpySCNAKALRDLRTH--TVSMVFQQFALLP 122
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV------LQDSARGIFLPPHrrRIGYVFQEARLFP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAgmPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDpli 202
Cdd:COG4148   91 HLSVRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD--- 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 203 rTRLQDELLEFQRRLKKT----ILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:COG4148  166 -LARKAEILPYLERLRDEldipILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
42-255 2.49e-43

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 149.76  E-value: 2.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYSCNAKALRDLRTHTvSMVFQQFALL 121
Cdd:TIGR02315  17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT----DITKLRGKKLRKLRRRI-GMIFQHYNLI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  122 PWRTVAENV--------GFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR02315  92 ERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADE 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053  194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:TIGR02315 172 PIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
43-252 7.96e-43

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: 147.65  E-value: 7.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYSCNAKalrdlrthtVSMVFQQFALLP 122
Cdd:cd03263   18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS---------LGYCPQFDALFD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:cd03263   89 ELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 516735053 203 RTRLQDELLEFQRrlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTP 252
Cdd:cd03263  169 RRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-255 2.39e-42

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 147.54  E-value: 2.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG1121    4 MPAIELENLTVSYGGRP----------------------VL--EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAVstttgpvnpyscNAKALRDLRtHTVSMVFQQFALlPWR---TVAENVGFGL----ELAGMPEAERKLRVGEQLE 153
Cdd:COG1121   60 SGTVRL------------FGKPPRRAR-RRIGYVPQRAEV-DWDfpiTVRDVVLMGRygrrGLFRRPSRADREAVDEALE 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 154 LVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDeLLEFQRRLKKTILFVSHDLDEAFR 233
Cdd:COG1121  126 RVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVRE 204
                        250       260
                 ....*....|....*....|..
gi 516735053 234 IGNRIAIMeSGRIIQCGTPHDI 255
Cdd:COG1121  205 YFDRVLLL-NRGLVAHGPPEEV 225
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
45-268 1.86e-41

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 145.13  E-value: 1.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavSTTTGPV-----NPYSCNAKALrDLRTHtVSMVFQQFA 119
Cdd:TIGR00972  19 NINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPG----VRIEGKVlfdgqDIYDKKIDVV-ELRRR-VGMVFQKPN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  120 LLPwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLtkWAGRK------VNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:TIGR00972  93 PFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAAL--WDEVKdrlhdsALGLSGGQQQRLCIARALAVEPEVLLLD 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053  193 EPFSALDPlIRTRlqdELLEFQRRLKK--TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:TIGR00972 170 EPTSALDP-IATG---KIEELIQELKKkyTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTEDYI 243
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
45-268 2.12e-40

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 142.48  E-value: 2.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNG---LAPVVRgdvavstTTGPV-----NPYSCNAKaLRDLRTHtVSMVFQ 116
Cdd:COG1117   29 DINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGAR-------VEGEIlldgeDIYDPDVD-VVELRRR-VGMVFQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWrTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLtkWagrkvNE-----------LSGGMQQRVGLARAFAT 184
Cdd:COG1117  100 KPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAAL--W-----DEvkdrlkksalgLSGGQQQRLCIARALAV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 185 GAPILLMDEPFSALDPlIRTRLQDELLefqRRLKK--TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQ 262
Cdd:COG1117  172 EPEVLLMDEPTSALDP-ISTAKIEELI---LELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247

                 ....*.
gi 516735053 263 YVADFV 268
Cdd:COG1117  248 RTEDYI 253
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
45-246 2.44e-40

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 141.11  E-value: 2.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV-----AVSTTTGPvnpyscnakalrDLRTHtVSMVFQQFA 119
Cdd:COG4619   18 PVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAMPPP------------EWRRQ-VAYVPQEPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LlpWR-TVAENVGFGLELAGMPEAERKLRvgEQLELVNLTKWA-GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4619   85 L--WGgTVRDNLPFPFQLRERKFDRERAL--ELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:COG4619  161 LDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
45-246 2.83e-40

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: 139.46  E-value: 2.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGpVNPYSCNAKALRDlrthtVSMVFQQFALLPWR 124
Cdd:cd03230   18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL---G-KDIKKEPEEVKRR-----IGYLPEEPSLYENL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVgfglelagmpeaerklrvgeqlelvnltkwagrkvnELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03230   89 TVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 516735053 205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:cd03230  133 EFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
45-245 7.67e-40

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 140.08  E-value: 7.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAKALrdLRTHtVSMVFQQFALLPWR 124
Cdd:TIGR02673  20 DVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGE--DVNRLRGRQLPL--LRRR-IGVVFQDFRLLPDR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:TIGR02673  95 TVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSE 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 516735053  205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGR 245
Cdd:TIGR02673 175 RILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
43-250 1.41e-39

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: 137.95  E-value: 1.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLrthtvsmvfqqfallP 122
Cdd:cd03214   15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL------------DGKDLASL---------------S 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFglelagMPEAerklrvgeqLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPli 202
Cdd:cd03214   68 PKELARKIAY------VPQA---------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI-- 130
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516735053 203 rtRLQDELLEFQRRLK----KTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03214  131 --AHQIELLELLRRLArergKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
43-257 1.52e-39

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 140.92  E-value: 1.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpysCNAKALRDLRTHtVSMVFQ----QF 118
Cdd:PRK13635  23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-------LSEETVWDVRRQ-VGMVFQnpdnQF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 AllpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK13635  95 V---GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 199 DPLIRtrlqDELLEFQRRLKK----TILFVSHDLDEAFRiGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:PRK13635 172 DPRGR----REVLETVRQLKEqkgiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
45-267 2.52e-39

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 139.38  E-value: 2.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV-------STTTGPvnpyscnaKALRDLRtHTVSMVFQQ 117
Cdd:PRK11124  20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfSKTPSD--------KAIRELR-RNVGMVFQQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVgfgLE----LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK11124  91 YNLWPHLTVQQNL---IEapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 194 PFSALDPLIRTRLQDELLEFQrRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTpHDIVKNPADQYVADF 267
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNY 239
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
45-258 4.96e-39

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 139.49  E-value: 4.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpySCNAKALRDLRTHtVSMVFQ----QF-- 118
Cdd:TIGR04520  20 NVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD------TLDEENLWEIRKK-VGMVFQnpdnQFvg 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  119 AllpwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:TIGR04520  93 A-----TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  199 DPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:TIGR04520 168 DPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
45-196 2.16e-38

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: 133.93  E-value: 2.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpySCNAKALRDLRTHtVSMVFQQFALLPWR 124
Cdd:pfam00005   3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ-------DLTDDERKSLRKE-IGYVFQDPQLFPRL 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053  125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKV----NELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:pfam00005  75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
45-267 5.81e-38

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 135.91  E-value: 5.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVST-----TTGPvnpyscNAKALRDLRtHTVSMVFQQFA 119
Cdd:COG4161   20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfSQKP------SEKAIRLLR-QKVGMVFQQYN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENVgfgLE----LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:COG4161   93 LWPHLTVMENL---IEapckVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 196 SALDPLIrtrlQDELLEFQRRLKKT-I--LFVSHDLDEAFRIGNRIAIMESGRIIQCGTpHDIVKNPADQYVADF 267
Cdd:COG4161  170 AALDPEI----TAQVVEIIRELSQTgItqVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHY 239
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
45-268 6.38e-38

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 136.06  E-value: 6.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVN---GLAPVVrgdvavsTTTGPV-----NPYSCNAKALrDLRTHtVSMVFQ 116
Cdd:PRK14239  23 SVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEV-------TITGSIvynghNIYSPRTDTV-DLRKE-IGMVFQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWrTVAENVGFGLELAGMPEAERKLRVGEQlELVNLTKWAGRK------VNELSGGMQQRVGLARAFATGAPILL 190
Cdd:PRK14239  94 QPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWDEVKdrlhdsALGLSGGQQQRVCIARVLATSPKIIL 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 191 MDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
34-263 9.80e-38

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 137.56  E-value: 9.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV---AVSTTTGpvnpyscNAKALRDLRTHt 110
Cdd:COG4608   25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIlfdGQDITGL-------SGRELRPLRRR- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 111 VSMVFQQ-FALL-PWRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:COG4608   97 MQMVFQDpYASLnPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNP 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:COG4608  177 KLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPY 253
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
43-260 1.29e-37

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: 135.17  E-value: 1.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHTVS---MV--FQQ 117
Cdd:COG0411   20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF------------DGRDITGLPPHRIArlgIArtFQN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENV---------------GFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAF 182
Cdd:COG0411   88 PRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 183 ATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:COG0411  168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
47-250 3.17e-37

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: 133.00  E-value: 3.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV---AVSTTTGPVnpyscnakALRdlrthTVSMVFQQFALLPW 123
Cdd:cd03298   18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlinGVDVTAAPP--------ADR-----PVSMLFQENNLFAH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 RTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIR 203
Cdd:cd03298   85 LTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 516735053 204 TRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03298  165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
45-245 1.54e-36

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: 129.29  E-value: 1.54e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYSCNAKALRDLRTHtVSMVFQqfallpwr 124
Cdd:cd00267   17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------DGKDIAKLPLEELRRR-IGYVPQ-------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 tvaenvgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd00267   81 -------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 516735053 205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGR 245
Cdd:cd00267  118 RLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
43-260 2.63e-36

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: 131.41  E-value: 2.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHT-----VSMVFQQ 117
Cdd:cd03219   16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF------------DGEDITGLPPHEiarlgIGRTFQI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENV--------GFGLELAGMPEAERKLR--VGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAP 187
Cdd:cd03219   84 PRLFPELTVLENVmvaaqartGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 188 ILLMDEPFSALDPlirtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:cd03219  164 LLLLDEPAAGLNP----EETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
PhnK COG4107
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ...
34-250 1.03e-35

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


Pssm-ID: 443283 [Multi-domain]  Cd Length: 262  Bit Score: 130.32  E-value: 1.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTT-TGPVNPYSCNAKALRDLRTHTVS 112
Cdd:COG4107   19 GPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRdGGPRDLFALSEAERRRLRRTDWG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 113 MVFQQ--FALLPWRTVAENVGFGLELAGMPEAER-KLRVGEQLELVNLTkwAGRKVNE---LSGGMQQRVGLARAFATGA 186
Cdd:COG4107   99 MVYQNprDGLRMDVSAGGNIAERLMAAGERHYGDiRARALEWLERVEIP--LERIDDLprtFSGGMQQRVQIARALVTNP 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:COG4107  177 RLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESG 240
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
45-248 1.11e-35

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: 129.48  E-value: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAKALrdLRTHTVSMVFQQFALLPWR 124
Cdd:COG4181   30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ--DLFALDEDARAR--LRARHVGFVFQSFQLLPTL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:COG4181  106 TALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGE 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 516735053 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGnRIAIMESGRIIQ 248
Cdd:COG4181  184 QIIDLLFELNRERGTTLVLVTHDPALAARCD-RVLRLRAGRLVE 226
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
47-231 2.82e-35

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: 127.60  E-value: 2.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyscNAKALRDLRTHTVSMVFQQFALLPWRTV 126
Cdd:COG4133   22 SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE---------PIRDAREDYRRRLAYLGHADGLKPELTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGFGLELAGMPEAERklRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:COG4133   93 RENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
                        170       180
                 ....*....|....*....|....*
gi 516735053 207 QDELLEFQRRlKKTILFVSHDLDEA 231
Cdd:COG4133  171 AELIAAHLAR-GGAVLLTTHQPLEL 194
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
43-263 3.40e-35

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: 128.26  E-value: 3.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP----VVRGDVAVSTTtgPVNPYScnakalrdLRTHTVSMVFQ-- 116
Cdd:TIGR02770   2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGR--PLLPLS--------IRGRHIATIMQnp 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  117 QFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKwaGRKV-----NELSGGMQQRVGLARAFATGAPILLM 191
Cdd:TIGR02770  72 RTAFNPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPD--PEEVlkkypFQLSGGMLQRVMIALALLLEPPFLIA 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053  192 DEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:TIGR02770 150 DEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHET 221
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
45-238 4.04e-35

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 127.35  E-value: 4.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV-STTTGPVNpyscNAKAlRDLRTHTVSMVFQQFALLPW 123
Cdd:TIGR03608  16 DLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLnGQETPPLN----SKKA-SKFRREKLGYLFQNFALIEN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  124 RTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPliR 203
Cdd:TIGR03608  91 ETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP--K 168
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 516735053  204 TRlqDELLEFQRRLK---KTILFVSHDLdEAFRIGNRI 238
Cdd:TIGR03608 169 NR--DEVLDLLLELNdegKTIIIVTHDP-EVAKQADRV 203
cbiO PRK13637
energy-coupling factor transporter ATPase;
45-258 5.52e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 129.40  E-value: 5.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYSCNAKaLRDLRTHtVSMVFQ--QFALLP 122
Cdd:PRK13637  25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII----DGVDITDKKVK-LSDIRKK-VGLVFQypEYQLFE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 wRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT--KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13637  99 -ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
38-252 5.93e-35

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: 127.10  E-value: 5.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavsttTGPVNPYScnakALRDLRT--HTVSMVF 115
Cdd:cd03265   11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-------RATVAGHD----VVREPREvrRRIGIVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 116 QQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:cd03265   80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTP 252
Cdd:cd03265  160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
45-265 1.04e-34

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: 130.23  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpySCNAKALRDLRTH--TVSMVFQQFALLP 122
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT------LFDSRKGIFLPPEkrRIGYVFQEARLFP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  123 WRTVAENVGFGLELAgMPEaERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDpli 202
Cdd:TIGR02142  89 HLSVRGNLRYGMKRA-RPS-ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD--- 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053  203 rTRLQDELLEFQRRLKKT----ILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVA 265
Cdd:TIGR02142 164 -DPRKYEILPYLERLHAEfgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
45-257 1.88e-34

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 132.06  E-value: 1.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttG-PVNPYScnakaLRDLRTHTVSMVFQQFALLPW 123
Cdd:COG1129   22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD---GePVRFRS-----PRDAQAAGIAIIHQELNLVPN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 RTVAENVGFGLELAGMP---EAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:COG1129   94 LSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 201 lirtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRIIQCG-----TPHDIVK 257
Cdd:COG1129  174 ----REVERLFRIIRRLKAqgvAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVR 234
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
47-262 1.93e-34

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 126.24  E-value: 1.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPvnpyscnakALRdlrthTVSMVFQQFALLP 122
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhTTTPP---------SRR-----PVSMLFQENNLFS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK10771  85 HLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 203 RT---RLQDELLEfQRRLkkTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQ 262
Cdd:PRK10771 165 RQemlTLVSQVCQ-ERQL--TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
41-261 3.16e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 127.44  E-value: 3.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  41 LGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPySCNAKALRDLRTHtVSMVFQqF-- 118
Cdd:PRK13634  21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--ITA-GKKNKKLKPLRKK-VGIVFQ-Fpe 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:PRK13634  96 HQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPAD 261
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
45-241 9.72e-34

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: 123.80  E-value: 9.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRtHTVSMVfQQFALLPWR 124
Cdd:cd03235   17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV------------FGKPLEKER-KRIGYV-PQRRSIDRD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 ---TVAENVGFGL----ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03235   83 fpiSVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 516735053 198 LDPLIRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIM 241
Cdd:cd03235  163 VDPKTQEDIY-ELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
40-246 1.15e-33

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: 123.67  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAKALrdLRTHtVSMVFQQFA 119
Cdd:cd03292   14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ--DVSDLRGRAIPY--LRRK-IGVVFQDFR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03292   89 LLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 516735053 200 PLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:cd03292  169 PDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
38-250 1.33e-33

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: 123.54  E-value: 1.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHTVSMVFQQ 117
Cdd:cd03269   11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF------------DGKPLDIAARNRIGYLPEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03269   79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 198 LDPLIRTRLQDELLEfQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03269  159 LDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
47-259 1.34e-33

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 124.91  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS------TTTGPVNPYSCNAKALRDLRTHtVSMVFQQFAL 120
Cdd:COG4598   28 SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlKPDRDGELVPADRRQLQRIRTR-LGMVFQSFNL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG4598  107 WSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 200 PlirtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:COG4598  187 P----ELVGEVLKVMRDLAeegRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
48-269 1.52e-33

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 124.48  E-value: 1.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  48 LTIEEGEILVLMGLSGSGKSTLLRAVNGL----APVVR-GDVAVSTTtgpvNPYSCNAKALRDLRTHtVSMVFQQFALLP 122
Cdd:PRK11264  24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLeqpeAGTIRvGDITIDTA----RSLSQQKGLIRQLRQH-VGFVFQNFNLFP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPl 201
Cdd:PRK11264  99 HRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP- 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 202 irtRLQDELLEFQRRL---KKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK11264 178 ---ELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
43-263 2.61e-33

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: 129.42  E-value: 2.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPvVRGDVAVSTTtgPVNPYScnAKALRDLRTHtVSMVFQQ-FALL 121
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQ--DLDGLS--RRALRPLRRR-MQVVFQDpFGSL 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 -PWRTVAENVGFGLEL--AGMPEAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4172  376 sPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:COG4172  456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPY 521
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
43-254 7.39e-33

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 121.43  E-value: 7.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPVVR--GDVAVstttgpvnpyscNAKALRDLRTHT--VSMVFQQ 117
Cdd:COG4136   17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFSasGEVLL------------NGRRLTALPAEQrrIGILFQD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLElAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4136   85 DLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAfrignriaiMESGRIIQCGTPHD 254
Cdd:COG4136  164 LDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA---------PAAGRVLDLGNWQH 211
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
4-245 7.77e-33

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: 120.18  E-value: 7.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPETALAmvdqgksrdeigaatglvlgvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03228    1 IEFKNVSFSYPGRPKPVLK----------------------DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVSTTtgPVNPYScnakaLRDLRTHtVSMVFQQFALLPwRTVAENVgfglelagmpeaerklrvgeqlelvnltkwagr 163
Cdd:cd03228   59 ILIDGV--DLRDLD-----LESLRKN-IAYVPQDPFLFS-GTIRENI--------------------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 164 kvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMES 243
Cdd:cd03228   97 ----LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDD 169

                 ..
gi 516735053 244 GR 245
Cdd:cd03228  170 GR 171
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
43-254 2.39e-32

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 121.38  E-value: 2.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPVnpySCNAKALRDLRTHTVSM---VFQQF 118
Cdd:COG4559   17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTP----------SSGEV---RLNGRPLAAWSPWELARrraVLPQH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALL--PWrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFA-------TGAPIL 189
Cdd:COG4559   84 SSLafPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 190 LMDEPFSALDPlirtRLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHD 254
Cdd:COG4559  163 FLDEPTSALDL----AHQHAVLRLARQLARrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
43-252 5.65e-32

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: 121.73  E-value: 5.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvavsttTGPVNPYSCNAKAlRDLRtHTVSMVFQQFALLP 122
Cdd:TIGR01188   9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSG-------TARVAGYDVVREP-RKVR-RSIGIVPQYASVDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:TIGR01188  80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 516735053  203 RTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTP 252
Cdd:TIGR01188 160 RRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
33-263 5.98e-32

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: 125.57  E-value: 5.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  33 IGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvrgdvAVSTTTGPV-----NPYSCNAKALRDLR 107
Cdd:COG4172   16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPD-----PAAHPSGSIlfdgqDLLGLSERELRRIR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 108 THTVSMVFQQ--FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKwAGRKVN----ELSGGMQQRVGLAR 180
Cdd:COG4172   91 GNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPD-PERRLDayphQLSGGQRQRVMIAM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 181 AFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:COG4172  170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249

                 ...
gi 516735053 261 DQY 263
Cdd:COG4172  250 HPY 252
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
43-255 6.66e-32

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 121.37  E-value: 6.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVnpySCNAKALRDLrthtvsmVFQQFALLP 122
Cdd:COG4152   17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI---------LAPDSGEV---LWDGEPLDPE-------DRRRIGYLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 -WR------TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFAtGAP-ILLMDEP 194
Cdd:COG4152   78 eERglypkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL-HDPeLLILDEP 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 195 FSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:COG4152  157 FSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
45-255 4.76e-31

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: 116.76  E-value: 4.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHT-----VSMVFQQFA 119
Cdd:cd03224   18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF------------DGRDITGLPPHEraragIGYVPEGRR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENvgfgLELAGM--PEAERKLRVGEQLELV-NLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:cd03224   86 IFPELTVEEN----LLLGAYarRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 197 ALDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:cd03224  162 GLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
48-246 5.79e-31

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 117.86  E-value: 5.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  48 LTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVnpyscnAKALRDLRthtvsMVFQQFALLPWRTVA 127
Cdd:PRK11247  33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA--PL------AEAREDTR-----LMFQDARLLPWKKVI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 128 ENVGFGLELAGMPEAErklrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQ 207
Cdd:PRK11247 100 DNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 516735053 208 DELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-255 7.79e-31

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: 117.11  E-value: 7.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPetalamvdqgksrdeigaatglVLGvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPV 79
Cdd:COG1119    1 DPLLELRNVTVRRGGKT----------------------ILD--DISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPT 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  80 VRGDVAV-STTTGPVNpyscnakaLRDLRTHT--VSMVFQQFalLPWRTVAENV---GF--GLELAGMPEAERKLRVGEQ 151
Cdd:COG1119   57 YGNDVRLfGERRGGED--------VWELRKRIglVSPALQLR--FPRDETVLDVvlsGFfdSIGLYREPTDEQRERAREL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 152 LELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEA 231
Cdd:COG1119  127 LELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEI 206
                        250       260
                 ....*....|....*....|....
gi 516735053 232 FRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:COG1119  207 PPGITHVLLLKDGRVVAAGPKEEV 230
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
43-268 9.70e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 116.94  E-value: 9.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-----APVVRGDVAVSTTtgpvNPYSCNAKALRdlrtHTVSMVFQQ 117
Cdd:PRK14247  19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQ----DIFKMDVIELR----RRVQMVFQI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMPEAERKL--RVGEQLELVNLTKWAGRKVN----ELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK14247  91 PNPIPNLSIFENVALGLKLNRLVKSKKELqeRVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLA 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 192 DEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
47-269 1.56e-30

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 116.61  E-value: 1.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVST--------TTGPVNPYscNAKALRDLRTHtVSMVFQQF 118
Cdd:PRK10619  25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdKDGQLKVA--DKNQLRLLRTR-LTMVFQHF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFG-LELAGMPEAERKLRVGEQLELVNLTKWA-GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK10619 102 NLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 197 ALDPlirtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQ 269
Cdd:PRK10619 182 ALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
34-250 3.68e-30

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: 114.39  E-value: 3.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  34 GAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvVRGDVAVSTTTGpVNPYSCNAKALRDLrthtvSM 113
Cdd:cd03266   12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL---LEPDAGFATVDG-FDVVKEPAEARRRL-----GF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 114 VFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03266   83 VSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 194 PFSALDpLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03266  163 PTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
45-270 4.60e-30

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: 121.09  E-value: 4.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYSCNAKALRDLRTHtVSMVFQQFALLPwR 124
Cdd:COG2274  493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-------DGIDLRQIDPASLRRQ-IGVVLQDVFLFS-G 563
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVN-LTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:COG2274  564 TIRENITLGDPDATDEEIIEAARLAGLHDFIEaLPMGYDTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALD 643
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 200 PLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTPHDIVKnpADQYVADFVQN 270
Cdd:COG2274  644 AETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLA--RKGLYAELVQQ 709
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
41-258 5.99e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 115.57  E-value: 5.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  41 LGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttgpvNPYSCNAKALRDLRThTVSMVFQQ--- 117
Cdd:PRK13633  24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD------GLDTSDEENLWDIRN-KAGMVFQNpdn 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 --FALLpwrtVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:PRK13633  97 qiVATI----VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
cbiO PRK13645
energy-coupling factor transporter ATPase;
45-258 6.29e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 115.88  E-value: 6.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYSCnaKALRDLRTHtVSMVFQ--QFALLP 122
Cdd:PRK13645  29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKI--KEVKRLRKE-IGLVFQfpEYQLFQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 wRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK13645 106 -ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 202 IRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
cbiO PRK13650
energy-coupling factor transporter ATPase;
45-255 7.51e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 115.21  E-value: 7.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpySCNAKALRDLRtHTVSMVFQ----QFAl 120
Cdd:PRK13650  25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-------LLTEENVWDIR-HKIGMVFQnpdnQFV- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 lpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13650  96 --GATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAfRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
45-252 1.10e-29

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 114.48  E-value: 1.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHTVSM---VFQQFALL 121
Cdd:PRK13548  20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL------------NGRPLADWSPAELARrraVLPQHSSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 --PWrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFA------TGAPILLMDE 193
Cdd:PRK13548  88 sfPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 194 PFSALDPlirtRLQDELLEFQRRLKK----TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTP 252
Cdd:PRK13548 167 PTSALDL----AHQHHVLRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
43-258 1.16e-29

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: 119.09  E-value: 1.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHTVsmvFQQFALLP 122
Cdd:COG4988  353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI------------NGVDLSDLDPASW---RRQIAWVP 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WR------TVAENVGFGLELAGMPEAERKLRvgeqleLVNLTKWAGR-------KVNE----LSGGMQQRVGLARAFATG 185
Cdd:COG4988  418 QNpylfagTIRENLRLGRPDASDEELEAALE------AAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALARALLRD 491
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAfRIGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:COG4988  492 APLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
43-260 1.27e-29

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: 119.10  E-value: 1.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttGPVNPYSCNAKALRDLrthtVSMVFQQFALLP 122
Cdd:COG4987  351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL----GGVDLRDLDEDDLRRR----IAVVPQRPHLFD 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 wRTVAENvgfgLELAGmPEA-ERKLRvgEQLELVNLTKW--------------AGRKvneLSGGMQQRVGLARAFATGAP 187
Cdd:COG4987  423 -TTLREN----LRLAR-PDAtDEELW--AALERVGLGDWlaalpdgldtwlgeGGRR---LSGGERRRLALARALLRDAP 491
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 188 ILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:COG4987  492 ILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNG 561
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
45-247 1.41e-29

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 118.59  E-value: 1.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttG-PVNPYSCNAkALRdlrtHTVSMVFQQFALLPW 123
Cdd:COG3845   23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID---GkPVRIRSPRD-AIA----LGIGMVHQHFMLVPN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 RTVAENVGFGLE-----LAGMPEAERKLR-VGEQLEL-VNLTkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:COG3845   95 LTVAENIVLGLEptkggRLDRKAARARIReLSERYGLdVDPD----AKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 197 ALDPlirtrlQ--DELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:COG3845  171 VLTP------QeaDELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRGKVV 220
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
38-256 1.44e-29

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: 118.75  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS--------TTTGPVNpyscnakalRDLRTH 109
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPGPDG---------RGRAKR 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  110 TVSMVFQQFALLPWRTVAENV--GFGLELagmPEAERKLRVGEQLELVNLTKWAGRKV-----NELSGGMQQRVGLARAF 182
Cdd:TIGR03269 366 YIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVL 442
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053  183 ATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIV 256
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
45-248 2.99e-29

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 113.63  E-value: 2.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYS-CNAKALRdlrtHTVSMVFQQF--ALL 121
Cdd:PRK10419  30 NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE--PLAKLNrAQRKAFR----RDIQMVFQDSisAVN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGFGLE-LAGMPEAERKLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:PRK10419 104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 516735053 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQ 248
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
45-247 7.19e-29

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: 109.44  E-value: 7.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnakaLRDLRTHTVSMVFQqfallpwr 124
Cdd:cd03216   18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--EVSFAS-----PRDARRAGIAMVYQ-------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 tvaenvgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPlirt 204
Cdd:cd03216   83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP---- 115
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 516735053 205 RLQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:cd03216  116 AEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
43-255 8.41e-29

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 112.03  E-value: 8.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAKAlrdlrthtvsmvfQQFALLP 122
Cdd:PRK11231  18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK--PISMLSSRQLA-------------RRLALLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WR-------TVAENVGFG----LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK11231  83 QHhltpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 192 DEPFSALDplirTRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:PRK11231 163 DEPTTYLD----INHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
cbiO PRK13641
energy-coupling factor transporter ATPase;
3-259 1.20e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 112.23  E-value: 1.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   3 AVSFNNVSIIFGdrPETALamvdQGKSRDEIgaatglvlgvadaSLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG 82
Cdd:PRK13641   2 SIKFENVDYIYS--PGTPM----EKKGLDNI-------------SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  83 DVAVSTTTgpVNPYSCNaKALRDLRTHtVSMVFQqF--ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL-TK 159
Cdd:PRK13641  63 TITIAGYH--ITPETGN-KNLKKLRKK-VSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsED 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 160 WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIA 239
Cdd:PRK13641 138 LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVL 216
                        250       260
                 ....*....|....*....|
gi 516735053 240 IMESGRIIQCGTPHDIVKNP 259
Cdd:PRK13641 217 VLEHGKLIKHASPKEIFSDK 236
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
48-253 1.29e-28

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 111.64  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  48 LTIEEGEILVLMGLSGSGKSTLLRAVNGLapvVRGDVAVSTTTGPV-NPYSCNAKALRDLR---THTvSMVFQQFALLPW 123
Cdd:PRK09984  25 LNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIELLgRTVQREGRLARDIRksrANT-GYIFQQFNLVNR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 RTVAENVGFGlELAGMP---------EAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PRK09984 101 LSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 195 FSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPH 253
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
43-247 1.60e-28

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: 110.00  E-value: 1.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYSCNAKALRdlrtHTVSMVFQQfALLP 122
Cdd:cd03268   16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-----KSYQKNIEALR----RIGALIEAP-GFYP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAerklRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL- 201
Cdd:cd03268   86 NLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDg 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 516735053 202 IRtrlqdELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:cd03268  162 IK-----ELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKLI 205
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
45-258 1.72e-28

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 116.03  E-value: 1.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnakaLRDLRTHtVSMVFQQFALLPwR 124
Cdd:COG1132  358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV--DIRDLT-----LESLRRQ-IGVVPQDTFLFS-G 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRvgeqleLVNLTKWA-----------GRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG1132  429 TIRENIRYGRPDATDEEVEEAAK------AAQAHEFIealpdgydtvvGERGVNLSGGQRQRIAIARALLKDPPILILDE 502
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 194 PFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:COG1132  503 ATSALDTETEALIQEALERLMKG--RTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
45-248 1.92e-28

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 110.29  E-value: 1.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAKAlrDLRTHTVSMVFQQFALLPWR 124
Cdd:PRK11629  27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKA--ELRNQKLGFIYQFHHLLPDF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 516735053 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIgNRIAIMESGRIIQ 248
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
45-231 1.98e-28

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 109.05  E-value: 1.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnPYSCNAKALRDLRTHtVSMVFQQ-----FA 119
Cdd:TIGR01166  10 GLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE-----PLDYSRKGLLERRQR-VGLVFQDpddqlFA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR01166  84 ----ADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 516735053  200 PLIRTRLQDELlefqRRLK---KTILFVSHDLDEA 231
Cdd:TIGR01166 160 PAGREQMLAIL----RRLRaegMTVVISTHDVDLA 190
cbiO PRK13643
energy-coupling factor transporter ATPase;
45-257 2.77e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 111.36  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-----APVVRGDVAVSTTTgpvnpyscNAKALRDLRThTVSMVFQ-QF 118
Cdd:PRK13643  24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlqpteGKVTVGDIVVSSTS--------KQKEIKPVRK-KVGVVFQfPE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTK--WAgRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK13643  95 SQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADefWE-KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 197 ALDPLIRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:PRK13643 174 GLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
44-268 3.00e-28

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 110.62  E-value: 3.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  44 ADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyscNAKALRDLRTHTV----SMVFQQFA 119
Cdd:PRK11831  24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---------NIPAMSRSRLYTVrkrmSMLFQSGA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENVGFGL-ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK11831  95 LFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 199 DPL---IRTRLQDELlefQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPaDQYVADFV 268
Cdd:PRK11831 175 DPItmgVLVKLISEL---NSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFL 243
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
45-250 3.11e-28

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: 109.20  E-value: 3.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGeILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPyscnakalRDLRTHtVSMVFQQFALLPWR 124
Cdd:cd03264   18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--------QKLRRR-IGYLPQEFGVYPNF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03264   88 TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 516735053 205 RLQDELLEFQRrlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03264  168 RFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
43-270 3.71e-28

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 110.31  E-value: 3.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKAL----RDLRTHTVSMVFQ-- 116
Cdd:COG4167   29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILI------------NGHKLeygdYKYRCKHIRMIFQdp 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWRTVAENVGFGLELA-GMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:COG4167   97 NTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 195 FSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVADFVQN 270
Cdd:COG4167  177 LAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIES 252
cbiO PRK13640
energy-coupling factor transporter ATPase;
3-259 3.72e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 111.05  E-value: 3.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   3 AVSFNNVSIIFGDRPETAlamvdqgksrdeigaatglvlgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapVVRG 82
Cdd:PRK13640   5 IVEFKHVSFTYPDSKKPA----------------------LNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPD 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  83 DVAVSTTTgpVNPYSCNAKALRDLRtHTVSMVFQ----QFAllpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLT 158
Cdd:PRK13640  61 DNPNSKIT--VDGITLTAKTVWDIR-EKVGIVFQnpdnQFV---GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGML 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 159 KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAfRIGNRI 238
Cdd:PRK13640 135 DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQV 213
                        250       260
                 ....*....|....*....|.
gi 516735053 239 AIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK13640 214 LVLDDGKLLAQGSPVEIFSKV 234
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
45-258 3.79e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 110.47  E-value: 3.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpysCNAKALRDLRTHtVSMVFQ----QFAL 120
Cdd:PRK13632  27 NVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT-------ISKENLKEIRKK-IGIIFQnpdnQFIG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LpwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13632  99 A---TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFrIGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
43-268 4.30e-28

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 109.93  E-value: 4.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV-----VRGDVAVSTttgpVNPYSCNAKALRDLRThtVSMVFQQ 117
Cdd:PRK14267  20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFG----RNIYSPDVDPIEVRRE--VGMVFQY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMpeaerklrVGEQLELVNLTKWAGRKV--------------NELSGGMQQRVGLARAFA 183
Cdd:PRK14267  94 PNPFPHLTIYDNVAIGVKLNGL--------VKSKKELDERVEWALKKAalwdevkdrlndypSNLSGGQRQRLVIARALA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 184 TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243

                 ....*
gi 516735053 264 VADFV 268
Cdd:PRK14267 244 TEKYV 248
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
45-260 4.87e-28

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: 109.30  E-value: 4.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHT-----VSMVFQQ-- 117
Cdd:COG0410   21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF------------DGEDITGLPPHRiarlgIGYVPEGrr 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 -FALLpwrTVAENvgfgLELAGMPEAERKlRVGEQLELV-----NLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:COG0410   89 iFPSL---TVEEN----LLLGAYARRDRA-EVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 192 DEPFSALDPLIRtrlqDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:COG0410  161 DEPSLGLAPLIV----EEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
45-257 1.06e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 109.46  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnakaLRDLRTHtVSMVFQ----QFAl 120
Cdd:PRK13648  27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ--AITDDN-----FEKLRKH-IGIVFQnpdnQFV- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 lpWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13648  98 --GSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 201 LIRTrlqdELLEFQRRLKK----TILFVSHDLDEAFRiGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:PRK13648 176 DARQ----NLLDLVRKVKSehniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
47-259 1.24e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 109.40  E-value: 1.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYSCNAKALRDLRtHTVSMVFQQ-----FAll 121
Cdd:PRK13639  22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-----EPIKYDKKSLLEVR-KTVGIVFQNpddqlFA-- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK13639  94 P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 202 IRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
43-247 1.92e-27

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: 106.96  E-value: 1.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpysCNAKALRDLRTHTVSMVFQ----QF 118
Cdd:cd03226   16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL-----------NGKPIKAKERRKSIGYVMQdvdyQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALlpwRTVAENVGFGLELAGmpeaERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03226   85 FT---DSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 516735053 199 DPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:cd03226  158 DYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
24-268 2.34e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 108.21  E-value: 2.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  24 VDQGKSRDEIGAATGLVLGVADASL------TIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGPV---- 93
Cdd:PRK14246   1 MEAGKSAEDVFNISRLYLYINDKAIlkditiKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVD---GKVlyfg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  94 -NPYSCNAKALRDlrthTVSMVFQQFALLPWRTVAENVGFGLELAGMPEA-ERKLRVGEQLELVNLTKWAGRKVN----E 167
Cdd:PRK14246  78 kDIFQIDAIKLRK----EVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRLNspasQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 168 LSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELV 231
                        250       260
                 ....*....|....*....|.
gi 516735053 248 QCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14246 232 EWGSSNEIFTSPKNELTEKYV 252
cbiO PRK13644
energy-coupling factor transporter ATPase;
47-264 6.18e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 107.38  E-value: 6.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpySCNAKALRDLRThTVSMVFQ----QFAllp 122
Cdd:PRK13644  22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID------TGDFSKLQGIRK-LVGIVFQnpetQFV--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK13644  92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 203 RTRLQDELLEFQRRlKKTILFVSHDLDEaFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYV 264
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
cbiO PRK13642
energy-coupling factor transporter ATPase;
47-261 1.05e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 106.72  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpySCNAKALRDLRtHTVSMVFQ----QFAllp 122
Cdd:PRK13642  27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-------LLTAENVWNLR-RKIGMVFQnpdnQFV--- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK13642  96 GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIMESGRIIQCGTPHDIVKNPAD 261
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
43-268 1.85e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 105.89  E-value: 1.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvRGDVAVStttGPVNPYSCNAKALR----DLRTHtVSMVFQQF 118
Cdd:PRK14258  23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVE---GRVEFFNQNIYERRvnlnRLRRQ-VSMVHPKP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVNLTKWAGRKVN----ELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK14258  98 NLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCIARALAVKPKVLLMDE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMES-----GRIIQCGTPHDIVKNPADQYVADFV 268
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYV 256
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
47-252 1.86e-26

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: 110.87  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYSCNAKALRdlrtHTVSMVFQQFALLPWRTV 126
Cdd:TIGR01257  950 NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-----KDIETNLDAVR----QSLGMCPQHNILFHHLTV 1020
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   127 AENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 516735053   207 QDELLEFqrRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTP 252
Cdd:TIGR01257 1101 WDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
43-260 3.20e-26

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: 104.16  E-value: 3.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA---VSTTTGPVNpyscnAKALRDLrthtvSMVFQQFA 119
Cdd:cd03218   16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgQDITKLPMH-----KRARLGI-----GYLPQEAS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03218   86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 200 PLIRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:cd03218  166 PIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1-257 3.99e-26

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 104.39  E-value: 3.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MT-AVSFNNVSIIF--GDRPETAL--AMVDQGKSRDEIgaatglVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNG 75
Cdd:COG1134    1 MSsMIEVENVSKSYrlYHEPSRSLkeLLLRRRRTRREE------FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  76 -LAP-----VVRGDVA--VSTTTGpVNPyscnakalrDLrthtvsmvfqqfallpwrTVAENVGFGLELAGMPEAERKLR 147
Cdd:COG1134   75 iLEPtsgrvEVNGRVSalLELGAG-FHP---------EL------------------TGRENIYLNGRLLGLSRKEIDEK 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 148 VGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHD 227
Cdd:COG1134  127 FDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHS 205
                        250       260       270
                 ....*....|....*....|....*....|
gi 516735053 228 LDEAFRIGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:COG1134  206 MGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
38-268 7.32e-26

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 104.09  E-value: 7.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRA---VNGLAPVVRGDVAVSTTTGPVNPYSCNAKALRdlrtHTVSMV 114
Cdd:PRK14243  21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEVR----RRIGMV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 115 FQQFALLPwRTVAENVGFGLELAG----MPE-AERKLRvgeQLELVNLTKwagRKVNE----LSGGMQQRVGLARAFATG 185
Cdd:PRK14243  97 FQKPNPFP-KSIYDNIAYGARINGykgdMDElVERSLR---QAALWDEVK---DKLKQsglsLSGGQQQRLCIARAIAVQ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMES---------GRIIQCGTPHDIV 256
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIF 247
                        250
                 ....*....|..
gi 516735053 257 KNPADQYVADFV 268
Cdd:PRK14243 248 NSPQQQATRDYV 259
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
40-250 9.91e-26

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: 102.73  E-value: 9.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvVRGDvavSTTTGPVnpySCNAKAL-RDLRTHTVSMVFQQF 118
Cdd:cd03234   20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGG---GTTSGQI---LFNGQPRkPDQFQKCVAYVRQDD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLELAG---MPEAERKLRVG-EQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:cd03234   91 ILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 195 FSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03234  171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
48-238 1.37e-25

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 102.55  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  48 LTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYSCNAKALRDLRTHTVSMVFQQFALLPWRTVA 127
Cdd:PRK10584  31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ----PLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNAL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 128 ENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQ 207
Cdd:PRK10584 107 ENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
                        170       180       190
                 ....*....|....*....|....*....|.
gi 516735053 208 DELLEFQRRLKKTILFVSHDLDEAFRIGNRI 238
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
31-246 1.48e-25

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: 100.97  E-value: 1.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  31 DEIGAATGLVLG--VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttG-PVNPYSCnakalRDLR 107
Cdd:cd03215    2 EPVLEVRGLSVKgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD---GkPVTRRSP-----RDAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 108 THTVSMV---FQQFALLPWRTVAENVGFGlelagmpeaerklrvgeqlelvnltkwagrkvNELSGGMQQRVGLARAFAT 184
Cdd:cd03215   74 RAGIAYVpedRKREGLVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLAR 121
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 185 GAPILLMDEPFSALDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:cd03215  122 DPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
43-257 1.78e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 104.91  E-value: 1.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYSCNAKalrdlrthtVSMVFQQFALLP 122
Cdd:PRK13536  57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR---------IGVVPQFDNLDL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP-- 200
Cdd:PRK13536 128 EFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPha 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 201 --LIRTRLQDELlefqrRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:PRK13536 208 rhLIWERLRSLL-----ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
43-263 2.60e-25

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 104.02  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV--STTTGpvnpysCNAKALRDLRTHtVSMVFQQ--F 118
Cdd:PRK15079  37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgKDLLG------MKDDEWRAVRSD-IQMIFQDplA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLEL--AGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:PRK15079 110 SLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
43-256 2.77e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 103.73  E-value: 2.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGdvAVSTTTGPVNPYSCNAKAlrdlrthTVSMVFQQFALLP 122
Cdd:PRK13537  23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAG--SISLCGEPVPSRARHARQ-------RVGVVPQFDNLDP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PRK13537  94 DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516735053 203 RTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIV 256
Cdd:PRK13537 174 RHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
45-278 3.70e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 103.24  E-value: 3.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGL-------------------APVVRGDVAVSTTTGPvnPYSCNAKALRD 105
Cdd:PRK13651  25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknkkKTKEKEKVLEKLVIQK--TRFKKIKKIKE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 106 LRTHtVSMVFQqFA--LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAF 182
Cdd:PRK13651 103 IRRR-VGVVFQ-FAeyQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 183 ATGAPILLMDEPFSALDPlirtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNp 259
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLNkqgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD- 255
                        250
                 ....*....|....*....
gi 516735053 260 aDQYVADfvQNLNPINMLT 278
Cdd:PRK13651 256 -NKFLIE--NNMEPPKLLN 271
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
43-260 3.88e-25

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 102.09  E-value: 3.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP----VVRGDVAVSTTtgPVNPyscnakalRDLRTHTVSMVFQ-- 116
Cdd:PRK10418  19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGK--PVAP--------CALRGRKIATIMQnp 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWRTVAENVGFGLELAGMPEAERKLRvgEQLELVNLTKwAGRKVN----ELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:PRK10418  89 RSAFNPLHTMHTHARETCLALGKPADDATLT--AALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIAD 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 193 EPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
43-231 5.17e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 100.00  E-value: 5.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyscnakalrdlrthTVSMVFQQFALlP 122
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-------------------RVAYVPQRSEV-P 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WR---TVAENVGFGL----ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:NF040873  68 DSlplTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 516735053 196 SALDPLIRTRLqDELLEFQRRLKKTILFVSHDLDEA 231
Cdd:NF040873 148 TGLDAESRERI-IALLAEEHARGATVVVVTHDLELV 182
cbiO PRK13649
energy-coupling factor transporter ATPase;
45-255 6.74e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 102.13  E-value: 6.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYSCNaKALRDLRTHtVSMVFqQFA--LLP 122
Cdd:PRK13649  25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTL--ITSTSKN-KDIKQIRKK-VGLVF-QFPesQLF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTK-WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 202 IRTrlqdELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:PRK13649 180 GRK----ELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
47-252 8.64e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 101.35  E-value: 8.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpySCNAKALRDLRTHtVSMVFQQ-----FALl 121
Cdd:PRK13647  25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR-------EVNAENEKWVRSK-VGLVFQDpddqvFSS- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 pwrTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPl 201
Cdd:PRK13647  96 ---TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP- 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516735053 202 irtRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTP 252
Cdd:PRK13647 172 ---RGQETLMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
29-260 9.00e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 102.62  E-value: 9.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  29 SRDEIGAATGL-----------VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV---------ST 88
Cdd:PRK13631  17 SDDIILRVKNLycvfdekqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  89 TTGPVNPYSCNAKALRDLRtHTVSMVFQ--QFALLPwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL-TKWAGRKV 165
Cdd:PRK13631  97 HELITNPYSKKIKNFKELR-RRVSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 166 NELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGR 245
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGK 253
                        250
                 ....*....|....*
gi 516735053 246 IIQCGTPHDIVKNPA 260
Cdd:PRK13631 254 ILKTGTPYEIFTDQH 268
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
3-228 1.20e-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: 104.68  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    3 AVSFNNVSIIFGDRPEtalamvdqgksrdeigaatglvlGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG 82
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRP-----------------------ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   83 DVAVstttGPVNPYSCNAKALRDlrthTVSMVFQQFALLPwRTVAENVGFG------------LELAGMPEAERKLRVGE 150
Cdd:TIGR02857 378 SIAV----NGVPLADADADSWRD----QIAWVPQHPFLFA-GTIAENIRLArpdasdaeireaLERAGLDEFVAALPQGL 448
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053  151 QLELvnltkwaGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDL 228
Cdd:TIGR02857 449 DTPI-------GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRL 517
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
42-245 2.62e-24

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: 99.05  E-value: 2.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYSCNAKALRDLRTHTVSMVFQQFALL 121
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILALRRRTIGYVSQFLRVI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PwRT-----VAEnvgfGLELAGMPEAERKLRVGEQLELVNLTK--WagrkvnEL-----SGGMQQRVGLARAFATGAPIL 189
Cdd:COG4778  106 P-RVsaldvVAE----PLLERGVDREEARARARELLARLNLPErlW------DLppatfSGGEQQRVNIARGFIADPPLL 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 190 LMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGR 245
Cdd:COG4778  175 LLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
4-250 3.10e-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: 98.76  E-value: 3.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIF--GDRPETALAMVDQGKSRDEIGAatglVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVR 81
Cdd:cd03220    1 IELENVSKSYptYKGGSSSLKKLGILGRKGEVGE----FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  82 GDVavsTTTGPVnpyscnakalrdlrthtVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWA 161
Cdd:cd03220   77 GTV---TVRGRV-----------------SSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 162 GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIM 241
Cdd:cd03220  137 DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL 215

                 ....*....
gi 516735053 242 ESGRIIQCG 250
Cdd:cd03220  216 EKGKIRFDG 224
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
43-259 3.68e-24

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 102.23  E-value: 3.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVNpyscnaKALRDLRTHTVSMVFQQFALLP 122
Cdd:PRK09536  19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT---------LTPTAGTVL------VAGDDVEALSARAASRRVASVP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRT-------VAENVGFGL-----ELAGMPEAERKLrVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILL 190
Cdd:PRK09536  84 QDTslsfefdVRQVVEMGRtphrsRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 191 MDEPFSALD--PLIRTrlqdelLEFQRRL---KKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK09536 163 LDEPTASLDinHQVRT------LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1-263 2.36e-23

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 98.66  E-value: 2.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRpETALAMVDQgksrdeigaatglvlgvadASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:PRK11022   1 MALLNVDKLSVHFGDE-SAPFRAVDR-------------------ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 RGDVAVSTTTGPVNPYSCNAKALRDLRTHTVSMVFQQ--FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNL 157
Cdd:PRK11022  61 GRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 158 TKWAGR---KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRI 234
Cdd:PRK11022 141 PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEA 220
                        250       260
                 ....*....|....*....|....*....
gi 516735053 235 GNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK11022 221 AHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
43-259 2.43e-23

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 96.64  E-value: 2.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpySCNAKALRDLRTHtvsmvfqQFAL-- 120
Cdd:COG1137   19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI------------FLDGEDITHLPMH-------KRARlg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 ---LP-----WR--TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILL 190
Cdd:COG1137   80 igyLPqeasiFRklTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 191 MDEPFSALDPLIRTRLQDELlefqRRLKKT---ILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:COG1137  160 LDEPFAGVDPIAVADIQKII----RHLKERgigVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
33-263 5.07e-23

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 97.73  E-value: 5.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  33 IGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG-------DVAVstttgpvnpyscNAKALRD 105
Cdd:PRK11308  21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGelyyqgqDLLK------------ADPEAQK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 106 LRTHTVSMVFQQ-FALL-PWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARA 181
Cdd:PRK11308  89 LLRQKIQIVFQNpYGSLnPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 182 FATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPAD 261
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRH 248

                 ..
gi 516735053 262 QY 263
Cdd:PRK11308 249 PY 250
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
43-255 1.52e-22

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: 98.64  E-value: 1.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnakaLRDLRTHtVSMVFQQFALLP 122
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH--DLADYT-----LASLRRQ-VALVSQDVVLFN 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  123 wRTVAENVGFG-LELAGMPEAERKLRVGEQLELVN-----LTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:TIGR02203 420 -DTIANNIAYGrTEQADRAEIERALAAAYAQDFVDklplgLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053  197 ALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQ--GRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNEL 554
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
45-245 2.90e-22

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: 92.92  E-value: 2.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyscnakalrdlrthtVSMVFQQfallPW- 123
Cdd:cd03250   23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------------------IAYVSQE----PWi 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 --RTVAENVGFGLELagmpEAERKLRV---------GEQLELVNLTKWAGRKVNeLSGGMQQRVGLARAFATGAPILLMD 192
Cdd:cd03250   78 qnGTIRENILFGKPF----DEERYEKVikacalepdLEILPDGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 193 EPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLdEAFRIGNRIAIMESGR 245
Cdd:cd03250  153 DPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
45-255 3.58e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 94.53  E-value: 3.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvNPYSCNAKALRDLRtHTVSMVFQQ-----FA 119
Cdd:PRK13636  24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-----KPIDYSRKGLMKLR-ESVGMVFQDpdnqlFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 llpwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:PRK13636  98 ----ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
45-247 4.76e-22

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 97.10  E-value: 4.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvNPYSCNAKALRDLRTHTVSMVFQQFALLPWR 124
Cdd:PRK10535  26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ----DVATLDADALAQLRREHFGFIFQRYHLLSHL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplirT 204
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD----S 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 516735053 205 RLQDELLEFQRRLKK---TILFVSHDLDEAFRiGNRIAIMESGRII 247
Cdd:PRK10535 178 HSGEEVMAILHQLRDrghTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
40-263 5.22e-22

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 97.23  E-value: 5.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstTTGPVNPYSCNAKALRDLRtHTVSMVFQQ-- 117
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI----IFNGQRIDTLSPGKLQALR-RDIQFIFQDpy 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPWRTVAENVGFGLELAGMPEAER-KLRVGEQLELVNLT-KWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:PRK10261 412 ASLDPRQTVGDSIMEPLRVHGLLPGKAaAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 196 SALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
45-256 6.53e-22

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: 96.41  E-value: 6.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTL---LRAVNGLAPV---VRGDVAVSTTTGPVNPYS--------------------- 97
Cdd:TIGR03269  18 NISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTsgrIIYHVALCEKCGYVERPSkvgepcpvcggtlepeevdfw 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   98 -CNAKALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRV 176
Cdd:TIGR03269  98 nLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  177 GLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIV 256
Cdd:TIGR03269 178 VLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVV 257
cbiO PRK13646
energy-coupling factor transporter ATPase;
43-267 1.21e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 93.31  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvNPYSCNAKALRDLRtHTVSMVFQqF--AL 120
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDIT---ITHKTKDKYIRPVR-KRIGMVFQ-FpeSQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENVGFGLELAGMPEAERK-------LRVGEQLELVNLTKWagrkvnELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK13646  98 LFEDTVEREIIFGPKNFKMNLDEVKnyahrllMDLGFSRDVMSQSPF------QMSGGQMRKIAIVSILAMNPDIIVLDE 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNpaDQYVADF 267
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADW 243
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
43-256 1.31e-21

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 92.07  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA-----VSTTTGPVNpyscnAKALRDLR--THTVSmvf 115
Cdd:COG4604   17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldVATTPSREL-----AKRLAILRqeNHINS--- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 116 qqfallpwR-TVAENVGFGle--laGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:COG4604   89 --------RlTVRELVAFGrfpyskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 193 EPFSALDP--------LIRtRLQDEllefqrrLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIV 256
Cdd:COG4604  161 EPLNNLDMkhsvqmmkLLR-RLADE-------LGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
42-263 1.69e-21

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: 92.20  E-value: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYSCNAKALRDLRTHTvsmvfqqfall 121
Cdd:TIGR02323  18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLMRT----------- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  122 PWRTVAENVGFGLEL---AGMPEAERKLRVGEQ------------LELVNLTkwAGR---KVNELSGGMQQRVGLARAFA 183
Cdd:TIGR02323  87 EWGFVHQNPRDGLRMrvsAGANIGERLMAIGARhygnirataqdwLEEVEID--PTRiddLPRAFSGGMQQRLQIARNLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  184 TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:TIGR02323 165 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPY 244
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
38-263 3.49e-21

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 92.48  E-value: 3.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLApVVRGDVAVSTTTGPVNPYSCNAKALRDLRTHTVSMVFQQ 117
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 --FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKwAGRKVN----ELSGGMQQRVGLARAFATGAPILL 190
Cdd:PRK09473 106 pmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPE-ARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLI 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 191 MDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
40-268 1.77e-20

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 92.28  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRavnglapVVRGDVAVSTTTGPVNPYSCNAKALRDLRTHTVSMVFQQFA 119
Cdd:PRK11288  17 VKALDDISFDCRAGQVHALMGENGAGKSTLLK-------ILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENvgfgLELAGMPEA-----ERKL--RVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:PRK11288  90 LVPEMTVAEN----LYLGQLPHKggivnRRLLnyEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 193 EPFSALDplirTRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRIIQcgTPHDIVKNPADQYVADFV 268
Cdd:PRK11288 166 EPTSSLS----AREIEQLFRVIRELRaegRVILYVSHRMEEIFALCDAITVFKDGRYVA--TFDDMAQVDRDQLVQAMV 238
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
47-206 2.63e-20

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 87.62  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAV--STTTGPVNPYSCNAKALRDlrthtvsmvfqqfALLPWR 124
Cdd:PRK13539  22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEACHYLGHRN-------------AMKPAL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEaerkLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP---- 200
Cdd:PRK13539  89 TVAENLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaava 164
                        170
                 ....*....|
gi 516735053 201 ----LIRTRL 206
Cdd:PRK13539 165 lfaeLIRAHL 174
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
56-259 3.87e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 88.71  E-value: 3.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  56 LVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNpyscnAKALRDLRtHTVSMVFQQ-----FAllpwRTVAENV 130
Cdd:PRK13652  33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE--PIT-----KENIREVR-KFVGLVFQNpddqiFS----PTVEQDI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 131 GFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRtrlqDEL 210
Cdd:PRK13652 101 AFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV----KEL 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 211 LEFQRRLKK----TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK13652 177 IDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
47-200 4.47e-20

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: 86.64  E-value: 4.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPvnpyscnakALRDLRTHTVSMVFQQFALLPWRTV 126
Cdd:TIGR01189  20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYLGHLPGLKPELSA 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053  127 AENVGFGLELAGmpeaERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:TIGR01189  91 LENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
35-272 4.48e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 88.61  E-value: 4.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  35 AATGLVLGVA------DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRG-----DVAVSTTTgpvnpySCNAKAL 103
Cdd:PRK14271  23 AAVNLTLGFAgktvldQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRS------IFNYRDV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 104 RDLRTHtVSMVFQQFALLPwRTVAENVGFGLElAGMPEAERKLRVGEQLELVNLTKWAGRKVN------ELSGGMQQRVG 177
Cdd:PRK14271  97 LEFRRR-VGMLFQRPNPFP-MSIMDNVLAGVR-AHKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdspfRLSGGQQQLLC 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 178 LARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
                        250
                 ....*....|....*
gi 516735053 258 NPADQYVADFVQNLN 272
Cdd:PRK14271 252 SPKHAETARYVAGLS 266
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
42-247 5.02e-20

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 90.85  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScNAKALRdlrtHTVSMV---FQQF 118
Cdd:COG1129  267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK--PVRIRS-PRDAIR----AGIAYVpedRKGE 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGfgleLAGMPEAERKLRVGEQLELVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPI 188
Cdd:COG1129  340 GLVLDLSIRENIT----LASLDRLSRGGLLDRRRERALAEEYIKRlriktpspeqPVGNLSGGNQQKVVLAKWLATDPKV 415
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 189 LLMDEPFSALDplIRTRlqDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:COG1129  416 LILDEPTRGID--VGAK--AEIYRLIRELAaegKAVIVISSELPELLGLSDRILVMREGRIV 473
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
39-247 5.43e-20

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: 87.39  E-value: 5.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  39 LVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGPVnPYSCNAKALRDLrthtvSMVFQQF 118
Cdd:cd03267   33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA---GLV-PWKRRKKFLRRI-----GVVFGQK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWR-TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:cd03267  104 TQLWWDlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:cd03267  184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
45-251 5.72e-20

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: 87.29  E-value: 5.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYScnakaLRDLRTHtVSMVFQQfALLPWR 124
Cdd:cd03251   20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD--VRDYT-----LASLRRQ-IGLVSQD-VFLFND 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNL------TKWAGRKVNeLSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03251   91 TVAENIAYGRPGATREEVEEAARAANAHEFIMElpegydTVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSAL 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 199 DPLIRTRLQDELLEFQRRlkKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGT 251
Cdd:cd03251  170 DTESERLVQAALERLMKN--RTTFVIAHRL-STIENADRIVVLEDGKIVERGT 219
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
45-247 6.00e-20

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 89.55  E-value: 6.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRD------LRTHT--VSMVFQ 116
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVL------------NGRVLFDaekgicLPPEKrrIGYVFQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWRTVAENVGFGLElAGMPEAERKLrvgeqLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK11144  84 DARLFPHYKVRGNLRYGMA-KSMVAQFDKI-----VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 197 ALDpLIRTRlqdELLEFQRRLKKT----ILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:PRK11144 158 SLD-LPRKR---ELLPYLERLAREinipILYVSHSLDEILRLADRVVVLEQGKVK 208
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
38-250 6.84e-20

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 87.67  E-value: 6.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAvstttgpvnpYSCNAKALRDLRTHTVSmvfQQ 117
Cdd:PRK11701  17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH----------YRMRDGQLRDLYALSEA---ER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALL--PWRTVAENVGFGLEL---AGMPEAERKLRVGEQ------------LELVNLtkwAGRKVNEL----SGGMQQRV 176
Cdd:PRK11701  84 RRLLrtEWGFVHQHPRDGLRMqvsAGGNIGERLMAVGARhygdiratagdwLERVEI---DAARIDDLpttfSGGMQQRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 177 GLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
43-263 8.07e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 90.15  E-value: 8.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGL---APVV--RGDVAVSTTTgpvnPYSCNAKALRDLRTHTVSMVFQQ 117
Cdd:PRK15134  25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsPPVVypSGDIRFHGES----LLHASEQTLRGVRGNKIAMIFQE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 --FALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKWAGRKVN---ELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK15134 101 pmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIA 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 192 DEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
45-250 8.48e-20

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: 85.68  E-value: 8.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV--VRGDVAVSTTTGPVNPYSCnakalrdlrthTVSMVFQQFALLP 122
Cdd:cd03213   27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK-----------IIGYVPQDDILHP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLELAGmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSALDPli 202
Cdd:cd03213   96 TLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS-- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516735053 203 RTRLQdeLLEFQRRLK---KTILFVSHDL-DEAFRIGNRIAIMESGRIIQCG 250
Cdd:cd03213  145 SSALQ--VMSLLRRLAdtgRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
4-246 1.20e-19

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: 86.37  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPETalamvdqgksrdeigaatgLVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:cd03248   12 VKFQNVTFAYPTRPDT-------------------LVL--QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVSTTtgPVNPYscNAKALRDlrthTVSMVFQQFALLPwRTVAENVGFGL---ELAGMPEAERKLRVGEQLELVNLTKW 160
Cdd:cd03248   71 VLLDGK--PISQY--EHKYLHS----KVSLVGQEPVLFA-RSLQDNIAYGLqscSFECVKEAAQKAHAHSFISELASGYD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 161 --AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAFRiGNRI 238
Cdd:cd03248  142 teVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQI 218

                 ....*...
gi 516735053 239 AIMESGRI 246
Cdd:cd03248  219 LVLDGGRI 226
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
43-247 1.51e-19

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: 85.91  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPV----NPYScnakaLRDLrtHTVSMVFQQF 118
Cdd:TIGR03740  16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI---------LRPTSGEIifdgHPWT-----RKDL--HKIGSLIESP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  119 ALLPWRTVAENVGFGLELAGMPEAerklRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:TIGR03740  80 PLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 516735053  199 DPL-IRtrlqdELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:TIGR03740 156 DPIgIQ-----ELRELIRSFPEqgiTVILSSHILSEVQQLADHIGIISEGVLG 203
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
47-259 1.73e-19

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 86.77  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAKAlrdlrtHTVSMVFQQFALLPWRTV 126
Cdd:PRK10575  31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ--PLESWSSKAFA------RKVAYLPQQLPAAEGMTV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGFGLE----LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDpli 202
Cdd:PRK10575 103 RELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--- 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 203 rTRLQDELLEFQRRLKK----TILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK10575 180 -IAHQVDVLALVHRLSQerglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
38-259 2.24e-19

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 86.20  E-value: 2.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHTVS---MV 114
Cdd:PRK11300  16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL------------RGQHIEGLPGHQIArmgVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 115 --FQQFALLPWRTVAEN--------VGFGLeLAGM--------PEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRV 176
Cdd:PRK11300  84 rtFQHVRLFREMTVIENllvaqhqqLKTGL-FSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 177 GLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIV 256
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242

                 ...
gi 516735053 257 KNP 259
Cdd:PRK11300 243 NNP 245
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
32-247 2.62e-19

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 88.83  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  32 EIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV--VRGDVAVSTTTgpvnpysCNAKALRDLRTH 109
Cdd:PRK13549  10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEE-------LQASNIRDTERA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 110 TVSMVFQQFALLPWRTVAENVGFGLEL--AG-MPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:PRK13549  83 GIAIIHQELALVKELSVLENIFLGNEItpGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 187 PILLMDEPFSALdplirTRLQDE-LLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:PRK13549 163 RLLILDEPTASL-----TESETAvLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDGRHI 222
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
43-247 3.31e-19

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: 84.95  E-value: 3.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTT-TGPVNPyscnakalRDLRTHtVSMVFQQFALL 121
Cdd:cd03245   20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdIRQLDP--------ADLRRN-IGYVPQDVTLF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 pWRTVAENVGFGLELAgmpEAERKLRVgeqLELVNLTKWAGR-------KVNE----LSGGMQQRVGLARAFATGAPILL 190
Cdd:cd03245   91 -YGTLRDNITLGAPLA---DDERILRA---AELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLNDPPILL 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 191 MDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAFRIGNRIAIMESGRII 247
Cdd:cd03245  164 LDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
47-250 5.82e-19

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: 83.13  E-value: 5.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGlapvvrgdvAVSTTTGPVNPYSCNAKALRDLRTHTVSmVFQQFALLPWRTV 126
Cdd:cd03247   22 SLELKQGEKIALLGRSGSGKSTLLQLLTG---------DLKPQQGEITLDGVPVSDLEKALSSLIS-VLNQRPYLFDTTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGfglelagmpeaerklrvgeqlelvnltkwagrkvNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:cd03247   92 RNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 516735053 207 QDELLEFQRrlKKTILFVSHDLD--EAFrigNRIAIMESGRIIQCG 250
Cdd:cd03247  138 LSLIFEVLK--DKTLIWITHHLTgiEHM---DKILFLENGKIIMQG 178
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
45-254 6.15e-19

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: 6.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYSCNAKALRDLRTHtVSMVFQQFALLPwR 124
Cdd:cd03252   20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-------DGHDLALADPAWLRRQ-VGVVLQENVLFN-R 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELV-NLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03252   91 SIRDNIALADPGMSMERVIEAAKLAGAHDFIsELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 200 PLIRTRLQDELlefQRRLK-KTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTpHD 254
Cdd:cd03252  171 YESEHAIMRNM---HDICAgRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS-HD 221
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-247 1.01e-18

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 87.04  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   6 FNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA 85
Cdd:COG0488    1 LENLSKSFGGRP----------------------LL--DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  86 VStttgpvnpyscnakalRDLRthtVSMVFQQFALLPWRTVAENVGFGLE-----LAGMPEAERKL--------RVGE-Q 151
Cdd:COG0488   57 IP----------------KGLR---IGYLPQEPPLDDDLTVLDTVLDGDAelralEAELEELEAKLaepdedleRLAElQ 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 152 LELVNLTKWA-------------------GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRTR--LQDEL 210
Cdd:COG0488  118 EEFEALGGWEaearaeeilsglgfpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LESIewLEEFL 195
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 516735053 211 LEFqrrlKKTILFVSHD---LDeafRIGNRIAIMESGRII 247
Cdd:COG0488  196 KNY----PGTVLVVSHDryfLD---RVATRILELDRGKLT 228
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
43-226 1.11e-18

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 87.17  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAvstttgpvnpyscnakalrdlRTHTVSMVFqqfalLP 122
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------------------RPAGARVLF-----LP 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WR------TVAENVGFGLELAGMPEAErklrVGEQLELVNLTKWAGRkVNE-------LSGGMQQRVGLARAFATGAPIL 189
Cdd:COG4178  433 QRpylplgTLREALLYPATAEAFSDAE----LREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWL 507
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 516735053 190 LMDEPFSALDPlirtRLQDELLE-FQRRLKK-TILFVSH 226
Cdd:COG4178  508 FLDEATSALDE----ENEAALYQlLREELPGtTVISVGH 542
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
32-273 1.26e-18

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 85.34  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  32 EIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP---VVRGDvavSTTTGPVNPYSCNAKALRDLRT 108
Cdd:COG4170   12 EIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwHVTAD---RFRWNGIDLLKLSPRERRKIIG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 109 HTVSMVFQ--QFALLPwrtvAENVGFGLELAgMPEAE-----------RKLRVGEQLELVNLTKWagRKV-----NELSG 170
Cdd:COG4170   89 REIAMIFQepSSCLDP----SAKIGDQLIEA-IPSWTfkgkwwqrfkwRKKRAIELLHRVGIKDH--KDImnsypHELTE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 171 GMQQRVGLARAFATGAPILLMDEPFSALDPLirTRLQD-ELLEFQRRLKKT-ILFVSHDLDEAFRIGNRIAIMESGRIIQ 248
Cdd:COG4170  162 GECQKVMIAMAIANQPRLLIADEPTNAMEST--TQAQIfRLLARLNQLQGTsILLISHDLESISQWADTITVLYCGQTVE 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 516735053 249 CGTPHDIVKNPADQY-------VADFVQNLNP 273
Cdd:COG4170  240 SGPTEQILKSPHHPYtkallrsMPDFRQPLPH 271
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
29-257 1.41e-18

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 86.76  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  29 SRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYSCNAKAlrdlrt 108
Cdd:PRK09700   7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL------ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 109 hTVSMVFQQFALLPWRTVAENVGFGLELA----GMP---EAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARA 181
Cdd:PRK09700  81 -GIGIIYQELSVIDELTVLENLYIGRHLTkkvcGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 182 FATGAPILLMDEPFSALDplirTRLQDELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESG-----RIIQCGTPH 253
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLT----NKEVDYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSND 235

                 ....
gi 516735053 254 DIVK 257
Cdd:PRK09700 236 DIVR 239
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
43-246 1.69e-18

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: 81.88  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYscnakALRDLRTHtVSMVFQQFALLP 122
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA--DISQW-----DPNELGDH-VGYLPQDDELFS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 wRTVAENVgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFaTGAP-ILLMDEPFSALDPL 201
Cdd:cd03246   90 -GSIAENI-------------------------------------LSGGQRQRLGLARAL-YGNPrILVLDEPNSHLDVE 130
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 516735053 202 IRTRLQDELLEFQRRlKKTILFVSHDLdEAFRIGNRIAIMESGRI 246
Cdd:cd03246  131 GERALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
3-271 1.88e-18

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 86.42  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   3 AVSFNNVSIIFGDRPETALAmvdqgksrdeigaatglvlgvaDASLTIEEGEILVLMGLSGSGKSTLL----RAVNglap 78
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLK----------------------GLSLQIKAGEKVALLGRTGCGKSTLLqlltRAWD---- 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  79 VVRGDVAVSTTtgPVNPYScnAKALRDlrthTVSMVFQQFALLPwRTVAENvgfgLELAGmPEA--ERKLRVGEQLELVN 156
Cdd:PRK11160 392 PQQGEILLNGQ--PIADYS--EAALRQ----AISVVSQRVHLFS-ATLRDN----LLLAA-PNAsdEALIEVLQQVGLEK 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 157 LTK-------WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLD 229
Cdd:PRK11160 458 LLEddkglnaWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT 535
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 516735053 230 --EAFrigNRIAIMESGRIIQCGTPHDIVKNpaDQYVADFVQNL 271
Cdd:PRK11160 536 glEQF---DRICVMDNGQIIEQGTHQELLAQ--QGRYYQLKQRL 574
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
43-258 2.15e-18

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 83.02  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYscNAKALRDlrthtVSMVFQQFALLP 122
Cdd:PRK10895  19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL--HARARRG-----IGYLPQEASIFR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL 201
Cdd:PRK10895  92 RLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 202 IRTRLQdELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:PRK10895 172 SVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
58-255 2.75e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 83.52  E-value: 2.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  58 LMGLSGSGKSTLLRAVNGLAPVVRGdvAVSTTTGPVNpYScnAKALRDLRTHtVSMVFQQFALLPWRT-VAENVGFGLEL 136
Cdd:PRK13638  32 LVGANGCGKSTLFMNLSGLLRPQKG--AVLWQGKPLD-YS--KRGLLALRQQ-VATVFQDPEQQIFYTdIDSDIAFSLRN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 137 AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTrlqdELLEFQRR 216
Cdd:PRK13638 106 LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT----QMIAIIRR 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 516735053 217 L---KKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:PRK13638 182 IvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
40-263 2.81e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 86.06  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVST------TTGPVNPYSCNAKALRDLRTHTVSM 113
Cdd:PRK10261  29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrSRQVIELSEQSAAQMRHVRGADMAM 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 114 VFQQ--FALLPWRTVAENV--------GFGLELAgMPEAERKLrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFA 183
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIaesirlhqGASREEA-MVEAKRML---DQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 184 TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
45-267 3.14e-18

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 83.33  E-value: 3.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavsTTTGPVNPYSCNAKALRDLrthtvsmvfqqfallpwr 124
Cdd:PRK13546  42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAISAGLSGQL------------------ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 205 RLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNpADQYVADF 267
Cdd:PRK13546 181 KCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK-YEAFLNDF 241
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
53-246 3.95e-18

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 81.84  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  53 GEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV-----AVSTTTGPVNPYscnakalrdLRTHtVSMVFQQFALLPWRTVA 127
Cdd:PRK10908  28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLKNREVPF---------LRRQ-IGMIFQDHHLLMDRTVY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 128 ENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQ 207
Cdd:PRK10908  98 DNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 516735053 208 DELLEFQrRLKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:PRK10908 178 RLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
47-258 4.56e-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: 82.20  E-value: 4.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgPVNPYSCNAKALRDLRTHtVSMVFQQFALLPwRTV 126
Cdd:cd03249   23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-------LLDGVDIRDLNLRWLRSQ-IGLVSQEPVLFD-GTI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGFGLELAGMPEAERKLRVGEQLELVnlTKW-------AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03249   94 AENIRYGKPDATDEEVEEAAKKANIHDFI--MSLpdgydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 200 PLIRTRLQDELLEFqrRLKKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:cd03249  172 AESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQ 227
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
45-228 9.38e-18

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 81.85  E-value: 9.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNpyscnakalRDLRTHTVSMVFQQ------F 118
Cdd:PRK15056  25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ--PTR---------QALQKNLVAYVPQSeevdwsF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK15056  94 PVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
                        170       180       190
                 ....*....|....*....|....*....|
gi 516735053 199 DPLIRTRLQDELLEFqRRLKKTILFVSHDL 228
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNL 202
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
38-247 1.01e-17

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: 84.11  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVnpyscNAKALRDLRTHTVSMVFQQ 117
Cdd:TIGR02633  12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPL-----KASNIRDTERAGIVIIHQE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  118 FALLPWRTVAENVGFGLEL----AGMPEAERKLRVGEQLELVNLTKW-AGRKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:TIGR02633  87 LTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053  193 EPFSALdplirTRLQDE-LLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:TIGR02633 167 EPSSSL-----TEKETEiLLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQHV 220
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
37-259 1.39e-17

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 81.37  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  37 TGL-----VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYScnakalrdLRTHTV 111
Cdd:PRK15112  18 TGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS--------YRSQRI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 112 SMVFQ--QFALLPWRTVAENVGFGLEL-AGMPEAERKLRVGEQLELVNL-TKWAGRKVNELSGGMQQRVGLARAFATGAP 187
Cdd:PRK15112  90 RMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPK 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 188 ILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
47-255 2.00e-17

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 80.65  E-value: 2.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPvVRGDVAVSTTtgPVNPYScnAKALRDLRthtvSMVFQQFALLPWRTV 126
Cdd:COG4138   16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGR--PLSDWS--AAELARHR----AYLSQQQSPPFAMPV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGFGLElAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAF--------ATGApILLMDEPFSAL 198
Cdd:COG4138   87 FQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinPEGQ-LLLLDEPMNSL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 199 DplIRTRLQ-DELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:COG4138  165 D--VAQQAAlDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
3-251 2.34e-17

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 83.09  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   3 AVSFNNVSIIFGDRPEtalamvdqgksrdeigaatglvlGVADASLTIEEGEILVLMGLSGSGKSTLL----RAVNGLAP 78
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQ-----------------------GVEDVSFEAKPGQTVAIVGPTGAGKSTLInllqRVFDPQSG 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  79 VVRGD-VAVSTTTgpvnpyscnakaLRDLRtHTVSMVFQQfALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELV-- 155
Cdd:PRK13657 391 RILIDgTDIRTVT------------RASLR-RNIAVVFQD-AGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIer 456
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 156 ---NLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRrlKKTILFVSHDLdEAF 232
Cdd:PRK13657 457 kpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRL-STV 533
                        250
                 ....*....|....*....
gi 516735053 233 RIGNRIAIMESGRIIQCGT 251
Cdd:PRK13657 534 RNADRILVFDNGRVVESGS 552
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
50-264 2.43e-17

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 83.17  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   50 IEEGEILVLMGLSGSGKSTLLravNGLAPVVRGDVAVSTTTgPVNPYSCNAKALRdlrthTVSMVFQQFAL-LPWRTVAE 128
Cdd:TIGR00955  48 AKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSV-LLNGMPIDAKEMR-----AISAYVQQDDLfIPTLTVRE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  129 NVGFGLEL---AGMPEAERKLRVGEQLELVNLTKWA------GRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053  200 PLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVK-------------NPADQYV 264
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPffsdlghpcpenyNPADFYV 276
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
45-253 6.43e-17

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: 78.81  E-value: 6.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnAKALRDLrthtVSMVFQQFALLPwR 124
Cdd:cd03254   21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI--DIRDIS--RKSLRSM----IGVVLQDTFLFS-G 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMPEAERKLR-VGEQLELVNLTK----WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03254   92 TIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNgydtVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516735053 200 PLIRTRLQDELLEFQRrlKKTILFVSHDLDeAFRIGNRIAIMESGRIIQCGTPH 253
Cdd:cd03254  172 TETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHD 222
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
32-263 6.73e-17

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 80.23  E-value: 6.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  32 EIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGlapVVRGDVAVSTTT---GPVNPYSCNAKALRDLRT 108
Cdd:PRK15093  12 EFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRmrfDDIDLLRLSPRERRKLVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 109 HTVSMVFQ--QFALLPwrtvAENVGFGLeLAGMPEAE-----------RKLRVGEQLELVNLT--KWAGRKVN-ELSGGM 172
Cdd:PRK15093  89 HNVSMIFQepQSCLDP----SERVGRQL-MQNIPGWTykgrwwqrfgwRKRRAIELLHRVGIKdhKDAMRSFPyELTEGE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 173 QQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTP 252
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
                        250
                 ....*....|.
gi 516735053 253 HDIVKNPADQY 263
Cdd:PRK15093 244 KELVTTPHHPY 254
hmuV PRK13547
heme ABC transporter ATP-binding protein;
45-257 7.00e-17

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 79.49  E-value: 7.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNG--LAPVVRGDVAVsttTGPVNPYSCNAKALRDLRTHTVSMVFQQFALLP 122
Cdd:PRK13547  19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARV---TGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVgfgLELAGMPEAER----KLRVGE----QLELVNLTKWAGRKVNELSGGMQQRVGLARAFA---------TG 185
Cdd:PRK13547  96 FAFSAREI---VLLGRYPHARRagalTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQP 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
4-245 1.05e-16

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: 75.95  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVnglapvvrgd 83
Cdd:cd03221    1 IELENLSKTYGGKL----------------------LL--KDISLTINPGDRIGLVGRNGAGKSTLLKLI---------- 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 vavsttTGPVNPYScnakalrdlrthtvsmvfqqfallpwrtvaenvgfglelaGMPEAERKLRVG--EQLelvnltkwa 161
Cdd:cd03221   47 ------AGELEPDE----------------------------------------GIVTWGSTVKIGyfEQL--------- 71
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 162 grkvnelSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRrlkkTILFVSHdlDEAF--RIGNRIA 239
Cdd:cd03221   72 -------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSH--DRYFldQVATKII 138

                 ....*.
gi 516735053 240 IMESGR 245
Cdd:cd03221  139 ELEDGK 144
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
43-228 1.07e-16

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: 77.76  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPYSCNAKALRDLRTHTVSMVFQQfallP 122
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----KNESEPSFEATRSRNRYSVAYAAQK----P 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 W---RTVAENVGFG-----------LELAGMPEAERKLRVGEQLELvnltkwAGRKVNeLSGGMQQRVGLARAFATGAPI 188
Cdd:cd03290   89 WllnATVEENITFGspfnkqrykavTDACSLQPDIDLLPFGDQTEI------GERGIN-LSGGQRQRICVARALYQNTNI 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 516735053 189 LLMDEPFSALDPLIRTRL-QDELLEFQRRLKKTILFVSHDL 228
Cdd:cd03290  162 VFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKL 202
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
43-257 2.44e-16

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: 79.79  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDV-----AVSTttgpVNPyscnakalRDLRTHtVSMVFQQ 117
Cdd:COG4618  348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgaDLSQ----WDR--------EELGRH-IGYLPQD 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 FALLPwRTVAENVG-FG----------LELAGMPEAERKL------RVGEqlelvnltkwAGRKvneLSGGMQQRVGLAR 180
Cdd:COG4618  415 VELFD-GTIAENIArFGdadpekvvaaAKLAGVHEMILRLpdgydtRIGE----------GGAR---LSGGQRQRIGLAR 480
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 181 AFAtGAP-ILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTPHDIVK 257
Cdd:COG4618  481 ALY-GDPrLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
45-253 3.69e-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: 76.89  E-value: 3.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvnpyscnakalRDLRTHTVSMVFQQFALLPWR 124
Cdd:cd03253   19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---------------QDIREVTLDSLRRAIGVVPQD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TV------AENVGFGLELAG---MPEAERKLRVGEqlELVNLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLM 191
Cdd:cd03253   84 TVlfndtiGYNIRYGRPDATdeeVIEAAKAAQIHD--KIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 192 DEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEafrIGN--RIAIMESGRIIQCGTPH 253
Cdd:cd03253  162 DEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLST---IVNadKIIVLKDGRIVERGTHE 220
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
45-228 4.17e-16

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: 79.33  E-value: 4.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstTTGPVNPYSCNAKALRdlrtHTVSmVFQQFALLPWR 124
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV----TLDGVPVSSLDQDEVR----RRVS-VCAQDAHLFDT 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  125 TVAENVGFGLELAGMPEAERKL-RVGEQLELVNLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR02868 424 TVRENLRLARPDATDEELWAALeRVGLADWLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLD 503
                         170       180
                  ....*....|....*....|....*....
gi 516735053  200 PLIRTRLQDELLEFQRRlkKTILFVSHDL 228
Cdd:TIGR02868 504 AETADELLEDLLAALSG--RTVVLITHHL 530
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
43-257 4.25e-16

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 79.40  E-value: 4.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVsttTG-PVNPyscnakalRDLRT-HTVSMVFQQFAL 120
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL---FGqPVDA--------GDIATrRRVGYMSQAFSL 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENvgfgLEL-A---GMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:NF033858 351 YGELTVRQN----LELhArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 197 ALDPLIRTRLQDELLEFQRRLKKTIlFVS-HDLDEAFRIgNRIAIMESGRIIQCGTPHDIVK 257
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREDGVTI-FIStHFMNEAERC-DRISLMHAGRVLASDTPAALVA 486
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
40-247 5.10e-16

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 78.92  E-value: 5.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS----TTTGPvnpyscnakalRDLRTHTVSMV- 114
Cdd:COG3845  271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgediTGLSP-----------RERRRLGVAYIp 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 115 --FQQFALLPWRTVAENvgFGLELAGMPEAERK--LRVGEqlelvnLTKWAGRKVNE--------------LSGGMQQRV 176
Cdd:COG3845  340 edRLGRGLVPDMSVAEN--LILGRYRRPPFSRGgfLDRKA------IRAFAEELIEEfdvrtpgpdtparsLSGGNQQKV 411
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 177 GLARAFATGAPILLMDEPFSALDP----LIRTRLQDellefQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:COG3845  412 ILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLE-----LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
45-247 8.80e-16

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 78.18  E-value: 8.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttgpvnpyscnakalrdlrtHTVSMVF--QQFALL- 121
Cdd:COG0488  333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------------------ETVKIGYfdQHQEELd 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGfglelAGMPEA-ERKLR--------VGEQlelvnltkwAGRKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:COG0488  392 PDKTVLDELR-----DGAPGGtEQEVRgylgrflfSGDD---------AFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 193 EPFSALDPLIRTRLQDELLEFqrrlKKTILFVSHD---LDeafRIGNRIAIMESGRII 247
Cdd:COG0488  458 EPTNHLDIETLEALEEALDDF----PGTVLLVSHDryfLD---RVATRILEFEDGGVR 508
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
47-247 1.16e-15

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 75.89  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvnpyscnakalRDL-------RTHTVSMVFQQfa 119
Cdd:COG1101   26 NLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---------------KDVtklpeykRAKYIGRVFQD-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 llPWR------TVAENvgfgLELAGMPEAERKLRVG----------EQLELVNLtkwaG---R---KVNELSGGmqQRVG 177
Cdd:COG1101   89 --PMMgtapsmTIEEN----LALAYRRGKRRGLRRGltkkrrelfrELLATLGL----GlenRldtKVGLLSGG--QRQA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 178 LARAFATGAP--ILLMDEPFSALDPliRTrlQDELLEFQRRL----KKTILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:COG1101  157 LSLLMATLTKpkLLLLDEHTAALDP--KT--AALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
47-199 1.22e-15

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 74.46  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpySCNAKALRDLRTHtvsmvFQQfALL----- 121
Cdd:PRK13538  21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV------------LWQGEPIRRQRDE-----YHQ-DLLylghq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 ----PWRTVAENVGFGLELAGMPEAERklrVGEQLELVNLtkwAGRK---VNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PRK13538  83 pgikTELTALENLRFYQRLHGPGDDEA---LWEALAQVGL---AGFEdvpVRQLSAGQQRRVALARLWLTRAPLWILDEP 156

                 ....*
gi 516735053 195 FSALD 199
Cdd:PRK13538 157 FTAID 161
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
47-259 1.47e-15

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 75.35  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvRGDVAVstttgpvnpyscNAKALRDLRTHTVSM------------- 113
Cdd:PRK03695  16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQF------------AGQPLEAWSAAELARhraylsqqqtppf 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 114 ---VFQQFAL-LPwrtvaenvgfglelAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAP-- 187
Cdd:PRK03695  83 ampVFQYLTLhQP--------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdi 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 188 -----ILLMDEPFSALDPLIRTRLqDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK03695 149 npagqLLLLDEPMNSLDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
45-229 1.82e-15

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 74.61  E-value: 1.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP--VVRGDVAVstttgPVNPYSCNAkALRDlrthtvsmvfqqfALLP 122
Cdd:COG2401   48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV-----PDNQFGREA-SLID-------------AIGR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 WRTVAENVGFgLELAGMPEAerklrvgeQLELvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:COG2401  109 KGDFKDAVEL-LNAVGLSDA--------VLWL--------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
                        170       180
                 ....*....|....*....|....*..
gi 516735053 203 RTRLQDELLEFQRRLKKTILFVSHDLD 229
Cdd:COG2401  172 AKRVARNLQKLARRAGITLVVATHHYD 198
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
31-230 1.90e-15

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 74.37  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  31 DEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYScnAKALRdlrtHT 110
Cdd:PRK10247  11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE--DISTLK--PEIYR----QQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 111 VSMVFQQFALLPwRTVAENVGFGLELAGM-PEAERKLRVGEQLELVN--LTKwagrKVNELSGGMQQRVGLARAFATGAP 187
Cdd:PRK10247  83 VSYCAQTPTLFG-DTVYDNLIFPWQIRNQqPDPAIFLDDLERFALPDtiLTK----NIAELSGGEKQRISLIRNLQFMPK 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 516735053 188 ILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDE 230
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
GguA NF040905
sugar ABC transporter ATP-binding protein;
40-248 3.62e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 76.37  E-value: 3.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP--------VVRGDVavstttgpvnpysCNAKALRDLRTHTV 111
Cdd:NF040905  14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeiLFDGEV-------------CRFKDIRDSEALGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 112 SMVFQQFALLPWRTVAENVGFGLELA--GM---PEAERKLRvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:NF040905  81 VIIHQELALIPYLSIAENIFLGNERAkrGVidwNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 187 PILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILfVSHDLDEAFRIGNRIAIMESGRIIQ 248
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRTIE 219
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
21-199 5.13e-15

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: 72.91  E-value: 5.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  21 LAMVDQGKSRDEIGAATGLvlgvadaSLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavSTTTGPVNpyscna 100
Cdd:cd03231    1 LEADELTCERDGRALFSGL-------SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV--LLNGGPLD------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 101 kALRDLRTHTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAErklrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLAR 180
Cdd:cd03231   66 -FQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALAR 138
                        170
                 ....*....|....*....
gi 516735053 181 AFATGAPILLMDEPFSALD 199
Cdd:cd03231  139 LLLSGRPLWILDEPTTALD 157
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
45-247 7.63e-15

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 75.15  E-value: 7.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNpYSCNAKALRdlrtHTVSMVFQQFALLPWR 124
Cdd:PRK10982  16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK--EID-FKSSKEALE----NGISMVHQELNLVLQR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFG-LELAGMPEAERKL-----RVGEQLEL-VNLTKwagrKVNELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:PRK10982  89 SVMDNMWLGrYPTKGMFVDQDKMyrdtkAIFDELDIdIDPRA----KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516735053 198 LDplirTRLQDELLEFQRRLKKT---ILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:PRK10982 165 LT----EKEVNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
43-263 1.26e-14

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 74.74  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKST----LLRAVNGlapvvRGDVAVSTTtgPVNPYscNAKALRDLRtHTVSMVFQ-- 116
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQ--PLHNL--NRRQLLPVR-HRIQVVFQdp 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWRTVAENVGFGLEL--AGMPEAERKLRVGEQLELVNL---TKWagRKVNELSGGMQQRVGLARAFATGAPILLM 191
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdpeTRH--RYPAEFSGGQRQRIAIARALILKPSLIIL 449
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 192 DEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQY 263
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
50-274 1.60e-14

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: 75.05  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    50 IEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNpyscnakalrdlrthtVSMVFQQFALLPWRTVAEN 129
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN----------------ISDVHQNMGYCPQFDAIDD 2025
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   130 VGFGLE-------LAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:TIGR01257 2026 LLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   203 RTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPADQYVA---------DFVQNLNP 273
Cdd:TIGR01257 2106 RRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVtmkikspkdDLLPDLNP 2184

                   .
gi 516735053   274 I 274
Cdd:TIGR01257 2185 V 2185
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
45-256 2.15e-14

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 72.33  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYSCNAKALRdlrthtVSMVFQQFALLPWR 124
Cdd:PRK10253  25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH--IQHYASKEVARR------IGLLAQNATTPGDI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFG----LELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK10253  97 TVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 201 LIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIV 256
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
45-251 2.71e-14

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 73.90  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYScnakaLRDLRTHtVSMVFQQFALLPwR 124
Cdd:PRK11176 361 NINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD--LRDYT-----LASLRNQ-VALVSQNVHLFN-D 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGL-ELAGMPEAERKLRVGEQLELVN-----LTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:PRK11176 432 TIANNIAYARtEQYSREQIEEAARMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053 199 DPLIRTRLQDELLEFQRrlKKTILFVSHDL------DEafrignrIAIMESGRIIQCGT 251
Cdd:PRK11176 512 DTESERAIQAALDELQK--NRTSLVIAHRLstiekaDE-------ILVVEDGEIVERGT 561
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
43-226 4.60e-14

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: 69.10  E-value: 4.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTG----PVNPYsCNAKALRDLrthtvsmvfqqf 118
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDllflPQRPY-LPLGTLREQ------------ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVaenvgfglelagmpeaerklrvgeqlelvnltkwagrkvneLSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03223   84 LIYPWDDV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
                        170       180
                 ....*....|....*....|....*...
gi 516735053 199 DPlirtRLQDELLEFQRRLKKTILFVSH 226
Cdd:cd03223  123 DE----ESEDRLYQLLKELGITVISVGH 146
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
40-247 5.86e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 72.73  E-value: 5.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  40 VLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVA----VSTTTGPvnpyscnakalRDLRTHTVSMVF 115
Cdd:PRK10762  17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkEVTFNGP-----------KSSQEAGIGIIH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 116 QQFALLPWRTVAENVGFGLELAG---------MPEAERKLrvgeqLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGA 186
Cdd:PRK10762  86 QELNLIPQLTIAENIFLGREFVNrfgridwkkMYAEADKL-----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 187 PILLMDEPFSALdplirTRLQDE-LLEFQRRLKKT---ILFVSHDLDEAFRIGNRIAIMESGRII 247
Cdd:PRK10762 161 KVIIMDEPTDAL-----TDTETEsLFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVFRDGQFI 220
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
8-246 6.84e-14

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 72.25  E-value: 6.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   8 NVSIIFGDRPEtalamvDQGKSRDEIGAATGLVLGvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS 87
Cdd:PRK11288 241 EIGDIYGYRPR------PLGEVRLRLDGLKGPGLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  88 TTtgPVNPYScNAKALRdlrthtVSMVF-----QQFALLPWRTVAENVG---------FGLELAGMPEAE------RKLR 147
Cdd:PRK11288 314 GK--PIDIRS-PRDAIR------AGIMLcpedrKAEGIIPVHSVADNINisarrhhlrAGCLINNRWEAEnadrfiRSLN 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 148 VGeqlelvnlTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHD 227
Cdd:PRK11288 385 IK--------TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSD 455
                        250
                 ....*....|....*....
gi 516735053 228 LDEAFRIGNRIAIMESGRI 246
Cdd:PRK11288 456 LPEVLGVADRIVVMREGRI 474
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
47-259 7.78e-14

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 72.18  E-value: 7.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvRGDVAVstttgpvnpyscNAKALRDL-----RTHtVSMVFQQfALL 121
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKI------------NGIELRELdpeswRKH-LSWVGQN-PQL 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGFG------------LELAGMPEAERKL------RVGEQlelvnltkwAGRkvneLSGGMQQRVGLARAFA 183
Cdd:PRK11174 435 PHGTLRDNVLLGnpdasdeqlqqaLENAWVSEFLPLLpqgldtPIGDQ---------AAG----LSVGQAQRLALARALL 501
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 184 TGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
47-248 9.84e-14

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 71.93  E-value: 9.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVnpyscNAKALRDLRTHtVSMVFQQFALlpWRTV 126
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK--PV-----TAEQPEDYRKL-FSAVFTDFHL--FDQL 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGFGLELAGMPEAERKLRVGEQLELVNltkwaGRKVN-ELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTR 205
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLELED-----GRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 516735053 206 LQDELLEFQRRLKKTILFVSHDlDEAFRIGNRIAIMESGRIIQ 248
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
45-252 1.28e-13

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: 69.06  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpvnpYSCNAKALRDLRTHtVSMVFQQFALLPwR 124
Cdd:cd03244   22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG-------VDISKIGLHDLRSR-ISIIPQDPVLFS-G 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVG-FG----------LELAGMPEAERKLRVGEQLELvnltkwAGRKVNeLSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:cd03244   93 TIRSNLDpFGeysdeelwqaLERVGLKEFVESLPGGLDTVV------EEGGEN-LSVGQRQLLCLARALLRKSKILVLDE 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516735053 194 PFSALDP--------LIRTRLQDellefqrrlkKTILFVSH------DLDeafrignRIAIMESGRIIQCGTP 252
Cdd:cd03244  166 ATASVDPetdaliqkTIREAFKD----------CTVLTIAHrldtiiDSD-------RILVLDKGRVVEFDSP 221
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
43-248 1.89e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 70.97  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYSCNAKALRdlrthTVSMVFQQFALL 121
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgKDISPRSPLDAVKKGMA-----YITESRRDNGFF 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGFG--LELAGM--------PEAERKLrVGEQLELVNLtKWAG--RKVNELSGGMQQRVGLARAFATGAPIL 189
Cdd:PRK09700 354 PNFSIAQNMAISrsLKDGGYkgamglfhEVDEQRT-AENQRELLAL-KCHSvnQNITELSGGNQQKVLISKWLCCCPEVI 431
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 190 LMDEPFSALDPLIRTrlqdELLEFQRRLK---KTILFVSHDLDEAFRIGNRIAIMESGRIIQ 248
Cdd:PRK09700 432 IFDEPTRGIDVGAKA----EIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-247 4.55e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.98  E-value: 4.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPetalaMVDqgksrdeigaatglvlgvaDASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP-- 78
Cdd:PRK11147   1 MSLISIHGAWLSFSDAP-----LLD-------------------NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLld 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  79 ----VVRGDVAVS--------TTTGPVnpYSCNAKALRDL-----RTHTVSmvfQQFALLPWRTVaenvgfgleLAGMPE 141
Cdd:PRK11147  57 dgriIYEQDLIVArlqqdpprNVEGTV--YDFVAEGIEEQaeylkRYHDIS---HLVETDPSEKN---------LNELAK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 142 AERKL----------RVGEQLELVNLTkwAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELL 211
Cdd:PRK11147 123 LQEQLdhhnlwqlenRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK 200
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 516735053 212 EFQrrlkKTILFVSHdlDEAF--RIGNRIAIMESGRII 247
Cdd:PRK11147 201 TFQ----GSIIFISH--DRSFirNMATRIVDLDRGKLV 232
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
47-255 1.24e-12

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 68.54  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCN-AKALrdlrthTVSMVFQQFALLPWRT 125
Cdd:PRK15439  31 DFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAkAHQL------GIYLVPQEPLLFPNLS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 126 VAENVGFGleLAGMPEAERKLrvgEQL--EL---VNLTKWAGrkvnELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK15439 103 VKENILFG--LPKRQASMQKM---KQLlaALgcqLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 201 LIRTRLQDELLEFQrRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDI 255
Cdd:PRK15439 174 AETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
29-260 1.58e-12

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 66.44  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  29 SRDEIGAATGLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavsTTTGPVNPYSCNAKALRDlrt 108
Cdd:PRK11614   7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI---VFDGKDITDWQTAKIMRE--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 109 hTVSMVFQQFALLPWRTVAENVGFGLELAGMPEAERKLRVGEQLeLVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPI 188
Cdd:PRK11614  81 -AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 189 LLMDEPFSALDPLIRTRLQDELLEFqRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKNPA 260
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
50-200 1.93e-12

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 65.64  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  50 IEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyscnakALRDLRTHTVSMVFQQFALLPWRTVAEN 129
Cdd:PRK13543  34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-----------ATRGDRSRFMAYLGHLPGLKADLSTLEN 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 130 VGFgleLAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13543 103 LHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
PLN03232 PLN03232
ABC transporter C family member; Provisional
43-293 1.98e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 68.46  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP-------VVRGDVAVStttgPVNPYSCNAkalrdlrthtvsmvf 115
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaetssvVIRGSVAYV----PQVSWIFNA--------------- 693
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  116 qqfallpwrTVAENVGFGLELagmpEAERKLR------VGEQLELV---NLTKWAGRKVNeLSGGMQQRVGLARAFATGA 186
Cdd:PLN03232  694 ---------TVRENILFGSDF----ESERYWRaidvtaLQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNS 759
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  187 PILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTPHDIVKN-------- 258
Cdd:PLN03232  760 DIYIFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSgslfkklm 837
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 516735053  259 ------PADQYVADFVQNLNPINMLTAADVMQSGLGQTAAG 293
Cdd:PLN03232  838 enagkmDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQG 878
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
45-259 2.04e-12

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 68.21  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCnakalRDLRTHTVSMvfQQFALLPWR 124
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV--PLVQYDH-----HYLHRQVALV--GQEPVLFSG 569
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  125 TVAENVGFGLELAGMPEAERKLRVGEQLELV-NLTKW----AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAHDFImEFPNGydteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  200 PLIRTRLQdELLEFQRRlkkTILFVSHDLDEAfRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:TIGR00958 650 AECEQLLQ-ESRSRASR---TVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-228 2.12e-12

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 66.29  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   1 MTAVSFNNVSIIFGDRPetalamvdqgksrdeigaatglVLgvADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvv 80
Cdd:PRK09544   2 TSLVSLENVSVSFGQRR----------------------VL--SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL---- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  81 rgdvavstttgpVNPYSCNAKALRDLRthtVSMVFQQFALLPwrTVAENVGFGLELAGmpeAERKLRVGEQLELVNLTKW 160
Cdd:PRK09544  54 ------------VAPDEGVIKRNGKLR---IGYVPQKLYLDT--TLPLTVNRFLRLRP---GTKKEDILPALKRVQAGHL 113
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 161 AGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDL 228
Cdd:PRK09544 114 IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
130-250 2.29e-12

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 67.07  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 130 VGFGLELAgmpEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDE 209
Cdd:NF000106 110 IGR*LDLS---RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 516735053 210 LLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCG 250
Cdd:NF000106 187 VRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
47-300 2.54e-12

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: 68.05  E-value: 2.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgpvnpyscnakalrdlrthtVSMVFQQfALLPWRTV 126
Cdd:TIGR00957  658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------------------VAYVPQQ-AWIQNDSL 715
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   127 AENVGFGLEL------------AGMPEAErKLRVGEQLELvnltkwaGRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:TIGR00957  716 RENILFGKALnekyyqqvleacALLPDLE-ILPSGDRTEI-------GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   195 FSALDPLIRTRLQDELLEFQRRLK-KTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDIVKNpaDQYVADFVQNLNP 273
Cdd:TIGR00957  788 LSAVDAHVGKHIFEHVIGPEGVLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR--DGAFAEFLRTYAP 864
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 516735053   274 INMLTAAD----VMQSGLGQTAA----GMSVSATA 300
Cdd:TIGR00957  865 DEQQGHLEdswtALVSGEGKEAKlienGMLVTDVV 899
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
43-284 4.39e-12

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 65.88  E-value: 4.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPV-----NPYScNAKALRdlrtHTVSMVFQ 116
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP----------TSGEVrvlgyVPFK-RRKEFA----RRIGVVFG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 QFALLPWR-TVAENvgFGL--ELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:COG4586  103 QRSQLWWDlPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 194 PFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVKN--PADQYVADFVQNL 271
Cdd:COG4586  181 PTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERfgPYKTIVLELAEPV 260
                        250
                 ....*....|...
gi 516735053 272 NPINMLTAADVMQ 284
Cdd:COG4586  261 PPLELPRGGEVIE 273
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
24-246 1.66e-11

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 65.02  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  24 VDQGKSRDEIGAATGLvlGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVS-TTTGPVNPYSCNAKA 102
Cdd:PRK10762 251 KAPGEVRLKVDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDgHEVVTRSPQDGLANG 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 103 L--------RDlrthtvsmvfqqfALLPWRTVAENVG------FGLELAGMPEAERKLRVGEQLELVNL-TKWAGRKVNE 167
Cdd:PRK10762 329 IvyisedrkRD-------------GLVLGMSVKENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGL 395
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 168 LSGGMQQRVGLARAFATGAPILLMDEPfsaldplirTRLQD-----ELLEFQRRLKK---TILFVSHDLDEAFRIGNRIA 239
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEP---------TRGVDvgakkEIYQLINQFKAeglSIILVSSEMPEVLGMSDRIL 466

                 ....*..
gi 516735053 240 IMESGRI 246
Cdd:PRK10762 467 VMHEGRI 473
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
47-294 1.09e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 62.60  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyscnakalrdlrthtvSMVFQQFALLPWRTV 126
Cdd:PRK13545  44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---------------------ALIAISSGLNGQLTG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRL 206
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 207 QDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHDIVknpaDQYvADFVQNLNPINMLTAADVMQSG 286
Cdd:PRK13545 183 LDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV----DHY-DEFLKKYNQMSVEERKDFREEQ 256

                 ....*...
gi 516735053 287 LGQTAAGM 294
Cdd:PRK13545 257 ISQFQHGL 264
PLN03130 PLN03130
ABC transporter C family member; Provisional
48-258 1.11e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 63.22  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   48 LTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPVVRGDVAVSTTTGPVNpyscnakalrdlrthTVSMVFQQfallpwrTV 126
Cdd:PLN03130  638 LDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVP---------------QVSWIFNA-------TV 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  127 AENVGFGLELAGmPEAERKLRVGE---QLELV---NLTKWAGRKVNeLSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PLN03130  696 RDNILFGSPFDP-ERYERAIDVTAlqhDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053  201 LIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:PLN03130  774 HVGRQVFDKCIKDELR-GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
45-247 1.33e-10

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: 59.97  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPV---VRGDVAVSTTTGPVNPYSCnakalrdlrTHTVSMVFQQ---F 118
Cdd:cd03233   25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFAEKY---------PGEIIYVSEEdvhF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLpwrTVAENVGFGLELAGmpeaerklrvgeqlelvnltkwaGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSAL 198
Cdd:cd03233   96 PTL---TVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 516735053 199 DPLIRTRLQDELLEFQRRLKKTILF-VSHDLDEAFRIGNRIAIMESGRII 247
Cdd:cd03233  150 DSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
47-247 1.66e-10

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: 62.12  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVnpyscNAKALRDLRTHtVSMVFQQFALLPwrtv 126
Cdd:COG4615  352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ--PV-----TADNREAYRQL-FSAVFSDFHLFD---- 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 aenvgfglELAGMPEAERKLRVGEQLELVNLtkwaGRKV---------NELSGGMQQRVGLARAFATGAPILLMDEPFSA 197
Cdd:COG4615  420 --------RLLGLDGEADPARARELLERLEL----DHKVsvedgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAAD 487
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 516735053 198 LDPLIRTRLQDELLEFQRRLKKTILFVSHDlDEAFRIGNRIAIMESGRII 247
Cdd:COG4615  488 QDPEFRRVFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
45-254 2.76e-10

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 61.37  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVStttGpvnpyscnakalRDLRTHTVSMVFQQFALLPWR 124
Cdd:COG5265  376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID---G------------QDIRDVTQASLRAAIGIVPQD 440
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TV------AENVGFGLELAGMPEAERKLR------------------VGEQlelvnltkwaGRKvneLSGGMQQRVGLAR 180
Cdd:COG5265  441 TVlfndtiAYNIAYGRPDASEEEVEAAARaaqihdfieslpdgydtrVGER----------GLK---LSGGEKQRVAIAR 507
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 181 AFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRlkKTILFVSH------DLDEafrignrIAIMESGRIIQCGTpHD 254
Cdd:COG5265  508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARG--RTTLVIAHrlstivDADE-------ILVLEAGRIVERGT-HA 577
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
45-259 2.84e-10

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 61.27  E-value: 2.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHTVS---MVFQQFALL 121
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF------------HDIPLTKLQLDSWRsrlAVVSQTPFL 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 122 PWRTVAENVGFGLELAGMPEAERKLRVGEQLE-LVNLTKWAGRKVNE----LSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALS 480
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 197 ALDplirTRLQDELLEFQRRL--KKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PRK10789 481 AVD----GRTEHQILHNLRQWgeGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
45-252 5.46e-10

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: 58.31  E-value: 5.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLA--PVVRGDVAVstttgpvnpyscNAKALRDLRTHtvsmvfqqfallp 122
Cdd:cd03217   18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILF------------KGEDITDLPPE------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 123 wrtvaENVGFGLELA-GMPEAERKLRVGEQLelvnltkwagRKVNE-LSGGMQQRVGLARAFATGAPILLMDEPFSALDp 200
Cdd:cd03217   73 -----ERARLGIFLAfQYPPEIPGVKNADFL----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD- 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 201 LIRTRLQDELLEFQRRLKKTILFVSHD---LDeaFRIGNRIAIMESGRIIQCGTP 252
Cdd:cd03217  137 IDALRLVAEVINKLREEGKSVLIITHYqrlLD--YIKPDRVHVLYDGRIVKSGDK 189
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
49-242 9.89e-10

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: 58.19  E-value: 9.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  49 TIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPYSCNAK---ALRDLrthtVSMVFQQFALLP-WR 124
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADyegTVRDL----LSSITKDFYTHPyFK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TvaenvgfglelagmpEAERKLRVGEQLElvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRT 204
Cdd:cd03237   97 T---------------EIAKPLQIEQILD---------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 516735053 205 RLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIME 242
Cdd:cd03237  153 MASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
38-255 2.00e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 58.98  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLL------RAV-NGLAPVVRGDVAvstttgpvnpyscNAKALRDLRTHT 110
Cdd:NF033858  12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIqQGRVEVLGGDMA-------------DARHRRAVCPRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 111 VSMVfQQFA--LLPWRTVAENVGFGLELAGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPI 188
Cdd:NF033858  79 AYMP-QGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 189 LLMDEPFSALDPLIRTR---LQDELLefQRRLKKTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDI 255
Cdd:NF033858 158 LILDEPTTGVDPLSRRQfweLIDRIR--AERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
42-246 2.21e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 58.52  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  42 GVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNPYSCNAKALRDL----RTHTVSMVFQQ 117
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKE--INALSTAQRLARGLvylpEDRQSSGLYLD 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 fALLPWRTVA---ENVGFGLElagmPEAERklRVGEQLELVNLTKWAG--RKVNELSGGMQQRVGLARAFATGAPILLMD 192
Cdd:PRK15439 356 -APLAWNVCAlthNRRGFWIK----PAREN--AVLERYRRALNIKFNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 193 EPFSALDPLIRTRLQDELlefqRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLI----RSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
47-226 7.06e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 54.96  E-value: 7.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVNPYSCNAKalRDLRTHTVSMVF--QQFALLPWR 124
Cdd:PRK13540  21 SFHLPAGGLLHLKGSNGAGKTTLLKLIAGL---------LNPEKGEILFERQSIK--KDLCTYQKQLCFvgHRSGINPYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAGMpeaerKLRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPL--- 201
Cdd:PRK13540  90 TLRENCLYDIHFSPG-----AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELsll 164
                        170       180
                 ....*....|....*....|....*.
gi 516735053 202 -IRTRLQDellefQRRLKKTILFVSH 226
Cdd:PRK13540 165 tIITKIQE-----HRAKGGAVLLTSH 185
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
51-228 1.41e-08

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 55.07  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  51 EEGEILVLMGLSGSGKSTLLRAVNG-LAPVVRGDVAVSTTTGPVNPYSCNA--KALRDLRTHTVSMVF--QQFALLPwRT 125
Cdd:cd03236   24 REGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDDPPDWDEILDEFRGSElqNYFTKLLEGDVKVIVkpQYVDLIP-KA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 126 VAENVGFGLELAGmpEAERKLRVGEQLELVNLTKwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRTR 205
Cdd:cd03236  103 VKGKVGELLKKKD--ERGKLDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQR 175
                        170       180
                 ....*....|....*....|....*.
gi 516735053 206 LQDELLefQRRL---KKTILFVSHDL 228
Cdd:cd03236  176 LNAARL--IRELaedDNYVLVVEHDL 199
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
43-246 1.52e-08

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: 55.99  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPvVRGDVAVSTTTGPVNPYSCnAKALRdlrtHTVSMV---FQQFA 119
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP-GKFEGNVFINGKPVDIRNP-AQAIR----AGIAMVpedRKRHG 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  120 LLPWRTVAENVgfglELAGMPEAERKLRVGEQLELVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPIL 189
Cdd:TIGR02633 350 IVPILGVGKNI----TLSVLKSFCFKMRIDAAAELQIIGSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLLTNPRVL 425
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053  190 LMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PLN03211 PLN03211
ABC transporter G-25; Provisional
53-254 1.70e-08

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 56.04  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  53 GEILVLMGLSGSGKSTLLRAvnglapvVRGDVAVSTTTGPVnpYSCNAKALRDLRTHTvSMVFQQFALLPWRTVAENVGF 132
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNA-------LAGRIQGNNFTGTI--LANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVF 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 133 gLELAGMPEA---ERKLRVGEQL--ELvNLTKWAGRKVNE-----LSGGMQQRVGLARAFATGAPILLMDEPFSALDPLI 202
Cdd:PLN03211 164 -CSLLRLPKSltkQEKILVAESVisEL-GLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516735053 203 RTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIMESGRIIQCGTPHD 254
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
103-254 3.97e-08

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 55.04  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  103 LRDLRtHTVSMVFQQFALLPwRTVAENVGFGLELAGMPEAERKLRVGEQLELVNL--TKW---AGRKVNELSGGMQQRVG 177
Cdd:PTZ00265 1291 LKDLR-NLFSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAIDEFIESlpNKYdtnVGPYGKSLSGGQKQRIA 1368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  178 LARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRiGNRIAIM----ESGRIIQCGTPH 253
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAHGTH 1447

                  .
gi 516735053  254 D 254
Cdd:PTZ00265 1448 E 1448
PTZ00243 PTZ00243
ABC transporter; Provisional
45-259 4.76e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 54.78  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpyscnakalrdLRTHTVSMVFQQfallPW- 123
Cdd:PTZ00243  678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------------------WAERSIAYVPQQ----AWi 732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  124 --RTVAENVGFGLElagmpeaERKLRVGE-----QLE--LVNL-----TKWAGRKVNeLSGGMQQRVGLARAFATGAPIL 189
Cdd:PTZ00243  733 mnATVRGNILFFDE-------EDAARLADavrvsQLEadLAQLgggleTEIGEKGVN-LSGGQKARVSLARAVYANRDVY 804
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053  190 LMDEPFSALDPLIRTRLQDELleFQRRLK-KTILFVSHDLDEAFRiGNRIAIMESGRIIQCGTPHDIVKNP 259
Cdd:PTZ00243  805 LLDDPLSALDAHVGERVVEEC--FLGALAgKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
45-251 6.04e-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: 53.32  E-value: 6.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRavnglapvvrgdvavsTTTGPVNPYSCNAKalrdlrtHTVSMVF-QQFALLPW 123
Cdd:cd03291   55 NINLKIEKGEMLAITGSTGSGKTSLLM----------------LILGELEPSEGKIK-------HSGRISFsSQFSWIMP 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 RTVAENVGFGLELagmpEAERKLRVGE--QLElVNLTKWA-------GRKVNELSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:cd03291  112 GTIKENIIFGVSY----DEYRYKSVVKacQLE-EDITKFPekdntvlGEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516735053 195 FSALDPLIRTRLQDELLeFQRRLKKTILFVSHDLdEAFRIGNRIAIMESGRIIQCGT 251
Cdd:cd03291  187 FGYLDVFTEKEIFESCV-CKLMANKTRILVTSKM-EHLKKADKILILHEGSSYFYGT 241
PTZ00243 PTZ00243
ABC transporter; Provisional
38-259 6.48e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 54.40  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAvstttgpVNPYSCNAKALRDLRthtvsmvfQQ 117
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR-------VNGREIGAYGLRELR--------RQ 1385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  118 FALLPWR------TVAENVGFGLELAgmpEAErklrVGEQLELVNLTkwaGRKVNE--------LSGGMQQRVG------ 177
Cdd:PTZ00243 1386 FSMIPQDpvlfdgTVRQNVDPFLEAS---SAE----VWAALELVGLR---ERVASEsegidsrvLEGGSNYSVGqrqlmc 1455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  178 LARA-FATGAPILLMDEPFSALDPLIRTRLQDELLE-FQrrlKKTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDI 255
Cdd:PTZ00243 1456 MARAlLKKGSGFILMDEATANIDPALDRQIQATVMSaFS---AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531

                  ....
gi 516735053  256 VKNP 259
Cdd:PTZ00243 1532 VMNR 1535
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
45-238 7.40e-08

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: 53.79  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyscnakalrdlrthTVSMVFQQF-ALLPW 123
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-------------------KLAYVDQSRdALDPN 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  124 RTVAENVGFGLELagmpeaerkLRVGEQLelVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR03719 401 KTVWEEISGGLDI---------IKLGKRE--IPSRAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 516735053  194 PFSALDplIRT--RLQDELLEFqrrlKKTILFVSHD---LDeafRIGNRI 238
Cdd:TIGR03719 470 PTNDLD--VETlrALEEALLNF----AGCAVVISHDrwfLD---RIATHI 510
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
150-228 2.01e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.50  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 150 EQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRTRLQ-----DELLEfqrrlKKTILFV 224
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLNvarliRELAE-----GKYVLVV 267

                 ....
gi 516735053 225 SHDL 228
Cdd:PRK13409 268 EHDL 271
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
143-228 2.02e-07

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.48  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 143 ERKlRVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRTRLQ-----DELLEfqrrL 217
Cdd:COG1245  189 ERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD--IYQRLNvarliRELAE----E 261
                         90
                 ....*....|.
gi 516735053 218 KKTILFVSHDL 228
Cdd:COG1245  262 GKYVLVVEHDL 272
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
43-246 3.73e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 51.47  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAP-VVRGDVAVSTTtgPVNPYSCnAKALRdlrtHTVSMV---FQQF 118
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGK--PVKIRNP-QQAIA----QGIAMVpedRKRD 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 119 ALLPWRTVAENVgfglELAGMPEAERKLRVGEQLELVNLTKWAGR----------KVNELSGGMQQRVGLARAFATGAPI 188
Cdd:PRK13549 351 GIVPVMGVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLLLNPKI 426
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 189 LLMDEPfsaldplirTRLQD-----ELLEFQRRLKK---TILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:PRK13549 427 LILDEP---------TRGIDvgakyEIYKLINQLVQqgvAIIVISSELPEVLGLSDRVLVMHEGKL 483
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
45-244 1.07e-06

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: 50.68  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPVNpyscnakalrdlrtHTVSMVFQ-QFALLP 122
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEP----------SEGKIK--------------HSGRISFSpQTSWIM 499
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   123 WRTVAENVGFGLELagmpEAERKLRVGE--QLElVNLTKWA-------GRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR01271  500 PGTIKDNIIFGLSY----DEYRYTSVIKacQLE-EDIALFPekdktvlGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053   194 PFSALDPLIRTRLqdelleFQRRL-----KKTILFVSHDLdEAFRIGNRIAIMESG 244
Cdd:TIGR01271  575 PFTHLDVVTEKEI------FESCLcklmsNKTRILVTSKL-EHLKKADKILLLHEG 623
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
45-251 1.22e-06

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 50.10  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTtgPVNPYSCNAkalrdLRTHtVSMVfQQFALLPWR 124
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR--PLSSLSHSV-----LRQG-VAMV-QQDPVVLAD 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFGLELAgmpEAerklRVGEQLELVNLTKWA-----------GRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:PRK10790 430 TFLANVTLGRDIS---EE----QVWQALETVQLAELArslpdglytplGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 194 PFSALDPLIRTRLQDELLEFqrRLKKTILFVSHDLD---EAfrigNRIAIMESGRIIQCGT 251
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGT 557
ycf16 CHL00131
sulfate ABC transporter protein; Validated
48-251 1.41e-06

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 48.87  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  48 LTIEEGEILVLMGLSGSGKSTllravngLAPVVRGDVAVSTTTGPVNPYSCNAKALR-DLRTHT-VSMVFQQFALLPWRT 125
Cdd:CHL00131  28 LSINKGEIHAIMGPNGSGKST-------LSKVIAGHPAYKILEGDILFKGESILDLEpEERAHLgIFLAFQYPIEIPGVS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 126 vaeNVGFgLELA--------GMPEAErKLR----VGEQLELVNLT-KWAGRKVNE-LSGGMQQRVGLARaFATGAPIL-L 190
Cdd:CHL00131 101 ---NADF-LRLAynskrkfqGLPELD-PLEfleiINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNEILQ-MALLDSELaI 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516735053 191 MDEPFSALDpLIRTRLQDELLEFQRRLKKTILFVSHD---LDeaFRIGNRIAIMESGRIIQCGT 251
Cdd:CHL00131 175 LDETDSGLD-IDALKIIAEGINKLMTSENSIILITHYqrlLD--YIKPDYVHVMQNGKIIKTGD 235
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
58-231 1.60e-06

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 49.55  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   58 LMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvnpyscnakalrdlrthTVSMVFQQFALLPWRTVAENVGFGL-EL 136
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI-------------------KVGYLPQEPQLDPTKTVRENVEEGVaEI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  137 AGM-------------PEAERKLRVGEQLELVNLTKWAG---------------------RKVNELSGGMQQRVGLARAF 182
Cdd:TIGR03719  97 KDAldrfneisakyaePDADFDKLAAEQAELQEIIDAADawdldsqleiamdalrcppwdADVTKLSGGERRRVALCRLL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 516735053  183 ATGAPILLMDEPFSALDPLIRTRLQDELLEFqrrlKKTILFVSHD---LDEA 231
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAESVAWLERHLQEY----PGTVVAVTHDryfLDNV 224
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
45-229 2.22e-06

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: 47.32  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAvnGLAPVVRGDVAVSTTTGPVNPyscnakalrdlrthtVSMVFQQFALLpwr 124
Cdd:cd03238   13 NLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYASGKARLISFLPKFSRNK---------------LIFIDQLQFLI--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 tvaeNVGFG-LELagmpeaerklrvgeqlelvnltkwaGRKVNELSGGMQQRVGLARAFATGAP--ILLMDEPFSALDPL 201
Cdd:cd03238   73 ----DVGLGyLTL-------------------------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
                        170       180
                 ....*....|....*....|....*...
gi 516735053 202 IRTRLQDELLEFqRRLKKTILFVSHDLD 229
Cdd:cd03238  124 DINQLLEVIKGL-IDLGNTVILIEHNLD 150
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
47-229 2.33e-06

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: 46.97  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVnGLAPVVRGDVAVSTTTGPVNPYSCnakalrdlrthTVSMVFQQFallpwrtv 126
Cdd:cd03227   15 DVTFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQSATRRRSGVKAGCIVA-----------AVSAELIFT-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 aenvgfglelagmpeaerklrvgeqlelvnltkwagrkVNELSGGMQQRVGLARAFA----TGAPILLMDEPFSALDPLI 202
Cdd:cd03227   75 --------------------------------------RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRD 116
                        170       180
                 ....*....|....*....|....*..
gi 516735053 203 RTRLQDELLEfQRRLKKTILFVSHDLD 229
Cdd:cd03227  117 GQALAEAILE-HLVKGAQVIVITHLPE 142
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
45-229 2.38e-06

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 48.02  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTL----------LRAVNGLAPVVRG--------DV----------AVSTTTGPVNPY 96
Cdd:cd03270   13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQflgqmdkpDVdsieglspaiAIDQKTTSRNPR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  97 SCNAkalrdlrthTVSMVFQQFALLPWRtvaenVGFGLELAGMpeaerkLRVGeqLELVNLTkwagRKVNELSGGMQQRV 176
Cdd:cd03270   93 STVG---------TVTEIYDYLRLLFAR-----VGIRERLGFL------VDVG--LGYLTLS----RSAPTLSGGEAQRI 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 177 GLARAFATG--APILLMDEPFSALDPlirtRLQDELLEFQRRLKK---TILFVSHDLD 229
Cdd:cd03270  147 RLATQIGSGltGVLYVLDEPSIGLHP----RDNDRLIETLKRLRDlgnTVLVVEHDED 200
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
43-246 2.61e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 48.96  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpVNpyscNAKALRDLRtHTVSMVFQQ----- 117
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKK--IN----NHNANEAIN-HGFALVTEErrstg 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 118 -FALLPwrtvaenVGFGLELAGMPEAERKLRVGEQLELVNLTKWA-----------GRKVNELSGGMQQRVGLARAFATG 185
Cdd:PRK10982 337 iYAYLD-------IGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVidsmrvktpghRTQIGSLSGGNQQKVIIGRWLLTQ 409
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516735053 186 APILLMDEPFSALDPLIRTRLQDELLEFQRRlKKTILFVSHDLDEAFRIGNRIAIMESGRI 246
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
50-271 2.66e-06

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 49.34  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    50 IEEGEILVLMGLSGSGKSTLLRAVNGlaPVVRGDVAVSTTTgpvnpySCNAKALRDLRTHTVSMVF---QQFALLPWRTV 126
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVI------TYDGITPEEIKKHYRGDVVynaETDVHFPHLTV 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   127 AENVGF-------GLELAGMPEAERKLRVGE------QLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDE 193
Cdd:TIGR00956  156 GETLDFaarcktpQNRPDGVSREEYAKHIADvymatyGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   194 PFSALDplirtrlQDELLEFQRRLK------KTILFVS--HDLDEAFRIGNRIAIMESGRIIQCGtPHDIVKN------- 258
Cdd:TIGR00956  236 ATRGLD-------SATALEFIRALKtsanilDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFG-PADKAKQyfekmgf 307
                          250
                   ....*....|....*
gi 516735053   259 --PADQYVADFVQNL 271
Cdd:TIGR00956  308 kcPDRQTTADFLTSL 322
PLN03232 PLN03232
ABC transporter C family member; Provisional
47-275 4.53e-06

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 48.82  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYSCNAKALRDLRtHTVSMVFQQFALLpwrtv 126
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-------DDCDVAKFGLTDLR-RVLSIIPQSPVLF----- 1322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  127 AENVGFGLElagmPEAERK-LRVGEQLELVNLTKWAGR-------KVNE----LSGGMQQRVGLARAFATGAPILLMDEP 194
Cdd:PLN03232 1323 SGTVRFNID----PFSEHNdADLWEALERAHIKDVIDRnpfgldaEVSEggenFSVGQRQLLSLARALLRRSKILVLDEA 1398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  195 FSALDPLIRTRLQDELLEFQRRLkkTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDIVKNPADQYvADFVQNLNPI 274
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSC--TMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAF-FRMVHSTGPA 1474

                  .
gi 516735053  275 N 275
Cdd:PLN03232 1475 N 1475
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
47-248 4.92e-06

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: 47.54  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVvRGDVAVSTTtgpvnpySCNAKALRDLRthtvsmvfQQFALLPWRTV 126
Cdd:cd03289   24 SFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGV-------SWNSVPLQKWR--------KAFGVIPQKVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 127 AENVGF--GLELAGMPEAERKLRVGEQLELVNLTKWAGRKVN--------ELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:cd03289   88 IFSGTFrkNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 197 ALDPL----IRTRLQdellefQRRLKKTILFVSHDLdEAFRIGNRIAIMESGRIIQ 248
Cdd:cd03289  168 HLDPItyqvIRKTLK------QAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQ 216
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
38-257 4.94e-06

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: 48.40  E-value: 4.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    38 GLVLGVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTttgpVNPyscnAK-ALRDLRTHtVSMVFQ 116
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----LNI----AKiGLHDLRFK-ITIIPQ 1367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   117 QFALL---------PWRTVA-ENVGFGLELAGMpeaerKLRVGEQLELVNLTKWAGRKvnELSGGMQQRVGLARAFATGA 186
Cdd:TIGR00957 1368 DPVLFsgslrmnldPFSQYSdEEVWWALELAHL-----KTFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKT 1440
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516735053   187 PILLMDEPFSALD--------PLIRTRLQDellefqrrlkKTILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDIVK 257
Cdd:TIGR00957 1441 KILVLDEATAAVDletdnliqSTIRTQFED----------CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
53-248 5.82e-06

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: 45.44  E-value: 5.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    53 GEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVavstttgpvnpYSCNAKALRdlrthtvsmvfqqfallpwrtvaenvgf 132
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-----------IYIDGEDIL---------------------------- 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   133 glelagmpeaerklrvgEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDE--- 209
Cdd:smart00382  43 -----------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 516735053   210 --LLEFQRRLKKTILFVSHDLDEafrIGNRIAIMESGRIIQ 248
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKD---LGPALLRRRFDRRIV 143
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
43-227 6.29e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 48.02  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLRAVNG-LAPvvrgdvavstTTGPVNpysCNakalrdlrTHTVSMVFQQF--A 119
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQA----------DSGRIH---CG--------TKLEVAYFDQHraE 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 120 LLPWRTVAENVgfglelagmpeAErklrvGEQLELVNltkwaGRK--------------------VNELSGGMQQRVGLA 179
Cdd:PRK11147 394 LDPEKTVMDNL-----------AE-----GKQEVMVN-----GRPrhvlgylqdflfhpkramtpVKALSGGERNRLLLA 452
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 516735053 180 RAFATGAPILLMDEPFSALDplIRT-RLQDELL-EFQrrlkKTILFVSHD 227
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLD--VETlELLEELLdSYQ----GTVLLVSHD 496
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
167-242 6.93e-06

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 46.03  E-value: 6.93e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516735053 167 ELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTILFVSHDLDEAFRIGNRIAIME 242
Cdd:cd03222   71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
45-243 8.04e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 47.72  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTgpvNPYSCNAKALRDlRTHTVSmvfqQFALLPWR 124
Cdd:PTZ00265  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH---NLKDINLKWWRS-KIGVVS----QDPLLFSN 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  125 TVAENVGFGL---------------------------------------------ELAGMPEAERKLRVGEQLELVNLTK 159
Cdd:PTZ00265  475 SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDSEVVDVSK 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  160 -----------------WAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFQRRLKKTIL 222
Cdd:PTZ00265  555 kvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
                         250       260
                  ....*....|....*....|.
gi 516735053  223 FVSHDLdEAFRIGNRIAIMES 243
Cdd:PTZ00265  635 IIAHRL-STIRYANTIFVLSN 654
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
4-239 1.28e-05

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 47.04  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   4 VSFNNVSIIFGDRpetalamvdqgksrdeigaatglVLgVADASLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGD 83
Cdd:PRK11819 325 IEAENLSKSFGDR-----------------------LL-IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  84 VAVstttGPvnpyscnakalrdlrthTVSMVF-QQF--ALLPWRTVAENVGFGLELagmpeaerkLRVGeQLElVNLTKW 160
Cdd:PRK11819 381 IKI----GE-----------------TVKLAYvDQSrdALDPNKTVWEEISGGLDI---------IKVG-NRE-IPSRAY 428
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 161 AGR----------KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplIRT--RLQDELLEFqrrlKKTILFVSHD- 227
Cdd:PRK11819 429 VGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD--VETlrALEEALLEF----PGCAVVISHDr 502
                        250
                 ....*....|....
gi 516735053 228 --LDeafrignRIA 239
Cdd:PRK11819 503 wfLD-------RIA 509
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
140-231 1.73e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 46.55  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 140 PEAERKLrVGEQLELVNLTKWAGRK-VNELSGGmQQRVGL-ARAFATGAPILLMDEPFSALDPLIRT---RLQDELL-EF 213
Cdd:PRK10938 374 SDRQQKL-AQQWLDILGIDKRTADApFHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLIsEG 451
                         90
                 ....*....|....*...
gi 516735053 214 QRRLkktiLFVSHDLDEA 231
Cdd:PRK10938 452 ETQL----LFVSHHAEDA 465
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
49-228 1.93e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 46.34  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  49 TIEEGEILVLMGLSGSGKSTLLRAVNG-LAPV---VRGDVAVStttgpVNP-YscnakaLRDLRTHTVSMVFqqfallpw 123
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDegeVDPELKIS-----YKPqY------IKPDYDGTVEDLL-------- 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 124 RTVAENVG---FGLELAgmpeaeRKLRVGEQLElvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDP 200
Cdd:PRK13409 422 RSITDDLGssyYKSEII------KPLQLERLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
                        170       180
                 ....*....|....*....|....*...
gi 516735053 201 LIRTRLQDELLEFQRRLKKTILFVSHDL 228
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEREATALVVDHDI 514
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
49-228 2.05e-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: 46.32  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  49 TIEEGEILVLMGLSGSGKSTLLRAVNG-LAP---VVRGDVAVS--------TTTGPVNPYscnakaLRDLRTHTVSMVFq 116
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKILAGvLKPdegEVDEDLKISykpqyispDYDGTVEEF------LRSANTDDFGSSY- 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 117 qfallpWRTvaenvgfglELAgmpeaeRKLRVGEQLElvnltkwagRKVNELSGGMQQRVGLARAFATGAPILLMDEPFS 196
Cdd:COG1245  435 ------YKT---------EII------KPLGLEKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 516735053 197 ALDplIRTRLqdELLEFQRRL----KKTILFVSHDL 228
Cdd:COG1245  485 HLD--VEQRL--AVAKAIRRFaenrGKTAMVVDHDI 516
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
162-259 3.41e-05

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: 45.77  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  162 GRKVNELSGGMQQRVGLARAFATG--APILLMDEPFSALDP-----LIRT--RLQDellefqrrLKKTILFVSHDlDEAF 232
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQrdnrrLINTlkRLRD--------LGNTLIVVEHD-EDTI 553
                          90       100       110
                  ....*....|....*....|....*....|...
gi 516735053  233 RIGNRI------AIMESGRIIQCGTPHDIVKNP 259
Cdd:TIGR00630 554 RAADYVidigpgAGEHGGEVVASGTPEEILANP 586
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
50-199 3.66e-05

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: 44.16  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  50 IEEGEILVLMGLSGSGKSTLLR--AVNGLAPVVRGDVAVstttgpvnpyscNAKALRDLRTHTVSMVFQQFALLPWRTVA 127
Cdd:cd03232   30 VKPGTLTALMGESGAGKTTLLDvlAGRKTAGVITGEILI------------NGRPLDKNFQRSTGYVEQQDVHSPNLTVR 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516735053 128 ENVGFGLELAGMPEAERKlRVGEQLELVnltkwagrkvnelsggmqqrvglARAFatgapILLMDEPFSALD 199
Cdd:cd03232   98 EALRFSALLRGLSVEQRK-RLTIGVELA-----------------------AKPS-----ILFLDEPTSGLD 140
PLN03140 PLN03140
ABC transporter G family member; Provisional
3-257 5.10e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 45.22  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    3 AVSFNNVSIiFGDRPETalaMVDQGKSRDEIGaatgLVLGVADAsltIEEGEILVLMGLSGSGKSTLLRAVNG--LAPVV 80
Cdd:PLN03140  867 AMSFDDVNY-FVDMPAE---MKEQGVTEDRLQ----LLREVTGA---FRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYI 935
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   81 RGDVAVS------TTTGPVNPYsCNAKalrDLRTHTV----SMVFQQFALLPWRTVAEnvgfglelagmpeaERKLRVGE 150
Cdd:PLN03140  936 EGDIRISgfpkkqETFARISGY-CEQN---DIHSPQVtvreSLIYSAFLRLPKEVSKE--------------EKMMFVDE 997
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  151 QLELVNLTKWAGR-----KVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD---PLIRTRLQDELLEFQRRLKKTIL 222
Cdd:PLN03140  998 VMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDaraAAIVMRTVRNTVDTGRTVVCTIH 1077
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 516735053  223 FVSHDLDEAFrigNRIAIME-SGRIIQCGT----PHDIVK 257
Cdd:PLN03140 1078 QPSIDIFEAF---DELLLMKrGGQVIYSGPlgrnSHKIIE 1114
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
45-199 5.75e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 43.32  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  45 DASLTIEEGEILVLMGLSGSGKSTLLRAVNGLapvvrgdvaVSTTTGPVNPYSCNakaLRDLRTHTVSMVFQQFALLPWR 124
Cdd:PRK13541  18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGI---------MQPSSGNIYYKNCN---INNIAKPYCTYIGHNLGLKLEM 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 125 TVAENVGFGLELAGMPEAerklrVGEQLELVNLTKWAGRKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:PRK13541  86 TVFENLKFWSEIYNSAET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
163-244 7.31e-05

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 43.41  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 163 RKVNELSGGMQQRVGLARAFA--------TGAPI--LLMDEPFSALDPLIRTRLQdELLEFQRRLKKTILFVSHDLDEAF 232
Cdd:cd03279  119 RPVSTLSGGETFLASLSLALAlsevlqnrGGARLeaLFIDEGFGTLDPEALEAVA-TALELIRTENRMVGVISHVEELKE 197
                         90
                 ....*....|..
gi 516735053 233 RIGNRIAIMESG 244
Cdd:cd03279  198 RIPQRLEVIKTP 209
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
163-270 1.45e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.05  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  163 RKVNELSGGMQQRVGLARAFatGAPIL----LMDEPFSALDPlirtRLQDELLEFQRRLK---KTILFVSHD------LD 229
Cdd:PRK00635  472 RALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHP----QDTHKLINVIKKLRdqgNTVLLVEHDeqmislAD 545
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 516735053  230 EAFRIGNRIAIMeSGRIIQCGTPHDIVKNpADQYVADFVQN 270
Cdd:PRK00635  546 RIIDIGPGAGIF-GGEVLFNGSPREFLAK-SDSLTAKYLRQ 584
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
166-252 2.69e-04

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: 41.63  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 166 NELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLE-FQrrlKKTILFVSHDLDEAFRIgNRIAIMESG 244
Cdd:cd03369  124 LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeFT---NSTILTIAHRLRTIIDY-DKILVMDAG 199

                 ....*...
gi 516735053 245 RIIQCGTP 252
Cdd:cd03369  200 EVKEYDHP 207
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
53-199 4.23e-04

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 42.40  E-value: 4.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053    53 GEILVLMGLSGSGKSTLLravNGLAP------VVRGDVAVstttgpvnpyscNAKALRDLRTHTVSMVFQQFALLPWRTV 126
Cdd:TIGR00956  789 GTLTALMGASGAGKTTLL---NVLAErvttgvITGGDRLV------------NGRPLDSSFQRSIGYVQQQDLHLPTSTV 853
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   127 AENVGFGLEL---AGMPEAERKLRVGEQLELVNLTKWAGRKVNELSGGM--QQR------VGLArafATGAPILLMDEPF 195
Cdd:TIGR00956  854 RESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnvEQRkrltigVELV---AKPKLLLFLDEPT 930

                   ....
gi 516735053   196 SALD 199
Cdd:TIGR00956  931 SGLD 934
PLN03073 PLN03073
ABC transporter F family; Provisional
43-226 4.83e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 42.15  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  43 VADASLTIEEGEILVLMGLSGSGKSTLLR-----AVNGLAPV-----VRGDVAVSTTTGpvnpYSC--NAKALRDLRTHT 110
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNcqilhVEQEVVGDDTTA----LQCvlNTDIERTQLLEE 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 111 VSMVFQQFALLPWRTVAENVGFGLE--LAGMPEAERKLRVGEQLELVNL--------TKWAG---------RKVNELSGG 171
Cdd:PLN03073 269 EAQLVAQQRELEFETETGKGKGANKdgVDKDAVSQRLEEIYKRLELIDAytaearaaSILAGlsftpemqvKATKTFSGG 348
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516735053 172 MQQRVGLARAFATGAPILLMDEPFSALDPLIRTRLQDELLEFqrrlKKTILFVSH 226
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSH 399
PLN03130 PLN03130
ABC transporter C family member; Provisional
47-258 9.56e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 41.26  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053   47 SLTIEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVstttgpvNPYSCNAKALRDLRThtVSMVFQQFALLPWRTV 126
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI-------DGCDISKFGLMDLRK--VLGIIPQAPVLFSGTV 1329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  127 AENVG-FG----------LELAGMPEAERKLRVGEQLELVNltkwAGRKvneLSGGMQQRVGLARAFATGAPILLMDEPF 195
Cdd:PLN03130 1330 RFNLDpFNehndadlwesLERAHLKDVIRRNSLGLDAEVSE----AGEN---FSVGQRQLLSLARALLRRSKILVLDEAT 1402
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053  196 SALDplIRTrlqDELLefQRRLKK-----TILFVSHDLDEAFRIgNRIAIMESGRIIQCGTPHDIVKN 258
Cdd:PLN03130 1403 AAVD--VRT---DALI--QKTIREefkscTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
167-228 1.05e-03

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 40.45  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516735053  167 ELSGGMQQ---RVGLARAFATGAPILLMDEPFSALDPLIRTRLQdELLEFQRRLKKTILFVSHDL 228
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLL-ELLKELSRNGAQLILTTHSP 299
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
168-237 1.83e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 39.13  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 168 LSGGmQQ-------RVGLARAFATGAPILLMDEPFSALDP-LIRTRLQDeLLEFQRRLK-KTILFVSHD------LDEAF 232
Cdd:cd03240  116 CSGG-EKvlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAE-IIEERKSQKnFQLIVITHDeelvdaADHIY 193

                 ....*
gi 516735053 233 RIGNR 237
Cdd:cd03240  194 RVEKD 198
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
125-229 1.90e-03

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: 39.52  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 125 TVAENVGFgleLAGMPEAERKLRVGEQLELVNLTkwAGRKVNELSGGMQQRVGLARAF---ATGAPILLMDEPFSALdpl 201
Cdd:cd03271  132 TVEEALEF---FENIPKIARKLQTLCDVGLGYIK--LGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGL--- 203
                         90       100       110
                 ....*....|....*....|....*....|...
gi 516735053 202 irtRLQD--ELLEFQRRLKK---TILFVSHDLD 229
Cdd:cd03271  204 ---HFHDvkKLLEVLQRLVDkgnTVVVIEHNLD 233
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
140-229 2.35e-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: 40.00  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  140 PEAERKLR----VGeqLELVNLtkwaGRKVNELSGGMQQRVGLARAF---ATGAPILLMDEPFSALdplirtRLQD--EL 210
Cdd:TIGR00630 804 PSISRKLQtlcdVG--LGYIRL----GQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL------HFDDikKL 871
                          90       100
                  ....*....|....*....|..
gi 516735053  211 LEFQRRLKK---TILFVSHDLD 229
Cdd:TIGR00630 872 LEVLQRLVDkgnTVVVIEHNLD 893
GguA NF040905
sugar ABC transporter ATP-binding protein;
164-247 2.49e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.77  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 164 KVNELSGGMQQRVGLARAFATGAPILLMDEPfsaldplirTRLQD-----ELLEFQRRLK---KTILFVSHDLDEAFRIG 235
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEP---------TRGIDvgakyEIYTIINELAaegKGVIVISSELPELLGMC 471
                         90
                 ....*....|..
gi 516735053 236 NRIAIMESGRII 247
Cdd:NF040905 472 DRIYVMNEGRIT 483
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
163-242 4.74e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 39.00  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 163 RKVNELSGGMQQRVGLARAFATGAPILLMDEPFSALDplirtrlQDELLEFQRRLKK---TILFVSHDLDEAFRIGNRIA 239
Cdd:PRK10636 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSyqgTLILISHDRDFLDPIVDKII 217

                 ...
gi 516735053 240 IME 242
Cdd:PRK10636 218 HIE 220
COG4639 COG4639
Predicted kinase [General function prediction only];
52-80 5.84e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 36.73  E-value: 5.84e-03
                         10        20
                 ....*....|....*....|....*....
gi 516735053  52 EGEILVLMGLSGSGKSTLLRAVNGLAPVV 80
Cdd:COG4639    1 MLSLVVLIGLPGSGKSTFARRLFAPTEVV 29
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
50-256 9.66e-03

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: 37.20  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053  50 IEEGEILVLMGLSGSGKSTLLRAVNGLAPVVRGDVAVSTTTGPVNPyscnakaLRDLRTHtVSMVFQ---------QFAL 120
Cdd:cd03288   44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP-------LHTLRSR-LSIILQdpilfsgsiRFNL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516735053 121 LPWRTVAENVGF-GLELAGMPEAERKLRVGeqleLVNLTKWAGRKvneLSGGMQQRVGLARAFATGAPILLMDEPFSALD 199
Cdd:cd03288  116 DPECKCTDDRLWeALEIAQLKNMVKSLPGG----LDAVVTEGGEN---FSVGQRQLFCLARAFVRKSSILIMDEATASID 188
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516735053 200 PLIRTRLQDELL-EFQRRLKKTILFVSHDLDEAfrigNRIAIMESGRIIQCGTPHDIV 256
Cdd:cd03288  189 MATENILQKVVMtAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENLL 242
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-73 9.68e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 9.68e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 516735053  44 ADASLTIEEGeILVLMGLSGSGKSTLLRAV 73
Cdd:PRK02224  15 ADADLRLEDG-VTVIHGVNGSGKSSLLEAC 43
 
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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