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Conserved domains on  [gi|1439757928|emb|STR14823|]
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putative transporter ATP-binding component [Klebsiella aerogenes]

Protein Classification

ABC-F family ATP-binding cassette domain-containing protein( domain architecture ID 11422672)

ABC-F family ATP-binding cassette domain-containing protein similar to Bacillus subtilis VmlR, a ribosomal protection protein that confers resistance to lincomycin (Lnc), the streptogramin A (SA) antibiotic virginiamycin M (VgM) and the pleuromutilin antibiotic tiamulin

Gene Ontology:  GO:0005524|GO:0016887
PubMed:  16124856|31563533
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
15-492 5.94e-130

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


:

Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 389.81  E-value: 5.94e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  15 AFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP--------------- 77
Cdd:COG0488     7 SFGgrPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPldddltvldtvldgd 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  78 ---------------------ETLHTQSLLQAVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLL 136
Cdd:COG0488    87 aelraleaeleeleaklaepdEDLERLAELQEEFEALGGWEAEAR---AEEILSGLGFPEEDLDRPVSELSGGWRRRVAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 137 ARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFalPC--------S 208
Cdd:COG0488   164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLY--PGnysayleqR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 209 AARQALQEQDESAALRHKAEQKE-IDRVSASARRlatwgrvydnedlARKAKQMEKQVARLKDEQTELSVGPPwRLVLQG 287
Cdd:COG0488   242 AERLEQEAAAYAKQQKKIAKEEEfIRRFRAKARK-------------AKQAQSRIKALEKLEREEPPRRDKTV-EIRFPP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 288 DALPADRLLEMDtlHVSPAPGQPSLFtTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPG 365
Cdd:COG0488   308 PERLGKKVLELE--GLSKSYGDKTLL-DDLsLRIDRGDRIGLIGPNGAGKSTLLKLL---AGELEPDSGtVKLGETVKIG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 366 YYDQTLAQLPDEASLLEALTPFAPSADTRK-RALIAA-GFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:COG0488   382 YFDQHQEELDPDKTVLDELRDGAPGGTEQEvRGYLGRfLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 444 HLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:COG0488   462 HLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
 
Name Accession Description Interval E-value
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
15-492 5.94e-130

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 389.81  E-value: 5.94e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  15 AFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP--------------- 77
Cdd:COG0488     7 SFGgrPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPldddltvldtvldgd 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  78 ---------------------ETLHTQSLLQAVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLL 136
Cdd:COG0488    87 aelraleaeleeleaklaepdEDLERLAELQEEFEALGGWEAEAR---AEEILSGLGFPEEDLDRPVSELSGGWRRRVAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 137 ARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFalPC--------S 208
Cdd:COG0488   164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLY--PGnysayleqR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 209 AARQALQEQDESAALRHKAEQKE-IDRVSASARRlatwgrvydnedlARKAKQMEKQVARLKDEQTELSVGPPwRLVLQG 287
Cdd:COG0488   242 AERLEQEAAAYAKQQKKIAKEEEfIRRFRAKARK-------------AKQAQSRIKALEKLEREEPPRRDKTV-EIRFPP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 288 DALPADRLLEMDtlHVSPAPGQPSLFtTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPG 365
Cdd:COG0488   308 PERLGKKVLELE--GLSKSYGDKTLL-DDLsLRIDRGDRIGLIGPNGAGKSTLLKLL---AGELEPDSGtVKLGETVKIG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 366 YYDQTLAQLPDEASLLEALTPFAPSADTRK-RALIAA-GFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:COG0488   382 YFDQHQEELDPDKTVLDELRDGAPGGTEQEvRGYLGRfLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 444 HLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:COG0488   462 HLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
19-484 1.04e-58

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 206.94  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP---------------ETLHTQ 83
Cdd:PRK10636   16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPalpqpaleyvidgdrEYRQLE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 SLLQA--------VLAPLPADAREAQRWL----AERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK10636   96 AQLHDanerndghAIATIHGKLDAIDAWTirsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 152 PGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFALPCS----------AARQALQE--QDE 219
Cdd:PRK10636  176 PTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSsfevqratrlAQQQAMYEsqQER 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 220 SAALrhkaeQKEIDRVSASarrlatwgrvydnedlARKAKQMEKQVARLkdEQTEL----SVGPPWRLVL-QGDALPaDR 294
Cdd:PRK10636  256 VAHL-----QSYIDRFRAK----------------ATKAKQAQSRIKML--ERMELiapaHVDNPFHFSFrAPESLP-NP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 295 LLEMDtlHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRLHPRLhpGYYDQ-TLAQ 373
Cdd:PRK10636  312 LLKME--KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL--GYFAQhQLEF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 374 LPDEASLLEALTPFAPSADTRKRALIAAGFGWarHSQKVST----LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEG 449
Cdd:PRK10636  388 LRADESPLQHLARLAPQELEQKLRDYLGGFGF--QGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1439757928 450 KAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLI 484
Cdd:PRK10636  466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLV 500
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
22-471 1.05e-52

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: 188.61  E-value: 1.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTlkKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA----------------GQCLMARVEQHLPETLHTQSL 85
Cdd:TIGR03719  25 SLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylpqepqldpTKTVRENVEEGVAEIKDALDR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 LQAVLAPL--PADAREA----QRWLAERLLAQMGFT--------------PAvMEQQTATLSGGQHTRLLLARALIRQPD 145
Cdd:TIGR03719 103 FNEISAKYaePDADFDKlaaeQAELQEIIDAADAWDldsqleiamdalrcPP-WDADVTKLSGGERRRVALCRLLLSKPD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 146 LLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNssWIL---RDQTL-----HSFALPCSAARQALQEQ 217
Cdd:TIGR03719 182 MLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILeldRGRGIpwegnYSSWLEQKQKRLEQEEK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 218 DESAalRHKAEQKEID--RVSASARRLATWGRVYDNEDLARKAKQMekqvarlKDEQTELSVGPPWRLvlqgdalpADRL 295
Cdd:TIGR03719 260 EESA--RQKTLKRELEwvRQSPKGRQAKSKARLARYEELLSQEFQK-------RNETAEIYIPPGPRL--------GDKV 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 296 LEMDtlHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTLAQL 374
Cdd:TIGR03719 323 IEAE--NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI---TGQEQPDSGtIEIGETVKLAYVDQSRDAL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 375 PDEASLLEALTPFAP-----SADTRKRALIAA-GFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDME 448
Cdd:TIGR03719 398 DPNKTVWEEISGGLDiiklgKREIPSRAYVGRfNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
                         490       500
                  ....*....|....*....|...
gi 1439757928 449 GKAALAQTLRDYPGGVLLVSHDR 471
Cdd:TIGR03719 478 TLRALEEALLNFAGCAVVISHDR 500
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
5-199 2.96e-48

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: 164.54  E-value: 2.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQhlpetlhtqs 84
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 llqavlaplpadareaqrwlaerllaqmgftpavmeqqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03221    71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1439757928 165 ESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQT 199
Cdd:cd03221   110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
20-152 5.35e-28

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: 109.27  E-value: 5.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP---------------ETLHTQS 84
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkeigyvfqdpqlfprLTVRENL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  85 LLQAVLAPLPADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
18-181 1.53e-21

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 92.30  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH--LPETLHTqSLLQAV------ 89
Cdd:NF040873    6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRseVPDSLPL-TVRDLVamgrwa 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 ----LAPLPADAREAqrwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:NF040873   85 rrglWRRLTRDDRAA----VDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
                         170
                  ....*....|....*....
gi 1439757928 166 SFLQTWQG---SFVLVSHD 181
Cdd:NF040873  160 ALLAEEHArgaTVVVVTHD 178
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-152 5.20e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 72.08  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR----------------------VEQHLpeTLH 81
Cdd:NF033858  286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiatrrrvgymsqafslygeltVRQNL--ELH 363
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928  82 tqsllqAVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF033858  364 ------ARLFHLPAAEIAAR---VAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
318-476 8.06e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 58.40  E-value: 8.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 318 ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTLA---QLPDEASLLEALTPFAP---- 389
Cdd:NF040873   13 LTIPAGSLTAVVGPNGSGKSTLLKVL---AGVLRPTSGtVRRAGGARVAYVPQRSEvpdSLPLTVRDLVAMGRWARrglw 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 390 ---SADTRK---RALIAAGFGWARHSQkVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG- 462
Cdd:NF040873   90 rrlTRDDRAavdDALERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAr 168
                         170
                  ....*....|....*.
gi 1439757928 463 --GVLLVSHDRQLISE 476
Cdd:NF040873  169 gaTVVVVTHDLELVRR 184
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
29-203 9.52e-09

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: 54.30  E-value: 9.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   29 KGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlPETLHTQSLLQAVLAPLPADAREaqrwlaerl 108
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------GEDILEEVLDQLLLIIVGGKKAS--------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  109 laqmgftpavmeqqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAV 188
Cdd:smart00382  61 -----------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
                          170
                   ....*....|....*
gi 1439757928  189 TNSSWILRDQTLHSF 203
Cdd:smart00382 124 NDEKDLGPALLRRRF 138
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
23-152 4.95e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 49.74  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVS-LAGQCLMARVEQHL-------PETL-----HTQSL---L 86
Cdd:NF033858   20 VSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVcpriaymPQGLgknlyPTLSVfenL 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  87 Q--AVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF033858  100 DffGRLFGQDAAERRRR---IDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
GguA NF040905
sugar ABC transporter ATP-binding protein;
105-152 2.30e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.54  E-value: 2.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 105 AERLLAQMGF-TPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF040905  384 AEEYRKKMNIkTPSV-FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
97-179 2.64e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.10  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  97 AREAQRWLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL--LWLESFLQTWQGS 174
Cdd:NF000106  117 SRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRneVWDEVRSMVRDGA 195

                  ....*
gi 1439757928 175 FVLVS 179
Cdd:NF000106  196 TVLLT 200
 
Name Accession Description Interval E-value
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
15-492 5.94e-130

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 389.81  E-value: 5.94e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  15 AFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP--------------- 77
Cdd:COG0488     7 SFGgrPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPldddltvldtvldgd 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  78 ---------------------ETLHTQSLLQAVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLL 136
Cdd:COG0488    87 aelraleaeleeleaklaepdEDLERLAELQEEFEALGGWEAEAR---AEEILSGLGFPEEDLDRPVSELSGGWRRRVAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 137 ARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFalPC--------S 208
Cdd:COG0488   164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLY--PGnysayleqR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 209 AARQALQEQDESAALRHKAEQKE-IDRVSASARRlatwgrvydnedlARKAKQMEKQVARLKDEQTELSVGPPwRLVLQG 287
Cdd:COG0488   242 AERLEQEAAAYAKQQKKIAKEEEfIRRFRAKARK-------------AKQAQSRIKALEKLEREEPPRRDKTV-EIRFPP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 288 DALPADRLLEMDtlHVSPAPGQPSLFtTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPG 365
Cdd:COG0488   308 PERLGKKVLELE--GLSKSYGDKTLL-DDLsLRIDRGDRIGLIGPNGAGKSTLLKLL---AGELEPDSGtVKLGETVKIG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 366 YYDQTLAQLPDEASLLEALTPFAPSADTRK-RALIAA-GFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:COG0488   382 YFDQHQEELDPDKTVLDELRDGAPGGTEQEvRGYLGRfLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 444 HLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:COG0488   462 HLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
19-484 1.04e-58

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 206.94  E-value: 1.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP---------------ETLHTQ 83
Cdd:PRK10636   16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPalpqpaleyvidgdrEYRQLE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 SLLQA--------VLAPLPADAREAQRWL----AERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK10636   96 AQLHDanerndghAIATIHGKLDAIDAWTirsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 152 PGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFALPCS----------AARQALQE--QDE 219
Cdd:PRK10636  176 PTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSsfevqratrlAQQQAMYEsqQER 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 220 SAALrhkaeQKEIDRVSASarrlatwgrvydnedlARKAKQMEKQVARLkdEQTEL----SVGPPWRLVL-QGDALPaDR 294
Cdd:PRK10636  256 VAHL-----QSYIDRFRAK----------------ATKAKQAQSRIKML--ERMELiapaHVDNPFHFSFrAPESLP-NP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 295 LLEMDtlHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRLHPRLhpGYYDQ-TLAQ 373
Cdd:PRK10636  312 LLKME--KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL--GYFAQhQLEF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 374 LPDEASLLEALTPFAPSADTRKRALIAAGFGWarHSQKVST----LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEG 449
Cdd:PRK10636  388 LRADESPLQHLARLAPQELEQKLRDYLGGFGF--QGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1439757928 450 KAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLI 484
Cdd:PRK10636  466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLV 500
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
16-506 5.35e-56

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 197.04  E-value: 5.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  16 FG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA--------------------------GQC 67
Cdd:PRK15064   11 FGakPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlgklrqdqfafeeftvldtvimGHT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  68 LMARVEQH------LPETLHTQSL----LQAVLAPL---PADAReaqrwlAERLLAQMGFTpavMEQQTATLSG---GQH 131
Cdd:PRK15064   91 ELWEVKQErdriyaLPEMSEEDGMkvadLEVKFAEMdgyTAEAR------AGELLLGVGIP---EEQHYGLMSEvapGWK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 132 TRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAV-TNSSWI----LR------DQTL 200
Cdd:PRK15064  162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVcTHMADLdygeLRvypgnyDEYM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 201 hsfalpcSAARQAlQEQDESAALRHKAEQKE----IDRVSASAR--RLATwgrvydnedlaRKAKQMEKqvarLK-DEQT 273
Cdd:PRK15064  242 -------TAATQA-RERLLADNAKKKAQIAElqsfVSRFSANASkaKQAT-----------SRAKQIDK----IKlEEVK 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 274 ELSVGPPWRLVLQGDALpaDRL-LEMDTLhvSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASP 352
Cdd:PRK15064  299 PSSRQNPFIRFEQDKKL--HRNaLEVENL--TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL---VGELEP 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 353 LPG-LRLHPRLHPGYYDQ-TLAQLPDEASLLEALTPFAPSAD-------TRKRALiaagFGWARHSQKVSTLSGGERSRL 423
Cdd:PRK15064  372 DSGtVKWSENANIGYYAQdHAYDFENDLTLFDWMSQWRQEGDdeqavrgTLGRLL----FSQDDIKKSVKVLSGGEKGRM 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 424 LFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:PRK15064  448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527

                  ...
gi 1439757928 504 AVA 506
Cdd:PRK15064  528 GIE 530
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
15-488 5.04e-54

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 193.63  E-value: 5.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  15 AFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------------------ 74
Cdd:PRK11147   12 SFSdaPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvydfvaegi 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  75 -HLPETL---HTQSLLQAV---------LAPLPADAREAQRWLAE----RLLAQMGFTPavmEQQTATLSGGQHTRLLLA 137
Cdd:PRK11147   92 eEQAEYLkryHDISHLVETdpseknlneLAKLQEQLDHHNLWQLEnrinEVLAQLGLDP---DAALSSLSGGWLRKAALG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 138 RALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTL----------LDAVTNSSWILRDQTLhsfalpc 207
Cdd:PRK11147  169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFirnmatrivdLDRGKLVSYPGNYDQY------- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 208 saarqaLQEQDEsaALRHKAEQK-EIDRVSAS----------ARRLATWGRVYdnedlARKAkqmekqvarLKDEQTEls 276
Cdd:PRK11147  242 ------LLEKEE--ALRVEELQNaEFDRKLAQeevwirqgikARRTRNEGRVR-----ALKA---------LRRERSE-- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 277 vgppwRLVLQGDAL----PADR----LLEMDTLHVSpAPGQPSL--FTTGVARlrsGDRVAIMGRNGGGKSSLLRLLWQQ 346
Cdd:PRK11147  298 -----RREVMGTAKmqveEASRsgkiVFEMENVNYQ-IDGKQLVkdFSAQVQR---GDKIALIGPNGCGKTTLLKLMLGQ 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 347 MNNASPlpglRLH--PRLHPGYYDQTLAQLPDEASLLEALtpfapsADTRKRALIAagfGWARH----------SQK--- 411
Cdd:PRK11147  369 LQADSG----RIHcgTKLEVAYFDQHRAELDPEKTVMDNL------AEGKQEVMVN---GRPRHvlgylqdflfHPKram 435
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 412 --VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAG 488
Cdd:PRK11147  436 tpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNG 514
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
22-471 1.05e-52

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: 188.61  E-value: 1.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTlkKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA----------------GQCLMARVEQHLPETLHTQSL 85
Cdd:TIGR03719  25 SLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylpqepqldpTKTVRENVEEGVAEIKDALDR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 LQAVLAPL--PADAREA----QRWLAERLLAQMGFT--------------PAvMEQQTATLSGGQHTRLLLARALIRQPD 145
Cdd:TIGR03719 103 FNEISAKYaePDADFDKlaaeQAELQEIIDAADAWDldsqleiamdalrcPP-WDADVTKLSGGERRRVALCRLLLSKPD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 146 LLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNssWIL---RDQTL-----HSFALPCSAARQALQEQ 217
Cdd:TIGR03719 182 MLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILeldRGRGIpwegnYSSWLEQKQKRLEQEEK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 218 DESAalRHKAEQKEID--RVSASARRLATWGRVYDNEDLARKAKQMekqvarlKDEQTELSVGPPWRLvlqgdalpADRL 295
Cdd:TIGR03719 260 EESA--RQKTLKRELEwvRQSPKGRQAKSKARLARYEELLSQEFQK-------RNETAEIYIPPGPRL--------GDKV 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 296 LEMDtlHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTLAQL 374
Cdd:TIGR03719 323 IEAE--NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI---TGQEQPDSGtIEIGETVKLAYVDQSRDAL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 375 PDEASLLEALTPFAP-----SADTRKRALIAA-GFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDME 448
Cdd:TIGR03719 398 DPNKTVWEEISGGLDiiklgKREIPSRAYVGRfNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
                         490       500
                  ....*....|....*....|...
gi 1439757928 449 GKAALAQTLRDYPGGVLLVSHDR 471
Cdd:TIGR03719 478 TLRALEEALLNFAGCAVVISHDR 500
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
11-203 6.84e-51

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 182.96  E-value: 6.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLpETLH-TQSLLQ 87
Cdd:COG0488   320 GLSKSYGdkTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDpDKTVLD 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 aVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESF 167
Cdd:COG0488   399 -ELRDGAPGGTEQE---VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1439757928 168 LQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSF 203
Cdd:COG0488   475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
5-199 2.96e-48

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: 164.54  E-value: 2.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQhlpetlhtqs 84
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 llqavlaplpadareaqrwlaerllaqmgftpavmeqqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03221    71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1439757928 165 ESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQT 199
Cdd:cd03221   110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
PLN03073 PLN03073
ABC transporter F family; Provisional
19-502 1.86e-47

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 176.59  E-value: 1.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQ-----VLDGTlaPTS-----------GSVSLAGQCLM-ARVE--QHLPET 79
Cdd:PLN03073  192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI--PKNcqilhveqevvGDDTTALQCVLnTDIErtQLLEEE 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 LH------------------------------TQSLLQAV--LAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLS 127
Cdd:PLN03073  270 AQlvaqqrelefetetgkgkgankdgvdkdavSQRLEEIYkrLELIDAYTAEAR---AASILAGLSFTPEMQVKATKTFS 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 128 GGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFALPC 207
Cdd:PLN03073  347 GGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDY 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 208 SAARQALQEQDESAALRHKAEQKE-------IDRVSASARRLATwgrvydnedLARKAKQMEK-----QVARLKDEQTEL 275
Cdd:PLN03073  427 DTFERTREEQLKNQQKAFESNERSrshmqafIDKFRYNAKRASL---------VQSRIKALDRlghvdAVVNDPDYKFEF 497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 276 SVgppwrlvlqgdalPADRlLEMDTLHVSPA----PGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNnas 351
Cdd:PLN03073  498 PT-------------PDDR-PGPPIISFSDAsfgyPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQ--- 560
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 352 PLPGLRLH-PRLHPGYYDQTLAQLPDEAS--LLEALTPFAPSADTRKRA-LIAAGFGWARHSQKVSTLSGGERSRLLFVG 427
Cdd:PLN03073  561 PSSGTVFRsAKVRMAVFSQHHVDGLDLSSnpLLYMMRCFPGVPEQKLRAhLGSFGVTGNLALQPMYTLSGGQKSRVAFAK 640
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 428 LSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARL 502
Cdd:PLN03073  641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKT 715
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
22-471 3.09e-46

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 170.68  E-value: 3.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTlkKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA-GqclmARV-----EQHLPETlhtQSLLQAVLAPLpA 95
Cdd:PRK11819   27 SLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApG----IKVgylpqEPQLDPE---KTVRENVEEGV-A 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 DAREAQR---WLAERLLAQMGFTPAVMEQQT----------------------------------ATLSGGQHTRLLLAR 138
Cdd:PRK11819   97 EVKAALDrfnEIYAAYAEPDADFDALAAEQGelqeiidaadawdldsqleiamdalrcppwdakvTKLSGGERRRVALCR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 139 ALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNssWIL---RDQTL-----HSFALPCSAA 210
Cdd:PRK11819  177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILeldRGRGIpwegnYSSWLEQKAK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 211 RQALQEQDESAalRHKAEQKEIDRVSASARrlatwgrvydnedlARKAK---------QMEKQVARLKDEQTELSVGPPW 281
Cdd:PRK11819  255 RLAQEEKQEAA--RQKALKRELEWVRQSPK--------------ARQAKskarlaryeELLSEEYQKRNETNEIFIPPGP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 282 RL---VLQGDALP---ADRLLeMDTLHVSPAPGqpslfttGVarlrsgdrVAIMGRNGGGKSSLLRLLWQQmnnASPLPG 355
Cdd:PRK11819  319 RLgdkVIEAENLSksfGDRLL-IDDLSFSLPPG-------GI--------VGIIGPNGAGKSTLFKMITGQ---EQPDSG 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 356 -LRLHPRLHPGYYDQTLAQLPDEASLLEALtpfAPSADTRK--------RALIAA-GFGWARHSQKVSTLSGGERSRllf 425
Cdd:PRK11819  380 tIKIGETVKLAYVDQSRDALDPNKTVWEEI---SGGLDIIKvgnreipsRAYVGRfNFKGGDQQKKVGVLSGGERNR--- 453
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 426 vgLSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDR 471
Cdd:PRK11819  454 --LHLAKTlkqggNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDR 502
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
319-486 1.49e-37

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: 135.65  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPglRLHPRLHPGYYDQtlaqlpdeasllealtpfapsadtrkral 398
Cdd:cd03221    22 TINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--TWGSTVKIGYFEQ----------------------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 399 iaagfgwarhsqkvstLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESC 478
Cdd:cd03221    71 ----------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVA 134

                  ....*...
gi 1439757928 479 NRFWLIDS 486
Cdd:cd03221   135 TKIIELED 142
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
5-197 6.64e-31

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 119.54  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA-------------- 70
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppewrrqvayvp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  71 --------RVEQHLPEtlhtqsllqavlaPLPADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:COG4619    81 qepalwggTVRDNLPF-------------PFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 143 QPDLLLLDEPGNHLDLPTLLWLESFLQTW----QGSFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:COG4619   148 QPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
4-181 8.77e-29

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: 114.76  E-value: 8.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MAR----V 72
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsrreLARriayV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  73 EQHLPETLHTqSLLQAVL----------APLPADAREAqrwlAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:COG1120    81 PQEPPAPFGL-TVRELVAlgryphlglfGRPSAEDREA----VEEALERTG-LEHLADRPVDELSGGERQRVLIARALAQ 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1439757928 143 QPDLLLLDEPGNHLDLP----TLLWLESFLQTWQGSFVLVSHD 181
Cdd:COG1120   155 EPPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHD 197
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
19-276 1.11e-28

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 120.66  E-value: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPEtlhtqsLLQAVLAPLPADAR 98
Cdd:PRK10636  327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLE------FLRADESPLQHLAR 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  99 EAQRWLAERL---LAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSF 175
Cdd:PRK10636  401 LAPQELEQKLrdyLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 176 VLVSHDNTLLDAVTNSSWILRDQTLHSFALPCSAARQALQEQDESAAlRHKAEQKEIDRVSASARR--------LATWGR 247
Cdd:PRK10636  481 VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQEN-QTDEAPKENNANSAQARKdqkrreaeLRTQTQ 559
                         250       260
                  ....*....|....*....|....*....
gi 1439757928 248 VYDNEdLARKAKQMEKQVARLKDEQTELS 276
Cdd:PRK10636  560 PLRKE-IARLEKEMEKLNAQLAQAEEKLG 587
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
4-188 2.58e-28

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: 112.19  E-value: 2.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVEtaFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------- 74
Cdd:COG4133     2 MLEAENLSCR--RGerLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrlay 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  75 --HLPETLHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG4133    80 lgHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1439757928 153 GNHLDLPTLLWLESFLQTW---QGSFVLVSHDNTLLDAV 188
Cdd:COG4133   159 FTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-189 3.33e-28

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 112.88  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVetAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR------V 72
Cdd:COG1121     3 MMPAIELENLTV--SYGgrPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrrigyV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  73 EQHLpetlhtqsllqAVLAPLPADARE------------------AQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRL 134
Cdd:COG1121    81 PQRA-----------EVDWDFPITVRDvvlmgrygrrglfrrpsrADREAVDEALERVGLE-DLADRPIGELSGGQQQRV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQG---SFVLVSHDntlLDAVT 189
Cdd:COG1121   149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD---LGAVR 203
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
20-152 5.35e-28

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: 109.27  E-value: 5.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP---------------ETLHTQS 84
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkeigyvfqdpqlfprLTVRENL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  85 LLQAVLAPLPADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
19-230 5.44e-28

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 118.51  E-value: 5.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----PE---------------- 78
Cdd:PRK11147  334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRaeldPEktvmdnlaegkqevmv 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 ---TLHTQSLLQAVLAPlPADAReaqrwlaerllaqmgfTPavmeqqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:PRK11147  414 ngrPRHVLGYLQDFLFH-PKRAM----------------TP------VKALSGGERNRLLLARLFLKPSNLLILDEPTND 470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 156 LDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWIL----------------RDQTLHSFALPCSAARQALQEQDE 219
Cdd:PRK11147  471 LDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFegngkigryvggyhdaRQQQAQYLALKQPAVKKKEEAAAP 550
                         250
                  ....*....|.
gi 1439757928 220 SAALRHKAEQK 230
Cdd:PRK11147  551 KAETVKRSSKK 561
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
18-197 6.75e-28

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: 111.02  E-value: 6.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------------------MARVE 73
Cdd:cd03225    15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslkelrrkvglvfqnpddqffGPTVE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  74 QHL---PETLHTQsllqavlaplPADAREAQRWLAERLLAQmgftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLD 150
Cdd:cd03225    95 EEVafgLENLGLP----------EEEIEERVEEALELVGLE-----GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1439757928 151 EPGNHLDLPTLLWLESFLQTWQG---SFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:cd03225   160 EPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
18-181 1.67e-27

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: 111.10  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-----QCLMAR-------VEQHLPETLHTQSL 85
Cdd:COG4555    15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkEPREARrqigvlpDERGLYDRLTVREN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 LQ--AVLAPLPADAREAqrwLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:COG4555    95 IRyfAELYGLFDEELKK---RIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRL 170
                         170       180
                  ....*....|....*....|.
gi 1439757928 164 LESFLQTW--QGSFVLVS-HD 181
Cdd:COG4555   171 LREILRALkkEGKTVLFSsHI 191
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
18-181 6.01e-27

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: 108.96  E-value: 6.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----------PET-LHTQSLL 86
Cdd:COG1122    15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvglvfqnPDDqLFAPTVE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAV---LAPLPADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:COG1122    95 EDVafgPENLGLPREEIRE-RVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRE 172
                         170       180
                  ....*....|....*....|.
gi 1439757928 164 LESFLQTWQG---SFVLVSHD 181
Cdd:COG1122   173 LLELLKRLNKegkTVIIVTHD 193
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
21-157 9.49e-27

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 108.61  E-value: 9.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-------CLMARV-----EQHLPETLhT--QSL- 85
Cdd:COG1131    17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaEVRRRIgyvpqEPALYPDL-TvrENLr 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928  86 LQAVLAPLPADAREAQrwlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG1131    96 FFARLYGLPRKEARER---IDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
6-181 1.11e-26

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: 106.75  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   6 TAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARveqhlpetlhtqsl 85
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 lqavlaplpaDAREAQRWLA--ERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:cd03214    67 ----------SPKELARKIAyvPQALELLGLAHLA-DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
                         170       180
                  ....*....|....*....|..
gi 1439757928 164 LESFLQTWQGSF----VLVSHD 181
Cdd:cd03214   136 LLELLRRLARERgktvVMVLHD 157
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-480 3.16e-25

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: 109.22  E-value: 3.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPT---SGSVSLAGQCL------- 68
Cdd:COG1123     1 MTPLLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelseal 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  69 -----------------MARVEQHLPETLHTQSLlqavlaplpadAREAQRWLAERLLAQMGFtPAVMEQQTATLSGGQH 131
Cdd:COG1123    81 rgrrigmvfqdpmtqlnPVTVGDQIAEALENLGL-----------SRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 132 TRLLLARALIRQPDLLLLDEPGNHLDLPT---LLWLESFLQTWQG-SFVLVSHDntlLDAVtnsswilrdqtlhsfalpc 207
Cdd:COG1123   149 QRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHD---LGVV------------------- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 208 saarqaLQEQDESAALRH--KAEQKEIDRVSASARRLATWGRVYDNEDLARKAKQMEKQVARLKDeqteLSV-----GPP 280
Cdd:COG1123   207 ------AEIADRVVVMDDgrIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRN----LSKrypvrGKG 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 281 WRLVLQGdalpadrllemdtlhVSpapgqpslFTtgvarLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHP 360
Cdd:COG1123   277 GVRAVDD---------------VS--------LT-----LRRGETLGLVGESGSGKSTLARLL------------LGLLR 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 361 ------RLH----PGYYDQTLAQL----------PD---------EASLLEALT--PFAPSADTRKRAL-------IAAG 402
Cdd:COG1123   317 ptsgsiLFDgkdlTKLSRRSLRELrrrvqmvfqdPYsslnprmtvGDIIAEPLRlhGLLSRAERRERVAellervgLPPD 396
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 403 FGWARHSQkvstLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDY---PG-GVLLVSHDRQL 473
Cdd:COG1123   397 LADRYPHE----LSGGQRQR-----VAIARAlalepKLLILDEPTSALDVSVQAQILNLLRDLqreLGlTYLFISHDLAV 467

                  ....*..
gi 1439757928 474 ISESCNR 480
Cdd:COG1123   468 VRYIADR 474
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
11-152 4.78e-25

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: 103.67  E-value: 4.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------MARVEQHl 76
Cdd:cd03219     5 GLTKRFGGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglppheiarlgIGRTFQI- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  77 PETLHTQSLLQAVLAPLPADAREAQRWL------------AERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQP 144
Cdd:cd03219    84 PRLFPELTVLENVMVAAQARTGSGLLLArarreerearerAEELLERVGLAD-LADRPAGELSYGQQRRLEIARALATDP 162

                  ....*...
gi 1439757928 145 DLLLLDEP 152
Cdd:cd03219   163 KLLLLDEP 170
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1-152 7.20e-25

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: 103.97  E-value: 7.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVetAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------- 68
Cdd:COG0411     1 SDPLLEVRGLTK--RFGGLvaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriar 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  69 --MARVEQH---LPE-----------TLHTQSLLQAVLAPLPADAREAQRWL--AERLLAQMGFTpAVMEQQTATLSGGQ 130
Cdd:COG0411    79 lgIARTFQNprlFPEltvlenvlvaaHARLGRGLLAALLRLPRARREEREARerAEELLERVGLA-DRADEPAGNLSYGQ 157
                         170       180
                  ....*....|....*....|..
gi 1439757928 131 HTRLLLARALIRQPDLLLLDEP 152
Cdd:COG0411   158 QRRLEIARALATEPKLLLLDEP 179
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
10-197 7.52e-25

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: 100.78  E-value: 7.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarveqhlpetlhtqsllqav 89
Cdd:cd00267     5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK----------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 laplpadarEAQRWLAERLLAQMGFTPavmeqQtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQ 169
Cdd:cd00267    62 ---------DIAKLPLEELRRRIGYVP-----Q---LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1439757928 170 TWQG---SFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:cd00267   125 ELAEegrTVIIVTHDPELAELAADRVIVLKD 155
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
21-181 7.99e-25

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: 102.97  E-value: 7.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLPETLH-TQSL 85
Cdd:cd03257    22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrlrkirrkeIQMVFQDPMSSLNpRMTI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 LQAVLAPL----PADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD---- 157
Cdd:cd03257   102 GEQIAEPLrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvq 181
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 158 ---LPTLLWLESFLQTwqgSFVLVSHD 181
Cdd:cd03257   182 aqiLDLLKKLQEELGL---TLLFITHD 205
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
23-203 9.02e-25

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: 102.23  E-value: 9.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--HLPETLHTQ-----SLLQAVL----- 90
Cdd:cd03235    18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVPQRRSIDrdfpiSVRDVVLmglyg 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  91 -APLPADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQ 169
Cdd:cd03235    98 hKGLFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1439757928 170 TWQG---SFVLVSHD-NTLLDAVTNSswILRDQTLHSF 203
Cdd:cd03235   177 ELRRegmTILVVTHDlGLVLEYFDRV--LLLNRTVVAS 212
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
21-197 9.27e-25

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: 100.94  E-value: 9.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarveqhlpetlhtqsllqavlaPLPADAREA 100
Cdd:cd03230    17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK-------------------------DIKKEPEEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 101 QRWLAerLLAQmgfTPAVMEQQTA----TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTW---QG 173
Cdd:cd03230    72 KRRIG--YLPE---EPSLYENLTVrenlKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGK 146
                         170       180
                  ....*....|....*....|....
gi 1439757928 174 SFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:cd03230   147 TILLSSHILEEAERLCDRVAILNN 170
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
24-181 2.18e-24

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: 101.22  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLK-----KGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-ARVEQHLPETLHTQSLL--QAVLAP--- 92
Cdd:cd03297    12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdSRKKINLPPQQRKIGLVfqQYALFPhln 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  93 --------LPADAREAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03297    92 vrenlafgLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
                         170       180
                  ....*....|....*....|.
gi 1439757928 165 ESFLQTWQGSF----VLVSHD 181
Cdd:cd03297   171 LPELKQIKKNLnipvIFVTHD 191
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
4-181 2.25e-24

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: 102.19  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVetAFG------PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR------ 71
Cdd:COG1124     1 MLEVRNLSV--SYGqggrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRrrkafr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  72 -----VEQHLPETLH-TQSLLQAVLAPLPA---DAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:COG1124    79 rrvqmVFQDPYASLHpRHTVDRILAEPLRIhglPDREER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALIL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1439757928 143 QPDLLLLDEPGNHLDLPT----LLWLESFLQTWQGSFVLVSHD 181
Cdd:COG1124   156 EPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHD 198
PLN03073 PLN03073
ABC transporter F family; Provisional
17-203 8.88e-24

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 105.71  E-value: 8.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  17 GP-LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSllqavlAPLPA 95
Cdd:PLN03073  521 GPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSS------NPLLY 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 DAREAQRWLAERL---LAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQ 172
Cdd:PLN03073  595 MMRCFPGVPEQKLrahLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1439757928 173 GSFVLVSHDNTLLDAVTNSSWILRDQTLHSF 203
Cdd:PLN03073  675 GGVLMVSHDEHLISGSVDELWVVSEGKVTPF 705
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
18-180 1.46e-23

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: 99.77  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSG-SVSLAGQCL----MARVEQHL----PETLH----TQS 84
Cdd:COG1119    17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRggedVWELRKRIglvsPALQLrfprDET 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAVL------APLPADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:COG1119    97 VLDVVLsgffdsIGLYREPTDEQRERARELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 159 PTLLWLESFLQTW--QG--SFVLVSH 180
Cdd:COG1119   176 GARELLLALLDKLaaEGapTLVLVTH 201
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
19-197 6.56e-23

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: 96.94  E-value: 6.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR--------VEQHLPETLHTQSLLQAVL 90
Cdd:cd03226    15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerrksigyVMQDVDYQLFTDSVREELL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  91 APLPADAREAQRwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL-ESFLQ 169
Cdd:cd03226    95 LGLKELDAGNEQ--AETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVgELIRE 171
                         170       180       190
                  ....*....|....*....|....*....|
gi 1439757928 170 -TWQGSFVLV-SHDNTLLDAVTNSSWILRD 197
Cdd:cd03226   172 lAAQGKAVIViTHDYEFLAKVCDRVLLLAN 201
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
23-181 1.28e-22

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: 96.39  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPET-LHTQ--------SLLQAVLAPL 93
Cdd:cd03293    23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE----PVTGPGPDRgYVFQqdallpwlTVLDNVALGL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  94 ---PADAREAQRwLAERLLAQMGFTPAvmEQQT-ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL-ESFL 168
Cdd:cd03293    99 elqGVPKAEARE-RAEELLELVGLSGF--ENAYpHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELL 175
                         170
                  ....*....|....*.
gi 1439757928 169 QTWQG---SFVLVSHD 181
Cdd:cd03293   176 DIWREtgkTVLLVTHD 191
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
24-184 2.42e-22

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: 95.63  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA---------RVEQ--------HLpetLHTQSLL 86
Cdd:cd03255    24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelaafRRRHigfvfqsfNL---LPDLTAL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAVLAPL---PADAREAQRWlAERLLAQMGFtPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP-GNhLDLPT-- 160
Cdd:cd03255   101 ENVELPLllaGVPKKERRER-AEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPtGN-LDSETgk 177
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 161 --LLWLESFLQTWQGSFVLVSHDNTL 184
Cdd:cd03255   178 evMELLRELNKEAGTTIVVVTHDPEL 203
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
24-181 2.89e-22

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: 96.75  E-value: 2.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL-------------PEtlhtQSLLQA-V 89
Cdd:TIGR04521  25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrkkvglvfqfPE----HQLFEEtV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 L-----AP--LPADAREAQRwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlP--- 159
Cdd:TIGR04521 101 YkdiafGPknLGLSEEEAEE-RVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD-Pkgr 178
                         170       180
                  ....*....|....*....|....
gi 1439757928 160 -TLLWLESFLQTWQG-SFVLVSHD 181
Cdd:TIGR04521 179 kEILDLFKRLHKEKGlTVILVTHS 202
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
11-181 3.05e-22

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: 94.89  E-value: 3.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR---------VEQHlPET 79
Cdd:cd03259     5 GLSKTYGsvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVpperrnigmVFQD-YAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 LHTQSLLQAVLAPL-----PADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03259    84 FPHLTVAENIAFGLklrgvPKAEIRAR---VRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1439757928 155 HLDLPTLLWLESFLQTWQGSF----VLVSHD 181
Cdd:cd03259   160 ALDAKLREELREELKELQRELgittIYVTHD 190
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
18-181 6.07e-22

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 95.54  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPET---------LHTQSLLQA 88
Cdd:COG1116    25 TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK----PVTGPGPDRgvvfqepalLPWLTVLDN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 VLAPLPA---DAREAQRWlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT--LLW 163
Cdd:COG1116   101 VALGLELrgvPKAERRER-ARELLELVGLAGF-EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTreRLQ 178
                         170       180
                  ....*....|....*....|.
gi 1439757928 164 LEsFLQTWQG---SFVLVSHD 181
Cdd:COG1116   179 DE-LLRLWQEtgkTVLFVTHD 198
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
18-157 6.19e-22

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: 92.83  E-value: 6.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarveqhlpetlhtqsllqavlaplpaDA 97
Cdd:cd03228    16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV-----------------------------DL 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  98 RE-AQRWLAERLlaqmgftpAVMEQQT----AT-----LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03228    67 RDlDLESLRKNI--------AYVPQDPflfsGTireniLSGGQRQRIAIARALLRDPPILILDEATSALD 128
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-186 6.91e-22

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 94.34  E-value: 6.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVEtaFG------PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------ 68
Cdd:COG1136     1 MSPLLELRNLTKS--YGtgegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslser 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  69 -MAR--------VEQ--HLPETLhtqSLLQAVLAPL---PADAREAQRWlAERLLAQMGFTpAVMEQQTATLSGGQHTRL 134
Cdd:COG1136    79 eLARlrrrhigfVFQffNLLPEL---TALENVALPLllaGVSRKERRER-ARELLERVGLG-DRLDHRPSQLSGGQQQRV 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 135 LLARALIRQPDLLLLDEP-GNhLDLPT------LlwLESFLQTWQGSFVLVSHDNTLLD 186
Cdd:COG1136   154 AIARALVNRPKLILADEPtGN-LDSKTgeevleL--LRELNRELGTTIVMVTHDPELAA 209
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
18-188 1.11e-21

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: 98.68  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE--TLHTQ-------SLLQA 88
Cdd:COG4987   349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRriAVVPQrphlfdtTLREN 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 VL--APlpaDAREAQRWLAerlLAQMGFTPAVMEQQT----------ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:COG4987   429 LRlaRP---DATDEELWAA---LERVGLGDWLAALPDgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGL 502
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1439757928 157 DLPT-LLWLESFLQTWQG-SFVLVSHDNTLLDAV 188
Cdd:COG4987   503 DAATeQALLADLLEALAGrTVLLITHRLAGLERM 536
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
23-181 1.46e-21

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: 93.94  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE----------------TLHTQSLL 86
Cdd:cd03267    40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRigvvfgqktqlwwdlpVIDSFYLL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAVLAPLPADAREAQRWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES 166
Cdd:cd03267   120 AAIYDLPPARFKKRLDELSELL--DLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
                         170
                  ....*....|....*....
gi 1439757928 167 FLQTW----QGSFVLVSHD 181
Cdd:cd03267   195 FLKEYnrerGTTVLLTSHY 213
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
18-181 1.53e-21

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 92.30  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH--LPETLHTqSLLQAV------ 89
Cdd:NF040873    6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRseVPDSLPL-TVRDLVamgrwa 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 ----LAPLPADAREAqrwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:NF040873   85 rrglWRRLTRDDRAA----VDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
                         170
                  ....*....|....*....
gi 1439757928 166 SFLQTWQG---SFVLVSHD 181
Cdd:NF040873  160 ALLAEEHArgaTVVVVTHD 178
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
2-186 2.44e-21

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: 92.88  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   2 STLLTAHALH--VETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MA 70
Cdd:COG4181     6 APIIELRGLTktVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedaRA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  71 RV-----------EQHLPetlhTQSLLQAVLAPLP-ADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLAR 138
Cdd:COG4181    86 RLrarhvgfvfqsFQLLP----TLTALENVMLPLElAGRRDARA-RARALLERVGLG-HRLDHYPAQLSGGEQQRVALAR 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 139 ALIRQPDLLLLDEP-GNhLDLPT------LLwlesF-LQTWQGS-FVLVSHDNTLLD 186
Cdd:COG4181   160 AFATEPAILFADEPtGN-LDAATgeqiidLL----FeLNRERGTtLVLVTHDPALAA 211
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
23-181 3.02e-21

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: 92.53  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR------VEQH---LPETLHTQSLLQAVLAPL 93
Cdd:TIGR01184   4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdrmvVFQNyslLPWLTVRENIALAVDRVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  94 PADAREAQRWLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL-ESFLQTWQ 172
Cdd:TIGR01184  84 PDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqEELMQIWE 162
                         170
                  ....*....|..
gi 1439757928 173 GS---FVLVSHD 181
Cdd:TIGR01184 163 EHrvtVLMVTHD 174
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
21-181 4.16e-21

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: 90.71  E-value: 4.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLLQ-AVLAPlpadare 99
Cdd:cd03229    17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGMVFQdFALFP------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 aqrwlaerllaqmgfTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSF---- 175
Cdd:cd03229    90 ---------------HLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgitv 154

                  ....*.
gi 1439757928 176 VLVSHD 181
Cdd:cd03229   155 VLVTHD 160
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
18-188 6.13e-21

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 89.97  E-value: 6.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmARVEQHLPETL--HTQSLLQAVLAplpa 95
Cdd:cd03246    16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDPNELgdHVGYLPQDDEL---- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 dareaqrwlaerllaqmgFTPAVMEqqtATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQ--- 172
Cdd:cd03246    88 ------------------FSGSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaag 146
                         170
                  ....*....|....*.
gi 1439757928 173 GSFVLVSHDNTLLDAV 188
Cdd:cd03246   147 ATRIVIAHRPETLASA 162
F420-0_ABC_ATP TIGR03873
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ...
18-184 7.96e-21

proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.


Pssm-ID: 163585 [Multi-domain]  Cd Length: 256  Bit Score: 92.18  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMARVEQHLPETLHTQSLL 86
Cdd:TIGR03873  15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrraraRRVALVEQDSDTAVPLTVRD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAVLAPLP-----ADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL 161
Cdd:TIGR03873  95 VVALGRIPhrslwAGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQ 173
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 162 LWLESFLQTWQGSFVLVS---HDNTL 184
Cdd:TIGR03873 174 LETLALVRELAATGVTVVaalHDLNL 199
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
21-152 1.63e-20

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 90.89  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQH--LPE------ 78
Cdd:COG3638    20 DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgralrrlrrrIGMIFQQfnLVPrlsvlt 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  79 -----TLHTQSLLQAVLAPLPADAREaqrwLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG3638   100 nvlagRLGRTSTWRSLLGLFPPEDRE----RALEALERVGLADK-AYQRADQLSGGQQQRVAIARALVQEPKLILADEP 173
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
22-189 4.62e-20

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: 88.80  E-value: 4.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG----QCLMARVEQHLPETLHTQSLLQA------VLA 91
Cdd:cd03245    22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirQLDPADLRRNIGYVPQDVTLFYGtlrdniTLG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  92 PLPADAREAQRwlAERLLAQMGFT---PAVMEQQT----ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03245   102 APLADDERILR--AAELAGVTDFVnkhPNGLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL 179
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 165 ESFLQTWQG--SFVLVSHDNTLLDAVT 189
Cdd:cd03245   180 KERLRQLLGdkTLIIITHRPSLLDLVD 206
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
11-188 5.92e-20

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: 93.46  E-value: 5.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLLQA 88
Cdd:TIGR03719 327 NLTKAFGdkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEE 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 V---LAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:TIGR03719 407 IsggLDIIKLGKREIP---SRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALE 483
                         170       180
                  ....*....|....*....|...
gi 1439757928 166 SFLQTWQGSFVLVSHDNTLLDAV 188
Cdd:TIGR03719 484 EALLNFAGCAVVISHDRWFLDRI 506
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
17-218 1.88e-19

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: 91.74  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  17 GPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHlpETLHTQSL 85
Cdd:COG4988   350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsdldpaswrrqIAWVPQN--PYLFAGTI 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 LQAVLAPLPaDAREAQRWLAERLLAQMGFTPAvMEQQTAT--------LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4988   428 RENLRLGRP-DASDEELEAALEAAGLDEFVAA-LPDGLDTplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 158 LPT-LLWLESFLQTWQGSFVL-VSHDntlLDAVTNSSWILRdqtLHSFALPCSAARQALQEQD 218
Cdd:COG4988   506 AETeAEILQALRRLAKGRTVIlITHR---LALLAQADRILV---LDDGRIVEQGTHEELLAKN 562
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
18-181 3.03e-19

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 87.94  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLPETLHTQ 83
Cdd:TIGR02769  25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldrkqrrafrrdVQLVFQDSPSAVNPR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 SLLQAVLA-PL----PADAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:TIGR02769 105 MTVRQIIGePLrhltSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 159 ----PTLLWLESFLQTWQGSFVLVSHD 181
Cdd:TIGR02769 184 vlqaVILELLRKLQQAFGTAYLFITHD 210
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
18-157 3.48e-19

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: 91.43  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQ-------------S 84
Cdd:COG2274   489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQIDPASLRRQigvvlqdvflfsgT 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQ--AVLAPLPADAReaqrwlAERLLAQMGFTPAVMEQ----QT------ATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG2274   565 IREniTLGDPDATDEE------IIEAARLAGLHDFIEALpmgyDTvvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638

                  ....*
gi 1439757928 153 GNHLD 157
Cdd:COG2274   639 TSALD 643
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
320-485 4.17e-19

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: 84.22  E-value: 4.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhpgyydqTLAQLPDEASLLEALTPFAPSADTRKRALI 399
Cdd:cd00267    22 LKAGEIVALVGPNGSGKSTLLRAI--------------------------AGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 400 AAgfgwarhsqkVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLLVSHDRQLISE 476
Cdd:cd00267    76 GY----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgrtVIIVTHDPELAEL 145

                  ....*....
gi 1439757928 477 SCNRFWLID 485
Cdd:cd00267   146 AADRVIVLK 154
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
11-181 6.19e-19

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 88.28  E-value: 6.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVE----------QH--- 75
Cdd:COG1118     7 NISKRFGsfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprerrvgfvfQHyal 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  76 -------------LPetlhtqsllqaVLAPLPADARE-AQRWL--------AERLLAQmgftpavmeqqtatLSGGQHTR 133
Cdd:COG1118    87 fphmtvaeniafgLR-----------VRPPSKAEIRArVEELLelvqleglADRYPSQ--------------LSGGQRQR 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 134 LLLARALIRQPDLLLLDEPGNHLD--LPTLL--WLESFLQTWQGSFVLVSHD 181
Cdd:COG1118   142 VALARALAVEPEVLLLDEPFGALDakVRKELrrWLRRLHDELGGTTVFVTHD 193
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
11-157 9.77e-19

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: 84.89  E-value: 9.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------------MARVEQH 75
Cdd:cd03262     5 NLHKSFGDFhvLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkkninelrqkVGMVFQQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  76 LPETLHTQSLLQAVLAPLPA---DAREAQRwLAERLLAQMGFTpavmEQQT---ATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:cd03262    85 FNLFPHLTVLENITLAPIKVkgmSKAEAEE-RALELLEKVGLA----DKADaypAQLSGGQQQRVAIARALAMNPKVMLF 159

                  ....*...
gi 1439757928 150 DEPGNHLD 157
Cdd:cd03262   160 DEPTSALD 167
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
18-181 1.04e-18

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 84.84  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAGQCLmarveQHLP-ETLHTQSLLQ-AVLAP 92
Cdd:COG4136    15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-----TALPaEQRRIGILFQdDLLFP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  93 -----------LPAD-AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:COG4136    90 hlsvgenlafaLPPTiGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
                         170       180
                  ....*....|....*....|....*
gi 1439757928 161 LLWLESF----LQTWQGSFVLVSHD 181
Cdd:COG4136   169 RAQFREFvfeqIRQRGIPALLVTHD 193
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
21-181 1.09e-18

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: 84.86  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---MARVEQH---------LPETLHTQSLLQ- 87
Cdd:cd03263    19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdRKAARQSlgycpqfdaLFDELTVREHLRf 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 -AVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPT---LLW 163
Cdd:cd03263    99 yARLKGLPKSEIKEE---VELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PAsrrAIW 173
                         170       180
                  ....*....|....*....|
gi 1439757928 164 leSFLQTWQG--SFVLVSHD 181
Cdd:cd03263   174 --DLILEVRKgrSIILTTHS 191
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
21-157 1.32e-18

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: 85.31  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLPET------- 79
Cdd:cd03256    18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlrrqIGMIFQQFNLIerlsvle 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 ------LHTQSLLQAVLAPLPadarEAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:cd03256    98 nvlsgrLGRRSTWRSLFGLFP----KEEKQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172

                  ....
gi 1439757928 154 NHLD 157
Cdd:cd03256   173 ASLD 176
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
21-181 2.84e-18

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 86.31  E-value: 2.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARV--EQ--------------HLpetlhtqS 84
Cdd:COG3842    22 DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-DVTGLppEKrnvgmvfqdyalfpHL-------T 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAVLAPL-----PADAREAQrwlAERLLAQMGftpavMEQQ----TATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:COG3842    94 VAENVAFGLrmrgvPKAEIRAR---VAELLELVG-----LEGLadryPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
                         170       180       190
                  ....*....|....*....|....*....|
gi 1439757928 156 LDLP----TLLWLESFLQTWQGSFVLVSHD 181
Cdd:COG3842   166 LDAKlreeMREELRRLQRELGITFIYVTHD 195
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
8-157 4.28e-18

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: 83.10  E-value: 4.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   8 HALHVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH---LPE---- 78
Cdd:cd03269     2 EVENVTKRFGRvtALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLPEergl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 ----TLHTQSLLQAVLAPLPadAREAQRWlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03269    82 ypkmKVIDQLVYLAQLKGLK--KEEARRR-IDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157

                  ...
gi 1439757928 155 HLD 157
Cdd:cd03269   158 GLD 160
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
18-181 5.91e-18

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: 87.03  E-value: 5.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-------QCLMARVEQHLPETLH--TQSLLQA 88
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldQDEVRRRVSVCAQDAHlfDTTVREN 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 VLAPLPaDAREAQRW-------LAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT- 160
Cdd:TIGR02868 429 LRLARP-DATDEELWaalervgLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETa 507
                         170       180
                  ....*....|....*....|..
gi 1439757928 161 LLWLESFLQTWQG-SFVLVSHD 181
Cdd:TIGR02868 508 DELLEDLLAALSGrTVVLITHH 529
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
23-181 6.39e-18

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 83.76  E-value: 6.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM------ARVEQH---LPetlhTQSLLQAV---- 89
Cdd:COG4525    26 VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgadrGVVFQKdalLP----WLNVLDNVafgl 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 -LAPLPADAREAQrwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT------LL 162
Cdd:COG4525   102 rLRGVPKAERRAR---AEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTreqmqeLL 177
                         170       180
                  ....*....|....*....|..
gi 1439757928 163 wlesfLQTWQGS---FVLVSHD 181
Cdd:COG4525   178 -----LDVWQRTgkgVFLITHS 194
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
21-189 7.36e-18

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 87.23  E-value: 7.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG----QCLMARVEQH---LPE--TLHTQSLLQ--AV 89
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdirQIDPADLRRNigyVPQdpRLFYGTLRDniAL 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 LAPLPADA---REAQRWLAERLLAQ--MGFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:TIGR03375 562 GAPYADDEeilRAAELAGVTEFVRRhpDGLDMQIGER-GRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERF 640
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 165 ESFLQTWQG--SFVLVSHDNTLLDAVT 189
Cdd:TIGR03375 641 KDRLKRWLAgkTLVLVTHRTSLLDLVD 667
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
17-181 7.95e-18

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: 86.57  E-value: 7.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  17 GPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE---------TLHTQSLLQ 87
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDqiawvpqhpFLFAGTIAE 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 AV-LAPLPADAREAQRwlAERLLAQMGFTPA-------VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP 159
Cdd:TIGR02857 415 NIrLARPDASDAEIRE--ALERAGLDEFVAAlpqgldtPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
                         170       180
                  ....*....|....*....|....
gi 1439757928 160 T-LLWLESFLQTWQG-SFVLVSHD 181
Cdd:TIGR02857 493 TeAEVLEALRALAQGrTVLLVTHR 516
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
18-157 8.92e-18

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: 82.63  E-value: 8.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLpETLHTQ 83
Cdd:cd03258    19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgkelrkarrrIGMIFQHF-NLLSSR 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  84 SLLQAVLAPL-----PADAREAQrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03258    98 TVFENVALPLeiagvPKAEIEER---VLELLELVGLEDKA-DAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
4-158 1.54e-17

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 82.47  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQHL 76
Cdd:COG4559     1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspweLARRRAVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  77 PEtlHTQ-----SLLQAV---LAPLPADAREAQRwLAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARAL--IRQPD- 145
Cdd:COG4559    81 PQ--HSSlafpfTVEEVValgRAPHGSSAAQDRQ-IVREALALVG-LAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVd 156
                         170
                  ....*....|....*..
gi 1439757928 146 ----LLLLDEPGNHLDL 158
Cdd:COG4559   157 ggprWLFLDEPTSALDL 173
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
21-179 1.89e-17

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: 81.11  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPETL-HTQSLLQAvlaplPA---- 95
Cdd:cd03268    17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEALrRIGALIEA-----PGfypn 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 -DAREAQRWLA----------ERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03268    87 lTARENLRLLArllgirkkriDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
                         170
                  ....*....|....*..
gi 1439757928 165 ESFLQTW--QGSFVLVS 179
Cdd:cd03268   166 RELILSLrdQGITVLIS 182
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
11-186 1.97e-17

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 85.56  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHlPETLH-TQSLLQ 87
Cdd:PRK11819  329 NLSKSFGDrlLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-RDALDpNKTVWE 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 AVlaplpADARE----AQRWLAER-LLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLL 162
Cdd:PRK11819  408 EI-----SGGLDiikvGNREIPSRaYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
                         170       180
                  ....*....|....*....|....
gi 1439757928 163 WLESFLQTWQGSFVLVSHDNTLLD 186
Cdd:PRK11819  483 ALEEALLEFPGCAVVISHDRWFLD 506
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
11-181 2.38e-17

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: 81.58  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG---PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETL------- 80
Cdd:cd03295     5 NVTKRYGggkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIgyviqqi 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  81 ----HTQSLLQAVLAP-LPADAREAQRWLAERLLAQMGFTPA-VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03295    85 glfpHMTVEENIALVPkLLKWPKEKIRERADELLALVGLDPAeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1439757928 155 HLDLPTLLWL-ESFL---QTWQGSFVLVSHD 181
Cdd:cd03295   165 ALDPITRDQLqEEFKrlqQELGKTIVFVTHD 195
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
319-489 2.44e-17

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 80.63  E-value: 2.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL------------WQQMN-NASPLPGLR-----LHPRlhPGYYDQTLAQ-LPDEAS 379
Cdd:COG4619    22 TLEAGECVAITGPSGSGKSTLLRALadldpptsgeiyLDGKPlSAMPPPEWRrqvayVPQE--PALWGGTVRDnLPFPFQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 380 LLEAltpfAPSADTRKRALIAAGFGWARHSQKVSTLSGGERSRLLFV-GLSLARySLLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:COG4619   100 LRER----KFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIrALLLQP-DVLLLDEPTSALDPENTRRVEELLR 174
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1439757928 459 DYP----GGVLLVSHDRQLISESCNRFWLIDSAGL 489
Cdd:COG4619   175 EYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
cbiO PRK13643
energy-coupling factor transporter ATPase;
19-218 3.39e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 82.09  E-value: 3.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--------------HLPET-LHTQ 83
Cdd:PRK13643   22 LFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpvrkkvgvvfQFPESqLFEE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 SLLQAV-LAP--LPADAREAQRWLAERlLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--- 157
Cdd:PRK13643  101 TVLKDVaFGPqnFGIPKEKAEKIAAEK-LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpka 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 158 -LPTLLWLESFLQTWQgSFVLVSHdntLLDAVTN-SSWILRDQTLHsfALPCSAARQALQEQD 218
Cdd:PRK13643  180 rIEMMQLFESIHQSGQ-TVVLVTH---LMDDVADyADYVYLLEKGH--IISCGTPSDVFQEVD 236
cbiO PRK13641
energy-coupling factor transporter ATPase;
23-181 3.87e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 82.18  E-value: 3.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--------------HLPET-LHTQSLLQ 87
Cdd:PRK13641   26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkklrkkvslvfQFPEAqLFENTVLK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 AV-LAPLPADAREAQ-RWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:PRK13641  106 DVeFGPKNFGFSEDEaKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
                         170
                  ....*....|....*....
gi 1439757928 166 SFLQTWQG---SFVLVSHD 181
Cdd:PRK13641  186 QLFKDYQKaghTVILVTHN 204
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
21-180 4.09e-17

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: 79.01  E-value: 4.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlhtqsllQAVLAPLPADAREA 100
Cdd:cd03216    17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------------KEVSFASPRDARRA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 101 qrwlaerllaqmgftPAVMEQQtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQ--TWQG-SFVL 177
Cdd:cd03216    76 ---------------GIAMVYQ---LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRrlRAQGvAVIF 137

                  ...
gi 1439757928 178 VSH 180
Cdd:cd03216   138 ISH 140
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
23-185 4.38e-17

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: 80.27  E-value: 4.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQC-----LMARVEQHLP--ETLHtqsLLQAVLAPLPA 95
Cdd:cd03220    41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssllgLGGGFNPELTgrENIY---LNGRLLGLSRK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 DAREAQRWLAErlLAQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEpgnhldlptllWL----ESF---- 167
Cdd:cd03220   118 EIDEKIDEIIE--FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE-----------VLavgdAAFqekc 181
                         170       180
                  ....*....|....*....|....
gi 1439757928 168 ---LQTWQ---GSFVLVSHDNTLL 185
Cdd:cd03220   182 qrrLRELLkqgKTVILVSHDPSSI 205
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
2-181 5.49e-17

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 81.27  E-value: 5.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   2 STLLTAHALHVETAFGPLF---------NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA-- 70
Cdd:PRK10419    1 MTLLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKln 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  71 ------------RVEQHLPETLHTQSLLQAVLAP----LPADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRL 134
Cdd:PRK10419   81 raqrkafrrdiqMVFQDSISAVNPRKTVREIIREplrhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLDL----PTLLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK10419  161 CLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHD 211
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
24-157 5.53e-17

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: 80.81  E-value: 5.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQH---------LPETL 80
Cdd:TIGR02315  22 NLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkklrklrrrIGMIFQHynlierltvLENVL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  81 H----TQSLLQAVLAPLPadarEAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:TIGR02315 102 HgrlgYKPTWRSLLGRFS----EEDKERALSALERVGLA-DKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASL 176

                  .
gi 1439757928 157 D 157
Cdd:TIGR02315 177 D 177
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
2-152 5.81e-17

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: 80.41  E-value: 5.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   2 STLLTAHALHVetAFGP---LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MAR 71
Cdd:COG0410     1 MPMLEVENLHA--GYGGihvLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpphrIAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  72 -----------------VEQHLpetlhtqsllqaVLAPLPADAREAQRWLAERL------LAQMgftpavMEQQTATLSG 128
Cdd:COG0410    78 lgigyvpegrrifpsltVEENL------------LLGAYARRDRAEVRADLERVyelfprLKER------RRQRAGTLSG 139
                         170       180
                  ....*....|....*....|....
gi 1439757928 129 GQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG0410   140 GEQQMLAIGRALMSRPKLLLLDEP 163
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
18-187 6.62e-17

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 79.71  E-value: 6.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPET-------------LHTQS 84
Cdd:COG2884    16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrigvvfqdfrlLPDRT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAVLAPL---PADAREAQRWLAErLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL 161
Cdd:COG2884    96 VYENVALPLrvtGKSRKEIRRRVRE-VLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLD-PET 172
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1439757928 162 LW-----LESFLQTwqGSFVLV-SHDNTLLDA 187
Cdd:COG2884   173 SWeimelLEEINRR--GTTVLIaTHDLELVDR 202
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
23-152 8.61e-17

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: 79.40  E-value: 8.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-----ARVEQ---HLPET---LHTQSLLQAVLA 91
Cdd:cd03224    19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpphERARAgigYVPEGrriFPELTVEENLLL 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928  92 PLPADAREAQRWLAERLLAQmgFtPAVME---QQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:cd03224    99 GAYARRRAKRKARLERVYEL--F-PRLKErrkQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
3-181 9.43e-17

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 80.06  E-value: 9.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   3 TLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARV--- 72
Cdd:PRK11231    1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssrqLARRlal 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  73 --EQHL-PETLHTQSLLQAVLAP-LPADAREAQ--RWLAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARALIRQPDL 146
Cdd:PRK11231   81 lpQHHLtPEGITVRELVAYGRSPwLSLWGRLSAedNARVNQAMEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1439757928 147 LLLDEPGNHLDLP---TLLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK11231  160 VLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD 197
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-234 1.70e-16

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 79.39  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--HLPE 78
Cdd:PRK09544    1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 TLHTQSLLQAVLAP-------LPAdareAQRWLAERLLaqmgftpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK09544   81 TLPLTVNRFLRLRPgtkkediLPA----LKRVQAGHLI----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 152 PGNHLDLPTLLWLESF---LQTWQGSFVL-VSHDNTLLDAVTNSSWILRDQtlhsfaLPCSAARQALQEQDESAAL--RH 225
Cdd:PRK09544  147 PTQGVDVNGQVALYDLidqLRRELDCAVLmVSHDLHLVMAKTDEVLCLNHH------ICCSGTPEVVSLHPEFISMfgPR 220

                  ....*....
gi 1439757928 226 KAEQKEIDR 234
Cdd:PRK09544  221 GAEQLGIYR 229
cbiO PRK13649
energy-coupling factor transporter ATPase;
19-190 1.75e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 79.79  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA--------RVEQHL------PET-LHTQ 83
Cdd:PRK13649   23 LFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdikQIRKKVglvfqfPESqLFEE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 SLLQAV-LAP--LPADAREAQRwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--- 157
Cdd:PRK13649  102 TVLKDVaFGPqnFGVSQEEAEA-LAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDpkg 180
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1439757928 158 ---LPTLlwlesFLQTWQG--SFVLVSHdntLLDAVTN 190
Cdd:PRK13649  181 rkeLMTL-----FKKLHQSgmTIVLVTH---LMDDVAN 210
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
23-181 1.76e-16

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 78.97  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmaRVeqhlpetlhtQSLLqAVLAPLPAD--ARE- 99
Cdd:COG1134    45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----RV----------SALL-ELGAGFHPEltGREn 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 AqrwlaeRLLAQ-MGFTPAVMEQQTA-----------------TLSGGQHTRLLLARALIRQPDLLLLDEpgnhldlptl 161
Cdd:COG1134   109 I------YLNGRlLGLSRKEIDEKFDeivefaelgdfidqpvkTYSSGMRARLAFAVATAVDPDILLVDE---------- 172
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1439757928 162 lWL---------------ESFLQTwQGSFVLVSHD 181
Cdd:COG1134   173 -VLavgdaafqkkclariRELRES-GRTVIFVSHS 205
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
18-157 3.11e-16

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: 78.24  E-value: 3.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGS---------VSLAG----QCLMAR------VEQHLpE 78
Cdd:COG4778    25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQasprEILALRrrtigyVSQFL-R 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 TLHTQSLLQAVLAPLPAD--AREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:COG4778   104 VIPRVSALDVVAEPLLERgvDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASL 183

                  .
gi 1439757928 157 D 157
Cdd:COG4778   184 D 184
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
24-181 3.86e-16

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 77.87  E-value: 3.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-CLMARVEQ--------------HLpetlhtqSLLQA 88
Cdd:COG3840    19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdLTALPPAErpvsmlfqennlfpHL-------TVAQN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 VLAPLPADAR--EAQRWLAERLLAQMGFTPavMEQQT-ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL---- 161
Cdd:COG3840    92 IGLGLRPGLKltAEQRAQVEQALERVGLAG--LLDRLpGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-PALrqem 168
                         170       180
                  ....*....|....*....|.
gi 1439757928 162 LWLESFLQTWQGSFVL-VSHD 181
Cdd:COG3840   169 LDLVDELCRERGLTVLmVTHD 189
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
11-181 4.36e-16

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: 77.93  E-value: 4.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--MARVEQhlpETLHTQ--- 83
Cdd:cd03261     5 GLTKSFGgrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsgLSEAEL---YRLRRRmgm 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 -----------SLLQAVLAPLPADAREAQRWLAERL---LAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:cd03261    82 lfqsgalfdslTVFENVAFPLREHTRLSEEEIREIVlekLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLY 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1439757928 150 DEPGNHLDLPTLLWLESFLQTWQGSF----VLVSHD 181
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHD 196
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
11-152 5.12e-16

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: 77.71  E-value: 5.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPEtLHTQ----- 83
Cdd:COG1127    10 NLTKSFGdrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE-LRRRigmlf 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 ---------SLLQAVLAPL-------PADAREaqrwLAERLLAQMGFtPAVMEQQTATLSGGQHTRLLLARALIRQPDLL 147
Cdd:COG1127    89 qggalfdslTVFENVAFPLrehtdlsEAEIRE----LVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEIL 163

                  ....*
gi 1439757928 148 LLDEP 152
Cdd:COG1127   164 LYDEP 168
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
11-152 5.18e-16

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 77.73  E-value: 5.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-------------VEQ- 74
Cdd:COG1126     6 NLHKSFGDLevLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkdinklrrkvgmVFQq 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  75 -----HLpetlhtqSLLQAV-LAPL------PADAREaqrwLAERLLAQMGftpavMEQQT----ATLSGGQHTRLLLAR 138
Cdd:COG1126    86 fnlfpHL-------TVLENVtLAPIkvkkmsKAEAEE----RAMELLERVG-----LADKAdaypAQLSGGQQQRVAIAR 149
                         170
                  ....*....|....
gi 1439757928 139 ALIRQPDLLLLDEP 152
Cdd:COG1126   150 ALAMEPKVMLFDEP 163
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
4-157 6.93e-16

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 76.38  E-value: 6.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETL--- 80
Cdd:PRK13538    1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  81 H---TQSLLQAV-----LAPLPADAREAQRWLAerlLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK13538   81 HqpgIKTELTALenlrfYQRLHGPGDDEALWEA---LAQVGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156

                  ....*
gi 1439757928 153 GNHLD 157
Cdd:PRK13538  157 FTAID 161
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
5-158 8.43e-16

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 79.50  E-value: 8.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR----VEQHLPETL 80
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraASRRVASVP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  81 HTQSLL------QAV-LAPLPADAR-----EAQRWLAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK09536   84 QDTSLSfefdvrQVVeMGRTPHRSRfdtwtETDRAAVERAMERTG-VAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
                         170
                  ....*....|
gi 1439757928 149 LDEPGNHLDL 158
Cdd:PRK09536  163 LDEPTASLDI 172
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
23-157 1.00e-15

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: 76.45  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL-----APTSGSVSLAGQCLMARveQHLPETLHTQ-------------S 84
Cdd:cd03260    19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDL--DVDVLELRRRvgmvfqkpnpfpgS 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928  85 LLQAVLAPLPA---DAREAQRWLAERLLAQMGFTPAVMEQQTAT-LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03260    97 IYDNVAYGLRLhgiKLKEELDERVEEALRKAALWDEVKDRLHALgLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
5-157 1.02e-15

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: 75.86  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmARVEQHLPETLH--- 81
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILylg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  82 TQSLLQAVLAPLP------ADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:TIGR01189  80 HLPGLKPELSALEnlhfwaAIHGGAQR-TIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157

                  ..
gi 1439757928 156 LD 157
Cdd:TIGR01189 158 LD 159
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
3-158 1.11e-15

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 77.12  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   3 TLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQH 75
Cdd:PRK13548    1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwspaeLARRRAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  76 LPEtlhtQSLL------QAV----LAPLPADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIR--- 142
Cdd:PRK13548   81 LPQ----HSSLsfpftvEEVvamgRAPHGLSRAEDDA-LVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAQlwe 154
                         170
                  ....*....|....*....
gi 1439757928 143 ---QPDLLLLDEPGNHLDL 158
Cdd:PRK13548  155 pdgPPRWLLLDEPTSALDL 173
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
20-157 1.47e-15

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: 75.69  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  20 FNSLSFTLKKGdRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------HLP------------ETLH 81
Cdd:cd03264    16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrrigYLPqefgvypnftvrEFLD 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928  82 TQSLLQAVlaplpADAREAQRwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03264    95 YIAWLKGI-----PSKEVKAR--VDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
21-157 1.47e-15

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: 75.87  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR----------VEQHL---PETLHTQSL-L 86
Cdd:cd03265    17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREprevrrrigiVFQDLsvdDELTGWENLyI 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928  87 QAVLAPLPADAReAQRwlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03265    97 HARLYGVPGAER-RER--IDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
7-152 1.56e-15

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 76.02  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   7 AHALHvetafgplfnSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-----ARVEQ---HLPE 78
Cdd:TIGR03410  13 SHILR----------GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITklpphERARAgiaYVPQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 ------TLHTQSLLQAVLAPLPADAREaqrwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:TIGR03410  83 greifpRLTVEENLLTGLAALPRRSRK----IPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
11-181 1.99e-15

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: 75.74  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQHLPET 79
Cdd:cd03300     5 NVSKFYGgfVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlpphkrpVNTVFQNYALF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 LHTqSLLQAV-----LAPLPADAREAQrwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03300    85 PHL-TVFENIafglrLKKLPKAEIKER---VAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1439757928 155 HLDLPTLLWLESFLQTWQGS----FVLVSHD 181
Cdd:cd03300   160 ALDLKLRKDMQLELKRLQKElgitFVFVTHD 190
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
21-157 2.00e-15

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: 78.96  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAPTSGSVSLAGQCLMA----------------------------RV 72
Cdd:COG4172   303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGlsrralrplrrrmqvvfqdpfgslsprmTV 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  73 EQHLPETLHtqsllqaVLAP-LPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:COG4172   382 GQIIAEGLR-------VHGPgLSAAERRAR---VAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451

                  ....*.
gi 1439757928 152 PGNHLD 157
Cdd:COG4172   452 PTSALD 457
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
21-181 2.20e-15

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 77.43  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQC-------LMARV-------EQ---HLP--ETLH 81
Cdd:COG4586    39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkeFARRIgvvfgqrSQlwwDLPaiDSFR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  82 tqsLLQAVLAPLPADAREAQRWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP--GnhLDLP 159
Cdd:COG4586   119 ---LLKAIYRIPDAEYKKRLDELVELL--DLG---ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPtiG--LDVV 188
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 160 TLLWLESFL----QTWQGSFVLVSHD 181
Cdd:COG4586   189 SKEAIREFLkeynRERGTTILLTSHD 214
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
18-157 2.35e-15

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: 74.27  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlHTQSLLQAVLaplpada 97
Cdd:cd03247    16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG---------------VPVSDLEKAL------- 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  98 REAQRWLAERLLAqmgFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03247    74 SSLISVLNQRPYL---FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
21-181 3.64e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 78.21  E-value: 3.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKST----LLQvldgtLAPTSGSVSLAGQCLMA-RVEQHLPETLHTQSLLQ---AVLAP 92
Cdd:PRK15134  303 KNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQGEIWFDGQPLHNlNRRQLLPVRHRIQVVFQdpnSSLNP 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  93 ------------------LPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:PRK15134  378 rlnvlqiieeglrvhqptLSAAQREQQ---VIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1439757928 155 HLDLPT----LLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK15134  455 SLDKTVqaqiLALLKSLQQKHQLAYLFISHD 485
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
18-203 3.71e-15

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 78.16  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmARVEQHLPETL--HTQSLLQAV------ 89
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG----ADLKQWDRETFgkHIGYLPQDVelfpgt 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 ----LAPLPADArEAQRWLAERLLAQ---------MGFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:TIGR01842 408 vaenIARFGENA-DPEKIIEAAKLAGvhelilrlpDGYDTVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1439757928 157 DLPTLLWLESFLQTWQ---GSFVLVSHDNTLLDAVtNSSWILRDQTLHSF 203
Cdd:TIGR01842 486 DEEGEQALANAIKALKargITVVVITHRPSLLGCV-DKILVLQDGRIARF 534
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
307-489 3.96e-15

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: 74.55  E-value: 3.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 307 PGQPSLFTTGVA-RLRSGDRVAIMGRNGGGKSSLLRL---LWQQMNNASPLPGL---RLHP---RLHPGYYDQTLAQLpd 376
Cdd:cd03245    13 PNQEIPALDNVSlTIRAGEKVAIIGRVGSGKSTLLKLlagLYKPTSGSVLLDGTdirQLDPadlRRNIGYVPQDVTLF-- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 377 EASLLEALTPFAPSADTRK--RALIAAGFG--WARH--------SQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNH 444
Cdd:cd03245    91 YGTLRDNITLGAPLADDERilRAAELAGVTdfVNKHpngldlqiGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1439757928 445 LDMEGKAALAQTLRDYPGG--VLLVSHdRQLISESCNRFWLIDSAGL 489
Cdd:cd03245   171 MDMNSEERLKERLRQLLGDktLIIITH-RPSLLDLVDRIIVMDSGRI 216
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
18-157 4.81e-15

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: 74.88  E-value: 4.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMARVEQ--HLPET----- 79
Cdd:cd03249    17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrSQIGLVSQepVLFDGtiaen 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 ----LHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGftpavmeQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:cd03249    97 irygKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVG-------ERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169

                  ..
gi 1439757928 156 LD 157
Cdd:cd03249   170 LD 171
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
23-181 4.85e-15

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: 76.69  E-value: 4.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmARVEQHLPETLHTQSL----LQAVLAPLPA--- 95
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-FDSRKGIFLPPEKRRIgyvfQEARLFPHLSvrg 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 -------DAREAQRWLA-ERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT----LLW 163
Cdd:TIGR02142  95 nlrygmkRARPSERRISfERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPY 173
                         170
                  ....*....|....*...
gi 1439757928 164 LESFLQTWQGSFVLVSHD 181
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHS 191
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
26-157 4.89e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 75.83  E-value: 4.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--------------HLPET-LHTQSLLQAV- 89
Cdd:PRK13634   29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkplrkkvgivfQFPEHqLFEETVEKDIc 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928  90 LAPL-----PADAREaqrwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13634  109 FGPMnfgvsEEDAKQ----KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
21-181 5.00e-15

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 75.10  E-value: 5.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVsLAGQCLMARVEQHlpetlhTQSLLQ-AVLAP------- 92
Cdd:PRK11247   29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEARED------TRLMFQdARLLPwkkvidn 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  93 ----LPADAREAqrwlAERLLAQMGFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFL 168
Cdd:PRK11247  102 vglgLKGQWRDA----ALQALAAVGLADRANEW-PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 176
                         170
                  ....*....|....*..
gi 1439757928 169 QT-WQG---SFVLVSHD 181
Cdd:PRK11247  177 ESlWQQhgfTVLLVTHD 193
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
319-498 5.19e-15

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 74.74  E-value: 5.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLH------PRLHPGYYDQTLA---QLPdeASLLE------ 382
Cdd:COG1121    28 TIPPGEFVAIVGPNGAGKSTLLKAI---LGLLPPTSGtVRLFgkpprrARRRIGYVPQRAEvdwDFP--ITVRDvvlmgr 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ----ALTPFAPSADTRK--RALIAAGFgWARHSQKVSTLSGGERSRLLfvglsLARY-----SLLLLDEPTNHLDMEGKA 451
Cdd:COG1121   103 ygrrGLFRRPSRADREAvdEALERVGL-EDLADRPIGELSGGQQQRVL-----LARAlaqdpDLLLLDEPFAGVDAATEE 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1439757928 452 ALAQTLRDYPG---GVLLVSHDRQLISESCNRFWLIDSaGLTEWHSLEEV 498
Cdd:COG1121   177 ALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEV 225
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
319-470 5.31e-15

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: 74.05  E-value: 5.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NASPLPGLRLHPRLHPGYYDQTLAqLPDEASLLE------AL 384
Cdd:COG4133    24 TLAAGEALALTGPNGSGKTTLLRILAGLLPpsagevlwNGEPIRDAREDYRRRLAYLGHADG-LKPELTVREnlrfwaAL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSADTRKRALiaAGFGWARHSQK-VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYP-- 461
Cdd:COG4133   103 YGLRADREAIDEAL--EAVGLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLar 180
                         170
                  ....*....|
gi 1439757928 462 -GGVLLVSHD 470
Cdd:COG4133   181 gGAVLLTTHQ 190
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
21-181 8.15e-15

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 76.41  E-value: 8.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQS--------LLQAVLAP 92
Cdd:PRK11607   36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSyalfphmtVEQNIAFG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  93 LPADaREAQRWLAERLLAQMGFtpaVMEQQTAT-----LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--LPTLLWLE 165
Cdd:PRK11607  116 LKQD-KLPKAEIASRVNEMLGL---VHMQEFAKrkphqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLE 191
                         170
                  ....*....|....*...
gi 1439757928 166 --SFLQTWQGSFVLVSHD 181
Cdd:PRK11607  192 vvDILERVGVTCVMVTHD 209
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
5-157 1.27e-14

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: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmARVEQHLPETLHTQS 84
Cdd:cd03231     1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAVLAPLpaDAREAQRWLA--------ERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:cd03231    80 HAPGIKTTL--SVLENLRFWHadhsdeqvEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156

                  .
gi 1439757928 157 D 157
Cdd:cd03231   157 D 157
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
319-475 1.60e-14

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 73.07  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLpglrlhprlhpGYYDQTLAQLPDEASLLEALTPfAPSADTRKRAL 398
Cdd:COG2401    52 EIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA-----------GCVDVPDNQFGREASLIDAIGR-KGDFKDAVELL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 399 IAAGFG----WARhsqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLD----MEGKAALAQTLRDYPGGVLLVSHD 470
Cdd:COG2401   120 NAVGLSdavlWLR---RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITLVVATHH 196

                  ....*
gi 1439757928 471 RQLIS 475
Cdd:COG2401   197 YDVID 201
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
23-157 1.65e-14

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 76.42  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLaPTSGSVSLAGQCL----MARVEQHL------PETLHtQSLLQAVLAP 92
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELreldPESWRKHLswvgqnPQLPH-GTLRDNVLLG 446
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928  93 LPaDAREAQRWLAerlLAQMG---FTPA-------VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11174  447 NP-DASDEQLQQA---LENAWvseFLPLlpqgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-180 1.90e-14

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 73.08  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA---------------------RVEQHLPETLHT 82
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtppsrrpvsmlfqennlfshlTVAQNIGLGLNP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  83 QSLLQAvlaplpadareAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL- 161
Cdd:PRK10771   99 GLKLNA-----------AQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD-PALr 165
                         170       180
                  ....*....|....*....|...
gi 1439757928 162 ----LWLESFLQTWQGSFVLVSH 180
Cdd:PRK10771  166 qemlTLVSQVCQERQLTLLMVSH 188
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
320-485 1.93e-14

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: 71.27  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG----LRLHPRLHPGYYDQTLAQLPDEASLLEALTPfapsadtrk 395
Cdd:cd03230    23 VEKGEIYGLLGPNGAGKTTLIKII---LGLLKPDSGeikvLGKDIKKEPEEVKRRIGYLPEEPSLYENLTV--------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 396 RALIaagfgwarhsqkvsTLSGGERSRLLFVgLSLARY-SLLLLDEPTNHLDMEGKAALAQTLRDY---PGGVLLVSHDR 471
Cdd:cd03230    91 RENL--------------KLSGGMKQRLALA-QALLHDpELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHIL 155
                         170
                  ....*....|....
gi 1439757928 472 QLISESCNRFWLID 485
Cdd:cd03230   156 EEAERLCDRVAILN 169
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
319-485 2.07e-14

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 72.50  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL------------WQQMN-NASPLPGLRLH-------PRlhpgyyDQTLAQLPDE- 377
Cdd:cd03225    23 TIKKGEFVLIVGPNGSGKSTLLRLLngllgptsgevlVDGKDlTKLSLKELRRKvglvfqnPD------DQFFGPTVEEe 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 378 -ASLLEALTpfAPSADTRKRALIAAGFG--WARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALA 454
Cdd:cd03225    97 vAFGLENLG--LPEEEIEERVEEALELVglEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1439757928 455 QTLRDYPG---GVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03225   175 ELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
16-152 2.20e-14

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 73.10  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  16 FGPLF--NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MAR--------------- 71
Cdd:PRK11300   15 FGGLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqIARmgvvrtfqhvrlfre 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  72 --------VEQHlpetLHTQSLLQAVLAPLPAdAREAQRWLAERL---LAQMGFTPaVMEQQTATLSGGQHTRLLLARAL 140
Cdd:PRK11300   95 mtvienllVAQH----QQLKTGLFSGLLKTPA-FRRAESEALDRAatwLERVGLLE-HANRQAGNLAYGQQRRLEIARCM 168
                         170
                  ....*....|..
gi 1439757928 141 IRQPDLLLLDEP 152
Cdd:PRK11300  169 VTQPEILMLDEP 180
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
4-181 2.47e-14

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 73.20  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------MARVEQH-- 75
Cdd:PRK11248    1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgaeRGVVFQNeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  76 -LPetlhTQSLLQAV-----LAPLPADAREAqrwLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:PRK11248   81 lLP----WRNVQDNVafglqLAGVEKMQRLE---IAHQMLKKVGLEGA-EKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1439757928 150 DEPGNHLDLPTLLWLES-FLQTWQGS---FVLVSHD 181
Cdd:PRK11248  153 DEPFGALDAFTREQMQTlLLKLWQETgkqVLLITHD 188
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
22-157 2.55e-14

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: 72.40  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-------QCLMARVEQH-----LPETLHTQSLLQ-- 87
Cdd:cd03266    23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepAEARRRLGFVsdstgLYDRLTARENLEyf 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928  88 AVLAPLPADAREAQ-RWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03266   103 AGLYGLKGDELTARlEELADRL--GME---ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
cbiO PRK13646
energy-coupling factor transporter ATPase;
23-181 2.57e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 73.66  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARV-EQHL-------------PET-LHTQSLLQ 87
Cdd:PRK13646   26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIrpvrkrigmvfqfPESqLFEDTVER 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 AVL-AP--LPADAREAQRWlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT---L 161
Cdd:PRK13646  106 EIIfGPknFKMNLDEVKNY-AHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqV 184
                         170       180
                  ....*....|....*....|.
gi 1439757928 162 LWLESFLQTWQG-SFVLVSHD 181
Cdd:PRK13646  185 MRLLKSLQTDENkTIILVSHD 205
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
24-152 3.03e-14

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 74.00  E-value: 3.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-ARVEQHLPETLHTQ--------SL------LQA 88
Cdd:COG4608    38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITgLSGRELRPLRRRMQmvfqdpyaSLnprmtvGDI 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  89 VLAPL----PADAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG4608   118 IAEPLrihgLASKAERRERVAE-LLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
21-152 3.51e-14

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 72.37  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL----M---AR-----------------VEQHL 76
Cdd:COG1137    20 KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpMhkrARlgigylpqeasifrkltVEDNI 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  77 petlhtqsllQAVL--APLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG1137   100 ----------LAVLelRKLSKKEREER---LEELLEEFGITH-LRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
21-181 3.58e-14

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: 72.68  E-value: 3.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------------MARVEQH---LPEtlht 82
Cdd:cd03294    41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrkelrelrrkkISMVFQSfalLPH---- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  83 QSLLQAV-----LAPLPADAREAQrwlAERLLAQMGFTPavMEQQTAT-LSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:cd03294   117 RTVLENVafgleVQGVPRAEREER---AAEALELVGLEG--WEHKYPDeLSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1439757928 157 DlPT--------LLWLESFLQTwqgSFVLVSHD 181
Cdd:cd03294   192 D-PLirremqdeLLRLQAELQK---TIVFITHD 220
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
23-157 3.88e-14

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 73.95  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQ------HLpetlhtqSLLQ 87
Cdd:COG3839    22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdrnIAMVFQsyalypHM-------TVYE 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928  88 AVLAPL-----PADAREAQ-RWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG3839    95 NIAFPLklrkvPKAEIDRRvREAAELL--GLE---DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
21-197 3.97e-14

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: 74.84  E-value: 3.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSL-----------AGQCLMARVEQHLpETLHTQ------ 83
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGRGRAKRYI-GILHQEydlyph 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 -----SLLQAVLAPLPadaREAQRWLAERLLAQMGFTP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:TIGR03269 380 rtvldNLTEAIGLELP---DELARMKAVITLKMVGFDEekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1439757928 155 HLDLPTLLWL-ESFLQT---WQGSFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:TIGR03269 457 TMDPITKVDVtHSILKAreeMEQTFIIVSHDMDFVLDVCDRAALMRD 503
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
5-186 4.64e-14

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 74.84  E-value: 4.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFG-PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAP-TSGSVSL-AGQCLMArveqhLPET-- 79
Cdd:COG4178   363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARpAGARVLF-----LPQRpy 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 LHTQSLLQAVLapLPADAREAQRWLAERLLAQMG---FTPAVMEQQ--TATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:COG4178   437 LPLGTLREALL--YPATAEAFSDAELREALEAVGlghLAERLDEEAdwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1439757928 155 HLDLPTLLWLESFLQT--WQGSFVLVSHDNTLLD 186
Cdd:COG4178   515 ALDEENEAALYQLLREelPGTTVISVGHRSTLAA 548
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
23-181 4.78e-14

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 71.77  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----MARVE------------QHLpetLHTQSL 85
Cdd:PRK11629   28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssAAKAElrnqklgfiyqfHHL---LPDFTA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 LQAVLAPL------PADAREAqrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP 159
Cdd:PRK11629  105 LENVAMPLligkkkPAEINSR----ALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 160 T---LLWLESFLQTWQGS-FVLVSHD 181
Cdd:PRK11629  180 NadsIFQLLGELNRLQGTaFLVVTHD 205
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
21-181 5.31e-14

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 73.07  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA----------------------------RV 72
Cdd:PRK11308   32 DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeaqkllrqkiqivfqnpygslnprkKV 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  73 EQHLPETLhtqsllqAVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11308  112 GQILEEPL-------LINTSLSAAERREK---ALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1439757928 153 GNHLDLPT---LLWLESFLQTWQG-SFVLVSHD 181
Cdd:PRK11308  182 VSALDVSVqaqVLNLMMDLQQELGlSYVFISHD 214
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
23-157 5.86e-14

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 71.92  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------------------MARVEQHLPE 78
Cdd:PRK10619   24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadknqlrllrtrLTMVFQHFNL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 TLHTQSLLQAVLAPL------PADAREAqrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK10619  104 WSHMTVLENVMEAPIqvlglsKQEARER----AVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179

                  ....*
gi 1439757928 153 GNHLD 157
Cdd:PRK10619  180 TSALD 184
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
23-180 6.30e-14

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: 70.98  E-value: 6.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQ--------SLLQAV-LAPL 93
Cdd:cd03298    17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQennlfahlTVEQNVgLGLS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  94 PA-DAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL------LWLES 166
Cdd:cd03298    97 PGlKLTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALraemldLVLDL 174
                         170
                  ....*....|....
gi 1439757928 167 FLQTwQGSFVLVSH 180
Cdd:cd03298   175 HAET-KMTVLMVTH 187
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
21-152 6.43e-14

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: 72.78  E-value: 6.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAGQCLMA--------------------------- 70
Cdd:COG0444    22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekelrkirgreiqmifqdpmtslnp 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  71 --RVEQHLPETLHTQsllqavlapLPADAREAQRwLAERLLAQMGFTPA--VMEQ---QtatLSGGQHTRLLLARALIRQ 143
Cdd:COG0444   102 vmTVGDQIAEPLRIH---------GGLSKAEARE-RAIELLERVGLPDPerRLDRyphE---LSGGMRQRVMIARALALE 168

                  ....*....
gi 1439757928 144 PDLLLLDEP 152
Cdd:COG0444   169 PKLLIADEP 177
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
319-485 6.54e-14

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: 71.03  E-value: 6.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS------PLPGLRLHPRLhpGYYDQTLAQLPD-----EASLLEALTPF 387
Cdd:cd03235    21 EVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSgsirvfGKPLEKERKRI--GYVPQRRSIDRDfpisvRDVVLMGLYGH 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 A-----PSADTRKRALIAAGFGWARH--SQKVSTLSGGERSRLLfvglsLARY-----SLLLLDEPTNHLDMEGKAALA- 454
Cdd:cd03235    99 KglfrrLSKADKAKVDEALERVGLSElaDRQIGELSGGQQQRVL-----LARAlvqdpDLLLLDEPFAGVDPKTQEDIYe 173
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1439757928 455 --QTLRDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03235   174 llRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
21-187 6.99e-14

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: 70.90  E-value: 6.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQHLPETLHTQSLL------Q 87
Cdd:cd03292    18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgraIPYLRRKIGVVFQDFRLLpdrnvyE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 AVLAPLP---ADAREAQRWLAErLLAQMGFTPAVMEqQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTLLW- 163
Cdd:cd03292    98 NVAFALEvtgVPPREIRKRVPA-ALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD-PDTTWe 174
                         170       180
                  ....*....|....*....|....*....
gi 1439757928 164 ----LESFLQtwQGSFVLVS-HDNTLLDA 187
Cdd:cd03292   175 imnlLKKINK--AGTTVVVAtHAKELVDT 201
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-152 7.73e-14

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 73.90  E-value: 7.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   3 TLLTAHALHVetafGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-----VEQ--- 74
Cdd:COG1129   255 VVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsprdaIRAgia 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  75 HLPETLHTQSLLQ-------AVLAPLPADAR------EAQRWLAERLLAQMGFTPAVMEQQTATLSGG--QhtRLLLARA 139
Cdd:COG1129   331 YVPEDRKGEGLVLdlsirenITLASLDRLSRgglldrRRERALAEEYIKRLRIKTPSPEQPVGNLSGGnqQ--KVVLAKW 408
                         170
                  ....*....|...
gi 1439757928 140 LIRQPDLLLLDEP 152
Cdd:COG1129   409 LATDPKVLILDEP 421
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
319-485 8.69e-14

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: 69.77  E-value: 8.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRLhprlhpgYYDQTLAQL-PDEASLLEALTPfapsadtrkRA 397
Cdd:cd03214    21 SIEAGEIVGILGPNGAGKSTLLKTL---AGLLKPSSGEIL-------LDGKDLASLsPKELARKIAYVP---------QA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 398 LIAAGFGWARHsQKVSTLSGGERSRLLfvglsLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYPG----GVLLVS 468
Cdd:cd03214    82 LELLGLAHLAD-RPFNELSGGERQRVL-----LARAlaqepPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVL 155
                         170
                  ....*....|....*..
gi 1439757928 469 HDRQLISESCNRFWLID 485
Cdd:cd03214   156 HDLNLAARYADRVILLK 172
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
320-443 9.38e-14

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: 68.83  E-value: 9.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQQM---------NNASPLPGLRLHPRLHPGYYDQTLAQLPDEA---SLLEALTPF 387
Cdd:pfam00005   8 LNPGEILALVGPNGAGKSTLLKLIAGLLsptegtillDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTvreNLRLGLLLK 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 388 APSADTRKR----ALIAAGFGWARH---SQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:pfam00005  88 GLSKREKDAraeeALEKLGLGDLADrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
21-157 1.00e-13

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 72.06  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH---LPE--------TLHTQSLLQAV 89
Cdd:COG4152    18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigyLPEerglypkmKVGEQLVYLAR 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928  90 LAPLP-ADARE-AQRWLaERLlaqmgftpAVMEQQTA---TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4152    98 LKGLSkAEAKRrADEWL-ERL--------GLGDRANKkveELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
296-480 1.17e-13

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: 69.17  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 296 LEMDTLHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRL---LWQQMNNASPLPGLRLHpRLHPGYYDQTLA 372
Cdd:cd03246     1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLilgLLRPTSGRVRLDGADIS-QWDPNELGDHVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 373 QLPDEASLLealtpfapsADTrkralIAAgfgwarhsqkvSTLSGGERSRllfVGLSLARY---SLLLLDEPTNHLDMEG 449
Cdd:cd03246    80 YLPQDDELF---------SGS-----IAE-----------NILSGGQRQR---LGLARALYgnpRILVLDEPNSHLDVEG 131
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1439757928 450 KAALAQTLRDYPGG---VLLVSHDRQLIsESCNR 480
Cdd:cd03246   132 ERALNQAIAALKAAgatRIVIAHRPETL-ASADR 164
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
18-157 1.22e-13

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 71.58  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHlPETlhtqsll 86
Cdd:PRK13635   21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvwdvrrqVGMVFQN-PDN------- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAVLAPLPADA----------REAqrwLAERL---LAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK13635   93 QFVGATVQDDVafglenigvpREE---MVERVdqaLRQVGMED-FLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168

                  ....
gi 1439757928 154 NHLD 157
Cdd:PRK13635  169 SMLD 172
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
26-157 1.23e-13

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: 70.90  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETlhtQSLLQAVLAPLPADAREAQRWLA 105
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY---EGTVRDLLSSITKDFYTHPYFKT 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 106 ErLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03237    98 E-IAKPLQIEQ-ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
18-157 1.37e-13

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 73.28  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQ-------------S 84
Cdd:COG1132   354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV----DIRDLTLESLRRQigvvpqdtflfsgT 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAV-LAPLPAD-------AREAQrwlAERLLAQMgftP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG1132   430 IRENIrYGRPDATdeeveeaAKAAQ---AHEFIEAL---PdgydTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEA 503

                  ....*
gi 1439757928 153 GNHLD 157
Cdd:COG1132   504 TSALD 508
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
5-197 1.65e-13

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 70.64  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   5 LTAHALHVETAFGPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAPTSGSVSLAGQCL-------MARVEQHLP 77
Cdd:COG4138     1 LQLNDVAVAGRLGPI----SAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLsdwsaaeLARHRAYLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  78 EtlhtQSLLQAVL---------APLPADAREAQRWLAErLLAQMGFTPAVMeQQTATLSGGQHTRLLLARALIR------ 142
Cdd:COG4138    76 Q----QQSPPFAMpvfqylalhQPAGASSEAVEQLLAQ-LAEALGLEDKLS-RPLTQLSGGEWQRVRLAAVLLQvwptin 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 143 -QPDLLLLDEPGNHLD----LPTLLWLESFLQTwQGSFVLVSHD--NTLLDAvtNSSWILRD 197
Cdd:COG4138   150 pEGQLLLLDEPMNSLDvaqqAALDRLLRELCQQ-GITVVMSSHDlnHTLRHA--DRVWLLKQ 208
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
320-502 1.83e-13

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 70.09  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASP-----------LPGLRLHPRLHPGYydqtlaqLPDEASLLEALTP-- 386
Cdd:COG1131    23 VEPGEIFGLLGPNGAGKTTTIRML---LGLLRPtsgevrvlgedVARDPAEVRRRIGY-------VPQEPALYPDLTVre 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 387 ----FA-----PSADTRKRA--LIAAgFG-WARHSQKVSTLSGGERSRLlfvGLSLA---RYSLLLLDEPTNHLDMEGKA 451
Cdd:COG1131    93 nlrfFArlyglPRKEARERIdeLLEL-FGlTDAADRKVGTLSGGMKQRL---GLALAllhDPELLILDEPTSGLDPEARR 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 452 ALAQTLRDYPGG---VLLVSHDRQLISESCNRFWLIDS---------AGLTEwHSLEEVYARL 502
Cdd:COG1131   169 ELWELLRELAAEgktVLLSTHYLEEAERLCDRVAIIDKgrivadgtpDELKA-RLLEDVFLEL 230
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
23-183 1.93e-13

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: 69.59  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQHLPETLHtQSLLQAVLAPL 93
Cdd:cd03301    19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdrdIAMVFQNYALYPH-MTVYDNIAFGL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  94 ------PADAREAQRWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD----LPTLLW 163
Cdd:cd03301    98 klrkvpKDEIDERVREVAELL--QIE---HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAE 172
                         170       180
                  ....*....|....*....|
gi 1439757928 164 LESFLQTWQGSFVLVSHDNT 183
Cdd:cd03301   173 LKRLQQRLGTTTIYVTHDQV 192
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
21-181 2.17e-13

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 71.90  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLP-ETLHTQSLLQA-VLAP------ 92
Cdd:PRK09452   31 SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPaENRHVNTVFQSyALFPhmtvfe 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  93 ----------LPADarEAQRWLAERL----LAQMGftpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD- 157
Cdd:PRK09452  106 nvafglrmqkTPAA--EITPRVMEALrmvqLEEFA------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDy 177
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 158 -LPTLLWLE-SFLQTWQG-SFVLVSHD 181
Cdd:PRK09452  178 kLRKQMQNElKALQRKLGiTFVFVTHD 204
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
24-181 2.24e-13

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: 71.67  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM---ARV--------------EQHLPETLHTQSLL 86
Cdd:COG4148    19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsaRGIflpphrrrigyvfqEARLFPHLSVRGNL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAVLAPLPADAREAQRwlaERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT----LL 162
Cdd:COG4148    99 LYGRKRAPRAERRISF---DEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLP 174
                         170
                  ....*....|....*....
gi 1439757928 163 WLESFLQTWQGSFVLVSHD 181
Cdd:COG4148   175 YLERLRDELDIPILYVSHS 193
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
22-198 2.40e-13

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: 69.67  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQ------HLPETLHTQSLL 86
Cdd:cd03299    17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItnlppekrdISYVPQnyalfpHMTVYKNIAYGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAVLAPLPADAREAqRWLAERLlaqmGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES 166
Cdd:cd03299    97 KKRKVDKKEIERKV-LEIAEML----GID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1439757928 167 FLQTWQGSF---VL-VSHDntLLDAvtnssWILRDQ 198
Cdd:cd03299   171 ELKKIRKEFgvtVLhVTHD--FEEA-----WALADK 199
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
319-480 2.46e-13

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: 72.94  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHP--------------RLHPGYYDQTLAQLPDEA-----S 379
Cdd:COG2274   497 TIKPGERVAIVGRSGSGKSTLLKLL------------LGLYEptsgrilidgidlrQIDPASLRRQIGVVLQDVflfsgT 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 380 LLEALTPFAPSADTRK--RALIAAGF---------GWARH-SQKVSTLSGGERSRLLfvglsLAR--Y---SLLLLDEPT 442
Cdd:COG2274   565 IRENITLGDPDATDEEiiEAARLAGLhdfiealpmGYDTVvGEGGSNLSGGQRQRLA-----IARalLrnpRILILDEAT 639
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1439757928 443 NHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLIsESCNR 480
Cdd:COG2274   640 SALDAETEAIILENLRRLLKGrtVIIIAHRLSTI-RLADR 678
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
19-157 2.58e-13

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 69.66  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG------------QCLMAR-----VEQ--HL-PE 78
Cdd:COG4161    18 LFD-INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpsekAIRLLRqkvgmVFQqyNLwPH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 TLHTQSLLQA---VLAPLPADAREAqrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:COG4161    97 LTVMENLIEApckVLGLSKEQAREK----AMKLLARLRLTDKA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171

                  ..
gi 1439757928 156 LD 157
Cdd:COG4161   172 LD 173
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
11-157 2.67e-13

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: 69.68  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR---------VEQHLPET 79
Cdd:cd03296     7 NVSKRFGdfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvqernvgfVFQHYALF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 LHtQSLLQAV--------LAPLPADAREAQR-----------WLAERLLAQmgftpavmeqqtatLSGGQHTRLLLARAL 140
Cdd:cd03296    87 RH-MTVFDNVafglrvkpRSERPPEAEIRAKvhellklvqldWLADRYPAQ--------------LSGGQRQRVALARAL 151
                         170
                  ....*....|....*..
gi 1439757928 141 IRQPDLLLLDEPGNHLD 157
Cdd:cd03296   152 AVEPKVLLLDEPFGALD 168
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
18-157 3.46e-13

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: 69.77  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqcLMARVEQHLPETLHTQSLL------QAVLA 91
Cdd:TIGR04520  16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKKVGMVfqnpdnQFVGA 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928  92 PLPAD----------AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR04520  94 TVEDDvafglenlgvPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
19-151 3.69e-13

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 69.73  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMARVEQHlP---------- 77
Cdd:COG1101    21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykraKYIGRVFQD-Pmmgtapsmti 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  78 -ETL-------HTQSLLQAVLAplpadareAQRWLAERLLAQMGF-TPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:COG1101   100 eENLalayrrgKRRGLRRGLTK--------KRRELFRELLATLGLgLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLL 171

                  ...
gi 1439757928 149 LDE 151
Cdd:COG1101   172 LDE 174
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
18-180 3.97e-13

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: 69.04  E-value: 3.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE---------TLHTQSLLQA 88
Cdd:cd03248    28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSkvslvgqepVLFARSLQDN 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 VLAPLPADARE-----AQRWLAERLLAQM--GFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL 161
Cdd:cd03248   108 IAYGLQSCSFEcvkeaAQKAHAHSFISELasGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
                         170       180
                  ....*....|....*....|.
gi 1439757928 162 LWLESFLQTW--QGSFVLVSH 180
Cdd:cd03248   187 QQVQQALYDWpeRRTVLVIAH 207
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
18-157 4.24e-13

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: 71.70  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmARVEQHLPETL--HTQSLLQAV------ 89
Cdd:COG4618   346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG----ADLSQWDREELgrHIGYLPQDVelfdgt 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 ----LAPLP-ADARE----AQRWLAERLLAQM--GF-TPavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4618   422 iaenIARFGdADPEKvvaaAKLAGVHEMILRLpdGYdTR--IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
21-181 4.32e-13

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 70.51  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLH-TQSLLQAVLAPL------ 93
Cdd:PRK15079   38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSdIQMIFQDPLASLnprmti 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  94 ------------PADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL 161
Cdd:PRK15079  118 geiiaeplrtyhPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
                         170       180
                  ....*....|....*....|....
gi 1439757928 162 LWLESFLQTWQG----SFVLVSHD 181
Cdd:PRK15079  198 AQVVNLLQQLQRemglSLIFIAHD 221
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
3-152 4.54e-13

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: 67.84  E-value: 4.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   3 TLLTAHALHVETAFGPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARveqhlpetlHT 82
Cdd:cd03215     3 PVLEVRGLSVKGAVRDV----SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR---------SP 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928  83 QSLLQAVLAPLPADAREaqrwlaERLLAQMGftpaVMEQQTAT--LSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:cd03215    70 RDAIRAGIAYVPEDRKR------EGLVLDLS----VAENIALSslLSGGNQQKVVLARWLARDPRVLILDEP 131
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
2-157 4.55e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 69.88  E-value: 4.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   2 STLLTAHALHVETAFGP-LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------ 68
Cdd:PRK13636    3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmklre 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  69 -MARVEQHLPETLHTQSLLQ-----AVLAPLPADarEAQRWLaERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:PRK13636   83 sVGMVFQDPDNQLFSASVYQdvsfgAVNLKLPED--EVRKRV-DNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVM 158
                         170
                  ....*....|....*
gi 1439757928 143 QPDLLLLDEPGNHLD 157
Cdd:PRK13636  159 EPKVLVLDEPTAGLD 173
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
24-152 4.62e-13

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 71.59  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarvEQHLPETLHTQSL-LQAV---LAPLP----A 95
Cdd:COG1129    24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE------PVRFRSPRDAQAAgIAIIhqeLNLVPnlsvA 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928  96 D----AREAQRW----------LAERLLAQMGFT--PavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG1129    98 EniflGREPRRGglidwramrrRARELLARLGLDidP---DTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
24-152 5.20e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 72.08  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR----------------------VEQHLpeTLH 81
Cdd:NF033858  286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiatrrrvgymsqafslygeltVRQNL--ELH 363
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928  82 tqsllqAVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF033858  364 ------ARLFHLPAAEIAAR---VAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
319-485 5.80e-13

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


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 68.73  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRL----HPRLHPGYYDQTLAQLPDEASLLEALTP------FA 388
Cdd:COG4555    23 TAKDGEITGLLGPNGAGKTTLLRML---AGLLKPDSGSILidgeDVRKEPREARRQIGVLPDERGLYDRLTVreniryFA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 PSADTRKRALIAA--------GFGWARHsQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQ---TL 457
Cdd:COG4555   100 ELYGLFDEELKKRieeliellGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrAL 178
                         170       180
                  ....*....|....*....|....*...
gi 1439757928 458 RDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:COG4555   179 KKEGKTVLFSSHIMQEVEALCDRVVILH 206
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
295-532 5.93e-13

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: 71.09  E-value: 5.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 295 LLEMDTLHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqmNNASPLPG------------LRLHPRL 362
Cdd:COG1123     4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL----MGLLPHGGrisgevlldgrdLLELSEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 363 HPGYYDQTLAQLPD--------EASLLEALTPFAPSADTRKR----ALIAAGFGwARHSQKVSTLSGGERSRLLFVGLSL 430
Cdd:COG1123    80 LRGRRIGMVFQDPMtqlnpvtvGDQIAEALENLGLSRAEARArvleLLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 431 ARYSLLLLDEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQAVA 506
Cdd:COG1123   159 LDPDLLIADEPTTALDVTTQAEILDLLrelqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
                         250       260
                  ....*....|....*....|....*.
gi 1439757928 507 PAPDSRLALQSTPAGADDDEEALLAR 532
Cdd:COG1123   239 AVPRLGAARGRAAPAAAAAEPLLEVR 264
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
21-152 5.98e-13

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: 68.34  E-value: 5.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPetLHTQSLL-------------- 86
Cdd:cd03218    17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-----TKLP--MHKRARLgigylpqeasifrk 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928  87 ----QAVLAPLP--ADAREAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:cd03218    90 ltveENILAVLEirGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
319-499 6.19e-13

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


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 68.92  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHPRLHpG--YYD-------------QTLAQLPDEASLLEA 383
Cdd:COG1120    23 SLPPGEVTALLGPNGSGKSTLLRAL------------AGLLKPSS-GevLLDgrdlaslsrrelaRRIAYVPQEPPAPFG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 384 LT--------------PFA-PSADTRK---RALIAAGFGWARHsQKVSTLSGGERSRLLfvglsLARY-----SLLLLDE 440
Cdd:COG1120    90 LTvrelvalgryphlgLFGrPSAEDREaveEALERTGLEHLAD-RPVDELSGGERQRVL-----IARAlaqepPLLLLDE 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 441 PTNHLDMEGKAALAQTLRDY----PGGVLLVSHDRQLISESCNRFWLID-----SAG-----LTEwHSLEEVY 499
Cdd:COG1120   164 PTSHLDLAHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKdgrivAQGppeevLTP-ELLEEVY 235
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
27-184 8.01e-13

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 68.27  E-value: 8.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  27 LKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH-----------------LPETLHTQSLLQaV 89
Cdd:PRK10584   33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvgfvfqsfmLIPTLNALENVE-L 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 LAPLPADAREAQRWLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT------LLW 163
Cdd:PRK10584  112 PALLRGESSRQSRNGAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiadLLF 190
                         170       180
                  ....*....|....*....|.
gi 1439757928 164 leSFLQTWQGSFVLVSHDNTL 184
Cdd:PRK10584  191 --SLNREHGTTLILVTHDLQL 209
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
319-485 8.67e-13

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: 66.64  E-value: 8.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhPGYYDqtlaqlPDEASLL---EALTPFAPSADTRK 395
Cdd:cd03228    24 TIKPGEKVAIVGPSGSGKSTLLKLL--------------------LRLYD------PTSGEILidgVDLRDLDLESLRKN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 396 RALIaagfgwarhSQKV----ST-----LSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYP 461
Cdd:cd03228    78 IAYV---------PQDPflfsGTireniLSGGQRQRI-----AIARAllrdpPILILDEATSALDPETEALILEALRALA 143
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 462 GG--VLLVSHDRQLIsESCNRFWLID 485
Cdd:cd03228   144 KGktVIVIAHRLSTI-RDADRIIVLD 168
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
19-157 1.56e-12

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 67.35  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------------------MARVEQHL-PE 78
Cdd:PRK11124   18 LFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsdkairelrrnvgMVFQQYNLwPH 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  79 TLHTQSLLQAVLAPLPADAREAQRwLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11124   97 LTVQQNLIEAPCRVLGLSKDQALA-RAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
18-157 1.67e-12

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 69.85  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE--TLHTQS--LLQAVL--- 90
Cdd:PRK11160  354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQaiSVVSQRvhLFSATLrdn 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  91 ----APLPADAReaqrwLAErLLAQMGFTpAVMEQQTA----------TLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PRK11160  434 lllaAPNASDEA-----LIE-VLQQVGLE-KLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506

                  .
gi 1439757928 157 D 157
Cdd:PRK11160  507 D 507
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
19-157 1.69e-12

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: 66.91  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL---APTSGSVSLAGQCL--------MARVEQH---LPETLHTQS 84
Cdd:cd03234    22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRkpdqfqkcVAYVRQDdilLPGLTVRET 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  85 LLQAVLAPLP---ADAREAQRWlAERLLAQMGFTPA---VMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03234   102 LTYTAILRLPrksSDAIRKKRV-EDVLLRDLALTRIggnLVKG----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
319-490 1.73e-12

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: 66.51  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwQQMNNASP----LPGLRLHP--RLHPGYYdqtLAQLPD----EASLLEALTPFA 388
Cdd:cd03226    22 DLYAGEIIALTGKNGAGKTTLAKIL-AGLIKESSgsilLNGKPIKAkeRRKSIGY---VMQDVDyqlfTDSVREELLLGL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 PSAD---TRKRALIAAGFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG--- 462
Cdd:cd03226    98 KELDagnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgk 177
                         170       180
                  ....*....|....*....|....*...
gi 1439757928 463 GVLLVSHDRQLISESCNRFWLIDSAGLT 490
Cdd:cd03226   178 AVIVITHDYEFLAKVCDRVLLLANGAIV 205
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
1-187 1.94e-12

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 66.91  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVETAFG--------PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL--APTSGSVSLagqclma 70
Cdd:COG2401    19 SVLDLSERVAIVLEAFGvelrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  71 rVEQHLPETLhtqSLLQAVLAPLPADAreaqrwlAERLLAQMGFTPAV-MEQQTATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:COG2401    92 -PDNQFGREA---SLIDAIGRKGDFKD-------AVELLNAVGLSDAVlWLRRFKELSTGQKFRFRLALLLAERPKLLVI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1439757928 150 DEPGNHLDLPTL----LWLESFLQTWQGSFVLVSHDNTLLDA 187
Cdd:COG2401   161 DEFCSHLDRQTAkrvaRNLQKLARRAGITLVVATHHYDVIDD 202
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
319-469 1.99e-12

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: 65.25  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRL---LWQqmnnasplpglrlhprlhpgYYDQTLAQLPDEASLLEALTPFAPSAdTRK 395
Cdd:cd03223    23 EIKPGDRLLITGPSGTGKSSLFRAlagLWP--------------------WGSGRIGMPEGEDLLFLPQRPYLPLG-TLR 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 396 RALIaagFGWARhsqkvsTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSH 469
Cdd:cd03223    82 EQLI---YPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
18-157 2.34e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 66.44  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmARVEQHLPETLHTQSLLQAVLAPLP--- 94
Cdd:PRK13539   16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHYLGHRNAMKPALTvae 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  95 -----ADAREAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13539   93 nlefwAAFLGGEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
22-202 2.65e-12

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 66.88  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLaPTSGSVSLAGQCL-------MARV-----EQHLPETL----HTQSL 85
Cdd:PRK03695   14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeawsaaeLARHraylsQQQTPPFAmpvfQYLTL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  86 LQAVLAPLpADAREAQRWLAERLLAQMgftpaVMEQQTATLSGGQHTRLLLArALIRQ--PD------LLLLDEPGNHLD 157
Cdd:PRK03695   93 HQPDKTRT-EAVASALNEVAEALGLDD-----KLGRSVNQLSGGEWQRVRLA-AVVLQvwPDinpagqLLLLDEPMNSLD 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1439757928 158 LPTLLWLESFLQTW--QGSFVLVS-HD--NTLLDAvtNSSWILRDQTLHS 202
Cdd:PRK03695  166 VAQQAALDRLLSELcqQGIAVVMSsHDlnHTLRHA--DRVWLLKQGKLLA 213
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
11-157 3.07e-12

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 68.21  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLlqa 88
Cdd:PRK11432   11 NITKRFGSntVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSY--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 VLAP----------------LPADAREAQRWLAERLLAQMGFTPAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11432   88 ALFPhmslgenvgyglkmlgVPKEERKQRVKEALELVDLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEP 163

                  ....*
gi 1439757928 153 GNHLD 157
Cdd:PRK11432  164 LSNLD 168
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
18-157 3.07e-12

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: 66.49  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------QCL---MARVEQhlpET-LHTQSL 85
Cdd:cd03251    16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlASLrrqIGLVSQ---DVfLFNDTV 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  86 LQAVLAPLPaDAREAQRWLAERLLAQMGF---TP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03251    93 AENIAYGRP-GATREEVEEAARAANAHEFimeLPegydTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
cbiO PRK13650
energy-coupling factor transporter ATPase;
18-195 3.08e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 67.45  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarVEQHLPETLHTQSLL------QAVLA 91
Cdd:PRK13650   21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHKIGMVfqnpdnQFVGA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  92 PLPAD----------AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD---- 157
Cdd:PRK13650   98 TVEDDvafglenkgiPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegr 176
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1439757928 158 LPTLLWLESFLQTWQGSFVLVSHDntlLDAVTNSSWIL 195
Cdd:PRK13650  177 LELIKTIKGIRDDYQMTVISITHD---LDEVALSDRVL 211
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
2-157 3.61e-12

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 66.28  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   2 STLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA----RVEQHLP 77
Cdd:PRK10247    5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeIYRQQVS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  78 ETLHTQSLL-----QAVLAP--LPADAREAQRWLAErlLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLD 150
Cdd:PRK10247   85 YCAQTPTLFgdtvyDNLIFPwqIRNQQPDPAIFLDD--LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162

                  ....*..
gi 1439757928 151 EPGNHLD 157
Cdd:PRK10247  163 EITSALD 169
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
11-157 4.34e-12

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 67.14  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH------LPE---- 78
Cdd:PRK13537   12 NVEKRYGDklVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqrvgvVPQfdnl 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 ----TLHTQSLLQAVLAPLPA-DAREAQRWLAE--RLLAQmgftpavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13537   92 dpdfTVRENLLVFGRYFGLSAaAARALVPPLLEfaKLENK-------ADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164

                  ....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK13537  165 PTTGLD 170
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
35-194 5.54e-12

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: 67.13  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  35 LIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQSLLQA-VLAPLPADAREAQRWLAERLLAQMG 113
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE----DVTNVPPHLRHINMVFQSyALFPHMTVEENVAFGLKMRKVPRAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 114 FTPAVME------------QQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--LPTLLWLEsfLQTWQG----SF 175
Cdd:TIGR01187  77 IKPRVLEalrlvqleefadRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQLE--LKTIQEqlgiTF 154
                         170
                  ....*....|....*....
gi 1439757928 176 VLVSHDNTllDAVTNSSWI 194
Cdd:TIGR01187 155 VFVTHDQE--EAMTMSDRI 171
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
312-492 5.94e-12

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 68.27  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 312 LFTTGVARLRSGDRVAIMGRNGGGKSSLLRLL----------------WQ-----QMNNASPLPGLRlhprlhpgYY--- 367
Cdd:PRK10636   16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadggsytfpgnWQlawvnQETPALPQPALE--------YVidg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 368 DQTLAQLpdEASLLEA--------LTPFAPSADT------RKRA---LIAAGFGWARHSQKVSTLSGGERSRLLFVGLSL 430
Cdd:PRK10636   88 DREYRQL--EAQLHDAnerndghaIATIHGKLDAidawtiRSRAaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALI 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 431 ARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:PRK10636  166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
23-152 7.46e-12

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 65.29  E-value: 7.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMarveqhlpeTLHTQSLLQAVLAPLPADAREAQR 102
Cdd:PRK11614   24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---------DWQTAKIMREAVAIVPEGRRVFSR 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 103 WLAERLLAQMGFT-----------------PAVME---QQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11614   95 MTVEENLAMGGFFaerdqfqerikwvyelfPRLHErriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
1-157 7.51e-12

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 65.59  E-value: 7.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLlTAHALHVET---AFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH 75
Cdd:COG4598     1 MTDT-APPALEVRDlhkSFGDLevLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  76 LP---------ETLHTQ--------------SLLQAVL-APL------PADAREAqrwlAERLLAQMGFtPAVMEQQTAT 125
Cdd:COG4598    80 GElvpadrrqlQRIRTRlgmvfqsfnlwshmTVLENVIeAPVhvlgrpKAEAIER----AEALLAKVGL-ADKRDAYPAH 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1439757928 126 LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4598   155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
12-157 8.44e-12

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 66.78  E-value: 8.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  12 VETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlhtqsllqav 89
Cdd:PRK13536   47 VSKSYGdkAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG------------------------ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 lAPLPADAREAQRWLA---------------ERLLAQMGF-----------TPAVME---------QQTATLSGGQHTRL 134
Cdd:PRK13536  103 -VPVPARARLARARIGvvpqfdnldleftvrENLLVFGRYfgmstreieavIPSLLEfarleskadARVSDLSGGMKRRL 181
                         170       180
                  ....*....|....*....|...
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13536  182 TLARALINDPQLLILDEPTTGLD 204
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
18-156 8.81e-12

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: 64.41  E-value: 8.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclMARVEQ---HLPETLHtqsllQAVLAPLP 94
Cdd:cd03250    19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQepwIQNGTIR-----ENILFGKP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  95 ADareaQRWLaERLLAQMGFTP--AVMEQ--QT------ATLSGGQHTRLLLARALIRQPDLLLLDEP--------GNHL 156
Cdd:cd03250    92 FD----EERY-EKVIKACALEPdlEILPDgdLTeigekgINLSGGQKQRISLARAVYSDADIYLLDDPlsavdahvGRHI 166
hmuV PRK13547
heme ABC transporter ATP-binding protein;
4-158 9.00e-12

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 65.62  E-value: 9.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL--------APTSGSVSLAGQCL------- 68
Cdd:PRK13547    1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLaaidapr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  69 MARVEQHLPETLHTQ---SLLQAVLAPLPADAREA------QRWLAERLLAQMGFTPAVMEQQTaTLSGGQHTRLLLARA 139
Cdd:PRK13547   81 LARLRAVLPQAAQPAfafSAREIVLLGRYPHARRAgalthrDGEIAWQALALAGATALVGRDVT-TLSGGELARVQFARV 159
                         170       180
                  ....*....|....*....|....*...
gi 1439757928 140 L---------IRQPDLLLLDEPGNHLDL 158
Cdd:PRK13547  160 LaqlwpphdaAQPPRYLLLDEPTAALDL 187
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1-181 9.60e-12

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 65.33  E-value: 9.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALhvETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV---------------SL 63
Cdd:PRK11701    3 DQPLLSVRGL--TKLYGPRkgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrdlyalSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  64 AGQCLMAR-----VEQHLPETLHTQ--------SLLQAVLAPLPADARE-AQRWLAERLLAqmgftPAVMEQQTATLSGG 129
Cdd:PRK11701   81 AERRRLLRtewgfVHQHPRDGLRMQvsaggnigERLMAVGARHYGDIRAtAGDWLERVEID-----AARIDDLPTTFSGG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 130 QHTRLLLARALIRQPDLLLLDEPGNHLDLPT----LLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK11701  156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHD 211
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
291-473 9.66e-12

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 67.52  E-value: 9.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 291 PADRLLEMDTLHVSPAPGQPsLFTTGVARLRSGDRVAIMGRNGGGKSSLLRL---LWqqmNNAS-----PlPGLRL---- 358
Cdd:COG4178   358 SEDGALALEDLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAiagLW---PYGSgriarP-AGARVlflp 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 359 -HPRLHPG------YYDQTLAQLPDEA--SLLEA--LTPFAPSADTRKRaliaagfgWARhsqkvsTLSGGERSRLLFVG 427
Cdd:COG4178   433 qRPYLPLGtlrealLYPATAEAFSDAElrEALEAvgLGHLAERLDEEAD--------WDQ------VLSLGEQQRLAFAR 498
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 428 LSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVS----------HDRQL 473
Cdd:COG4178   499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISvghrstlaafHDRVL 554
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
24-180 1.03e-11

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 64.50  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHLPETLHTQSLLQAVLAP 92
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHtglapyqrpvsMLFQENNLFAHLTVRQNIGLGLHP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  93 -LPADAREAQRwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD----LPTLLWLESF 167
Cdd:TIGR01277  98 gLKLNAEQQEK--VVDAAQQVGIAD-YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLALVKQL 174
                         170
                  ....*....|...
gi 1439757928 168 LQTWQGSFVLVSH 180
Cdd:TIGR01277 175 CSERQRTLLMVTH 187
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
18-160 1.03e-11

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: 65.65  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-CLMARVEQHLPETLHtqsllQAVLAPLPAD 96
Cdd:cd03291    51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSWIMPGTIK-----ENIIFGVSYD 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  97 AREAQR-----WLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:cd03291   126 EYRYKSvvkacQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
321-476 1.37e-11

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: 64.16  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 321 RSGDRVAIMGRNGGGKSSLLRLL-------------WQQ--MNNASPLPglrlhpRL-----HPGYYDQTLAQlpdEASL 380
Cdd:cd03268    24 KKGEIYGFLGPNGAGKTTTMKIIlglikpdsgeitfDGKsyQKNIEALR------RIgalieAPGFYPNLTAR---ENLR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 381 LEALTPFAPSADTrKRALIAAGFGWARHsQKVSTLSGGERSRLlfvGLSLA---RYSLLLLDEPTNHLDMEGKAALAQTL 457
Cdd:cd03268    95 LLARLLGIRKKRI-DEVLDVVGLKDSAK-KKVKGFSLGMKQRL---GIALAllgNPDLLILDEPTNGLDPDGIKELRELI 169
                         170       180
                  ....*....|....*....|..
gi 1439757928 458 RDYP---GGVLLVSHdrqLISE 476
Cdd:cd03268   170 LSLRdqgITVLISSH---LLSE 188
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
18-201 1.74e-11

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: 62.56  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAP-TSGSVSLAGQCLMARVEQH--LPETlhtqSLLQAVLAPlp 94
Cdd:cd03223    15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIGMPEGEDLLFLPQRpyLPLG----TLREQLIYP-- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  95 adareaqrWlaerllaqmgftpavmeqqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGS 174
Cdd:cd03223    88 --------W-------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGIT 140
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 175 FVLVSHDNTLldavtnssWILRDQTLH 201
Cdd:cd03223   141 VISVGHRPSL--------WKFHDRVLD 159
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
18-157 1.98e-11

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: 63.34  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP--TSGSVSLAGQ--------CLMARVEQHlpETLHTQSllq 87
Cdd:cd03213    23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrKIIGYVPQD--DILHPTL--- 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 avlaplpaDAREAqrwlaerllaqMGFTpAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03213    98 --------TVRET-----------LMFA-AKLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
18-171 2.34e-11

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 66.67  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQ-------------- 83
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV----PLVQYDHHYLHRQvalvgqepvlfsgs 570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 -------SLLQAVLAPLPADAREAQrwlAERLLAQM--GFTPAVMEQQTaTLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:TIGR00958 571 vreniayGLTDTPDEEIMAAAKAAN---AHDFIMEFpnGYDTEVGEKGS-QLSGGQKQRIAIARALVRKPRVLILDEATS 646
                         170
                  ....*....|....*..
gi 1439757928 155 HLDLPTllwlESFLQTW 171
Cdd:TIGR00958 647 ALDAEC----EQLLQES 659
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
296-501 2.55e-11

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 66.32  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 296 LEMDTLHVSPAPGQPSLftTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NASPLPGLRL-------- 358
Cdd:COG4988   337 IELEDVSFSYPGGRPAL--DGLsLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpysgsiliNGVDLSDLDPaswrrqia 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 359 ----HPRLHPGyydqtlaqlpdeaSLLEALTPFAPSADTR--KRALIAAGF---------GWARH-SQKVSTLSGGERSR 422
Cdd:COG4988   415 wvpqNPYLFAG-------------TIRENLRLGRPDASDEelEAALEAAGLdefvaalpdGLDTPlGEGGRGLSGGQAQR 481
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 423 LlfvglSLAR-----YSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLISEsCNRFWLIDSAGLTEWHSL 495
Cdd:COG4988   482 L-----ALARallrdAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555

                  ....*.
gi 1439757928 496 EEVYAR 501
Cdd:COG4988   556 EELLAK 561
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
319-469 3.33e-11

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: 63.57  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnNAsplpglRLHP---------------------RLHPGYYDQTLAQ-LPD 376
Cdd:COG1119    25 TVKPGEHWAILGPNGAGKSTLLSLI-----TG------DLPPtygndvrlfgerrggedvwelRKRIGLVSPALQLrFPR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 377 EASLLEA-LTPF--------APSADTRKRAL-IAAGFGWARHSQK-VSTLSGGERSRLLfvglsLARY-----SLLLLDE 440
Cdd:COG1119    94 DETVLDVvLSGFfdsiglyrEPTDEQRERAReLLELLGLAHLADRpFGTLSQGEQRRVL-----IARAlvkdpELLILDE 168
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1439757928 441 PTNHLDMEGKAALAQTLRDYPGG----VLLVSH 469
Cdd:COG1119   169 PTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
22-181 4.00e-11

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 63.85  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQSLLQAVLAPLPADAREAQ 101
Cdd:PRK10253   25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE----HIQHYASKEVARRIGLLAQNATTPGDITVQE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 102 --------------RWLAE------RLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP-- 159
Cdd:PRK10253  101 lvargryphqplftRWRKEdeeavtKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShq 179
                         170       180
                  ....*....|....*....|....
gi 1439757928 160 -TLLWLESFLQTWQG-SFVLVSHD 181
Cdd:PRK10253  180 iDLLELLSELNREKGyTLAAVLHD 203
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
23-187 4.31e-11

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: 63.01  E-value: 4.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTqsLLQAVLApLPADARE--- 99
Cdd:cd03254    22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV--VLQDTFL-FSGTIMEnir 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 -----AQRWLAERLLAQMGFTPAVM----------EQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03254    99 lgrpnATDEEVIEAAKEAGAHDFIMklpngydtvlGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI 178
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 165 ESFLQTWQG---SFVLVSHDNTLLDA 187
Cdd:cd03254   179 QEALEKLMKgrtSIIIAHRLSTIKNA 204
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
23-157 4.35e-11

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: 63.27  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------QCLMARVEQHLPE-TLHTQSLLQAVLAPL 93
Cdd:cd03252    21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpAWLRRQVGVVLQEnVLFNRSIRDNIALAD 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928  94 PADARE-----AQRWLAERLLAQM--GFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03252   101 PGMSMErvieaAKLAGAHDFISELpeGYDTIVGEQ-GAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
18-160 4.49e-11

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: 66.09  E-value: 4.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-CLMARVEQHLPETLHtqsllQAVLAPLPAD 96
Cdd:TIGR01271  440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTSWIMPGTIK-----DNIIFGLSYD 514
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928   97 A-REAQRWLAERLLAQMGFTP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:TIGR01271  515 EyRYTSVIKACQLEEDIALFPekdkTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
323-492 4.91e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 65.36  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLLWQ-------QMNNASPLPGLRLH---PRLHPG-YYDQTLAQLPDEASLLEA------LT 385
Cdd:PRK11147   29 NERVCLVGRNGAGKSTLMKILNGevllddgRIIYEQDLIVARLQqdpPRNVEGtVYDFVAEGIEEQAEYLKRyhdishLV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 PFAPSADTRKR-----ALIAAGFGWARHSQ--------------KVSTLSGGERSRllfVGLSLARYS---LLLLDEPTN 443
Cdd:PRK11147  109 ETDPSEKNLNElaklqEQLDHHNLWQLENRinevlaqlgldpdaALSSLSGGWLRK---AALGRALVSnpdVLLLDEPTN 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 444 HLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:PRK11147  186 HLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSY 234
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
21-157 4.92e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 63.56  E-value: 4.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ--------CLMAR-----VEQHLPETLHTQSLLQ 87
Cdd:PRK13639   19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksLLEVRktvgiVFQNPDDQLFAPTVEE 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928  88 AV-LAP----LPADarEAQRWLAERLLA--QMGFTpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13639   99 DVaFGPlnlgLSKE--EVEKRVKEALKAvgMEGFE----NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-157 5.01e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 65.21  E-value: 5.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA------GQCLMA----RVEQHL---PETLHTQSLLQAVLAP 92
Cdd:PRK13409  361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPdydgTVEDLLrsiTDDLGSSYYKSEIIKP 440
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928  93 LpadareaqrwLAERLlaqmgftpavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13409  441 L----------QLERL----------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
cbiO PRK13644
energy-coupling factor transporter ATPase;
18-157 5.32e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 63.47  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG------------QCLMARVEQHlPETLHTQSL 85
Cdd:PRK13644   16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgiRKLVGIVFQN-PETQFVGRT 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928  86 LQAVLAPLPAD---AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13644   95 VEEDLAFGPENlclPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
22-158 5.60e-11

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 63.27  E-value: 5.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHLPETLHT-QSLLQAV 89
Cdd:PRK15112   31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyrsqrIRMIFQDPSTSLNPrQRISQIL 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928  90 LAPL------PADAREAQRWLAERllaQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:PRK15112  111 DFPLrlntdlEPEQREKQIIETLR---QVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
11-181 6.05e-11

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 64.33  E-value: 6.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---CLMAR------VEQHLPET 79
Cdd:PRK10851    7 NIKKSFGrtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARdrkvgfVFQHYALF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 LHtQSLLQAV---LAPLPADAR---EAQRWLAERLLaQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK10851   87 RH-MTVFDNIafgLTVLPRRERpnaAAIKAKVTQLL-EMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1439757928 154 NHLDLPTLL----WLESFLQTWQGSFVLVSHD 181
Cdd:PRK10851  165 GALDAQVRKelrrWLRQLHEELKFTSVFVTHD 196
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
286-474 6.38e-11

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: 65.00  E-value: 6.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 286 QGDALPAD-RLLEMDTLHVS-----PAPGQPSLfttgvaRLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NAS 351
Cdd:TIGR02857 311 KAPVTAAPaSSLEFSGVSVAypgrrPALRPVSF------TVPPGERVALVGPSGAGKSTLLNLLLGFVDptegsiavNGV 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 352 PLPGLRLHprlhpGYYDQT--LAQLPD--EASLLEAL---TPFAPSADTRkRALIAAGF---------GWARHSQKVST- 414
Cdd:TIGR02857 385 PLADADAD-----SWRDQIawVPQHPFlfAGTIAENIrlaRPDASDAEIR-EALERAGLdefvaalpqGLDTPIGEGGAg 458
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 415 LSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLI 474
Cdd:TIGR02857 459 LSGGQAQRL-----ALARAflrdaPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALA 520
cbiO PRK13637
energy-coupling factor transporter ATPase;
21-157 7.76e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 63.14  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-------------VEQHlPETLHTQSLLQ 87
Cdd:PRK13637   24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklsdirkkvglVFQY-PEYQLFEETIE 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928  88 AVLAPLPADAREAQRWLAERLLAQM---GFTPAVMEQQTA-TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13637  103 KDIAFGPINLGLSEEEIENRVKRAMnivGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-474 8.66e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 64.44  E-value: 8.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclMARVEQHLPET-LHT--QSL----LQAVLAP-----L 93
Cdd:PRK13409   95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS--WDEVLKRFRGTeLQNyfKKLyngeIKVVHKPqyvdlI 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  94 P-------------ADAREAQRWLAERLlaqmGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:PRK13409  173 PkvfkgkvrellkkVDERGKLDEVVERL----GLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 161 LLWLESFLQTW-QGSFVL-VSHDNTLLDAVTNSSWILrdqtlhsfalpcsaarqalqeQDESAALrhkaeqkeiDRVSas 238
Cdd:PRK13409  248 RLNVARLIRELaEGKYVLvVEHDLAVLDYLADNVHIA---------------------YGEPGAY---------GVVS-- 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 239 aRRLATwgRVYDNEDLA--RKAKQMekqvaRLKDEQTELSVGPPWRLVlqgdalPADRLLEMD---------TLHVSPap 307
Cdd:PRK13409  296 -KPKGV--RVGINEYLKgyLPEENM-----RIRPEPIEFEERPPRDES------ERETLVEYPdltkklgdfSLEVEG-- 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 308 GQpslfttgvarLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--NASPLPGLRLHPRlhPGY----YDQTLAQLpdeaslL 381
Cdd:PRK13409  360 GE----------IYEGEVIGIVGPNGIGKTTFAKLLAGVLKpdEGEVDPELKISYK--PQYikpdYDGTVEDL------L 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALTPfaPSADTRKRALIAAGFGWAR-HSQKVSTLSGGERSRLLfVGLSLARYS-LLLLDEPTNHLDMEGKAALAQTLRD 459
Cdd:PRK13409  422 RSITD--DLGSSYYKSEIIKPLQLERlLDKNVKDLSGGELQRVA-IAACLSRDAdLYLLDEPSAHLDVEQRLAVAKAIRR 498
                         490
                  ....*....|....*....
gi 1439757928 460 Y----PGGVLLVSHDRQLI 474
Cdd:PRK13409  499 IaeerEATALVVDHDIYMI 517
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
26-157 1.09e-10

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: 64.42  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA------GQclmaRVEQHLPETLhtQSLLQAVLAPLPADAre 99
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQ----YISPDYDGTV--EEFLRSANTDDFGSS-- 433
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 100 aqrWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG1245   434 ---YYKTEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
286-501 1.29e-10

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 64.02  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 286 QGDALPADRLLEMDTLHVS-PAPGQPSLftTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHPrLH 363
Cdd:COG4987   324 EPAPAPGGPSLELEDVSFRyPGAGRPVL--DGLsLTLPPGERVAIVGPSGSGKSTLLALL------------LRFLD-PQ 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 364 PGYY---DQTLAQLPDE-----------------ASLLEALTPFAPSADTRK--RALIAAGFG-WARHSQK-----V--- 412
Cdd:COG4987   389 SGSItlgGVDLRDLDEDdlrrriavvpqrphlfdTTLRENLRLARPDATDEElwAALERVGLGdWLAALPDgldtwLgeg 468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 413 -STLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLIsESCNRFWLIDSAGL 489
Cdd:COG4987   469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGL-ERMDRILVLEDGRI 547
                         250
                  ....*....|..
gi 1439757928 490 TEWHSLEEVYAR 501
Cdd:COG4987   548 VEQGTHEELLAQ 559
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
18-219 1.30e-10

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 62.09  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLL----------- 86
Cdd:PRK11831   21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLfqsgalftdmn 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 --QAVLAPLpadaREAQRWLAERL-------LAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP---GN 154
Cdd:PRK11831  101 vfDNVAYPL----REHTQLPAPLLhstvmmkLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPfvgQD 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 155 HLDLPTLLWLESFLQTWQG-SFVLVSHDNTLLDAVTNSSWILRDQTLHSFALPcsaarQALQEQDE 219
Cdd:PRK11831  176 PITMGVLVKLISELNSALGvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA-----QALQANPD 236
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
18-160 1.36e-10

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: 61.36  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPetLHTqslLQAVLAPLPADA 97
Cdd:cd03244    18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI-----SKIG--LHD---LRSRISIIPQDP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  98 -------R----------EAQRW-------LAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:cd03244    88 vlfsgtiRsnldpfgeysDEELWqalervgLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167

                  ....*..
gi 1439757928 154 NHLDLPT 160
Cdd:cd03244   168 ASVDPET 174
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
11-160 1.39e-10

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


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 63.99  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFG---PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARVEQH--------LPET 79
Cdd:TIGR01193 478 DVSYSYGygsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF-SLKDIDRHtlrqfinyLPQE 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 --LHTQSLLQAVLAPLPADAREAQRWLAERLLA--------QMGFTPAVMEQQTaTLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:TIGR01193 557 pyIFSGSILENLLLGAKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGS-SISGGQKQRIALARALLTDSKVLIL 635
                         170
                  ....*....|.
gi 1439757928 150 DEPGNHLDLPT 160
Cdd:TIGR01193 636 DESTSNLDTIT 646
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
319-469 1.40e-10

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: 60.84  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NASPLPGLRLHPRLHPGYYDQtLAQLPDEASLLEALTPFAPS 390
Cdd:TIGR01189  22 TLNAGEALQVTGPNGIGKTTLLRILAGLLRpdsgevrwNGTPLAEQRDEPHENILYLGH-LPGLKPELSALENLHFWAAI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 391 ADTRKR----ALIAAGFGWARHSqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY---PGG 463
Cdd:TIGR01189 101 HGGAQRtiedALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGI 179

                  ....*.
gi 1439757928 464 VLLVSH 469
Cdd:TIGR01189 180 VLLTTH 185
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
286-470 1.40e-10

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: 63.92  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 286 QGDALPADRLLEMDTLHVSPAPGQPSLftTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRLHPRLHP 364
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVL--DGVsLDLPPGERVAILGPSGSGKSTLLATL---AGLLDPLQGEVTLDGVPV 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 365 GYYDQT--------LAQLPD--EASLLEALTPFAPSADTRK--RALIAAGFG-WARH-----SQKV----STLSGGERSR 422
Cdd:TIGR02868 400 SSLDQDevrrrvsvCAQDAHlfDTTVRENLRLARPDATDEElwAALERVGLAdWLRAlpdglDTVLgeggARLSGGERQR 479
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1439757928 423 LLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHD 470
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHH 529
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
19-158 1.46e-10

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 62.11  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQHLPETL-----HTQSLL 86
Cdd:PRK10575   26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskaFARKVAYLPQQLpaaegMTVREL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  87 QAV--------LAPLPADAREAqrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:PRK10575  106 VAIgrypwhgaLGRFGAADREK----VEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
cbiO PRK13640
energy-coupling factor transporter ATPase;
18-157 1.56e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 62.12  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGS---VSLAGQCLMAR-----------VEQHlPETlhtq 83
Cdd:PRK13640   21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKtvwdirekvgiVFQN-PDN---- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 sllQAVLAPLPADA----------REAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK13640   96 ---QFVGATVGDDVafglenravpRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171

                  ....
gi 1439757928 154 NHLD 157
Cdd:PRK13640  172 SMLD 175
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
21-157 1.67e-10

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 61.69  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV-----------SLAGQ-CLMARVEQHLPETL-------H 81
Cdd:PRK11264   20 HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarSLSQQkGLIRQLRQHVGFVFqnfnlfpH 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  82 TQSLLQAVLAPL--PADAREAQRWLAERLLAQMGFTpavmEQQTA---TLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PRK11264  100 RTVLENIIEGPVivKGEPKEEATARARELLAKVGLA----GKETSyprRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175

                  .
gi 1439757928 157 D 157
Cdd:PRK11264  176 D 176
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
18-160 1.76e-10

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: 61.48  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveqhlpeTLHTQSLLQAVLAPLPAD- 96
Cdd:cd03253    15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----------REVTLDSLRRAIGVVPQDt 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  97 -----------------AREAQRWLAERlLAQMGFTPAVMEQQTAT--------LSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:cd03253    85 vlfndtigynirygrpdATDEEVIEAAK-AAQIHDKIMRFPDGYDTivgerglkLSGGEKQRVAIARAILKNPPILLLDE 163

                  ....*....
gi 1439757928 152 PGNHLDLPT 160
Cdd:cd03253   164 ATSALDTHT 172
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
18-157 1.83e-10

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 64.20  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclMARVEQHlpETLHTQSLLQAVLAPLPADA 97
Cdd:TIGR00957  652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ--AWIQNDSLRENILFGKALNE 727
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928   98 REAQRWL-AERLLAQMGFTPA----VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR00957  728 KYYQQVLeACALLPDLEILPSgdrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
24-157 2.03e-10

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 62.40  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM---------AR-----VEQH--LpetLHTQSLLQ 87
Cdd:COG1135    25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalserelraARrkigmIFQHfnL---LSSRTVAE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 AVLAPL-----PADAREAQrwlAERLLAQMGFT------PAvmeQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:COG1135   102 NVALPLeiagvPKAEIRKR---VAELLELVGLSdkadayPS---Q----LSGGQKQRVGIARALANNPKVLLCDEATSAL 171

                  .
gi 1439757928 157 D 157
Cdd:COG1135   172 D 172
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
12-161 2.31e-10

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 60.88  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  12 VETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-------------VEQHL 76
Cdd:PRK09493    7 VSKHFGPtqVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvderlirqeagmVFQQF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  77 PETLHTQSLLQAVLAPLP--ADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:PRK09493   87 YLFPHLTALENVMFGPLRvrGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165

                  ....*..
gi 1439757928 155 HLDlPTL 161
Cdd:PRK09493  166 ALD-PEL 171
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
18-217 2.80e-10

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 61.18  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------------MARVEQHlPETLHTQS 84
Cdd:PRK13638   15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllalrqqVATVFQD-PEQQIFYT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAVLAPLPADAREAQRWLAERLLAQMGFTPA--VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLL 162
Cdd:PRK13638   94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAqhFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 163 WLESFLQ--TWQGSFVLV-SHDNTLLDAVTNSSWILRDQTLHSFALPCSA-ARQALQEQ 217
Cdd:PRK13638  174 QMIAIIRriVAQGNHVIIsSHDIDLIYEISDAVYVLRQGQILTHGAPGEVfACTEAMEQ 232
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
24-152 3.81e-10

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 62.24  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---------CLMARV-----EQHL-PETLHTQSLLqa 88
Cdd:PRK11288   24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVaiiyqELHLvPEMTVAENLY-- 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928  89 vLAPLPA-----DAREAQRWLAERlLAQMG--FTPavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11288  102 -LGQLPHkggivNRRLLNYEAREQ-LEHLGvdIDP---DTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
35-180 4.77e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 60.31  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  35 LIGHNGCGKSTLLQVLDGTL-----APTSGSVSLAGQC--------LMARVEQ--HLPETLHTQSLLQAV-----LAPLP 94
Cdd:PRK14247   34 LMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDifkmdvieLRRRVQMvfQIPNPIPNLSIFENValglkLNRLV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  95 ADAREAQ---RWLAERllAQM-GFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES-FLQ 169
Cdd:PRK14247  114 KSKKELQervRWALEK--AQLwDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESlFLE 191
                         170
                  ....*....|..
gi 1439757928 170 TWQG-SFVLVSH 180
Cdd:PRK14247  192 LKKDmTIVLVTH 203
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
23-157 4.80e-10

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 62.43  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQC--------LMARVEQH----------LPETLHTQS 84
Cdd:PRK10535   27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldadaLAQLRREHfgfifqryhlLSHLTAAQN 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928  85 L-LQAVLAPLPADAREAQrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10535  107 VeVPAVYAGLERKQRLLR---AQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
10-152 4.93e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 61.94  E-value: 4.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARveqhlpetlHTQSLLQAV 89
Cdd:PRK10762  258 LKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR---------SPQDGLANG 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 LAPLPAD-----------AREAQRWLAERLLAQMGF---------------------TPAvMEQQTATLSGGQHTRLLLA 137
Cdd:PRK10762  329 IVYISEDrkrdglvlgmsVKENMSLTALRYFSRAGGslkhadeqqavsdfirlfnikTPS-MEQAIGLLSGGNQQKVAIA 407
                         170
                  ....*....|....*
gi 1439757928 138 RALIRQPDLLLLDEP 152
Cdd:PRK10762  408 RGLMTRPKVLILDEP 422
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
23-502 5.83e-10

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 61.74  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGT--LAPTSGSV----------------SLAGQ----C------------- 67
Cdd:TIGR03269  19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvCggtlepeevdfwn 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  68 --------LMARVEQHLPETL---HTQSLLQAVLAPLPADAREAQRWL--AERLLAQMGFTPAVMeQQTATLSGGQHTRL 134
Cdd:TIGR03269  99 lsdklrrrIRKRIAIMLQRTFalyGDDTVLDNVLEALEEIGYEGKEAVgrAVDLIEMVQLSHRIT-HIARDLSGGEKQRV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLDLPTllwlesflqtwqgsfVLVSHdNTLLDAVTNS--SWILrdqTLHsfaLPcsaarQ 212
Cdd:TIGR03269 178 VLARQLAKEPFLFLADEPTGTLDPQT---------------AKLVH-NALEEAVKASgiSMVL---TSH---WP-----E 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 213 ALQEQDESAALRHKAEQKEI---DRVSasarrlatwgrvydnedlarkAKQMEkQVARLKDEqtelsvgppwRLVLQGDa 289
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEgtpDEVV---------------------AVFME-GVSEVEKE----------CEVEVGE- 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 290 lPADRLLEMDTLHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLL------------------WQQMNNAS 351
Cdd:TIGR03269 278 -PIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsgevnvrvgdeWVDMTKPG 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 352 PLPGLRLHPRLhpGYYDQTLAQLPDEA---SLLEALTPFAPSADTRKRALI---AAGFG--WARH--SQKVSTLSGGERS 421
Cdd:TIGR03269 357 PDGRGRAKRYI--GILHQEYDLYPHRTvldNLTEAIGLELPDELARMKAVItlkMVGFDeeKAEEilDKYPDELSEGERH 434
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 422 RLLFVGLSLARYSLLLLDEPTNHLD-----------MEGKAALAQTLrdypggvLLVSHDRQLISESCNRFWLIDSAGLT 490
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDpitkvdvthsiLKAREEMEQTF-------IIVSHDMDFVLDVCDRAALMRDGKIV 507
                         570
                  ....*....|..
gi 1439757928 491 EWHSLEEVYARL 502
Cdd:TIGR03269 508 KIGDPEEIVEEL 519
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
319-504 6.51e-10

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 59.71  E-value: 6.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLlwqqmnnasplpglrlhprlhpgyydqtLAQL--PDE---------ASLLEALTPF 387
Cdd:COG1134    48 EVERGESVGIIGRNGAGKSTLLKL----------------------------IAGIlePTSgrvevngrvSALLELGAGF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 APS------------------ADTRKR-ALIA--AGFGWARHsQKVSTLSGGERSRLLFvGLSLA-RYSLLLLDEptnhl 445
Cdd:COG1134   100 HPEltgreniylngrllglsrKEIDEKfDEIVefAELGDFID-QPVKTYSSGMRARLAF-AVATAvDPDILLVDE----- 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 446 dmegkaALA--------------QTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQA 504
Cdd:COG1134   173 ------VLAvgdaafqkkclariRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEA 239
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
24-189 6.98e-10

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 60.28  E-value: 6.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLLQAVLAPLPAD------- 96
Cdd:PRK15056   27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDvvmmgry 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  97 --------AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFL 168
Cdd:PRK15056  107 ghmgwlrrAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
                         170       180
                  ....*....|....*....|...
gi 1439757928 169 QTW--QGSFVLVSHDNtlLDAVT 189
Cdd:PRK15056  186 RELrdEGKTMLVSTHN--LGSVT 206
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
26-474 7.29e-10

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: 61.72  E-value: 7.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPT-----------------SGS---------------VSLAGQclmaRVE 73
Cdd:COG1245    95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTelqdyfkklangeikVAHKPQ----YVD 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  74 QhLPETLH--TQSLLQAVlaplpaDAREAQRWLAERLlaqmGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:COG1245   171 L-IPKVFKgtVRELLEKV------DERGKLDELAEKL----GLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 152 PGNHLDLPTLLWLESFLQTWQG---SFVLVSHDNTLLDAVTNSSWILrdqtlhsfalpcsaarqalqeQDESAALrhkae 228
Cdd:COG1245   239 PSSYLDIYQRLNVARLIRELAEegkYVLVVEHDLAILDYLADYVHIL---------------------YGEPGVY----- 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 229 qkeiDRVSasaRRLATwgRVYDNEDLA--RKAKQMekqvaRLKDEQTELSVGPPwrlvlqGDALPADRLLEMDTLHVSPa 306
Cdd:COG1245   293 ----GVVS---KPKSV--RVGINQYLDgyLPEENV-----RIRDEPIEFEVHAP------RREKEEETLVEYPDLTKSY- 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 307 pGQPSLFTTGvARLRSGDRVAIMGRNGGGKSSLLRLLW--QQMNNASPLPGLRLHPRlhPGY----YDQTLAQLpdeasL 380
Cdd:COG1245   352 -GGFSLEVEG-GEIREGEVLGIVGPNGIGKTTFAKILAgvLKPDEGEVDEDLKISYK--PQYispdYDGTVEEF-----L 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 381 LEALTPFAPSadTRKRALIAAGFGWAR-HSQKVSTLSGGERSRLLfVGLSLARYS-LLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:COG1245   423 RSANTDDFGS--SYYKTEIIKPLGLEKlLDKNVKDLSGGELQRVA-IAACLSRDAdLYLLDEPSAHLDVEQRLAVAKAIR 499
                         490       500
                  ....*....|....*....|
gi 1439757928 459 DYPGG----VLLVSHDRQLI 474
Cdd:COG1245   500 RFAENrgktAMVVDHDIYLI 519
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
321-458 7.93e-10

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: 58.72  E-value: 7.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 321 RSGDRVAIMGRNGGGKSSLLRLLWQQMN----------NASPLPglRLHPRLHPGYYDQtlaqlpdEASLLEALTPfaps 390
Cdd:cd03213    33 KPGELTAIMGPSGAGKSTLLNALAGRRTglgvsgevliNGRPLD--KRSFRKIIGYVPQ-------DDILHPTLTV---- 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 391 adtrKRALiaagfgwaRHSQKVSTLSGGERSRLLfVGLSL-ARYSLLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:cd03213   100 ----RETL--------MFAAKLRGLSGGERKRVS-IALELvSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
318-476 8.06e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 58.40  E-value: 8.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 318 ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTLA---QLPDEASLLEALTPFAP---- 389
Cdd:NF040873   13 LTIPAGSLTAVVGPNGSGKSTLLKVL---AGVLRPTSGtVRRAGGARVAYVPQRSEvpdSLPLTVRDLVAMGRWARrglw 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 390 ---SADTRK---RALIAAGFGWARHSQkVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG- 462
Cdd:NF040873   90 rrlTRDDRAavdDALERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAr 168
                         170
                  ....*....|....*.
gi 1439757928 463 --GVLLVSHDRQLISE 476
Cdd:NF040873  169 gaTVVVVTHDLELVRR 184
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
15-151 8.63e-10

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 61.14  E-value: 8.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  15 AFGPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL----MARVEQHLPETLHTQSLLQAVL 90
Cdd:PRK10522  338 SVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqPEDYRKLFSAVFTDFHLFDQLL 413
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928  91 AP--LPADAREAQRWLaERLlaQMGFTPAVMEQQTAT--LSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK10522  414 GPegKPANPALVEKWL-ERL--KMAHKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDE 475
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
319-480 9.42e-10

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 59.06  E-value: 9.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS--------PLPGLRLHPRLHPGYYDQTLAQLPDEA---------SLL 381
Cdd:cd03257    27 SIKKGETLGLVGESGSGKSTLARAILGLLKPTSgsiifdgkDLLKLSRRLRKIRRKEIQMVFQDPMSSlnprmtigeQIA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALT----PFAPSADTRKRALIAAGFGWARH--SQKVSTLSGGERSRLLFVgLSLA-RYSLLLLDEPTNHLDMEGKAALA 454
Cdd:cd03257   107 EPLRihgkLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAIA-RALAlNPKLLIADEPTSALDVSVQAQIL 185
                         170       180       190
                  ....*....|....*....|....*....|
gi 1439757928 455 QTLRD----YPGGVLLVSHDRQLISESCNR 480
Cdd:cd03257   186 DLLKKlqeeLGLTLLFITHDLGVVAKIADR 215
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
302-474 1.21e-09

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 58.97  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 302 HVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTL---AQLPDE 377
Cdd:PRK09544    9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV---LGLVAPDEGvIKRNGKLRIGYVPQKLyldTTLPLT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 378 ASLLEALTPFAPSADTrkraLIAAGFGWARH--SQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAAL-- 453
Cdd:PRK09544   86 VNRFLRLRPGTKKEDI----LPALKRVQAGHliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALyd 161
                         170       180
                  ....*....|....*....|...
gi 1439757928 454 --AQTLRDYPGGVLLVSHDRQLI 474
Cdd:PRK09544  162 liDQLRRELDCAVLMVSHDLHLV 184
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
24-158 1.43e-09

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 58.94  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARV------EQHLPETL---------- 80
Cdd:COG4604    21 SLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsreLAKRlailrqENHINSRLtvrelvafgr 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  81 --HTQSLLQAvlaplpADAReaqrwLAERLLAQMGFTPavMEQQTA-TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4604   101 fpYSKGRLTA------EDRE-----IIDEAIAYLDLED--LADRYLdELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167

                  .
gi 1439757928 158 L 158
Cdd:COG4604   168 M 168
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
36-181 1.58e-09

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 59.03  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  36 IGHNGCGKSTLLQVLDGT--LAPT---SGSVSLAGQCLMAR-------------VEQH---LPETLHTQSLLQAVLAPLP 94
Cdd:PRK14243   42 IGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPdvdpvevrrrigmVFQKpnpFPKSIYDNIAYGARINGYK 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  95 ADAREaqrwLAERLLAQMGFTPAV---MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTW 171
Cdd:PRK14243  122 GDMDE----LVERSLRQAALWDEVkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL 197
                         170
                  ....*....|..
gi 1439757928 172 --QGSFVLVSHD 181
Cdd:PRK14243  198 keQYTIIIVTHN 209
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
34-181 1.75e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 58.91  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  34 GLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----MARVEQ-----------HLPETLHTQSLLQAVLAPLPA-- 95
Cdd:PRK14246   40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdIFQIDAiklrkevgmvfQQPNPFPHLSIYDNIAYPLKShg 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 --DAREAQRwLAERLLAQMGFTPAV---MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQT 170
Cdd:PRK14246  120 ikEKREIKK-IVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
                         170
                  ....*....|...
gi 1439757928 171 WQG--SFVLVSHD 181
Cdd:PRK14246  199 LKNeiAIVIVSHN 211
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
10-152 2.23e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 60.06  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA-----RVEQ---HLPE--- 78
Cdd:PRK15439  269 LTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqRLARglvYLPEdrq 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  79 ----------TLHTQSLLQAVLAPLPADAREAQRWlaERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK15439  349 ssglyldaplAWNVCALTHNRRGFWIKPARENAVL--ERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426

                  ....
gi 1439757928 149 LDEP 152
Cdd:PRK15439  427 VDEP 430
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
17-151 2.74e-09

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: 59.81  E-value: 2.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  17 GPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-MARVEQHlpetlhtQSLLQAVLA---- 91
Cdd:COG4615   349 GPI----DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAY-------RQLFSAVFSdfhl 417
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  92 -------PLPADAREAQRWLaERLlaQMGFTPAVMEQQTAT--LSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:COG4615   418 fdrllglDGEADPARARELL-ERL--ELDHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDE 483
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
10-188 3.01e-09

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: 57.15  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDG--TLAPTSGSVSLAGQclmarveqhlpetlhtqSLLQ 87
Cdd:cd03217     6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE-----------------DITD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 avlapLPADAReaqrwlaerllAQMGFT-----PAVMEQQT---------ATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:cd03217    69 -----LPPEER-----------ARLGIFlafqyPPEIPGVKnadflryvnEGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1439757928 154 NHLDLPTLLWLESFLQTWQG---SFVLVSHDNTLLDAV 188
Cdd:cd03217   133 SGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYI 170
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-157 3.43e-09

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: 59.31  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVetAFG------PLFNSLSFTLKKGDRIGLIGHNGCGKS----TLLQVLDGTLAPTSGSVSLAGQCLMA 70
Cdd:COG4172     3 SMPLLSVEDLSV--AFGqgggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  71 RVEQHL--------------PET----LHT--QSLLQAVLAPLPADAREAQRWLAErLLAQMGFTPAvmEQQTAT----L 126
Cdd:COG4172    81 LSERELrrirgnriamifqePMTslnpLHTigKQIAEVLRLHRGLSGAAARARALE-LLERVGIPDP--ERRLDAyphqL 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1439757928 127 SGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4172   158 SGGQRQRVMIAMALANEPDLLIADEPTTALD 188
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
18-157 6.37e-09

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: 58.57  E-value: 6.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------QCL---MARVEQHLpeTLHTQSLL 86
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlASLrrqVALVSQDV--VLFNDTIA 423
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  87 QAVLAPLPADAREAQRWLAERLLAQMGFTPAVME-------QQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
320-485 6.72e-09

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: 56.39  E-value: 6.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhPGYYdqtlaqLPDE---------ASLLEALTPFAPS 390
Cdd:cd03220    45 VPRGERIGLIGRNGAGKSTLLRLL--------------------AGIY------PPDSgtvtvrgrvSSLLGLGGGFNPE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 391 ADTRKRA-LIAAGFGWARHS-------------------QKVSTLSGGERSRLLFvGLSLA-RYSLLLLDEPTNHLD--- 446
Cdd:cd03220    99 LTGRENIyLNGRLLGLSRKEidekideiiefselgdfidLPVKTYSSGMKARLAF-AIATAlEPDILLIDEVLAVGDaaf 177
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1439757928 447 MEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03220   178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLE 216
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
319-486 6.88e-09

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 56.29  E-value: 6.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRL---LWQQMN-----NASPLPGLRLHPRLHPGyydqtLAQLPDEASLLEALTP---F 387
Cdd:cd03224    22 TVPEGEIVALLGRNGAGKTTLLKTimgLLPPRSgsirfDGRDITGLPPHERARAG-----IGYVPEGRRIFPELTVeenL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 APSADTRKRALIAAGFGWA---------RHSQKVSTLSGGERsRLLFVGLSL-ARYSLLLLDEPTnhldmEGKA------ 451
Cdd:cd03224    97 LLGAYARRRAKRKARLERVyelfprlkeRRKQLAGTLSGGEQ-QMLAIARALmSRPKLLLLDEPS-----EGLApkivee 170
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1439757928 452 --ALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDS 486
Cdd:cd03224   171 ifEAIRELRDEGVTILLVEQNARFALEIADRAYVLER 207
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
319-477 7.15e-09

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: 56.34  E-value: 7.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLW--------------QQMNNASP--LPGLRlhpRLHPGYYDQTLAQLPDeASLLE 382
Cdd:cd03255    26 SIEKGEFVAIVGPSGSGKSTLLNILGgldrptsgevrvdgTDISKLSEkeLAAFR---RRHIGFVFQSFNLLPD-LTALE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 -ALTPF----APSADTRKRA---LIAAGFGwARHSQKVSTLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEG 449
Cdd:cd03255   102 nVELPLllagVPKKERRERAeelLERVGLG-DRLNHYPSELSGGQQQR-----VAIARAlandpKIILADEPTGNLDSET 175
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1439757928 450 KAALAQTLRD----YPGGVLLVSHDRQLISES 477
Cdd:cd03255   176 GKEVMELLRElnkeAGTTIVVVTHDPELAEYA 207
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
18-163 7.30e-09

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: 58.87  E-value: 7.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------HLPE--------TLHTQ 83
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDvhqnmgYCPQfdaiddllTGREH 2032
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   84 SLLQAVLAPLPADAREAqrwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT--L 161
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEK---VANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQArrM 2108

                   ..
gi 1439757928  162 LW 163
Cdd:TIGR01257 2109 LW 2110
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
24-152 7.86e-09

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 58.11  E-value: 7.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGdRI-GLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------MAR------VEQH--LPETLhtqSLLQA 88
Cdd:COG3845    25 SLTVRPG-EIhALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprDAIalgigmVHQHfmLVPNL---TVAEN 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928  89 V---LAPLPA---DAREAQRWLAErLLAQMGFT--PavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG3845   101 IvlgLEPTKGgrlDRKAARARIRE-LSERYGLDvdP---DAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
24-157 8.11e-09

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 57.50  E-value: 8.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPET-------------LHTQSLLQAVL 90
Cdd:PRK11153   25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqigmifqhfnlLSSRTVFDNVA 104
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  91 APLPA---DAREAQRWLAErLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11153  105 LPLELagtPKAEIKARVTE-LLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
4-158 8.13e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.01  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQClMARVEQ--------H 75
Cdd:PRK13543   11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRsrfmaylgH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  76 LPETLHTQSLLQAVLAPLPADAREAQRWLAERL--LAQMGFTPAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK13543   90 LPGLKADLSTLENLHFLCGLHGRRAKQMPGSALaiVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPY 165

                  ....*
gi 1439757928 154 NHLDL 158
Cdd:PRK13543  166 ANLDL 170
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1-152 8.18e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 58.14  E-value: 8.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM----ARVEQ-- 74
Cdd:PRK15439    8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpAKAHQlg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  75 -----HLPETLHTQSLLQAVLAPLPADAREAQRwlAERLLAQMG--FTPAVmeqQTATLSGGQHTRLLLARALIRQPDLL 147
Cdd:PRK15439   88 iylvpQEPLLFPNLSVKENILFGLPKRQASMQK--MKQLLAALGcqLDLDS---SAGSLEVADRQIVEILRGLMRDSRIL 162

                  ....*
gi 1439757928 148 LLDEP 152
Cdd:PRK15439  163 ILDEP 167
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
29-203 9.52e-09

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: 54.30  E-value: 9.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   29 KGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlPETLHTQSLLQAVLAPLPADAREaqrwlaerl 108
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------GEDILEEVLDQLLLIIVGGKKAS--------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  109 laqmgftpavmeqqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAV 188
Cdd:smart00382  61 -----------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
                          170
                   ....*....|....*
gi 1439757928  189 TNSSWILRDQTLHSF 203
Cdd:smart00382 124 NDEKDLGPALLRRRF 138
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
11-197 1.11e-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: 57.53  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL--APTSGSVSLAGQCLMAR------------VEQ 74
Cdd:TIGR02633   6 GIVKTFGGVkaLDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASnirdteragiviIHQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  75 HL---PET-------LHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAVMEqqtatLSGGQHTRLLLARALIRQP 144
Cdd:TIGR02633  86 ELtlvPELsvaenifLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-----YGGGQQQLVEIAKALNKQA 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 145 DLLLLDEPGNHL---DLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:TIGR02633 161 RLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
18-157 1.32e-08

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: 58.10  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---MARVEQHL---PE---TLHTQSLLQA 88
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnLDAVRQSLgmcPQhniLFHHLTVAEH 1023
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928   89 VL--APLPADAREAQRWLAERLLAQMGFTPAVMEqQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR01257 1024 ILfyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
320-459 1.62e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 55.79  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLR-----------------LLWQQMNNASPLPGLRLHPRLHPGYYDQTLaQLPDEASLLE 382
Cdd:PRK09984   27 IHHGEMVALLGPSGSGKSTLLRhlsglitgdksagshieLLGRTVQREGRLARDIRKSRANTGYIFQQF-NLVNRLSVLE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 AL-------TP--------FAPSADTRK-RALIAAGFGWARHsQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLD 446
Cdd:PRK09984  106 NVligalgsTPfwrtcfswFTREQKQRAlQALTRVGMVHFAH-QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
                         170
                  ....*....|...
gi 1439757928 447 MEGKAALAQTLRD 459
Cdd:PRK09984  185 PESARIVMDTLRD 197
F420-0_ABC_ATP TIGR03873
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ...
323-485 1.71e-08

proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.


Pssm-ID: 163585 [Multi-domain]  Cd Length: 256  Bit Score: 55.59  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLL---WQQMNNASPLPGLRLH--PRLHPGYYDQTLAQLPDEASLLEAL-------TPF--- 387
Cdd:TIGR03873  27 GSLTGLLGPNGSGKSTLLRLLagaLRPDAGTVDLAGVDLHglSRRARARRVALVEQDSDTAVPLTVRdvvalgrIPHrsl 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 ----APSADTRKRALIAAGFGWARHSQKVSTLSGGERSRLlFVGLSLA-RYSLLLLDEPTNHLDMEGKAALAQTLRDYPG 462
Cdd:TIGR03873 107 wagdSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRV-HVARALAqEPKLLLLDEPTNHLDVRAQLETLALVRELAA 185
                         170       180
                  ....*....|....*....|....*.
gi 1439757928 463 G---VLLVSHDRQLISESCNRFWLID 485
Cdd:TIGR03873 186 TgvtVVAALHDLNLAASYCDHVVVLD 211
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
21-157 1.76e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 55.91  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL----MARVEQHL------PETLHTQSLLQAVL 90
Cdd:PRK13648   26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLRKHIgivfqnPDNQFVGSIVKYDV 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928  91 A------PLPADarEAQRWLAErLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13648  106 AfglenhAVPYD--EMHRRVSE-ALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
23-157 1.77e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 55.90  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----------PETLHTQSLLQAVLAP 92
Cdd:PRK13647   24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdPDDQVFSSTVWDDVAF 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  93 LPADAREAQRWLAERL---LAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13647  104 GPVNMGLDKDEVERRVeeaLKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
14-65 2.29e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 55.38  E-value: 2.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1439757928  14 TAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG 65
Cdd:PRK13632   19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG 70
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
313-470 2.39e-08

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: 54.61  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 313 FTTGVARLRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNASPLPglrLHPRlHPGYYDQTLAQLP 375
Cdd:cd03297    13 FTLKIDFDLNEEVTGIFGASGAGKSTLLRCIaglekpdggtivlngtvLFDSRKKINLP---PQQR-KIGLVFQQYALFP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 376 D---EASLLEALTPFAPSADTRKRALIAAGFGWAR-HSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKA 451
Cdd:cd03297    89 HlnvRENLAFGLKRKRNREDRISVDELLDLLGLDHlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
                         170       180
                  ....*....|....*....|...
gi 1439757928 452 ALAQTLR----DYPGGVLLVSHD 470
Cdd:cd03297   169 QLLPELKqikkNLNIPVIFVTHD 191
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
27-190 2.41e-08

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: 53.73  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  27 LKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlhtqsllqavlaplpadareaqrwlae 106
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 107 rllaqmgFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLL----WLESFLQTWQGSFVLVSHDN 182
Cdd:cd03222    61 -------ITPVY-KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLnaarAIRRLSEEGKKTALVVEHDL 132

                  ....*...
gi 1439757928 183 TLLDAVTN 190
Cdd:cd03222   133 AVLDYLSD 140
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
21-478 2.81e-08

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 56.64  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKS-TLLQVLDGTLAP----TSGSVSLAGQCLMARVEQHLPET---------------- 79
Cdd:PRK15134   26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkiamifqepmvsl 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 --LHT-QSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAV--MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:PRK15134  106 npLHTlEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAkrLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 155 HLDLPT----LLWLESFLQTWQGSFVLVSHDntlLDAVtnsswilrdqtlhsfalpcsaarqalqeqdesaalrhkaeqk 230
Cdd:PRK15134  186 ALDVSVqaqiLQLLRELQQELNMGLLFITHN---LSIV------------------------------------------ 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 231 eidrvsasaRRLAtwgrvyDNEDLARKAKQMEKQVARlkdeqtELSVGP--PWRLVL-----QGDALPADR----LLEMD 299
Cdd:PRK15134  221 ---------RKLA------DRVAVMQNGRCVEQNRAA------TLFSAPthPYTQKLlnsepSGDPVPLPEpaspLLDVE 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 300 TLHVSpAPGQPSLFTTGVAR----------LRSGDRVAIMGRNGGGKSS----LLRLLWQQMN---NASPLPGLRLHPRL 362
Cdd:PRK15134  280 QLQVA-FPIRKGILKRTVDHnvvvknisftLRPGETLGLVGESGSGKSTtglaLLRLINSQGEiwfDGQPLHNLNRRQLL 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 363 HPGYYDQTLAQLPDEA---------SLLEALTPFAP--SADTRKRALIAA----GFGWARHSQKVSTLSGGERSRLLFVG 427
Cdd:PRK15134  359 PVRHRIQVVFQDPNSSlnprlnvlqIIEEGLRVHQPtlSAAQREQQVIAVmeevGLDPETRHRYPAEFSGGQRQRIAIAR 438
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 428 LSLARYSLLLLDEPTNHLDMEGKA---ALAQTLR-DYPGGVLLVSHDRQLISESC 478
Cdd:PRK15134  439 ALILKPSLIILDEPTSSLDKTVQAqilALLKSLQqKHQLAYLFISHDLHVVRALC 493
PLN03073 PLN03073
ABC transporter F family; Provisional
250-475 3.20e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.41  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 250 DNEDLARKAKQMEKQvaRLKDEQTELS------VGPPWRLVLQG--DALPADRLLEMDTLHVSPapGQPSLFTTGVARLR 321
Cdd:PLN03073  126 DLAKIERRKRKEERQ--REVQYQAHVAemeaakAGMPGVYVNHDgnGGGPAIKDIHMENFSISV--GGRDLIVDASVTLA 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 322 SGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRLHPRLHPGYYDQTLAQ------------LPDEASLL--EALTPF 387
Cdd:PLN03073  202 FGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQEVVGDDTTALQcvlntdiertqlLEEEAQLVaqQRELEF 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 -----------------------------------APSADTRKrALIAAGFGWARHSQ--KVSTLSGGERSRLLFVGLSL 430
Cdd:PLN03073  282 etetgkgkgankdgvdkdavsqrleeiykrlelidAYTAEARA-ASILAGLSFTPEMQvkATKTFSGGWRMRIALARALF 360
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1439757928 431 ARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLIS 475
Cdd:PLN03073  361 IEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLN 405
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
20-157 3.60e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 54.63  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLA--PTSGS-VSLAGQCLM--ARVEQHLPET-LHTQSLLQ------ 87
Cdd:PRK09984   20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQreGRLARDIRKSrANTGYIFQqfnlvn 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 --AVLAPLPADA-------REAQRWL-------AERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK09984  100 rlSVLENVLIGAlgstpfwRTCFSWFtreqkqrALQALTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178

                  ....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK09984  179 PIASLD 184
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
28-186 4.04e-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: 54.68  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  28 KKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVS-----------LAGQCLMARVEQHLPETLHTQSLLQAV-LAPLPA 95
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLEGDVKVIVKPQYVdLIPKAV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 DA-------REAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFL 168
Cdd:cd03236   104 KGkvgellkKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
                         170       180
                  ....*....|....*....|.
gi 1439757928 169 Q---TWQGSFVLVSHDNTLLD 186
Cdd:cd03236   183 RelaEDDNYVLVVEHDLAVLD 203
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
18-160 5.62e-08

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: 53.57  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPetLHTqslLQAVLAPLPADA 97
Cdd:cd03369    22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----STIP--LED---LRSSLTIIPQDP 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  98 -------REAQRWLAERLLAQMgFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:cd03369    92 tlfsgtiRSNLDPFDEYSDEEI-YGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
23-157 5.85e-08

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 53.73  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG----------------QCLMARVEQHLpetLHTQSLL 86
Cdd:PRK10908   21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQIGMIFQDHHL---LMDRTVY 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928  87 QAVLAPL--PADAREAQRWLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10908   98 DNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKA-KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
cbiO PRK13642
energy-coupling factor transporter ATPase;
20-195 6.32e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 54.33  E-value: 6.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----------PETLHTQSLLQAV 89
Cdd:PRK13642   23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrkigmvfqnPDNQFVGATVEDD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  90 LA------PLPADarEAQRWLAERLLA--QMGFTpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPT- 160
Cdd:PRK13642  103 VAfgmenqGIPRE--EMIKRVDEALLAvnMLDFK----TREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD-PTg 175
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1439757928 161 ----LLWLESFLQTWQGSFVLVSHDntlLDAVTNSSWIL 195
Cdd:PRK13642  176 rqeiMRVIHEIKEKYQLTVLSITHD---LDEAASSDRIL 211
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
19-157 6.53e-08

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 55.44  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAG-----QCLMAR---VEQH---LP-----ET 79
Cdd:TIGR00955  40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGmpidaKEMRAIsayVQQDdlfIPtltvrEH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 LHTQSLLQavlapLPADAREAQRWLA-ERLLAQMGFTPAvmeQQTAT--------LSGGQHTRLLLARALIRQPDLLLLD 150
Cdd:TIGR00955 120 LMFQAHLR-----MPRRVTKKEKRERvDEVLQALGLRKC---ANTRIgvpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191

                  ....*..
gi 1439757928 151 EPGNHLD 157
Cdd:TIGR00955 192 EPTSGLD 198
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
27-157 6.70e-08

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 54.65  E-value: 6.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  27 LKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARVEqhlPETLHTQSLLQA-VLAP------------- 92
Cdd:PRK11000   26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVP---PAERGVGMVFQSyALYPhlsvaenmsfglk 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  93 -LPADAREAQRWL---AERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11000  102 lAGAKKEEINQRVnqvAEVL--QLA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
319-480 7.18e-08

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: 52.88  E-value: 7.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS------PLPGLRLHPRLHPG-YYDQTLAQLPDEASLLEALTPFAP-- 389
Cdd:cd03231    22 TLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAgrvllnGGPLDFQRDSIARGlLYLGHAPGIKTTLSVLENLRFWHAdh 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 390 SADTRKRALIAAGFGWARHSqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLL 466
Cdd:cd03231   102 SDEQVEEALARVGLNGFEDR-PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARggmVVL 180
                         170
                  ....*....|....
gi 1439757928 467 VSHDRQLISESCNR 480
Cdd:cd03231   181 TTHQDLGLSEAGAR 194
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
18-185 7.23e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.02  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTlAPTSGSVSLAgqcLMAR----------VEQHL---PETLHTQ- 83
Cdd:PRK10938  274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGYSNDLT---LFGRrrgsgetiwdIKKHIgyvSSSLHLDy 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  84 ------------------SLLQAVlaplpadaREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPD 145
Cdd:PRK10938  350 rvstsvrnvilsgffdsiGIYQAV--------SDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPT 421
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1439757928 146 LLLLDEPGNHLDLPTLLWLESFLQtwqgsfVLVSHDNTLL 185
Cdd:PRK10938  422 LLILDEPLQGLDPLNRQLVRRFVD------VLISEGETQL 455
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
320-473 7.60e-08

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 53.28  E-value: 7.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLW--------------QQMNNASPLPGLRLHPRlHPGYYDQTLAQLPDEASLLEALT 385
Cdd:PRK11629   32 IGEGEMMAIVGSSGSGKSTLLHLLGgldtptsgdvifngQPMSKLSSAAKAELRNQ-KLGFIYQFHHLLPDFTALENVAM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 PF----APSADTRKRAL-IAAGFGWARHSQ-KVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTL-- 457
Cdd:PRK11629  111 PLligkKKPAEINSRALeMLAAVGLEHRANhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLge 190
                         170
                  ....*....|....*...
gi 1439757928 458 --RDYPGGVLLVSHDRQL 473
Cdd:PRK11629  191 lnRLQGTAFLVVTHDLQL 208
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
21-157 7.65e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 54.04  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-----------VEQHLPETLHTQSLLQAV 89
Cdd:PRK13652   21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevrkfvglVFQNPDDQIFSPTVEQDI 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928  90 lAPLPADAREAQRWLAERL---LAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13652  101 -AFGPINLGLDEETVAHRVssaLHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
24-157 7.95e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.02  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVslagQCLMARVEQHLPETLhtQSLLQA--------VLAPLPA 95
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER----QSQFSHITRLSFEQL--QKLVSDewqrnntdMLSPGED 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928  96 D----ARE------AQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10938   97 DtgrtTAEiiqdevKDPARCEQLAQQFGIT-ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
21-152 7.99e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 54.94  E-value: 7.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAPT---SGSVSLAGQCLMARveqHLPET-------LHTQSLLQAVL 90
Cdd:PRK13549   22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQAS---NIRDTeragiaiIHQELALVKEL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  91 APL-----------------PADAREAQRWLAErllAQMGFTPA--VMEqqtatLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13549   98 SVLeniflgneitpggimdyDAMYLRAQKLLAQ---LKLDINPAtpVGN-----LGLGQQQLVEIAKALNKQARLLILDE 169

                  .
gi 1439757928 152 P 152
Cdd:PRK13549  170 P 170
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
18-186 1.13e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 52.26  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---MARVEQHLPETLHtQSLLQAVLAplp 94
Cdd:PRK13540   15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdLCTYQKQLCFVGH-RSGINPYLT--- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  95 adAREAQRWLAERLLAQMGFTPAV--------MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES 166
Cdd:PRK13540   91 --LRENCLYDIHFSPGAVGITELCrlfslehlIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
                         170       180
                  ....*....|....*....|...
gi 1439757928 167 FLQTWQ---GSFVLVSHDNTLLD 186
Cdd:PRK13540  169 KIQEHRakgGAVLLTSHQDLPLN 191
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
3-152 1.31e-07

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 54.26  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   3 TLLTAHALHVETAFG-PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----MARVEQ-- 74
Cdd:COG3845   256 VVLEVENLSVRDDRGvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRLgv 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  75 -HLPETLHTQ------SLLQ-AVL-----APLPA----DAREAQRWlAERLLAQMGFTPAVMEQQTATLSGG--QhtRLL 135
Cdd:COG3845   336 aYIPEDRLGRglvpdmSVAEnLILgryrrPPFSRggflDRKAIRAF-AEELIEEFDVRTPGPDTPARSLSGGnqQ--KVI 412
                         170
                  ....*....|....*..
gi 1439757928 136 LARALIRQPDLLLLDEP 152
Cdd:COG3845   413 LARELSRDPKLLIAAQP 429
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
13-157 1.33e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 53.17  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  13 ETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV-----------------SLAG--------QC 67
Cdd:PRK13633   19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenlwdirNKAGmvfqnpdnQI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  68 LMARVEQHL---PETLHTQsllqavlaplPADAREAqrwlAERLLAQMG------FTPAVmeqqtatLSGGQHTRLLLAR 138
Cdd:PRK13633   99 VATIVEEDVafgPENLGIP----------PEEIRER----VDESLKKVGmyeyrrHAPHL-------LSGGQKQRVAIAG 157
                         170
                  ....*....|....*....
gi 1439757928 139 ALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13633  158 ILAMRPECIIFDEPTAMLD 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
396-485 1.35e-07

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: 51.55  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 396 RALIAAGFGWARHSQKVSTLSGGERSRL---LFVGLSLARySLLLLDEPTNHLDMEGKAALA---QTLRDYPGGVLLVSH 469
Cdd:cd03238    69 QFLIDVGLGYLTLGQKLSTLSGGELQRVklaSELFSEPPG-TLFILDEPSTGLHQQDINQLLeviKGLIDLGNTVILIEH 147
                          90
                  ....*....|....*.
gi 1439757928 470 DRQLISESCnrfWLID 485
Cdd:cd03238   148 NLDVLSSAD---WIID 160
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
319-475 1.61e-07

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 52.35  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpGLRLHP-----RLHpgyyDQTLAQLPDEAS-------------- 379
Cdd:COG1136    30 SIEAGEFVAIVGPSGSGKSTLLNIL-----------GGLDRPtsgevLID----GQDISSLSERELarlrrrhigfvfqf 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 380 --LLEALTPF-----------APSADTRKRALIAA---GFGwARHSQKVSTLSGGERSRllfvgLSLARY-----SLLLL 438
Cdd:COG1136    95 fnLLPELTALenvalplllagVSRKERRERARELLervGLG-DRLDHRPSQLSGGQQQR-----VAIARAlvnrpKLILA 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1439757928 439 DEPTNHLDME-GKAALA--QTLRDYPG-GVLLVSHDRQLIS 475
Cdd:COG1136   169 DEPTGNLDSKtGEEVLEllRELNRELGtTIVMVTHDPELAA 209
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
23-152 2.05e-07

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 52.20  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----CLMARVEQ---HLPET------LHTQSLLQA 88
Cdd:PRK10895   22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRgigYLPQEasifrrLSVYDNLMA 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928  89 VLAPLPADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK10895  102 VLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
320-484 2.29e-07

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 51.51  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQ---------QMNNAsplpGLRLHPRLHPGYydqtlaqLPDEASL------LEAL 384
Cdd:cd03269    23 VEKGEIFGLLGPNGAGKTTTIRMILGiilpdsgevLFDGK----PLDIAARNRIGY-------LPEERGLypkmkvIDQL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSADTRKRALIAAGFGW-------ARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTL 457
Cdd:cd03269    92 VYLAQLKGLKKEEARRRIDEWlerlelsEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
                         170       180       190
                  ....*....|....*....|....*....|
gi 1439757928 458 RDYPGG---VLLVSHDRQLISESCNRFWLI 484
Cdd:cd03269   172 RELARAgktVILSTHQMELVEELCDRVLLL 201
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
319-474 2.65e-07

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 51.64  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGL---------RLHPRLHPgYYDQTLAQLPDEASLLEALTPF-- 387
Cdd:cd03292    23 SISAGEFVFLVGPSGAGKSTLLKLI---YKEELPTSGTirvngqdvsDLRGRAIP-YLRRKIGVVFQDFRLLPDRNVYen 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 ---------APSADTRKR---ALIAAGFGwARHSQKVSTLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGK 450
Cdd:cd03292    99 vafalevtgVPPREIRKRvpaALELVGLS-HKHRALPAELSGGEQQRV-----AIARAivnspTILIADEPTGNLDPDTT 172
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 451 AALAQTLRDYPGG---VLLVSHDRQLI 474
Cdd:cd03292   173 WEIMNLLKKINKAgttVVVATHAKELV 199
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
35-181 3.23e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 52.02  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  35 LIGHNGCGKSTLLQVLDGTLAPTSG-----SVSLAGQCLM---------ARVEQ--HLPETLhTQSLLQAVLAPLPADA- 97
Cdd:PRK14271   52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFnyrdvlefrRRVGMlfQRPNPF-PMSIMDNVLAGVRAHKl 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  98 --REAQRWLAERLLAQMGFTPAVMEQQTAT---LSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQ 172
Cdd:PRK14271  131 vpRKEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
                         170
                  ....*....|.
gi 1439757928 173 G--SFVLVSHD 181
Cdd:PRK14271  211 DrlTVIIVTHN 221
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
21-66 3.86e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 51.74  E-value: 3.86e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ 66
Cdd:PRK13546   41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
318-533 4.43e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 52.54  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 318 ARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASP---LPGLRLHpRLHPGYYDQTLAQLPDEASL-----LEAL----- 384
Cdd:PRK09536   24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtvlVAGDDVE-ALSARAASRRVASVPQDTSLsfefdVRQVvemgr 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TP----FAPSADTRKRAL---IAAGFGWARHSQKVSTLSGGERSRLLfVGLSLARYS-LLLLDEPTNHLDMEGKA---AL 453
Cdd:PRK09536  103 TPhrsrFDTWTETDRAAVeraMERTGVAQFADRPVTSLSGGERQRVL-LARALAQATpVLLLDEPTASLDINHQVrtlEL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 454 AQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARlQAVAPAPDSRLALQSTPA----------GAD 523
Cdd:PRK09536  182 VRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA-DTLRAAFDARTAVGTDPAtgaptvtplpDPD 260
                         250
                  ....*....|
gi 1439757928 524 DDEEALLARL 533
Cdd:PRK09536  261 RTEAAADTRV 270
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
290-485 5.06e-07

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 50.93  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 290 LPADRLLEMDTL--HVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLL--------------RLLWQQMNNASPL 353
Cdd:PRK10584    1 MPAENIVEVHHLkkSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLailaglddgssgevSLVGQPLHQMDEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 354 PGLRLHPRlHPGYYDQTLAQLPDEASL----LEALTPFAPSADTRKRA---LIAAGFGwARHSQKVSTLSGGERSRLLFV 426
Cdd:PRK10584   81 ARAKLRAK-HVGFVFQSFMLIPTLNALenveLPALLRGESSRQSRNGAkalLEQLGLG-KRLDHLPAQLSGGEQQRVALA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 427 GLSLARYSLLLLDEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:PRK10584  159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRLRLVN 221
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
11-156 5.33e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 52.48  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------------------QCL 68
Cdd:PRK09700   10 GIGKSFGPVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlgigiiyQEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  69 MARVEQHLPETLHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK09700   90 SVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVII 168

                  ....*...
gi 1439757928 149 LDEPGNHL 156
Cdd:PRK09700  169 MDEPTSSL 176
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
319-469 5.68e-07

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 50.19  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL------------WQqmnnasplpGLRLHpRLHPGYYDQTL-----AQLPDEASLL 381
Cdd:PRK13538   23 TLNAGELVQIEGPNGAGKTSLLRILaglarpdagevlWQ---------GEPIR-RQRDEYHQDLLylghqPGIKTELTAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALTPFAP-----SADTRKRALIAAGFGwARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQT 456
Cdd:PRK13538   93 ENLRFYQRlhgpgDDEALWEALAQVGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
                         170
                  ....*....|....*.
gi 1439757928 457 LRDY--PGG-VLLVSH 469
Cdd:PRK13538  172 LAQHaeQGGmVILTTH 187
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
21-157 6.77e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 51.39  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSL------AGQCLMARVEQHLPETLHTQSLLQAVLA--- 91
Cdd:PRK13631   43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYSKKIKNFKELRRRVSmvf 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  92 -------------------PLP-ADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13631  123 qfpeyqlfkdtiekdimfgPVAlGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDE 202

                  ....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK13631  203 PTAGLD 208
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
1-214 6.85e-07

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 50.85  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVETAfGPLFNSLSFTLKKGDRIGLIGHNGCGKS----TLLQVLDGTLAPTSGSVSLAGQCLmarveqhL 76
Cdd:PRK10418    1 MPQQIELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV-------A 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  77 PETL---HTQSLLQA------VLAPLPADAREAQRWLA-----ERLLAQM-----GFTPAVMEQQTATLSGGQHTRLLLA 137
Cdd:PRK10418   73 PCALrgrKIATIMQNprsafnPLHTMHTHARETCLALGkpaddATLTAALeavglENAARVLKLYPFEMSGGMLQRMMIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 138 RALIRQPDLLLLDEPGNHLDLPT----LLWLESFLQTWQGSFVLVSHD----NTLLD--AVTNSSWILRDQTLHS-FALP 206
Cdd:PRK10418  153 LALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDmgvvARLADdvAVMSHGRIVEQGDVETlFNAP 232

                  ....*...
gi 1439757928 207 CSAARQAL 214
Cdd:PRK10418  233 KHAVTRSL 240
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
320-470 7.46e-07

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 50.54  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQQMnnaSPLPG-LRLHPRLHPGYYDQTLAQ----LPDEASLLEALT--------- 385
Cdd:PRK13548   25 LRPGEVVAILGPNGAGKSTLLRALSGEL---SPDSGeVRLNGRPLADWSPAELARrravLPQHSSLSFPFTveevvamgr 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 -PFAPSADTRKRALIAA-------GFGwarhSQKVSTLSGGERSRLlfvglSLAR-----------YSLLLLDEPTNHLD 446
Cdd:PRK13548  102 aPHGLSRAEDDALVAAAlaqvdlaHLA----GRDYPQLSGGEQQRV-----QLARvlaqlwepdgpPRWLLLDEPTSALD 172
                         170       180
                  ....*....|....*....|....*...
gi 1439757928 447 MEGKAALAQTLRDY----PGGVLLVSHD 470
Cdd:PRK13548  173 LAHQHHVLRLARQLaherGLAVIVVLHD 200
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
33-157 8.23e-07

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 52.03  E-value: 8.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  33 IGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveqhlpETLHTQSLLQ---------AVLA-------PLPAD 96
Cdd:PRK10790  370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL---------SSLSHSVLRQgvamvqqdpVVLAdtflanvTLGRD 440
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  97 AREAQRW-------LAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10790  441 ISEEQVWqaletvqLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
319-480 8.80e-07

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: 50.42  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL----------------------------------WQqmnNASPLPGLR------- 357
Cdd:COG0411    26 EVERGEIVGLIGPNGAGKTTLFNLItgfyrptsgrilfdgrditglpphriarlgiartFQ---NPRLFPELTvlenvlv 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 358 -LHPRLHPGYYdqtlaqlpdeASLLEALTPFAPSADTRKRAL-IAAGFG-WARHSQKVSTLSGGERsRLLFVGLSLA-RY 433
Cdd:COG0411   103 aAHARLGRGLL----------AALLRLPRARREEREARERAEeLLERVGlADRADEPAGNLSYGQQ-RRLEIARALAtEP 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 434 SLLLLDEPTNHLDMEGKAALAQTLRDYPGG----VLLVSHDRQLISESCNR 480
Cdd:COG0411   172 KLLLLDEPAAGLNPEETEELAELIRRLRDErgitILLIEHDMDLVMGLADR 222
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
23-160 1.06e-06

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 51.50  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---------------------CLMAR-VEQHL---- 76
Cdd:PRK13657  354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrniavvfqdaGLFNRsIEDNIrvgr 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  77 PETLHTQSLLQAVLAplpadarEAQRWLAERLlaqMGFTPAVMEQQTAtLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PRK13657  434 PDATDEEMRAAAERA-------QAHDFIERKP---DGYDTVVGERGRQ-LSGGERQRLAIARALLKDPPILILDEATSAL 502

                  ....
gi 1439757928 157 DLPT 160
Cdd:PRK13657  503 DVET 506
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
35-152 1.21e-06

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 50.04  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  35 LIGHNGCGKSTLLQVL-------DGtlAPTSGSVSLAGQCLMAR-------------VEQH---LPET----------LH 81
Cdd:COG1117    42 LIGPSGCGKSTLLRCLnrmndliPG--ARVEGEILLDGEDIYDPdvdvvelrrrvgmVFQKpnpFPKSiydnvayglrLH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  82 ------------TQSLLQAVLaplpadareaqrW--LAERLlaqmgftpavmeQQTAT-LSGGQHTRLLLARALIRQPDL 146
Cdd:COG1117   120 gikskseldeivEESLRKAAL------------WdeVKDRL------------KKSALgLSGGQQQRLCIARALAVEPEV 175

                  ....*.
gi 1439757928 147 LLLDEP 152
Cdd:COG1117   176 LLMDEP 181
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
318-460 1.31e-06

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: 49.58  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 318 ARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPG---LRLHPRlHPGYYDQTLAQLPDEASLLEALT-----PFA- 388
Cdd:cd03234    28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGqilFNGQPR-KPDQFQKCVAYVRQDDILLPGLTvretlTYTa 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 --------PSADTRKRA----LIAAGFGWARHsQKVSTLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEGKA 451
Cdd:cd03234   107 ilrlprksSDAIRKKRVedvlLRDLALTRIGG-NLVKGISGGERRR-----VSIAVQllwdpKVLILDEPTSGLDSFTAL 180

                  ....*....
gi 1439757928 452 ALAQTLRDY 460
Cdd:cd03234   181 NLVSTLSQL 189
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
18-157 1.33e-06

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 51.17  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-------------QClmARVEQHLpetlHtqs 84
Cdd:PRK11176  357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQV--ALVSQNV----H--- 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAVLAPLPADARE-----AQRWLAERLLAQMGFTPAvMEQ--------QTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK11176  428 LFNDTIANNIAYARTeqysrEQIEEAARMAYAMDFINK-MDNgldtvigeNGVLLSGGQRQRIAIARALLRDSPILILDE 506

                  ....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK11176  507 ATSALD 512
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
326-480 1.37e-06

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: 49.43  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 326 VAIMGRNGGGKSSLLRLLWQQMNNASP---LPGL-----RLHPRLHPGYYDQTLAqLPDEASLLEALTPFA-----PSAD 392
Cdd:cd03263    31 FGLLGHNGAGKTTTLKMLTGELRPTSGtayINGYsirtdRKAARQSLGYCPQFDA-LFDELTVREHLRFYArlkglPKSE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 393 TRKRA---LIAAGFGWARHSqKVSTLSGGERsRLLFVGLSLARYS-LLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLL 466
Cdd:cd03263   110 IKEEVellLRVLGLTDKANK-RARTLSGGMK-RKLSLAIALIGGPsVLLLDEPTSGLDPASRRAIWDLILEVRKGrsIIL 187
                         170
                  ....*....|....
gi 1439757928 467 VSHDRQLISESCNR 480
Cdd:cd03263   188 TTHSMDEAEALCDR 201
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
319-471 1.43e-06

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: 49.44  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL--WQQMNNASPLPGLRLHPRLHPgyYDQTLAQLPDEASLLEALTPF--------- 387
Cdd:cd03259    22 TVEPGEFLALLGPSGCGKTTLLRLIagLERPDSGEILIDGRDVTGVPP--ERRNIGMVFQDYALFPHLTVAeniafglkl 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 --APSADTRKRAL-IAAGFGWARHSQ-KVSTLSGGERSRllfVGL--SLARY-SLLLLDEPTNHLDMEGKAALAQTLRDY 460
Cdd:cd03259   100 rgVPKAEIRARVReLLELVGLEGLLNrYPHELSGGQQQR---VALarALAREpSLLLLDEPLSALDAKLREELREELKEL 176
                         170
                  ....*....|....*
gi 1439757928 461 PGG----VLLVSHDR 471
Cdd:cd03259   177 QRElgitTIYVTHDQ 191
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
320-485 1.55e-06

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: 49.64  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL------------------WQQMN------------------NASPLPGLRLHP--- 360
Cdd:cd03267    44 IEKGEIVGFIGPNGAGKTTTLKILsgllqptsgevrvaglvpWKRRKkflrrigvvfgqktqlwwDLPVIDSFYLLAaiy 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 361 RLHPGYYDQTLAQLPDeasLLEaLTPFApsadtrkraliaagfgwarhSQKVSTLSGGERSRLLFVGLSLARYSLLLLDE 440
Cdd:cd03267   124 DLPPARFKKRLDELSE---LLD-LEELL--------------------DTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 441 PTNHLDMEGKAALAQTLRDY----PGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03267   180 PTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVID 228
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
23-179 1.55e-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: 51.45  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDgTLAPTSGSVSLAGQCLMARVEQH-------LPETLHTQS-LLQAVLAPLP 94
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTwrkafgvIPQKVFIFSgTFRKNLDPYE 1316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   95 ADARE---------AQRWLAERLLAQMGFtpaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:TIGR01271 1317 QWSDEeiwkvaeevGLKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
                          170
                   ....*....|....*
gi 1439757928  166 SFL-QTWQGSFVLVS 179
Cdd:TIGR01271 1394 KTLkQSFSNCTVILS 1408
PRK01156 PRK01156
chromosome segregation protein; Provisional
410-477 1.61e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.06  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 410 QKVSTLSGGERSRLLF-VGLSLARY-----SLLLLDEPTNHLDMEGKAALAQ----TLRDYPG--GVLLVSHDRQLISES 477
Cdd:PRK01156  797 EGIDSLSGGEKTAVAFaLRVAVAQFlnndkSLLIMDEPTAFLDEDRRTNLKDiieySLKDSSDipQVIMISHHRELLSVA 876
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
126-181 1.76e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 49.65  E-value: 1.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 126 LSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTW----QGSFVLVSHD 181
Cdd:PRK14258  151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1-157 1.91e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 49.39  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   1 MSTLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLD--GTLAP---TSGSVSLAGQCLMAR---- 71
Cdd:PRK14239    2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPrtdt 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  72 ---------VEQH---LPETLH--------------TQSLLQAVLAPLpadaREAQRW--LAERLlaqmgftpavmEQQT 123
Cdd:PRK14239   82 vdlrkeigmVFQQpnpFPMSIYenvvyglrlkgikdKQVLDEAVEKSL----KGASIWdeVKDRL-----------HDSA 146
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1439757928 124 ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK14239  147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
21-151 2.11e-06

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 50.66  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP------ETLHTQSLLQAVlaplp 94
Cdd:PRK13545   41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNgqltgiENIELKGLMMGL----- 115
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928  95 adAREAQRWLAERLL--AQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13545  116 --TKEKIKEIIPEIIefADIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
310-477 2.27e-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: 47.74  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 310 PSLFTTGVARLRSGDRVAIMGRNGGGKSSLLR----LLWQQMNNasplpgLRLHPRLHPGYYdqtlaqlpdeasllealt 385
Cdd:cd03227     8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSA------TRRRSGVKAGCI------------------ 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 pfapsadtrkRALIAAGFGWARHsqkvsTLSGGERSR----LLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYP 461
Cdd:cd03227    64 ----------VAAVSAELIFTRL-----QLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
                         170
                  ....*....|....*....
gi 1439757928 462 GG---VLLVSHDRQLISES 477
Cdd:cd03227   129 VKgaqVIVITHLPELAELA 147
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
24-181 3.80e-06

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 49.26  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE-------------------TLHTQS 84
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkiamvfqsfalmphmTVLDNT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  85 LLQAVLAPLPADAREAQRWLAERLLAQMGFTPAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:PRK10070  128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
                         170       180
                  ....*....|....*....|.
gi 1439757928 165 ESFLQTWQG----SFVLVSHD 181
Cdd:PRK10070  204 QDELVKLQAkhqrTIVFISHD 224
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
320-480 4.14e-06

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: 48.20  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASP-----------LPGLRLHPRLHPG----------YYDQT------LA 372
Cdd:cd03219    23 VRPGEIHGLIGPNGAGKTTLFNLI---SGFLRPtsgsvlfdgedITGLPPHEIARLGigrtfqiprlFPELTvlenvmVA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 373 QLPDEASLLEALTPFAPSADTRKRAL-IAAGFG-WARHSQKVSTLSGGERsRLLFVGLSLA-RYSLLLLDEPTNHLDMEG 449
Cdd:cd03219   100 AQARTGSGLLLARARREEREARERAEeLLERVGlADLADRPAGELSYGQQ-RRLEIARALAtDPKLLLLDEPAAGLNPEE 178
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1439757928 450 KAALAQTLRDYPG---GVLLVSHDRQLISESCNR 480
Cdd:cd03219   179 TEELAELIRELRErgiTVLLVEHDMDVVMSLADR 212
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
319-497 4.41e-06

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 49.46  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnASPLP--------GLRLHpRLHPGYYDQTLA------QLPdEASLLEAL 384
Cdd:PRK11174  372 TLPAGQRIALVGPSGAGKTSLLNAL------LGFLPyqgslkinGIELR-ELDPESWRKHLSwvgqnpQLP-HGTLRDNV 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSA-DTRKRALIAAGFGW---ARHSQKVSTLSgGERSRLLFVG----LSLAR-----YSLLLLDEPTNHLDMEGKA 451
Cdd:PRK11174  444 LLGNPDAsDEQLQQALENAWVSeflPLLPQGLDTPI-GDQAAGLSVGqaqrLALARallqpCQLLLLDEPTASLDAHSEQ 522
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 452 ALAQTLRDYPGG--VLLVSHdrQLIS-ESCNRFWLIDSAGLTEWHSLEE 497
Cdd:PRK11174  523 LVMQALNAASRRqtTLMVTH--QLEDlAQWDQIWVMQDGQIVQQGDYAE 569
hmuV PRK13547
heme ABC transporter ATP-binding protein;
319-484 4.53e-06

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 48.67  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRLHPRLhpGYYDQTLAQLPD------EASLLEALTP-FAPSA 391
Cdd:PRK13547   23 RIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDV--TLNGEPLAAIDAprlarlRAVLPQAAQPaFAFSA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 392 DT------------------RKRALIAAGFGWARHS----QKVSTLSGGERSRLLFV-----------GLSLARYslLLL 438
Cdd:PRK13547  101 REivllgrypharragalthRDGEIAWQALALAGATalvgRDVTTLSGGELARVQFArvlaqlwpphdAAQPPRY--LLL 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1439757928 439 DEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFWLI 484
Cdd:PRK13547  179 DEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAARHADRIAML 228
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
23-152 4.95e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 49.74  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVS-LAGQCLMARVEQHL-------PETL-----HTQSL---L 86
Cdd:NF033858   20 VSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVcpriaymPQGLgknlyPTLSVfenL 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928  87 Q--AVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF033858  100 DffGRLFGQDAAERRRR---IDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
319-469 5.22e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 49.39  E-value: 5.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhPGYYDQT----------LAQLPDEA---------- 378
Cdd:COG1132   362 TIPPGETVALVGPSGSGKSTLVNLL--------------------LRFYDPTsgrilidgvdIRDLTLESlrrqigvvpq 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 379 -------SLLEALTPFAPSADTR--KRALIAAGF-GWARH---------SQKVSTLSGGERSRLlfvglSLARY-----S 434
Cdd:COG1132   422 dtflfsgTIRENIRYGRPDATDEevEEAAKAAQAhEFIEAlpdgydtvvGERGVNLSGGQRQRI-----AIARAllkdpP 496
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1439757928 435 LLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSH 469
Cdd:COG1132   497 ILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
124-180 5.49e-06

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 48.72  E-value: 5.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 124 ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP----TLLWLESFLQTWQGSFVLVSH 180
Cdd:PRK11144  127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPrkreLLPYLERLAREINIPILYVSH 187
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
23-186 5.57e-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: 49.56  E-value: 5.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqCLMARVEQH--------LPE--TLHTQSLlQAVLAP 92
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-LNIAKIGLHdlrfkitiIPQdpVLFSGSL-RMNLDP 1382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   93 LPADAREaQRWLAERLLAQMGFT---PAVMEQQTA----TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:TIGR00957 1383 FSQYSDE-EVWWALELAHLKTFVsalPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
                          170       180
                   ....*....|....*....|....
gi 1439757928  166 SFLQT-WQGSFVL-VSHD-NTLLD 186
Cdd:TIGR00957 1462 STIRTqFEDCTVLtIAHRlNTIMD 1485
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
322-477 6.00e-06

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 48.14  E-value: 6.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 322 SGDRVAIMGRNGGGKSSLLRLL--------WQQMNNASPLPGLRLHPRLHpgYYDQTLaqLP-----DEASLlealtpfA 388
Cdd:PRK11247   37 AGQFVAVVGRSGCGKSTLLRLLagletpsaGELLAGTAPLAEAREDTRLM--FQDARL--LPwkkviDNVGL-------G 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 PSADTRKRALIA-AGFGWARHSQK-VSTLSGGERSRllfVGLSLA---RYSLLLLDEPTNHLD----MEGKAALAQTLRD 459
Cdd:PRK11247  106 LKGQWRDAALQAlAAVGLADRANEwPAALSGGQKQR---VALARAlihRPGLLLLDEPLGALDaltrIEMQDLIESLWQQ 182
                         170
                  ....*....|....*...
gi 1439757928 460 YPGGVLLVSHDrqlISES 477
Cdd:PRK11247  183 HGFTVLLVTHD---VSEA 197
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
320-469 6.72e-06

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 46.92  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRLHPRLHPGYYDQTLAQ----LPDEASLLealtpfapsaDTRK 395
Cdd:cd03247    25 LKQGEKIALLGRSGSGKSTLLQLL---TGDLKPQQGEITLDGVPVSDLEKALSSlisvLNQRPYLF----------DTTL 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 396 RALIAAGFgwarhsqkvstlSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSH 469
Cdd:cd03247    92 RNNLGRRF------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDktLIWITH 155
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
23-181 7.17e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 49.08  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---CLMARVEQHLPETLH------------TQSLLQ 87
Cdd:PRK10261  343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQfifqdpyasldpRQTVGD 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  88 AVLAPLPA----DAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:PRK10261  423 SIMEPLRVhgllPGKAAAARVAW-LLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
                         170       180
                  ....*....|....*....|..
gi 1439757928 164 LESFLQTWQG----SFVLVSHD 181
Cdd:PRK10261  502 IINLLLDLQRdfgiAYLFISHD 523
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
320-480 7.34e-06

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 46.80  E-value: 7.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNASPLPglrlhpRLHPGYYDQTlAQLPDEASLLE 382
Cdd:cd03229    23 IEAGEIVALLGPSGSGKSTLLRCIagleepdsgsilidgedLTDLEDELPPL------RRRIGMVFQD-FALFPHLTVLE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ALTpfapsadtrkraliaagFGwarhsqkvstLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKA---ALA 454
Cdd:cd03229    96 NIA-----------------LG----------LSGGQQQRV-----ALARAlamdpDVLLLDEPTSALDPITRRevrALL 143
                         170       180
                  ....*....|....*....|....*..
gi 1439757928 455 QTLRDYPG-GVLLVSHDRQLISESCNR 480
Cdd:cd03229   144 KSLQAQLGiTVVLVTHDLDEAARLADR 170
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
19-157 8.88e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 48.87  E-value: 8.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGS-----------------------VSLAGQCLMARVEQH 75
Cdd:PTZ00265   400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDiiindshnlkdinlkwwrskigvVSQDPLLFSNSIKNN 479
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   76 LPETLHTQSLLQAVLAPLPADAREAQRWLAERL---------------------LAQM---------------------- 112
Cdd:PTZ00265   480 IKYSLYSLKDLEALSNYYNEDGNDSQENKNKRNscrakcagdlndmsnttdsneLIEMrknyqtikdsevvdvskkvlih 559
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1439757928  113 GFTPAVMEQ-------QTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PTZ00265   560 DFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
319-474 9.56e-06

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: 46.75  E-value: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNnasplpglrlhprlHPGYY---------DQTLAQL-PDEasllealtpfa 388
Cdd:cd03217    22 TIKKGEVHALMGPNGSGKSTLAKTI---MG--------------HPKYEvtegeilfkGEDITDLpPEE----------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 psadtrkRALIAAGFGWARHSQ----KVSTL--------SGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQ- 455
Cdd:cd03217    74 -------RARLGIFLAFQYPPEipgvKNADFlryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEv 146
                         170       180
                  ....*....|....*....|.
gi 1439757928 456 --TLRDYPGGVLLVSHDRQLI 474
Cdd:cd03217   147 inKLREEGKSVLIITHYQRLL 167
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
18-195 1.23e-05

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: 46.56  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARVEQHLPETLHTQSLLQAVLAP--LPA 95
Cdd:cd03290    15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAYAAQKPwlLNA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  96 DARE---------AQRWLAerLLAQMGFTPAV----------MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:cd03290    94 TVEEnitfgspfnKQRYKA--VTDACSLQPDIdllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1439757928 157 D--LPTLLWLE---SFLQTWQGSFVLVSHDntlLDAVTNSSWIL 195
Cdd:cd03290   172 DihLSDHLMQEgilKFLQDDKRTLVLVTHK---LQYLPHADWII 212
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
21-188 1.25e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 47.39  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV------------SLAGQCLMARVEQHLPET--------- 79
Cdd:PRK13651   24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkkTKEKEKVLEKLVIQKTRFkkikkikei 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  80 --------------LHTQSLLQAVL-APL-----PADAREaqrwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARA 139
Cdd:PRK13651  104 rrrvgvvfqfaeyqLFEQTIEKDIIfGPVsmgvsKEEAKK----RAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGI 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 140 LIRQPDLLLLDEPGNHLDlP--TLLWLESF--LQTWQGSFVLVSHDntlLDAV 188
Cdd:PRK13651  180 LAMEPDFLVFDEPTAGLD-PqgVKEILEIFdnLNKQGKTIILVTHD---LDNV 228
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
326-472 1.27e-05

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


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 46.79  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 326 VAIMGRNGGGKSSLLRLLwQQMN--------------------------------------NASPLPG-----LRLHPRL 362
Cdd:cd03260    29 TALIGPSGCGKSTLLRLL-NRLNdlipgapdegevlldgkdiydldvdvlelrrrvgmvfqKPNPFPGsiydnVAYGLRL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 363 HpGYYDQTLAQLPDEASLLEALTPfapsaDTRKRALIAAGfgwarhsqkvstLSGGERSRLlfvglSLARY-----SLLL 437
Cdd:cd03260   108 H-GIKLKEELDERVEEALRKAALW-----DEVKDRLHALG------------LSGGQQQRL-----CLARAlanepEVLL 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1439757928 438 LDEPTNHLDMEGKAALAQTL----RDYPggVLLVSHDRQ 472
Cdd:cd03260   165 LDEPTSALDPISTAKIEELIaelkKEYT--IVIVTHNMQ 201
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
407-508 1.31e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 46.92  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 407 RHsQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLLVSHDRQLISESCNRFWL 483
Cdd:PRK13638  130 RH-QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYV 208
                          90       100
                  ....*....|....*....|....*
gi 1439757928 484 IDSAGLTEWHSLEEVYARLQAVAPA 508
Cdd:PRK13638  209 LRQGQILTHGAPGEVFACTEAMEQA 233
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
124-180 1.31e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 46.76  E-value: 1.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 124 ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSF--VLVSH 180
Cdd:PRK14267  148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYtiVLVTH 206
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
415-519 1.64e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 46.72  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG----GVLLVSHDRQLISESCNRFWLIDSAGLT 490
Cdd:PRK13652  138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
                          90       100
                  ....*....|....*....|....*....
gi 1439757928 491 EWHSLEEVYARLQAVAPApdsRLALQSTP 519
Cdd:PRK13652  218 AYGTVEEIFLQPDLLARV---HLDLPSLP 243
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
19-151 1.90e-05

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 47.44  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLdGTLAPT-SGSVSLAGQCLMARVEQHLPETLHTqsLLQAVLAPlpaDA 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVPQRPYMTLGT--LRDQIIYP---DS 540
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  98 REAQ--RWLAERLLAQM--------------GFTpaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:TIGR00954 541 SEDMkrRGLSDKDLEQIldnvqlthileregGWS--AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
379-518 1.99e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 47.90  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  379 SLLEALTPFAPSA-------DTRKRALIAAGFGWARHSQKVSTLSGGERSRL-----LFVGLSLARYsllLLDEPTNHL- 445
Cdd:PRK00635   434 IFLSQLPSKSLSIeevlqglKSRLSILIDLGLPYLTPERALATLSGGEQERTalakhLGAELIGITY---ILDEPSIGLh 510
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  446 --DMEGKAALAQTLRDYPGGVLLVSHDRQLISeSCNRfwLID---SAG---------------LTEWHSLEEVYARLQAV 505
Cdd:PRK00635   511 pqDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LADR--IIDigpGAGifggevlfngsprefLAKSDSLTAKYLRQELT 587
                          170
                   ....*....|...
gi 1439757928  506 APAPDSRLALQST 518
Cdd:PRK00635   588 IPIPEKRTNSLGT 600
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
315-459 2.26e-05

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 47.35  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 315 TGVARlrSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRL------------------------------------ 358
Cdd:TIGR00955  45 SGVAK--PGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLlngmpidakemraisayvqqddlfiptltvrehlmf 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 359 --HPRLHPGYYDQTLAQLPDEasLLEALTpFAPSADTRkralIAAGfgwarhsQKVSTLSGGERSRLLFVGLSLARYSLL 436
Cdd:TIGR00955 123 qaHLRMPRRVTKKEKRERVDE--VLQALG-LRKCANTR----IGVP-------GRVKGLSGGERKRLAFASELLTDPPLL 188
                         170       180
                  ....*....|....*....|...
gi 1439757928 437 LLDEPTNHLDMEGKAALAQTLRD 459
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKG 211
cbiO PRK13645
energy-coupling factor transporter ATPase;
20-157 2.53e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 46.15  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ---------------HLPETLHTQS 84
Cdd:PRK13645   27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkrlrkeiglvfQFPEYQLFQE 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928  85 LLQAVLAPLP----ADAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13645  107 TIEKDIAFGPvnlgENKQEAYKKVPE-LLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
319-470 2.71e-05

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 45.78  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMnnaSPLPGLRLHprlhpgyYDQTLAQLPDEA-----SLL--EALTPfapsA 391
Cdd:PRK11231   24 SLPTGKITALIGPNGCGKSTLLKCFARLL---TPQSGTVFL-------GDKPISMLSSRQlarrlALLpqHHLTP----E 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 392 DTRKRALIAAGFG-----WARHSQK---------------------VSTLSGGERSRlLFVGLSLARYS-LLLLDEPTNH 444
Cdd:PRK11231   90 GITVRELVAYGRSpwlslWGRLSAEdnarvnqameqtrinhladrrLTDLSGGQRQR-AFLAMVLAQDTpVVLLDEPTTY 168
                         170       180
                  ....*....|....*....|....*....
gi 1439757928 445 LDMEGKA---ALAQTLRDYPGGVLLVSHD 470
Cdd:PRK11231  169 LDINHQVelmRLMRELNTQGKTVVTVLHD 197
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
319-474 3.12e-05

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 45.43  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLW--------------QQMNNASP--LPGLRLH-------PRLHPgyyDQTLAQ-- 373
Cdd:COG2884    24 EIEKGEFVFLTGPSGAGKSTLLKLLYgeerptsgqvlvngQDLSRLKRreIPYLRRRigvvfqdFRLLP---DRTVYEnv 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 374 -LPdeaslLEALTpfAPSADTRKRalIAAGFGW----ARHSQKVSTLSGGERSRLlfvglSLARY-----SLLLLDEPTN 443
Cdd:COG2884   101 aLP-----LRVTG--KSRKEIRRR--VREVLDLvglsDKAKALPHELSGGEQQRV-----AIARAlvnrpELLLADEPTG 166
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1439757928 444 HLDMEGKAALAQTLRDYP-GG--VLLVSHDRQLI 474
Cdd:COG2884   167 NLDPETSWEIMELLEEINrRGttVLIATHDLELV 200
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
10-152 3.35e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 46.44  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  10 LHVETAFGP-LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH--------LPETL 80
Cdd:PRK11288  258 LRLDGLKGPgLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairagimlCPEDR 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  81 HTQSLLQ-----------AVLAPLPA-----DAREAQrwLAERLLAQMGF-TPAvMEQQTATLSGGQHTRLLLARALIRQ 143
Cdd:PRK11288  338 KAEGIIPvhsvadninisARRHHLRAgclinNRWEAE--NADRFIRSLNIkTPS-REQLIMNLSGGNQQKAILGRWLSED 414

                  ....*....
gi 1439757928 144 PDLLLLDEP 152
Cdd:PRK11288  415 MKVILLDEP 423
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
319-486 3.78e-05

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 45.95  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLR-LLWQQMNNA-------SPLPGLRLHPRLHPGYYDQtLAQLPDEASLLEALTPFA-- 388
Cdd:PRK13537   29 HVQRGECFGLLGPNGAGKTTTLRmLLGLTHPDAgsislcgEPVPSRARHARQRVGVVPQ-FDNLDPDFTVRENLLVFGry 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 ---PSADTrkRALIAAGFGWARHSQK----VSTLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEGKAALAQT 456
Cdd:PRK13537  108 fglSAAAA--RALVPPLLEFAKLENKadakVGELSGGMKRR-----LTLARAlvndpDVLVLDEPTTGLDPQARHLMWER 180
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1439757928 457 LRDYPGG---VLLVSHDRQLISESCNRFWLIDS 486
Cdd:PRK13537  181 LRSLLARgktILLTTHFMEEAERLCDRLCVIEE 213
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
108-474 3.93e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 46.75  E-value: 3.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  108 LLAQMGFTPAVMEQQTATLSGGQHTRLLLARAL-IRQPDLL-LLDEP--GNH-LDLPTLLwleSFLQTwqgsfvLVSHDN 182
Cdd:PRK00635  1370 FIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKIsSNLTDIIyLLEDPlsGLHpQDAPTLL---QLIKE------LVTNNN 1440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  183 TLLdaVTNSSWILR---DQTLH---------SFALPCSAARQ--------ALQEQDESAALRHKAEQKEIDRVSASARRL 242
Cdd:PRK00635  1441 TVI--ATDRSGSLAehaDHLIHlgpgsgpqgGYLLSTSALKQsqpdlhntRSSEETPTLSVSLSIHTIQNLNVSAPLHSL 1518
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  243 ATWGRVYDNEDLARKAKQMEKQVARLKDEQTELSVGppwRLVLQGDALPADRLLEMDTlHVSPApgqPSL--FTTGVARL 320
Cdd:PRK00635  1519 VAISGVSGSGKTSLLLEGFYKQACALIEKGPSVFSE---IIFLDSHPQISSQRSDIST-YFDIA---PSLrnFYASLTQA 1591
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  321 RSGDRVAIM---GRNGGGKSSLLRLLWQQMNNA------SPLP---GLRLHPR----LHPGYYDQTLAQLPDEASLLeaL 384
Cdd:PRK00635  1592 KALNISASMfstNTKQGQCSDCWGLGYQWIDRAfyalekRPCPtcsGFRIQPLaqevVYEGKHFGQLLQTPIEEVAE--T 1669
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  385 TPFAPSADTRKRALIAAGFGWARHSQKVSTLSGGERsrllfVGLSLARY--------SLLLLDEPTNHLDMEGKAALAQT 456
Cdd:PRK00635  1670 FPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEK-----IAIKIAKFlylppkhpTLFLLDEIATSLDNQQKSALLVQ 1744
                          410       420
                   ....*....|....*....|.
gi 1439757928  457 LRDYPG---GVLLVSHDRQLI 474
Cdd:PRK00635  1745 LRTLVSlghSVIYIDHDPALL 1765
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
23-157 3.94e-05

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 45.99  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMA----------RVEQHLPETLH 81
Cdd:PRK11650   23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVfqnyalyphmSVRENMAYGLK 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928  82 tqsllqavLAPLPADAREAQRWLAERLLAQMGFtpavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11650  103 --------IRGMPKAEIEERVAEAARILELEPL----LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
415-473 4.04e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 4.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 415 LSGGERSRL-LFVGLSLARY-----SLLLLDEPTNHLDMEGKAAL----AQTLRDYPgGVLLVSHDRQL 473
Cdd:PRK03918  789 LSGGERIALgLAFRLALSLYlagniPLLILDEPTPFLDEERRRKLvdimERYLRKIP-QVIIVSHDEEL 856
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
323-459 5.03e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 45.36  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLLWQQMnnaSPLPGLRLHPRLHPGYYDQT--------LAQ---LPDEASLLEALT----PF 387
Cdd:PRK10253   33 GHFTAIIGPNGCGKSTLLRTLSRLM---TPAHGHVWLDGEHIQHYASKevarriglLAQnatTPGDITVQELVArgryPH 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 AP--------SADTRKRALIAAGFGwARHSQKVSTLSGGERSRlLFVGLSLAR-YSLLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:PRK10253  110 QPlftrwrkeDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQR-AWIAMVLAQeTAIMLLDEPTTWLDISHQIDLLELLS 187

                  .
gi 1439757928 459 D 459
Cdd:PRK10253  188 E 188
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
15-203 5.18e-05

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: 44.52  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  15 AFGPLFNSLSFTLKKGdrIGLI-GHNGCGKSTLLQ----VLDGTLAPTSgsvslagqclmaRVEQHLPETLHTQS-LLQA 88
Cdd:cd03240     8 NIRSFHERSEIEFFSP--LTLIvGQNGAGKTTIIEalkyALTGELPPNS------------KGGAHDPKLIREGEvRAQV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  89 VLAPLPADAREaqrWLAERLLAQmgFTPAVMEQQ----------TATLSGGQHT------RLLLARALIRQPDLLLLDEP 152
Cdd:cd03240    74 KLAFENANGKK---YTITRSLAI--LENVIFCHQgesnwplldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEP 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 153 GNHLD-------LPTLlwLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSF 203
Cdd:cd03240   149 TTNLDeenieesLAEI--IEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGRQKSR 204
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
125-157 5.72e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 46.18  E-value: 5.72e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1439757928  125 TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PTZ00265  1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
410-470 5.72e-05

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 44.71  E-value: 5.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 410 QKVSTLSGGERSRLLfVGLSLAR-YSLLLLDEPTNHLDMEGKAALAQTLRDY----PGGVLLVSHD 470
Cdd:cd03237   111 REVPELSGGELQRVA-IAACLSKdADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHD 175
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
323-470 5.81e-05

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 44.75  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLL------------RLLWQQMNNASPLPGLR------------------------LHPRLHpgy 366
Cdd:COG3840    25 GERVAILGPSGAGKSTLLnliagflppdsgRILWNGQDLTALPPAERpvsmlfqennlfphltvaqniglgLRPGLK--- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 367 ydqtlaqlpdeaslleaLTPfapsADTRKRALIAAGFGWARHSQ-KVSTLSGGERSRllfVGLS---LARYSLLLLDEPT 442
Cdd:COG3840   102 -----------------LTA----EQRAQVEQALERVGLAGLLDrLPGQLSGGQRQR---VALArclVRKRPILLLDEPF 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1439757928 443 NHLD----MEGKAALAQTLRDYPGGVLLVSHD 470
Cdd:COG3840   158 SALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
320-513 6.09e-05

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 45.23  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQQMN------------NASPLPGLR----------------LHPRLHP--GYYDQ 369
Cdd:cd03289    27 ISPGQRVGLLGRTGSGKSTLLSAFLRLLNtegdiqidgvswNSVPLQKWRkafgvipqkvfifsgtFRKNLDPygKWSDE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 370 TLAQLPDEASLLEALTPFAPSADTrkrALIAAGFgwarhsqkvsTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEG 449
Cdd:cd03289   107 EIWKVAEEVGLKSVIEQFPGQLDF---VLVDGGC----------VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 450 KAALAQTLRDYPGG--VLLVSHDRQLISEsCNRFWLIDSAGLTEWHSLEEVYARL----QAVAPAPDSRL 513
Cdd:cd03289   174 YQVIRKTLKQAFADctVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKshfkQAISPSDRLKL 242
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
412-470 6.12e-05

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 44.92  E-value: 6.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 412 VSTLSGGE--RSRLLFVGLSLARYS-----LLLLDEPTNHLDMEGKAALAQTLRDYP---GGVLLVSHD 470
Cdd:PRK03695  124 VNQLSGGEwqRVRLAAVVLQVWPDInpagqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
320-470 6.19e-05

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: 44.38  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQ---------QMNNAsPLPGlrlhPRLHPGYYDQTLAQLP-----DEASL-LEAl 384
Cdd:cd03293    27 VEEGEFVALVGPSGCGKSTLLRIIAGlerptsgevLVDGE-PVTG----PGPDRGYVFQQDALLPwltvlDNVALgLEL- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 tPFAPSADTRKRA--LIA----AGFGWARHSQkvstLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAAL 453
Cdd:cd03293   101 -QGVPKAEARERAeeLLElvglSGFENAYPHQ----LSGGMRQRV-----ALARAlavdpDVLLLDEPFSALDALTREQL 170
                         170       180
                  ....*....|....*....|.
gi 1439757928 454 AQTL----RDYPGGVLLVSHD 470
Cdd:cd03293   171 QEELldiwRETGKTVLLVTHD 191
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
416-530 7.27e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 45.10  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 416 SGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFwLIDSAGLT- 490
Cdd:PRK09473  163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITHDLGVVAGICDKV-LVMYAGRTm 241
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1439757928 491 EWHSLEEVYARlqavaPA-PDSRLALQSTPAgADDDEEALL 530
Cdd:PRK09473  242 EYGNARDVFYQ-----PShPYSIGLLNAVPR-LDAEGESLL 276
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
8-195 7.50e-05

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 45.47  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   8 HALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQhl 76
Cdd:PRK10789  319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswrsrLAVVSQ-- 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  77 PETLHTQSLLQAVLAPLPaDAREAQRWLAERL---------LAQmGFTPAVMEqQTATLSGGQHTRLLLARALIRQPDLL 147
Cdd:PRK10789  397 TPFLFSDTVANNIALGRP-DATQQEIEHVARLasvhddilrLPQ-GYDTEVGE-RGVMLSGGQKQRISIARALLLNAEIL 473
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 148 LLDEPGNHLDLPTLLWLESFLQTW-QGSFVLVSHDNtlLDAVTNSSWIL 195
Cdd:PRK10789  474 ILDDALSAVDGRTEHQILHNLRQWgEGRTVIISAHR--LSALTEASEIL 520
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
320-503 1.08e-04

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: 43.72  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNAsplpGLRlHPRLHPGYYDQTLaqlpdeaSLLE 382
Cdd:cd03258    28 VPKGEIFGIIGRSGAGKSTLIRCInglerptsgsvlvdgtdLTLLSGK----ELR-KARRRIGMIFQHF-------NLLS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ALTPF-----------APSADTRKRA--LIA-AGFGwARHSQKVSTLSGGERSRllfVGL--SLARY-SLLLLDEPTNHL 445
Cdd:cd03258    96 SRTVFenvalpleiagVPKAEIEERVleLLElVGLE-DKADAYPAQLSGGQKQR---VGIarALANNpKVLLCDEATSAL 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 446 DMEGKAALAQTLRDYPG----GVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:cd03258   172 DPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
319-503 1.30e-04

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 43.73  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQM-----------NNASPLPglrLHPRLHPGyydqtLAQLPDEASLLEALTPF 387
Cdd:PRK10895   25 TVNSGEIVGLLGPNGAGKTTTFYMVVGIVprdagniiiddEDISLLP---LHARARRG-----IGYLPQEASIFRRLSVY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 --------------APSADTRKRALIAAGFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLD---MEGK 450
Cdd:PRK10895   97 dnlmavlqirddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDI 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 451 AALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:PRK10895  177 KRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
412-524 1.32e-04

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 44.33  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 412 VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLR------DYPggVLLVSHDRQLISESCNRFWLID 485
Cdd:TIGR02142 129 PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLErlhaefGIP--ILYVSHSLQEVLRLADRVVVLE 206
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1439757928 486 SAGLTEWHSLEEVYARLQ-AVAPAPDSRLALQSTPAGADD 524
Cdd:TIGR02142 207 DGRVAAAGPIAEVWASPDlPWLAREDQGSLIEGVVAEHDQ 246
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
411-470 1.39e-04

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: 43.48  E-value: 1.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 411 KVSTLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRD----YPGGVLLVSHD 470
Cdd:cd03299   126 KPETLSGGEQQRV-----AIARAlvvnpKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
407-499 1.73e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 43.50  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 407 RHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG--GVLLVSHDRQLISESCNRFWLI 484
Cdd:PRK14246  146 RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFL 225
                          90
                  ....*....|....*
gi 1439757928 485 DSAGLTEWHSLEEVY 499
Cdd:PRK14246  226 YNGELVEWGSSNEIF 240
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
322-474 1.74e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.98  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  322 SGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHPRLHPGYYDQTLAQLPDEASLLEALTPFAPsadtrkraliaa 401
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARAL------------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------ 56
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928  402 gfgwarhsqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLI 474
Cdd:smart00382  57 ---------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
cbiO PRK13650
energy-coupling factor transporter ATPase;
413-470 1.76e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 43.57  E-value: 1.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 413 STLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLR----DYPGGVLLVSHD 470
Cdd:PRK13650  139 ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKgirdDYQMTVISITHD 200
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
319-442 2.09e-04

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: 43.05  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS--------PLPGLRLHPRLHPGyydqtLAQLPDEASLLEALT----- 385
Cdd:COG0410    25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSgsirfdgeDITGLPPHRIARLG-----IGYVPEGRRIFPSLTveenl 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 ---PFAPSADTRKRALIAAGFGW-----ARHSQKVSTLSGGER-----SRLLfvglsLARYSLLLLDEPT 442
Cdd:COG0410   100 llgAYARRDRAEVRADLERVYELfprlkERRRQRAGTLSGGEQqmlaiGRAL-----MSRPKLLLLDEPS 164
PLN03140 PLN03140
ABC transporter G family member; Provisional
19-157 2.38e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.45  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDG--TLAPTSGSVSLAG----QCLMARV----EQ---HLPETLHTQSL 85
Cdd:PLN03140   895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGfpkkQETFARIsgycEQndiHSPQVTVRESL 974
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   86 LQAVLAPLPADAREAQRwlaerllaqMGFTPAVME--------------QQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PLN03140   975 IYSAFLRLPKEVSKEEK---------MMFVDEVMElveldnlkdaivglPGVTGLSTEQRKRLTIAVELVANPSIIFMDE 1045

                   ....*.
gi 1439757928  152 PGNHLD 157
Cdd:PLN03140  1046 PTSGLD 1051
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
414-484 2.69e-04

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: 42.21  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 414 TLSGGERSRL-LFVGLSLARY-----SLLLLDEPTNHLDMEGKA-ALAQTLRDYPGG----VLLVSHDRQLIsESCNRFW 482
Cdd:cd03240   115 RCSGGEKVLAsLIIRLALAETfgsncGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELV-DAADHIY 193

                  ..
gi 1439757928 483 LI 484
Cdd:cd03240   194 RV 195
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
320-480 3.05e-04

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 42.42  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL------------------WQQMNNASPLPGLRLHpRLHPGYYDQTLAQLP-----D 376
Cdd:COG4778    34 VAAGECVALTGPSGAGKSTLLKCIygnylpdsgsilvrhdggWVDLAQASPREILALR-RRTIGYVSQFLRVIPrvsalD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 377 --EASLLEALTPfAPSADTRKRALIAAgFGWARHSQKVS--TLSGGERSRLlfvglSLAR-----YSLLLLDEPTNHLDM 447
Cdd:COG4778   113 vvAEPLLERGVD-REEARARARELLAR-LNLPERLWDLPpaTFSGGEQQRV-----NIARgfiadPPLLLLDEPTASLDA 185
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1439757928 448 EGKAALAQTLRDY-PGGVLLVS--HDRQLISESCNR 480
Cdd:COG4778   186 ANRAVVVELIEEAkARGTAIIGifHDEEVREAVADR 221
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
319-503 3.10e-04

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 43.69  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKS----SLLRLLWQQMNNASPLPG-LRLHPRLHPGYYDQTLAQL-----PDEASLLE----AL 384
Cdd:PRK10261   38 SLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMlLRRRSRQVIELSEQSAAQMrhvrgADMAMIFQepmtSL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSAD------------TRKRALIAAGF---------GWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:PRK10261  118 NPVFTVGEqiaesirlhqgaSREEAMVEAKRmldqvripeAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTT 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 444 HLDMEGKAALAQTLR----DYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:PRK10261  198 ALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
382-485 3.61e-04

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: 42.60  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALTPFA--PSADTRKRALIAAGFGWARHSQKVSTLSGGERSRllfVGLS--LARYS----LLLLDEPTNHLDMEGKAAL 453
Cdd:cd03271   135 EALEFFEniPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQR---IKLAkeLSKRStgktLYILDEPTTGLHFHDVKKL 211
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1439757928 454 A---QTLRDYPGGVLLVSHDRQLIsESCNrfWLID 485
Cdd:cd03271   212 LevlQRLVDKGNTVVVIEHNLDVI-KCAD--WIID 243
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
21-195 3.74e-04

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: 41.54  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQvldgtlaptsgsvslagQCLMARVEQHLPETLHTQSLLQAV-LAPLpadare 99
Cdd:cd03238    12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLPKFSRNKLIfIDQL------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 aqrwlaeRLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPD--LLLLDEPG---NHLDLPTLL-WLESFLQtwQG 173
Cdd:cd03238    69 -------QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPStglHQQDINQLLeVIKGLID--LG 139
                         170       180
                  ....*....|....*....|...
gi 1439757928 174 -SFVLVSHDNTLLDAvtnSSWIL 195
Cdd:cd03238   140 nTVILIEHNLDVLSS---ADWII 159
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
393-485 3.74e-04

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: 42.24  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 393 TRKRALIAAGFGWARHSQKVSTLSGGE--RSRL---LFVGLSLARYsllLLDEPTNHLDMEGKAALAQT---LRDYPGGV 464
Cdd:cd03270   116 ERLGFLVDVGLGYLTLSRSAPTLSGGEaqRIRLatqIGSGLTGVLY---VLDEPSIGLHPRDNDRLIETlkrLRDLGNTV 192
                          90       100
                  ....*....|....*....|.
gi 1439757928 465 LLVSHDRQLISESCnrfWLID 485
Cdd:cd03270   193 LVVEHDEDTIRAAD---HVID 210
PLN03211 PLN03211
ABC transporter G-25; Provisional
19-157 3.98e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 43.33  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTS--GSVSLAGQCL----MAR---VEQ------HLP--ETLH 81
Cdd:PLN03211   83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPtkqiLKRtgfVTQddilypHLTvrETLV 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  82 TQSLLQavlapLPAD-AREAQRWLAERLLAQMGFTPA----VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PLN03211  163 FCSLLR-----LPKSlTKQEKILVAESVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237

                  .
gi 1439757928 157 D 157
Cdd:PLN03211  238 D 238
cbiO PRK13641
energy-coupling factor transporter ATPase;
415-500 4.71e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 42.51  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLLVSHDRQLISESCNRFWLIDSAGLTE 491
Cdd:PRK13641  146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIK 225

                  ....*....
gi 1439757928 492 WHSLEEVYA 500
Cdd:PRK13641  226 HASPKEIFS 234
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
414-470 6.18e-04

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 41.61  E-value: 6.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 414 TLSGGERSRLlFVGLSLA---RYslLLLDEPTNHLDMEGKAALAQTLR----DYPGGVLLVSHD 470
Cdd:COG4604   135 ELSGGQRQRA-FIAMVLAqdtDY--VLLDEPLNNLDMKHSVQMMKLLRrladELGKTVVIVLHD 195
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
320-474 8.56e-04

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


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 41.30  E-value: 8.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqmNNASPLPGLRLHPRLHP------GYYDQTLAQLPDEASL------------- 380
Cdd:cd03248    37 LHPGEVTALVGPSGSGKSTVVALL----ENFYQPQGGQVLLDGKPisqyehKYLHSKVSLVGQEPVLfarslqdniaygl 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 381 ----LEALTPFAPSADTRKR-ALIAAGFgWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQ 455
Cdd:cd03248   113 qscsFECVKEAAQKAHAHSFiSELASGY-DTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ 191
                         170       180
                  ....*....|....*....|.
gi 1439757928 456 TLRDYPGG--VLLVSHDRQLI 474
Cdd:cd03248   192 ALYDWPERrtVLVIAHRLSTV 212
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
412-470 1.18e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 40.38  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 412 VSTLSGGERSRllfvgLSLARYSLLLLDepTNHLDMEGKAALAQTLRDypggVLLVSHD 470
Cdd:COG0419   156 IETLSGGERLR-----LALADLLSLILD--FGSLDEERLERLLDALEE----LAIITHV 203
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
320-485 1.23e-03

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: 40.56  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNASplpglRLHPRLHPGYYDQTLAqlpdeasLLE 382
Cdd:cd03261    23 VRRGEILAIIGPSGSGKSTLLRLIvgllrpdsgevlidgedISGLSEAE-----LYRLRRRMGMLFQSGA-------LFD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ALTPFA------------PSADTRKRA---LIAAGFGWARHsQKVSTLSGGERSRLlfvglSLARY-----SLLLLDEPT 442
Cdd:cd03261    91 SLTVFEnvafplrehtrlSEEEIREIVlekLEAVGLRGAED-LYPAELSGGMKKRV-----ALARAlaldpELLLYDEPT 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1439757928 443 NHLDMEGKAALAQTLRD----YPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03261   165 AGLDPIASGVIDDLIRSlkkeLGLTSIMVTHDLDTAFAIADRIAVLY 211
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
4-157 1.71e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 39.85  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   4 LLTAHALHVETAFGPLFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV---------------SLAGQCL 68
Cdd:PRK13541    1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniakpycTYIGHNL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  69 MARVEQHLPETLHTQSLLQAVLAPLPAdareAQRWLAERLLaqmgftpavMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK13541   80 GLKLEMTVFENLKFWSEIYNSAETLYA----AIHYFKLHDL---------LDEKCYSLSSGMQKIVAIARLIACQSDLWL 146

                  ....*....
gi 1439757928 149 LDEPGNHLD 157
Cdd:PRK13541  147 LDEVETNLS 155
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
327-470 1.74e-03

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: 40.85  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 327 AIMGRNGGGKSSLLRLL-----------------WQQMNNASPLPglrLHPRlHPGYYDQtlaqlpdEASLLEALT---- 385
Cdd:COG4148    29 ALFGPSGSGKTTLLRAIaglerpdsgrirlggevLQDSARGIFLP---PHRR-RIGYVFQ-------EARLFPHLSvrgn 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 -----PFAPSADTRKR--ALIAA-GFGwarH--SQKVSTLSGGERSRllfVGLS---LARYSLLLLDEPTNHLDMEGKA- 451
Cdd:COG4148    98 llygrKRAPRAERRISfdEVVELlGIG---HllDRRPATLSGGERQR---VAIGralLSSPRLLLMDEPLAALDLARKAe 171
                         170       180
                  ....*....|....*....|....*
gi 1439757928 452 ------ALAQTLrDYPggVLLVSHD 470
Cdd:COG4148   172 ilpyleRLRDEL-DIP--ILYVSHS 193
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
323-480 1.96e-03

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 40.16  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLL--WQQMNNASPLPGLRLHPRLHPGYYDQTLAQLPDEASLLEALTpfapsadtrKRALIA 400
Cdd:PRK10575   37 GKVTGLIGHNGSGKSTLLKMLgrHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMT---------VRELVA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 401 AG----------FGWARHSQK----------------VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKA--- 451
Cdd:PRK10575  108 IGrypwhgalgrFGAADREKVeeaislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVdvl 187
                         170       180       190
                  ....*....|....*....|....*....|
gi 1439757928 452 ALAQTLRDYPG-GVLLVSHDRQLISESCNR 480
Cdd:PRK10575  188 ALVHRLSQERGlTVIAVLHDINMAARYCDY 217
GguA NF040905
sugar ABC transporter ATP-binding protein;
105-152 2.30e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.54  E-value: 2.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1439757928 105 AERLLAQMGF-TPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF040905  384 AEEYRKKMNIkTPSV-FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
323-484 2.39e-03

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: 39.66  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRL---LWQQMNNASPLPGLRLHPrlHPGYYDQTLAQLPDEASLLEALTpfapsadTRKRALI 399
Cdd:cd03266    31 GEVTGLLGPNGAGKTTTLRMlagLLEPDAGFATVDGFDVVK--EPAEARRRLGFVSDSTGLYDRLT-------ARENLEY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 400 AAGF-GWARHSQK-------------------VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRD 459
Cdd:cd03266   102 FAGLyGLKGDELTarleeladrlgmeelldrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ 181
                         170       180
                  ....*....|....*....|....*...
gi 1439757928 460 YPGG---VLLVSHDRQLISESCNRFWLI 484
Cdd:cd03266   182 LRALgkcILFSTHIMQEVERLCDRVVVL 209
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
97-179 2.64e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.10  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928  97 AREAQRWLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL--LWLESFLQTWQGS 174
Cdd:NF000106  117 SRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRneVWDEVRSMVRDGA 195

                  ....*
gi 1439757928 175 FVLVS 179
Cdd:NF000106  196 TVLLT 200
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
327-485 2.72e-03

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 40.09  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 327 AIMGRNGGGKSSLLRLLwqqMNNASPLPG--------LRLHPRLHPGYydqtlaqLPDEASL------LEALTPFA---- 388
Cdd:COG4152    31 GLLGPNGAGKTTTIRII---LGILAPDSGevlwdgepLDPEDRRRIGY-------LPEERGLypkmkvGEQLVYLArlkg 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 -PSADTRKRAL-------IAagfGWARHsqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY 460
Cdd:COG4152   101 lSKAEAKRRADewlerlgLG---DRANK--KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL 175
                         170       180
                  ....*....|....*....|....*...
gi 1439757928 461 --PG-GVLLVSHDRQLISESCNRFWLID 485
Cdd:COG4152   176 aaKGtTVIFSSHQMELVEELCDRIVIIN 203
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
415-510 2.83e-03

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: 40.56  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVgLSLARYSLLLL-DEPTNHLDMEG----KAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGL 489
Cdd:TIGR03269 169 LSGGEKQRVVLA-RQLAKEPFLFLaDEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEI 247
                          90       100
                  ....*....|....*....|.
gi 1439757928 490 TEWHSLEEVYARLQAVAPAPD 510
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGVSEVE 268
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
415-538 3.29e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.07  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG----GVLLVSHDRQLISEscnrfwLIDS-AGL 489
Cdd:PRK15134  157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRK------LADRvAVM 230
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1439757928 490 TEWHSLEEVYARLQAVAPA-PDSRLALQSTPAGADDDEEALLARLIDLEQ 538
Cdd:PRK15134  231 QNGRCVEQNRAATLFSAPThPYTQKLLNSEPSGDPVPLPEPASPLLDVEQ 280
cbiO PRK13637
energy-coupling factor transporter ATPase;
415-469 3.29e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 39.65  E-value: 3.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKA---ALAQTLRD-YPGGVLLVSH 469
Cdd:PRK13637  145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDeilNKIKELHKeYNMTIILVSH 203
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
410-470 3.35e-03

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 38.71  E-value: 3.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 410 QKVStLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY----PGGVLLVSHD 470
Cdd:cd03222    68 QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHD 131
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
412-485 3.51e-03

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 39.69  E-value: 3.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 412 VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY--PGG--VLLVSHDRQLISESCNRFWLID 485
Cdd:COG4586   152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGttILLTSHDMDDIEALCDRVIVID 229
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
320-491 3.97e-03

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 40.19  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL---WQQMNNASPLPGLRLHprlhpGYYDQTL-------AQLPD--EASLLEALTPF 387
Cdd:PRK11160  363 IKAGEKVALLGRTGCGKSTLLQLLtraWDPQQGEILLNGQPIA-----DYSEAALrqaisvvSQRVHlfSATLRDNLLLA 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 APSADTRKRALIAAGFGWARHSQKVS-----------TLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKA 451
Cdd:PRK11160  438 APNASDEALIEVLQQVGLEKLLEDDKglnawlgeggrQLSGGEQRRL-----GIARAllhdaPLLLLDEPTEGLDAETER 512
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1439757928 452 ALAQTLRDYPGG--VLLVSHdRQLISESCNRFWLIDSAGLTE 491
Cdd:PRK11160  513 QILELLAEHAQNktVLMITH-RLTGLEQFDRICVMDNGQIIE 553
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
393-485 5.00e-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: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 393 TRKRALIAAGFGWARHSQKVSTLSGGERSRL-----LFVGLSLARYsllLLDEPTNHLDMEGKAALAQT---LRDYPGGV 464
Cdd:TIGR00630 467 ERLGFLIDVGLDYLSLSRAAGTLSGGEAQRIrlatqIGSGLTGVLY---VLDEPSIGLHQRDNRRLINTlkrLRDLGNTL 543
                          90       100
                  ....*....|....*....|.
gi 1439757928 465 LLVSHDRQLISESCnrfWLID 485
Cdd:TIGR00630 544 IVVEHDEDTIRAAD---YVID 561
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
415-501 6.26e-03

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 38.84  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY--PGG--VLLVSHDrqlISE--SCNRFWLIDSAG 488
Cdd:PRK13635  141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGitVLSITHD---LDEaaQADRVIVMNKGE 217
                          90
                  ....*....|...
gi 1439757928 489 LTEWHSLEEVYAR 501
Cdd:PRK13635  218 ILEEGTPEEIFKS 230
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
307-484 6.29e-03

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


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 38.47  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 307 PGQPSLFTTGVaRLRSGDRVAIMGRNGGGKSSLLRLLWQQM---------NNASPLPGLRLHPRLHPGYYDQTLAQLP-- 375
Cdd:cd03290    12 SGLATLSNINI-RIPTGQLTMIVGQVGCGKSSLLLAILGEMqtlegkvhwSNKNESEPSFEATRSRNRYSVAYAAQKPwl 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 376 DEASLLEALTPFAPSADTRKRALIAA----------GFG-WARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNH 444
Cdd:cd03290    91 LNATVEENITFGSPFNKQRYKAVTDAcslqpdidllPFGdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1439757928 445 LDMEGKAALAQT-----LRDYPGGVLLVSHDRQLISESCnrfWLI 484
Cdd:cd03290   171 LDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYLPHAD---WII 212
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
19-157 8.87e-03

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 39.32  E-value: 8.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928   19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAGQCL---MAR----VEQ---HLPETLHTQSL 85
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLdssFQRsigyVQQqdlHLPTSTVRESL 857
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928   86 LQAVLAPLPADA--REAQRWLAE--RLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL-LDEPGNHLD 157
Cdd:TIGR00956  858 RFSAYLRQPKSVskSEKMEYVEEviKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
415-508 9.54e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 38.13  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY--PGGVLLVS-HDRQLISESCNRFWLIDSAGLTE 491
Cdd:PRK13639  138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKIIK 217
                          90
                  ....*....|....*..
gi 1439757928 492 WHSLEEVYARLQAVAPA 508
Cdd:PRK13639  218 EGTPKEVFSDIETIRKA 234
 
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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