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Conserved domains on  [gi|346645039|gb|AEO37664|]
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ABC transporter [Listeria monocytogenes Finland 1998]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438555)

ABC transporter ATP-binding protein ABC transporter ATP-binding protein containing both ATPase and permease components of an ABC-type transport system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
14-587 0e+00

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 673.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  14 TAFSAAHLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYR 93
Cdd:COG1132    2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  94 IRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDP 173
Cdd:COG1132   82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 174 VLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAV 253
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 254 KIQFLLWPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMD 330
Cdd:COG1132  242 RLSALFFPLMELLGNLGLALVLLVG--GLLVlsgSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 331 VEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILV 410
Cdd:COG1132  320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 411 DGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSA 490
Cdd:COG1132  400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHE 570
Cdd:COG1132  480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
                        570
                 ....*....|....*..
gi 346645039 571 ELMAQHGYYYNLYQSQF 587
Cdd:COG1132  560 ELLARGGLYARLYRLQF 576
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
14-587 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 673.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  14 TAFSAAHLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYR 93
Cdd:COG1132    2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  94 IRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDP 173
Cdd:COG1132   82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 174 VLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAV 253
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 254 KIQFLLWPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMD 330
Cdd:COG1132  242 RLSALFFPLMELLGNLGLALVLLVG--GLLVlsgSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 331 VEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILV 410
Cdd:COG1132  320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 411 DGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSA 490
Cdd:COG1132  400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHE 570
Cdd:COG1132  480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
                        570
                 ....*....|....*..
gi 346645039 571 ELMAQHGYYYNLYQSQF 587
Cdd:COG1132  560 ELLARGGLYARLYRLQF 576
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
35-325 7.13e-131

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 384.51  E-value: 7.13e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18545    2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18545   82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18545  162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 275 YFVGIKG-YGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18545  242 YWYGGKLvLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
19-587 6.17e-130

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 392.53  E-value: 6.17e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   19 AHLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSIT 98
Cdd:TIGR02204   4 RPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   99 LIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLY 178
Cdd:TIGR02204  84 WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  179 SLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIF-TEVSNEYR--------RSW 249
Cdd:TIGR02204 164 VLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFgGAVEKAYEaarqrirtRAL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  250 MKAVKIQF-------LLWPGVQNIavmttcliyfvgIKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYL 322
Cdd:TIGR02204 244 LTAIVIVLvfgaivgVLWVGAHDV------------IAG---KMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  323 ERIFETMDVEPDIKDIPNAKKMP-PIVGNVDFKDVYFRYEEGVD--ILKGINFHVDAGESIALVGPTGAGKTTIINLLSR 399
Cdd:TIGR02204 309 ERLIELLQAEPDIKAPAHPKTLPvPLRGEIEFEQVNFAYPARPDqpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLR 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  400 FYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYT 479
Cdd:TIGR02204 389 FYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDT 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  480 EVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYID 559
Cdd:TIGR02204 469 YLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMD 548
                         570       580
                  ....*....|....*....|....*...
gi 346645039  560 NGRIQEAGSHEELMAQHGYYYNLYQSQF 587
Cdd:TIGR02204 549 QGRIVAQGTHAELIAKGGLYARLARLQF 576
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
23-591 2.78e-107

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 334.62  E-value: 2.78e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  23 RILVYVKPYQK-SIYITLFVILLAnVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcmryrirsITLIG 101
Cdd:PRK13657   9 RVLQYLGAEKRlGILLAVANVLLA-AATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGV--------LVARH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 102 QDILKDMR-----TAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDpvlt 176
Cdd:PRK13657  80 ADRLAHRRrlavlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMN---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 177 lYSLALIPVLFVIVMVIKTA--QRKAY---QVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEyrrswMK 251
Cdd:PRK13657 156 -WRLSLVLVVLGIVYTLITTlvMRKTKdgqAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADN-----LL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 252 AVKIQFLLWPGVQNI-----AVMTTCLIYFVGI----KGygvDVSTGTLIAFIGyvgnFWNPVI----NIGNFYNSLITA 318
Cdd:PRK13657 230 AAQMPVLSWWALASVlnraaSTITMLAILVLGAalvqKG---QLRVGEVVAFVG----FATLLIgrldQVVAFINQVFMA 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 319 TTYLERIFETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLS 398
Cdd:PRK13657 303 APKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 399 RFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYY 478
Cdd:PRK13657 383 RVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYD 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 479 TEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYI 558
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF 542
                        570       580       590
                 ....*....|....*....|....*....|...
gi 346645039 559 DNGRIQEAGSHEELMAQHGYYYNLYQSQFdMLQ 591
Cdd:PRK13657 543 DNGRVVESGSFDELVARGGRFAALLRAQG-MLQ 574
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
367-516 7.54e-39

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: 139.71  E-value: 7.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039  446 RYGkldATEEEIIAAAKVVRAHDFIS--GLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
GguA NF040905
sugar ABC transporter ATP-binding protein;
363-549 9.41e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 77.14  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGenvEEVTLRSLRS--QMGVML--QD-TF 435
Cdd:NF040905  13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRDseALGIVIihQElAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 IFSGTIIENI-------RYGKLDATEEEIIAA---AKVvrahdfisGLKDGYYTEVKERGstlsAGQRQLISFARALLAD 505
Cdd:NF040905  90 IPYLSIAENIflgneraKRGVIDWNETNRRARellAKV--------GLDESPDTLVTDIG----VGKQQLVEIAKALSKD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 346645039 506 PKILILDEATSSI-DTQTEILLQEGLERLLEGRTSFIIAHRLSTI 549
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEI 202
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
359-544 1.21e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 63.79  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnvEEVTLRSLRSQmgvmLQDTFifS 438
Cdd:NF040873   1 GYG-GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSE----VPDSL--P 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENIRYG---------KLDATEEEIIAAA-KVVRAHDFisglkdgyyteVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:NF040873  72 LTVRDLVAMGrwarrglwrRLTRDDRAAVDDAlERVGLADL-----------AGRQLGELSGGQRQRALLAQGLAQEADL 140
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAH 544
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTH 177
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
377-564 1.44e-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: 57.00  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   377 GESIALVGPTGAGKTTIINLLSRFYNINSGE-ILVDGENVEEVTLRSLRsqmgvmlqdtfifsgtiienirygkldatee 455
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   456 eiiaaakvvrahdfisglkdgyYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLE---- 531
Cdd:smart00382  51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 346645039   532 --RLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQ 564
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
GguA NF040905
sugar ABC transporter ATP-binding protein;
366-519 5.24e-09

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 58.65  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTI-INLLSRFYNIN-SGEILVDGEnveEVTLRSL--------------RSQMGV 429
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGK---EVDVSTVsdaidaglayvtedRKGYGL 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTfifsgtIIENI---------RYGKLDATEEEIIA----AAKVVRAHDfisglkdgyyteVKERGSTLSAGQRQLI 496
Cdd:NF040905 352 NLIDD------IKRNItlanlgkvsRRGVIDENEEIKVAeeyrKKMNIKTPS------------VFQKVGNLSGGNQQKV 413
                        170       180
                 ....*....|....*....|...
gi 346645039 497 SFARALLADPKILILDEATSSID 519
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGID 436
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
488-577 2.15e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 41.26  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 488 LSAGQRQLISFARALLADPKILILDEATSSIDTQT-----EILLQegLERlLEGRTSFIIAHRLSTIKNSSRIFYIDNGR 562
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVArdmfwRLLIE--LSR-EDGVTIFISTHFMNEAERCDRISLMHAGR 474
                         90
                 ....*....|....*
gi 346645039 563 IQEAGSHEELMAQHG 577
Cdd:NF033858 475 VLASDTPAALVAARG 489
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
14-587 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 673.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  14 TAFSAAHLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYR 93
Cdd:COG1132    2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  94 IRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDP 173
Cdd:COG1132   82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 174 VLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAV 253
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 254 KIQFLLWPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMD 330
Cdd:COG1132  242 RLSALFFPLMELLGNLGLALVLLVG--GLLVlsgSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 331 VEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILV 410
Cdd:COG1132  320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 411 DGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSA 490
Cdd:COG1132  400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHE 570
Cdd:COG1132  480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
                        570
                 ....*....|....*..
gi 346645039 571 ELMAQHGYYYNLYQSQF 587
Cdd:COG1132  560 ELLARGGLYARLYRLQF 576
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
21-586 3.11e-169

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: 498.20  E-value: 3.11e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  21 LKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRY-RIRSITL 99
Cdd:COG2274  144 LRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGL-LRLlRSYLLLR 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 100 IGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYS 179
Cdd:COG2274  223 LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 180 LALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLL 259
Cdd:COG2274  302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 260 WPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIK 336
Cdd:COG2274  382 STLSGLLQQLATVALLWLG--AYLVidgQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPERE 459
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 337 DIPNAKKMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV 415
Cdd:COG2274  460 EGRSKLSLPRLKGDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL 539
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 416 EEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQL 495
Cdd:COG2274  540 RQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 496 ISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:COG2274  620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
                        570
                 ....*....|.
gi 346645039 576 HGYYYNLYQSQ 586
Cdd:COG2274  700 KGLYAELVQQQ 710
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
35-325 7.13e-131

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 384.51  E-value: 7.13e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18545    2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18545   82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18545  162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 275 YFVGIKG-YGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18545  242 YWYGGKLvLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
19-587 6.17e-130

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 392.53  E-value: 6.17e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   19 AHLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSIT 98
Cdd:TIGR02204   4 RPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   99 LIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLY 178
Cdd:TIGR02204  84 WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  179 SLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIF-TEVSNEYR--------RSW 249
Cdd:TIGR02204 164 VLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFgGAVEKAYEaarqrirtRAL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  250 MKAVKIQF-------LLWPGVQNIavmttcliyfvgIKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYL 322
Cdd:TIGR02204 244 LTAIVIVLvfgaivgVLWVGAHDV------------IAG---KMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  323 ERIFETMDVEPDIKDIPNAKKMP-PIVGNVDFKDVYFRYEEGVD--ILKGINFHVDAGESIALVGPTGAGKTTIINLLSR 399
Cdd:TIGR02204 309 ERLIELLQAEPDIKAPAHPKTLPvPLRGEIEFEQVNFAYPARPDqpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLR 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  400 FYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYT 479
Cdd:TIGR02204 389 FYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDT 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  480 EVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYID 559
Cdd:TIGR02204 469 YLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMD 548
                         570       580
                  ....*....|....*....|....*...
gi 346645039  560 NGRIQEAGSHEELMAQHGYYYNLYQSQF 587
Cdd:TIGR02204 549 QGRIVAQGTHAELIAKGGLYARLARLQF 576
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
20-588 7.09e-130

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: 392.16  E-value: 7.09e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   20 HLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITL 99
Cdd:TIGR02203   1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  100 IGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYS 179
Cdd:TIGR02203  81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  180 LALIPVLFVIVMVIktaqRKAYQVLSNKQSNMNA----YIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKI 255
Cdd:TIGR02203 161 VVMLPVLSILMRRV----SKRLRRISKEIQNSMGqvttVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  256 QFLLWPGVQNIA-VMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPD 334
Cdd:TIGR02203 237 GSISSPITQLIAsLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  335 IKDipNAKKMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE 413
Cdd:TIGR02203 317 KDT--GTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  414 NVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKL-DATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQ 492
Cdd:TIGR02203 395 DLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQ 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  493 RQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNEL 554
                         570
                  ....*....|....*.
gi 346645039  573 MAQHGYYYNLYQSQFD 588
Cdd:TIGR02203 555 LARNGLYAQLHNMQFR 570
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
351-583 7.69e-124

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: 364.24  E-value: 7.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYE-EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:cd03251    1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLY 583
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
349-577 1.53e-119

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: 353.07  E-value: 1.53e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:cd03254    1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03254   81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHG 577
Cdd:cd03254  161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
39-586 4.58e-114

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 352.59  E-value: 4.58e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDDtiPNKNMTQLFWIAVIFIVSVIVTGLCMRY--RIRSI--TLIGQDILKDMRTAIFG 114
Cdd:COG5265   42 LLLLLLAAALALVVPPLLKDAIDA--LLSGAAALLVVPVGLLLAYGLLRLLSVLfgELRDAlfARVTQRAVRRLALEVFR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHG---KILIRVVNYInmlSDLLSNGLINLISDILSVIVTLGFML-MIDPVLTLYSLALIpVLFVIV 190
Cdd:COG5265  120 HLHALSLRFHLERQTGglsRDIERGTKGI---EFLLRFLLFNILPTLLEIALVAGILLvKYDWWFALITLVTV-VLYIAF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 191 MVIKTAQRKAYQVLSNKQ-SNMNAYIHESIAGIKVTQSFSREEenFEiftevSNEYRRSWMK----AVKIQFLLwpGVQN 265
Cdd:COG5265  196 TVVVTEWRTKFRREMNEAdSEANTRAVDSLLNYETVKYFGNEA--RE-----ARRYDEALARyeraAVKSQTSL--ALLN 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 266 I---AVMTTCLIYFVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDIP 339
Cdd:COG5265  267 FgqaLIIALGLTAMMLMAAQGVvagTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAP 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 340 NAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT 419
Cdd:COG5265  347 DAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT 426
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 420 LRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFA 499
Cdd:COG5265  427 QASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYY 579
Cdd:COG5265  507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586

                 ....*..
gi 346645039 580 YNLYQSQ 586
Cdd:COG5265  587 AQMWARQ 593
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
351-586 2.83e-113

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: 337.59  E-value: 2.83e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEE--GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:cd03249    1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
22-577 1.27e-111

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: 344.82  E-value: 1.27e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  22 KRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTI-PNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLI 100
Cdd:COG4988    6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 101 GQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLIsdiLSVIVT---LGFMLMIDPV--- 174
Cdd:COG4988   86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLF---LAALVPlliLVAVFPLDWLsgl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 175 LTLYSLALIPVLFVIVMVI-KTAQRKAYQVLSNkqsnMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAV 253
Cdd:COG4988  163 ILLVTAPLIPLFMILVGKGaAKASRRQWRALAR----LSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 254 KIQFLlwpgvqNIAVM-------TTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIF 326
Cdd:COG4988  239 RVAFL------SSAVLeffaslsIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIF 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 327 ETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSG 406
Cdd:COG4988  313 ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 407 EILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGS 486
Cdd:COG4988  393 SILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGR 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 487 TLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEA 566
Cdd:COG4988  473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
                        570
                 ....*....|.
gi 346645039 567 GSHEELMAQHG 577
Cdd:COG4988  553 GTHEELLAKNG 563
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
23-591 2.78e-107

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 334.62  E-value: 2.78e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  23 RILVYVKPYQK-SIYITLFVILLAnVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcmryrirsITLIG 101
Cdd:PRK13657   9 RVLQYLGAEKRlGILLAVANVLLA-AATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGV--------LVARH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 102 QDILKDMR-----TAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDpvlt 176
Cdd:PRK13657  80 ADRLAHRRrlavlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMN---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 177 lYSLALIPVLFVIVMVIKTA--QRKAY---QVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEyrrswMK 251
Cdd:PRK13657 156 -WRLSLVLVVLGIVYTLITTlvMRKTKdgqAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADN-----LL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 252 AVKIQFLLWPGVQNI-----AVMTTCLIYFVGI----KGygvDVSTGTLIAFIGyvgnFWNPVI----NIGNFYNSLITA 318
Cdd:PRK13657 230 AAQMPVLSWWALASVlnraaSTITMLAILVLGAalvqKG---QLRVGEVVAFVG----FATLLIgrldQVVAFINQVFMA 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 319 TTYLERIFETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLS 398
Cdd:PRK13657 303 APKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 399 RFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYY 478
Cdd:PRK13657 383 RVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYD 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 479 TEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYI 558
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF 542
                        570       580       590
                 ....*....|....*....|....*....|...
gi 346645039 559 DNGRIQEAGSHEELMAQHGYYYNLYQSQFdMLQ 591
Cdd:PRK13657 543 DNGRVVESGSFDELVARGGRFAALLRAQG-MLQ 574
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
22-588 8.97e-107

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 333.14  E-value: 8.97e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  22 KRILVYVKPYqKSIYITLFVILLANVAT---MIgpYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSIT 98
Cdd:PRK11176  14 RRLWPTIAPF-KAGLIVAGVALILNAASdtfML--SLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCIS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  99 LIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMidpvltlY 178
Cdd:PRK11176  91 WVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFY-------Y 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 179 SLALIPVLFVIVMVIKTAQR---KAYQVLS-NKQSNM---NAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMK 251
Cdd:PRK11176 164 SWQLSLILIVIAPIVSIAIRvvsKRFRNISkNMQNTMgqvTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 252 AVKIQFLLWPGVQNIAVMT-TCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVinignfyNSLITATTYLER------ 324
Cdd:PRK11176 244 MVSASSISDPIIQLIASLAlAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPL-------KSLTNVNAQFQRgmaacq 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 325 -IFETMDVEPDiKDIpNAKKMPPIVGNVDFKDVYFRYEeGVDI--LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY 401
Cdd:PRK11176 317 tLFAILDLEQE-KDE-GKRVIERAKGDIEFRNVTFTYP-GKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 402 NINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDA-TEEEIIAAAKVVRAHDFISGLKDGYYTE 480
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 481 VKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDN 560
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
                        570       580
                 ....*....|....*....|....*...
gi 346645039 561 GRIQEAGSHEELMAQHGYYYNLYQSQFD 588
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQFG 581
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
351-586 1.59e-106

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: 320.33  E-value: 1.59e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:cd03253    1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILI 510
Cdd:cd03253   81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 511 LDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:cd03253  161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
24-586 5.11e-106

type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 334.40  E-value: 5.11e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   24 ILVYVKPYQKSIYITLFVILLAnvatMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQD 103
Cdd:TIGR01846 134 IIRYRKQFREVLLISLALQLFA----LVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSR 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  104 ILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALI 183
Cdd:TIGR01846 210 IDVELGARLYRHLLGLPLGYFESRRVGDTVARV-RELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSL 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  184 PVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGV 263
Cdd:TIGR01846 289 VCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAI 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  264 QNIAVMTTCLIYFVGIKGY-GVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDvEPDIKDIPNAK 342
Cdd:TIGR01846 369 ELIQKLTFAILLWFGAHLViGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLA 447
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  343 KMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR 421
Cdd:TIGR01846 448 ALPELRGAITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA 527
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  422 SLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARA 501
Cdd:TIGR01846 528 WLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  502 LLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYN 581
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687

                  ....*
gi 346645039  582 LYQSQ 586
Cdd:TIGR01846 688 LWQQQ 692
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
2-582 9.69e-106

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 334.00  E-value: 9.69e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039    2 ARNKFDIDEELETAfsaAHLKRILVYVKPyQKSIYITLFVIL-LANVATMIGPYLTKIVIDdTIPNKNMTQLFWIAVIF- 79
Cdd:TIGR00958 133 ASEKEAEQGQSETA---DLLFRLLGLSGR-DWPWLISAFVFLtLSSLGEMFIPFYTGRVID-TLGGDKGPPALASAIFFm 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   80 ----IVSVIVTGL---CMRYRIRSITLigqdilkDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLI 152
Cdd:TIGR00958 208 cllsIASSVSAGLrggSFNYTMARINL-------RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVN 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  153 NLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKtaqrKAYQVLSNK------QSNMNAyiHESIAGIKVTQ 226
Cdd:TIGR00958 281 VLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFG----KRYQLLSEElqeavaKANQVA--EEALSGMRTVR 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  227 SFSREEENFEIFTEVSNEYRR-SWMKAVKIQFLLWpgvqNIAVMTtcLIYFVGIKGYGV------DVSTGTLIAFIGYVG 299
Cdd:TIGR00958 355 SFAAEEGEASRFKEALEETLQlNKRKALAYAGYLW----TTSVLG--MLIQVLVLYYGGqlvltgKVSSGNLVSFLLYQE 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  300 NFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKdiPNAKKMP-PIVGNVDFKDVYFRY--EEGVDILKGINFHVDA 376
Cdd:TIGR00958 429 QLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP--LTGTLAPlNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHP 506
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  377 GESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEE 456
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEE 586
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  457 IIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERllEG 536
Cdd:TIGR00958 587 IMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--AS 664
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 346645039  537 RTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNL 582
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
78-584 2.47e-98

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: 310.54  E-value: 2.47e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  78 IFIVSVIVTGLCM-----RY--RIRS--ITLigqDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLS 148
Cdd:COG4987   54 LFVPIVGVRAFAIgrtvfRYleRLVShdATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 149 NGLINLISDILSVIVTLGFMLMIDPVLTL-YSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQS 227
Cdd:COG4987  131 RVLLPLLVALLVILAAVAFLAFFSPALALvLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAA 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 228 FSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGY----VGNFWN 303
Cdd:COG4987  211 YGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLaalaLFEALA 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 304 PVINIGNFYNSLITAttyLERIFETMDVEPDIKDiPNAKKMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIAL 382
Cdd:COG4987  291 PLPAAAQHLGRVRAA---ARRLNELLDAPPAVTE-PAEPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAI 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 383 VGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAK 462
Cdd:COG4987  367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALE 446
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 463 VVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFII 542
Cdd:COG4987  447 RVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLI 526
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 346645039 543 AHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQ 584
Cdd:COG4987  527 THRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
21-586 8.89e-96

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 304.72  E-value: 8.89e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  21 LKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNM--TQLFWIAVIFIVSVIVTGLCMRYRIRSIT 98
Cdd:PRK10790  11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLplGLVAGLAAAYVGLQLLAAGLHYAQSLLFN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  99 LIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLsnglINLISDILSVIVTLGFML----MIDPV 174
Cdd:PRK10790  91 RAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLY----VTVVATVLRSAALIGAMLvamfSLDWR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 175 LTLYSLALIPVLFvIVMVIktAQRKAYQVLSNKQS---NMNAYIHESIAGIKVTQSFsREEENF-EIFTEVSNEYRRSWM 250
Cdd:PRK10790 167 MALVAIMIFPAVL-VVMVI--YQRYSTPIVRRVRAylaDINDGFNEVINGMSVIQQF-RQQARFgERMGEASRSHYMARM 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 251 KAVKIQ-FLLWPGVQNIAVMTTC-LIYFVGIKGYGVdVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFET 328
Cdd:PRK10790 243 QTLRLDgFLLRPLLSLFSALILCgLLMLFGFSASGT-IEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 329 MDVE-----PDIKdipnakkmPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNI 403
Cdd:PRK10790 322 MDGPrqqygNDDR--------PLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 404 NSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKE 483
Cdd:PRK10790 394 TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 484 RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
                        570       580
                 ....*....|....*....|...
gi 346645039 564 QEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:PRK10790 553 VEQGTHQQLLAAQGRYWQMYQLQ 575
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
28-586 4.27e-85

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 279.15  E-value: 4.27e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   28 VKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRyrIRSITLIGQDILKD 107
Cdd:TIGR03797 131 LRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQL--AQSLAVLRLETRMD 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  108 MRT--AIFGHLQKLPFSYFDSRPHGKILIRVVNyINMLSDLLSN-GLINLISDILSVIvTLGFMLMIDPVLTLYSLALIP 184
Cdd:TIGR03797 209 ASLqaAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGsTLTTLLSGIFALL-NLGLMFYYSWKLALVAVALAL 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  185 VLFVIVMVIK----TAQRKAyQVLSNKQSNMNAYIHESIAGIKVTQSfsrEEENFEIFTEVSNEYRRSWMKAVKIQFLL- 259
Cdd:TIGR03797 287 VAIAVTLVLGllqvRKERRL-LELSGKISGLTVQLINGISKLRVAGA---ENRAFARWAKLFSRQRKLELSAQRIENLLt 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  260 -----WPGVQNIAvmttcLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPD 334
Cdd:TIGR03797 363 vfnavLPVLTSAA-----LFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPE 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  335 IkdipNAKKMPP--IVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVD 411
Cdd:TIGR03797 438 V----DEAKTDPgkLSGAIEVDRVTFRYrPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYD 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  412 GENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIrYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAG 491
Cdd:TIGR03797 514 GQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGG 592
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  492 QRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLleGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEE 571
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDE 670
                         570
                  ....*....|....*
gi 346645039  572 LMAQHGYYYNLYQSQ 586
Cdd:TIGR03797 671 LMAREGLFAQLARRQ 685
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
351-586 7.31e-83

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: 259.34  E-value: 7.31e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYE-EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:cd03252    1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:cd03252   81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:cd03252  161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
35-325 5.49e-81

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 256.55  E-value: 5.49e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTI--PNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18544    1 FILALLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18544   81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18544  161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 346645039 273 LI-YFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18544  241 LVlWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
41-582 5.80e-80

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 262.90  E-value: 5.80e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   41 VILLANVA----TMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRyriRSITLIGQDILKDMRTAIFGHL 116
Cdd:TIGR01192  23 LIVIANITlaaiTIAEPILFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVA---READRLAHGRRATLLTEAFGRI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:TIGR01192 100 ISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQR 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSR-EEENFEI--FTE--VSNEYR--RSWMKAVKIQFLlwpgVQNIAVM 269
Cdd:TIGR01192 180 TKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRiEAETSALkqFTNnlLSAQYPvlDWWALASGLNRM----ASTISMM 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  270 TTCLI-YFVGIKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDIPNAKKMPPIV 348
Cdd:TIGR01192 256 CILVIgTVLVIKG---ELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELPNVK 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  349 GNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:TIGR01192 333 GAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIA 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  429 VMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:TIGR01192 413 TVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPI 492
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039  509 LILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNL 582
Cdd:TIGR01192 493 LVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
32-583 1.20e-78

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: 262.75  E-value: 1.20e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   32 QKS-IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRT 110
Cdd:TIGR01193 154 QKKlIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIIL 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  111 AIFGHLQKLPFSYFDSRPHGKILIRVVNyINMLSDLLSNGLINLISDiLSVIVTLGFMLMI-DPVLTLYSLALIPVLFVI 189
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLD-MWILVIVGLFLVRqNMLLFLLSLLSIPVYAVI 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  190 VMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENF-EIFTEVSNEYRRS--WMKAVKIQFLLWPGVQNI 266
Cdd:TIGR01193 312 IILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYsKIDSEFGDYLNKSfkYQKADQGQQAIKAVTKLI 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  267 avMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDIPNAKKMPP 346
Cdd:TIGR01193 392 --LNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNN 469
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  347 IVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQ 426
Cdd:TIGR01193 470 LNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  427 MGVMLQDTFIFSGTIIENIRYG-KLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLAD 505
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039  506 PKILILDEATSSIDTQTEILLQEGLERLLEgRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLY 583
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
38-582 3.63e-77

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 258.72  E-value: 3.63e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   38 TLFVILLANVATMIG----PYLTKIVIDDTIPNKN---MTQLFWIAVIfivSVIVTGLCMRYRIRSITLIGQDILKDMRT 110
Cdd:TIGR03796 155 ALLYLLLAGLLLVLPglviPAFSQIFVDEILVQGRqdwLRPLLLGMGL---TALLQGVLTWLQLYYLRRLEIKLAVGMSA 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  111 AIFGHLQKLPFSYFDSRPHGKILIRV-VNyiNMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIpVLFVI 189
Cdd:TIGR03796 232 RFLWHILRLPVRFFAQRHAGDIASRVqLN--DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFA-AINVL 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  190 VMVIKTAQRkayqVLSNKQSNMNA--YIHESIAGIKVTQSF--SREEENFeiFTEVSNEYRRSWMKAVKIQFLL-WPGV- 263
Cdd:TIGR03796 309 ALQLVSRRR----VDANRRLQQDAgkLTGVAISGLQSIETLkaSGLESDF--FSRWAGYQAKLLNAQQELGVLTqILGVl 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  264 -QNIAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDI 338
Cdd:TIGR03796 383 pTLLTSLNSALILVVGglrvMEG---QLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPLLE 459
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  339 ------PNAKKMPPIVGNVDFKDVYFRYEE-GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVD 411
Cdd:TIGR03796 460 epegsaATSEPPRRLSGYVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  412 GENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYgkLDAT--EEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLS 489
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTL--WDPTipDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLS 617
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERllEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSH 569
Cdd:TIGR03796 618 GGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTH 695
                         570
                  ....*....|...
gi 346645039  570 EELMAQHGYYYNL 582
Cdd:TIGR03796 696 EELWAVGGAYARL 708
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
68-555 5.39e-73

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: 242.96  E-value: 5.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   68 NMTQLFWIAVIFIVsVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLL 147
Cdd:TIGR02857  40 LAELLPALGALALV-LLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYF 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  148 SNGLINLIsdiLSVIVTLGFMLMIDP------VLTLYSLALIPVLFVIV-MVIKTAQRKAYQVLSNkqsnMNAYIHESIA 220
Cdd:TIGR02857 119 ARYLPQLV---LAVIVPLAILAAVFPqdwisgLILLLTAPLIPIFMILIgWAAQAAARKQWAALSR----LSGHFLDRLR 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  221 GIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI-YFVGIK--GYGVDVSTGTLIAFIgy 297
Cdd:TIGR02857 192 GLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVaVYIGFRllAGDLDLATGLFVLLL-- 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  298 VGNFWNPVINIGNFYNSLITATTYLERIFETMD----VEPDIKDIPnAKKMPPIVgnvdFKDVYFRYEEGVDILKGINFH 373
Cdd:TIGR02857 270 APEFYLPLRQLGAQYHARADGVAAAEALFAVLDaaprPLAGKAPVT-AAPASSLE----FSGVSVAYPGRRPALRPVSFT 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  374 VDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDAT 453
Cdd:TIGR02857 345 VPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDAS 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  454 EEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL 533
Cdd:TIGR02857 425 DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL 504
                         490       500
                  ....*....|....*....|..
gi 346645039  534 LEGRTSFIIAHRLSTIKNSSRI 555
Cdd:TIGR02857 505 AQGRTVLLVTHRLALAALADRI 526
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
351-562 6.75e-73

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: 230.73  E-value: 6.75e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:cd03228    1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSGTIIENIrygkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPKIL 509
Cdd:cd03228   81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGR 562
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
37-325 1.75e-72

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 234.37  E-value: 1.75e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd07346    3 LALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd07346   83 QRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd07346  163 IRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd07346  243 YG--GYLVlqgSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
349-568 2.01e-71

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: 228.92  E-value: 2.01e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03244    1 GDIEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENirygkLD----ATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALL 503
Cdd:cd03244   81 SIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGS 568
Cdd:cd03244  156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
35-325 3.60e-71

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 230.84  E-value: 3.60e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18546    1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18546   81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18546  161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 346645039 275 YFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18546  241 LLVG--AWRVaagTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
41-586 2.06e-70

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 237.30  E-value: 2.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  41 VILLANVATM--IGPYLTKIVIDDtIPNKNMTQ---LFWIAVIFIVSVIVTGLcmRYRIRsITLIGQD--ILKDMRTAIF 113
Cdd:PRK10789   1 VALLIIIAMLqlIPPKVVGIIVDG-VTEQHMTTgqiLMWIGTMVLIAVVVYLL--RYVWR-VLLFGASyqLAVELREDFY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 114 GHL-QKLPFSYFDSRPhGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFM-LMIDPVLTLYSLALIPVLfviVM 191
Cdd:PRK10789  77 RQLsRQHPEFYLRHRT-GDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVM---AI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 192 VIKTAQRKAYQVLSNKQ---SNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQnIAV 268
Cdd:PRK10789 153 MIKRYGDQLHERFKLAQaafSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIY-IAI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 269 MTTCLIYfVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDipNAKKMP 345
Cdd:PRK10789 232 GMANLLA-IGGGSWMVvngSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKD--GSEPVP 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 346 PIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLR 424
Cdd:PRK10789 309 EGRGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK10789 389 SRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQ 584
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548

                 ..
gi 346645039 585 SQ 586
Cdd:PRK10789 549 YQ 550
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
349-563 7.77e-67

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: 216.95  E-value: 7.77e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVD--ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQ 426
Cdd:cd03248   10 GIVKFQNVTFAYPTRPDtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:cd03248   90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03248  170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
31-582 3.99e-64

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: 229.06  E-value: 3.99e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039    31 YQKSI--YITLFVILL---ANVATMIGPYLTKIVIDDTIPN--KNMTQlFWIAVIFIVSVIVTGLCMRYRIrSITLIGQD 103
Cdd:TIGR00957  958 YMKAIglFITFLSIFLfvcNHVSALASNYWLSLWTDDPMVNgtQNNTS-LRLSVYGALGILQGFAVFGYSM-AVSIGGIQ 1035
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   104 ILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALI 183
Cdd:TIGR00957 1036 ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLG 1115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   184 PVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSrEEENFEIFTEVS-NEYRRSWMKAVKIQFLLWPG 262
Cdd:TIGR00957 1116 LLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE-EQERFIHQSDLKvDENQKAYYPSIVANRWLAVR 1194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   263 VQNIAvmtTCLIYFVGIkgYGVdVSTGTLIAfiGYVGNFWNPVINIGNFYNSLI-------TATTYLERIFETMDVEPDI 335
Cdd:TIGR00957 1195 LECVG---NCIVLFAAL--FAV-ISRHSLSA--GLVGLSVSYSLQVTFYLNWLVrmssemeTNIVAVERLKEYSETEKEA 1266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   336 KDIPNAKKMP---PIVGNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVD 411
Cdd:TIGR00957 1267 PWQIQETAPPsgwPPRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   412 GENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIR-YGKLdaTEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSA 490
Cdd:TIGR00957 1347 GLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHE 570
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPS 1504
                          570
                   ....*....|..
gi 346645039   571 ELMAQHGYYYNL 582
Cdd:TIGR00957 1505 NLLQQRGIFYSM 1516
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
349-563 1.27e-63

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: 208.60  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03245    1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03245   81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03245  161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
35-325 8.45e-62

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 206.49  E-value: 8.45e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDD------TIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDM 108
Cdd:cd18547    1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 109 RTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFV 188
Cdd:cd18547   81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 189 IVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAV 268
Cdd:cd18547  161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 269 MTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18547  241 LGYVLVAVVGgllvING---ALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
323-586 1.55e-59

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 208.14  E-value: 1.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 323 ERIFETMDVEPDIKdIPNAKKMPPIVGNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY 401
Cdd:PRK11160 312 RRINEITEQKPEVT-FPTTSTAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 402 NINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGlKDGYYTEV 481
Cdd:PRK11160 391 DPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWL 469
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 482 KERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEillQEGLERLLE---GRTSFIIAHRLSTIKNSSRIFYI 558
Cdd:PRK11160 470 GEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE---RQILELLAEhaqNKTVLMITHRLTGLEQFDRICVM 546
                        250       260
                 ....*....|....*....|....*...
gi 346645039 559 DNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:PRK11160 547 DNGQIIEQGTHQELLAQQGRYYQLKQRL 574
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
37-325 7.05e-58

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 195.73  E-value: 7.05e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18542    3 LAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18542   83 QRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEenFEI--FTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18542  163 VRPAFEEIREQEGELNTVLQENLTGVRVVKAFARED--YEIekFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 275 YFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18542  241 LWVGgylvING---EITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
43-584 3.44e-57

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 202.00  E-value: 3.44e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  43 LLANVatmigpyLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcmRYRIRSITliGQDILKDMRTAIFGHLQKLPFS 122
Cdd:PRK11174  44 LLATI-------LQALIIENIPREALLPPFILLILLFVLRALLAWL--RERVGFKA--GQHIRQQIRQQVLDKLQQLGPA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 123 YFDSRPHGKILIRVVNYINMLSDLLSNGLINLIsdiLSVIVTLGFMLMIDPV-----LTLYSLA-LIPvLFVIVMVIKTA 196
Cdd:PRK11174 113 WIQGKPAGSWATLVLEQVEDMHDFYARYLPQMA---LAVLVPLLILIAVFPInwaagLILLGTApLIP-LFMALVGMGAA 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 Q--RKAYQVLSNkqsnMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLwPGVQ------NIAV 268
Cdd:PRK11174 189 DanRRNFLALAR----LSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLS-SAVLeffasiSIAL 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 269 MTtclIYF---------VGIKGYGVDVSTGTLIAFIGyvGNFWNPVINIGNFYNS---LITATTYLERIFETmdvepDIK 336
Cdd:PRK11174 264 VA---VYFgfsylgelnFGHYGTGVTLFAGFFVLILA--PEFYQPLRDLGTFYHAkaqAVGAAESLVTFLET-----PLA 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 337 DIPNAKKMPPIVGNVDF--KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNinsGEILVDG 412
Cdd:PRK11174 334 HPQQGEKELASNDPVTIeaEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKING 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 413 ENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQ 492
Cdd:PRK11174 411 IELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQ 490
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 493 RQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
                        570
                 ....*....|..
gi 346645039 573 MAQHGYYYNLYQ 584
Cdd:PRK11174 571 SQAGGLFATLLA 582
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
91-546 3.81e-56

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: 197.97  E-value: 3.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   91 RYRIRsitLIGQD----ILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLG 166
Cdd:TIGR02868  70 RYLER---LVGHDaalrSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  167 FMLMIDPVLTLySLALIPVLFVIVM--VIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNE 244
Cdd:TIGR02868 147 AIAVLSVPAAL-ILAAGLLLAGFVAplVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRE 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  245 YRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIA-FIGYVGNFWNPVINIGNFYNSLITATTYLE 323
Cdd:TIGR02868 226 LTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAvLVLLPLAAFEAFAALPAAAQQLTRVRAAAE 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  324 RIFETMDVEP--DIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY 401
Cdd:TIGR02868 306 RIVEVLDAAGpvAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  402 NINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEV 481
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVL 465
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039  482 KERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRL 546
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
308-575 6.41e-55

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: 195.35  E-value: 6.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 308 IGNfYNSLITATTYLERIFETMDVEPdikdiPNAKKM--PPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVG 384
Cdd:COG4618  292 IGG-WKQFVSARQAYRRLNELLAAVP-----AEPERMplPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIG 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 385 PTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI-RYGklDATEEEIIAAAKV 463
Cdd:COG4618  366 PSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKL 443
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 464 VRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFII 542
Cdd:COG4618  444 AGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVI 523
                        250       260       270
                 ....*....|....*....|....*....|...
gi 346645039 543 AHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:COG4618  524 THRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
37-325 9.15e-55

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 187.72  E-value: 9.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDD----TIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18563    3 LGFLLMLLGTALGLVPPYLTKILIDDvliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18563   83 YEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18563  163 FWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 273 LIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18563  243 IVWYFG--GRQVlsgTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
37-325 1.08e-54

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 187.36  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDD-TIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGH 115
Cdd:cd18778    3 LTLLCALLSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18778   83 LQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIY 275
Cdd:cd18778  163 KVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 346645039 276 FVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18778  243 GFG--GRLVlagELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
28-575 2.95e-54

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: 192.95  E-value: 2.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   28 VKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKD 107
Cdd:TIGR01842   1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  108 MRTAIFghlqKLPFSYFDSRPHGKILiRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLF 187
Cdd:TIGR01842  81 LNQPIF----AASFSATLRRGSGDGL-QALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  188 VIVMVIKTAQRKAYqvlsnKQSNMnayihESIAGIKVTQSFSREEENFEIFTEVSNEYRRsWMkAVKIQFLLWpgvQNIA 267
Cdd:TIGR01842 156 GLALLNNRATKKPL-----KEATE-----ASIRANNLADSALRNAEVIEAMGMMGNLTKR-WG-RFHSKYLSA---QSAA 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  268 ---------------VMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFET 328
Cdd:TIGR01842 221 sdragmlsnlskyfrIVLQSLVLGLGaylaIDG---EITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNEL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  329 MDVEPdikdiPNAKKM--PPIVGNVDFKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS 405
Cdd:TIGR01842 298 LANYP-----SRDPAMplPEPEGHLSVENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTS 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  406 GEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI-RYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKER 484
Cdd:TIGR01842 373 GSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPG 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  485 GSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:TIGR01842 452 GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRI 531
                         570
                  ....*....|..
gi 346645039  564 QEAGSHEELMAQ 575
Cdd:TIGR01842 532 ARFGERDEVLAK 543
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
37-325 5.85e-54

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 185.79  E-value: 5.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDDTIPNK---------------NMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIG 101
Cdd:cd18564    3 LALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTALVG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 102 QDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLA 181
Cdd:cd18564   83 QRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 182 LIPVLFVIVMV----IKTAQRKAYQvlsnKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQF 257
Cdd:cd18564  163 VAPLLLLAARRfsrrIKEASREQRR----REGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQA 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 258 LLWPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18564  239 LLSPVVDVLVAVGTALVLWFG--AWLVlagRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
31-579 3.27e-51

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 190.63  E-value: 3.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   31 YQKSIYITLFVILLAN-----VATMIGPYLTKIV-IDDTIPNKNMTQLFwIAVIFIVSVIVTGLCMRYRirsiTLIGQDI 104
Cdd:PTZ00265  823 YKKDVTIIALSILVAGglypvFALLYAKYVSTLFdFANLEANSNKYSLY-ILVIAIAMFISETLKNYYN----NVIGEKV 897
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  105 LKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVvnYINMLSDLLSNGLIN--------LISDILSVIVTLGFMLMIDPVLT 176
Cdd:PTZ00265  898 EKTMKRRLFENILYQEISFFDQDKHAPGLLSA--HINRDVHLLKTGLVNnivifthfIVLFLVSMVMSFYFCPIVAAVLT 975
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  177 LyslalIPVLFVIVMVIKtAQRKAYQVLSNKQSNM--NAYIHESIAGIKVTQSFSREEENFEIFT--------------E 240
Cdd:PTZ00265  976 G-----TYFIFMRVFAIR-ARLTANKDVEKKEINQpgTVFAYNSDDEIFKDPSFLIQEAFYNMNTviiygledyfcnliE 1049
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  241 VSNEYRRSWMK-AVKIQFLLWPGVQNIAVMTTCLIYFVG---IK--GYGVDVSTGTLIAFIgYVGNFWNPVINI-GNFYN 313
Cdd:PTZ00265 1050 KAIDYSNKGQKrKTLVNSMLWGFSQSAQLFINSFAYWFGsflIRrgTILVDDFMKSLFTFL-FTGSYAGKLMSLkGDSEN 1128
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  314 SLITATTYLERIFETMDVepDIKD-----IPNAKKmppIVGNVDFKDVYFRY--EEGVDILKGINFHVDAGESIALVGPT 386
Cdd:PTZ00265 1129 AKLSFEKYYPLIIRKSNI--DVRDnggirIKNKND---IKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGET 1203
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  387 GAGKTTIINLLSRFYNI------------------------------------------------------NSGEILVDG 412
Cdd:PTZ00265 1204 GSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDG 1283
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  413 ENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQ 492
Cdd:PTZ00265 1284 VDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQ 1363
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  493 RQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKNSSRIFYIDN-----GRIQE 565
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQA 1443
                         650
                  ....*....|....*
gi 346645039  566 AGSHEELM-AQHGYY 579
Cdd:PTZ00265 1444 HGTHEELLsVQDGVY 1458
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
346-568 1.02e-50

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: 173.75  E-value: 1.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 346 PIVGNVDFKDVYFRYEEGV-DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLR 424
Cdd:cd03369    2 PEHGEIEVENLSVRYAPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSGTIIENI-RYGKLDatEEEIIAAAKVvrahdfisglkdgyytevKERGSTLSAGQRQLISFARALL 503
Cdd:cd03369   82 SSLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGS 568
Cdd:cd03369  142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
35-325 2.85e-50

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 175.30  E-value: 2.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18552    1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18552   81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNI-AVMTTCL 273
Cdd:cd18552  161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLgAIAIALV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 274 IYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18552  241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
33-325 4.23e-50

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 174.98  E-value: 4.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18540    2 KLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18540   82 FEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKT----AQRKAYQVLSNKQSNMNayihESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAV 268
Cdd:cd18540  162 FQKkilkAYRKVRKINSRITGAFN----EGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGS 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 269 MTTCLIYFVGikgyGVDV-----STGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18540  238 IATALVLWYG----GILVlagaiTIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
39-325 2.91e-49

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 172.60  E-value: 2.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDD-TIPNKNMTQLFWIAVIFIVSVIVTGLcMRYrIRSITLIG--QDILKDMRTAIFGH 115
Cdd:cd18541    5 ILFLILVDLLQLLIPRIIGRAIDAlTAGTLTASQLLRYALLILLLALLIGI-FRF-LWRYLIFGasRRIEYDLRNDLFAH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18541   83 LLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIY 275
Cdd:cd18541  163 KIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 346645039 276 FVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18541  243 WYG--GRLVirgTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
36-311 1.55e-48

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 170.71  E-value: 1.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  36 YITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGH 115
Cdd:cd18549    5 FLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18549   85 LQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIY 275
Cdd:cd18549  165 KMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVL 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 346645039 276 FVG----IKGYgvdVSTGTLIAFIGYVGNFWNPVINIGNF 311
Cdd:cd18549  245 VAGgyfiIKGE---ITLGDLVAFLLYVNVFIKPIRRLVNF 281
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
79-560 1.10e-47

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 180.22  E-value: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   79 FIVSVIvTGLCMryrirsiTLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDI 158
Cdd:PTZ00265  111 FILSFI-SSFCM-------DVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYA 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  159 LSVIVTLGFMLMIDPVLTLYSLALIPVLFV--IVMVIKTAQRKAYQVLSNkqSNMNAYIHESIAGIKVTQSFSREEENFE 236
Cdd:PTZ00265  183 SAFLGLYIWSLFKNARLTLCITCVFPLIYIcgVICNKKVKINKKTSLLYN--NNTMSIIEEALVGIRTVVSYCGEKTILK 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  237 IFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVST---------GTLIA-FIGYVGNFWNPVI 306
Cdd:PTZ00265  261 KFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNqqpnndfhgGSVISiLLGVLISMFMLTI 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  307 ---NIGNFYNSLiTATTYLeriFETMDVEPDIKDIPNAKKMPPIvGNVDFKDVYFRYE--EGVDILKGINFHVDAGESIA 381
Cdd:PTZ00265  341 ilpNITEYMKSL-EATNSL---YEIINRKPLVENNDDGKKLKDI-KKIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYA 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  382 LVGPTGAGKTTIINLLSRFYNINSGEILV-DGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYG-----KLDATEE 455
Cdd:PTZ00265  416 FVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkDLEALSN 495
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  456 ----------------------------------------------------EIIAAAKVVRAHDFISGLKDGYYTEVKE 483
Cdd:PTZ00265  496 yynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGS 575
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039  484 RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL--EGRTSFIIAHRLSTIKNSSRIFYIDN 560
Cdd:PTZ00265  576 NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
37-325 1.72e-47

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 168.04  E-value: 1.72e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18550    3 LVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVI-KT 195
Cdd:cd18550   83 QRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVgRR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLsNKQSNMNAYIHE--SIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCL 273
Cdd:cd18550  163 RRKLTREQQ-EKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPAL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 274 IYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18550  242 VYWVG--GLLViggGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
PLN03232 PLN03232
ABC transporter C family member; Provisional
106-577 3.35e-45

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 172.47  E-value: 3.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  106 KDMRTAIFGHLQKLPFSYFDSRPHGKILIRV---VNYINMLSDLLSNGLINLISDILSVIVTLGFmlmidpVLTLYSLAL 182
Cdd:PLN03232  983 KRLHDAMLNSILRAPMLFFHTNPTGRVINRFskdIGDIDRNVANLMNMFMNQLWQLLSTFALIGT------VSTISLWAI 1056
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  183 IPVL---FVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLL 259
Cdd:PLN03232 1057 MPLLilfYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWL 1136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  260 WPGVQNIAVMTTCLIYFVGIKGYGvdvSTGTLIAFIGYVGNFWNPVINIGNFYNSLI-------TATTYLERIFETMDVE 332
Cdd:PLN03232 1137 TIRLETLGGVMIWLTATFAVLRNG---NAENQAGFASTMGLLLSYTLNITTLLSGVLrqaskaeNSLNSVERVGNYIDLP 1213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  333 PDIKDIPNAKKMP---PIVGNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEI 408
Cdd:PLN03232 1214 SEATAIIENNRPVsgwPSRGSIKFEDVHLRYRPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  409 LVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIrygklDATEEEIIAA--AKVVRAH--DFISGLKDGYYTEVKER 484
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPFSEHNDADlwEALERAHikDVIDRNPFGLDAEVSEG 1368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  485 GSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQ 564
Cdd:PLN03232 1369 GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
                         490
                  ....*....|...
gi 346645039  565 EAGSHEELMAQHG 577
Cdd:PLN03232 1449 EYDSPQELLSRDT 1461
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
351-576 3.09e-44

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: 157.11  E-value: 3.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:COG1122    1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQ--DTFIFSGTIIENIRYG--KLDATEEEIIA-AAKVVRAHDfISGLKDgyytevkERGSTLSAGQRQLISFARALLAD 505
Cdd:COG1122   81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRErVEEALELVG-LEHLAD-------RPPHELSGGQKQRVAIAGVLAME 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIA-HRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG1122  153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
PLN03130 PLN03130
ABC transporter C family member; Provisional
106-577 1.45e-43

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 167.61  E-value: 1.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  106 KDMRTAIFGHLQKLPFSYFDSRPHGKILIR-----------VVNYINMLsdllsnglINLISDILSVIVTLGFmlmidpV 174
Cdd:PLN03130  986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRfakdlgdidrnVAVFVNMF--------LGQIFQLLSTFVLIGI------V 1051
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  175 LTLYSLALIPVL---FVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEI----------FTEV 241
Cdd:PLN03130 1052 STISLWAIMPLLvlfYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEIngrsmdnnirFTLV 1131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  242 SNEYRRsWMkAVKIQFLlwPGVqniavmttcLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIgnfyNSLITATTY 321
Cdd:PLN03130 1132 NMSSNR-WL-AIRLETL--GGL---------MIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNI----TSLLTAVLR 1194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  322 L-----------ERIFETMDVEPDIKDIPNAKKMPP---IVGNVDFKDVYFRYE-EGVDILKGINFHVDAGESIALVGPT 386
Cdd:PLN03130 1195 LaslaenslnavERVGTYIDLPSEAPLVIENNRPPPgwpSSGSIKFEDVVLRYRpELPPVLHGLSFEISPSEKVGIVGRT 1274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  387 GAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENirygkLDATEEEIIAA--AKVV 464
Cdd:PLN03130 1275 GAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-----LDPFNEHNDADlwESLE 1349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  465 RAHdfisgLKD-------GYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGR 537
Cdd:PLN03130 1350 RAH-----LKDvirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSC 1424
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 346645039  538 TSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHG 577
Cdd:PLN03130 1425 TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
37-325 1.64e-42

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 154.51  E-value: 1.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDDTIPNK-NMTQLFWIAVIFIVSVIVTGLCMRYrirsITLIGQDILKDMRTAIFGH 115
Cdd:cd18551    3 LALLLSLLGTAASLAQPLLVKNLIDALSAGGsSGGLLALLVALFLLQAVLSALSSYL----LGRTGERVVLDLRRRLWRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18551   79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPgVQNIAVMTTcliy 275
Cdd:cd18551  159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP-LMGLAVQLA---- 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 276 FVGIKGYGV------DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18551  234 LLVVLGVGGarvasgALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
37-325 1.89e-42

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 154.18  E-value: 1.89e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18543    3 LALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLInLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIkta 196
Cdd:cd18543   83 QRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRF--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 qRKAYQVLS----NKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18543  159 -RRRYFPASrraqDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLA 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 273 LIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18543  238 AVLALG--GWLVangSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
354-563 3.04e-42

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: 149.67  E-value: 3.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQ 432
Cdd:cd03246    4 ENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSGTIIENIrygkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPKILILD 512
Cdd:cd03246   84 DDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 513 EATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03246  122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
351-576 7.80e-40

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 145.21  E-value: 7.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVM 430
Cdd:COG1131    1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRY-GKLDATEEEIIAAakvvRAHDFIS--GLKDgyytEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:COG1131   79 PQEPALYPDlTVRENLRFfARLYGLPRKEARE----RIDELLElfGLTD----AADRKVGTLSGGMKQRLGLALALLHDP 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG1131  151 ELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
367-516 7.54e-39

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: 139.71  E-value: 7.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039  446 RYGkldATEEEIIAAAKVVRAHDFIS--GLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
353-562 1.17e-38

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: 141.45  E-value: 1.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVML 431
Cdd:cd03225    2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 Q--DTFIFSGTIIENIRYG--KLDATEEEIIAAAKVVRAHDFISGLKDgyytevkERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03225   82 QnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMDPD 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGR 562
Cdd:cd03225  155 ILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
353-567 2.52e-38

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: 139.37  E-value: 2.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVML 431
Cdd:cd03247    3 INNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 QDTFIFSGTIIENIrygkldateeeiiaaakvvrahdfisglkdgyytevkerGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:cd03247   82 QRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 512 DEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03247  123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
PTZ00243 PTZ00243
ABC transporter; Provisional
122-593 5.56e-38

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 150.70  E-value: 5.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  122 SYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDP-VLtlysLALIPVLFV---IVMVIKTAQ 197
Cdd:PTZ00243 1047 SFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPfVL----VALVPCGYLyyrLMQFYNSAN 1122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  198 RKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFE-------------IFTEVSNEyrrsWMkAVKIQFLlwpgvQ 264
Cdd:PTZ00243 1123 REIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQealrrldvvyscsYLENVANR----WL-GVRVEFL-----S 1192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  265 NIAVmttcliyfvgikgygvdvstgTLIAFIGYVGN-FWNPVINIGNFYNSLITATT------YLERIFETMD-----VE 332
Cdd:PTZ00243 1193 NIVV---------------------TVIALIGVIGTmLRATSQEIGLVSLSLTMAMQttatlnWLVRQVATVEadmnsVE 1251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  333 --------------PDIKDIPNAKK-----------------------MPPIV--GNVDFKDVYFRYEEGVD-ILKGINF 372
Cdd:PTZ00243 1252 rllyytdevphedmPELDEEVDALErrtgmaadvtgtvviepasptsaAPHPVqaGSLVFEGVQMRYREGLPlVLRGVSF 1331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  373 HVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRyGKLDA 452
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEA 1410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  453 TEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILIL-DEATSSIDTQTEILLQEGLE 531
Cdd:PTZ00243 1411 SSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVM 1490
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039  532 RLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHgyyynlyQSQF-DMLQAL 593
Cdd:PTZ00243 1491 SAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR-------QSIFhSMVEAL 1546
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
356-588 6.84e-38

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: 140.32  E-value: 6.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDT- 434
Cdd:COG1124   10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPy 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 ------FIFSGTIIENIRYGKLDATEEEIIAAAKVVrahdfisGLKDGYYTEvkeRGSTLSAGQRQLISFARALLADPKI 508
Cdd:COG1124   90 aslhprHTVDRILAEPLRIHGLPDREERIAELLEQV-------GLPPSFLDR---YPHQLSGGQRQRVAIARALILEPEL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 509 LILDEATSSID--TQTEILlqegleRLLE------GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELM--AQHG 577
Cdd:COG1124  160 LLLDEPTSALDvsVQAEIL------NLLKdlreerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLagPKHP 233
                        250
                 ....*....|.
gi 346645039 578 YYYNLYQSQFD 588
Cdd:COG1124  234 YTRELLAASLA 244
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
354-577 2.01e-36

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: 136.14  E-value: 2.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRsLRSQMGVMLQD 433
Cdd:COG4555    5 ENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSG-TIIENIRY-GKL--DATEEEIIAAAKVVRAHDFISGLkdgyytevKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:COG4555   83 RGLYDRlTVRENIRYfAELygLFDEELKKRIEELIELLGLEEFL--------DRRVGELSTGMKKKVALARALVHDPKVL 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQHG 577
Cdd:COG4555  155 LLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
351-578 2.37e-36

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: 142.35  E-value: 2.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYE----EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSL 423
Cdd:COG1123  261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDTF--------IFSgTIIENIR-YGKLDATEeeiiAAAKVVRAHDFIsGLKdgyyTEVKER-GSTLSAGQR 493
Cdd:COG1123  341 RRRVQMVFQDPYsslnprmtVGD-IIAEPLRlHGLLSRAE----RRERVAELLERV-GLP----PDLADRyPHELSGGQR 410
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 494 QLISFARALLADPKILILDEATSSID--TQTEIL-----LQEGLerlleGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQE 565
Cdd:COG1123  411 QRVAIARALALEPKLLILDEPTSALDvsVQAQILnllrdLQREL-----GLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
                        250
                 ....*....|....*
gi 346645039 566 AGSHEELMA--QHGY 578
Cdd:COG1123  486 DGPTEEVFAnpQHPY 500
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
33-325 2.62e-36

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 137.19  E-value: 2.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18570    2 KLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRV--VNYINmlsDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIV 190
Cdd:cd18570   82 FKHLLKLPLSFFETRKTGEIISRFndANKIR---EAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 191 MVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLlwpgvQNIAVMT 270
Cdd:cd18570  159 LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNL-----QSSIKGL 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 271 TCLIYFVGIKGYGV------DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18570  234 ISLIGSLLILWIGSylvikgQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
349-575 1.50e-35

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


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 134.27  E-value: 1.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03288   18 GEIKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENIRYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03288   98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03288  177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
351-574 1.73e-35

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: 133.40  E-value: 1.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQM 427
Cdd:cd03261    1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSG-TIIENI-----RYGKLDATEEEIIAAAKVVRAhdfisGLKDgyytEVKERGSTLSAGQRQLISFARA 501
Cdd:cd03261   80 GMLFQSGALFDSlTVFENVafplrEHTRLSEEEIREIVLEKLEAV-----GLRG----AEDLYPAELSGGMKKRVALARA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 502 LLADPKILILDEATSSID--TQTEIL-----LQEGLerlleGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:cd03261  151 LALDPELLLYDEPTAGLDpiASGVIDdlirsLKKEL-----GLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225

                 .
gi 346645039 574 A 574
Cdd:cd03261  226 A 226
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
351-544 4.65e-35

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: 131.83  E-value: 4.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlrslRSQM 427
Cdd:cd03293    1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFS-GTIIENIRYGkLDATeeEIIAAAKVVRAHDFIS--GLKD--GYYTevkergSTLSAGQRQLISFARAL 502
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALG-LELQ--GVPKAEARERAEELLElvGLSGfeNAYP------HQLSGGMRQRVALARAL 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 346645039 503 LADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH 544
Cdd:cd03293  147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH 190
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
354-573 5.96e-35

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: 132.47  E-value: 5.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:COG1120    5 ENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFI-FSGTIIENIRYG---------KLDATEEEIIAAA-KVVRahdfISGLKDGYYTEvkergstLSAGQRQLISFARAL 502
Cdd:COG1120   84 PPApFGLTVRELVALGryphlglfgRPSAEDREAVEEAlERTG----LEHLADRPVDE-------LSGGERQRVLIARAL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 503 LADPKILILDEATSSID--TQTEILlqEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:COG1120  153 AQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
39-325 6.59e-35

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 133.38  E-value: 6.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18576    2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18576   82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEenFEI--FTEVSNEYRRSWMKAVKIQFLLWPGVqnIAVMTTCLIYF 276
Cdd:cd18576  162 KLSKKVQDELAEANTIVEETLQGIRVVKAFTRED--YEIerYRKALERVVKLALKRARIRALFSSFI--IFLLFGAIVAV 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18576  238 LWYGGRLVlagELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
353-562 7.39e-35

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 128.90  E-value: 7.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQ 432
Cdd:cd00267    2 IENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 dtfifsgtiienirygkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPKILILD 512
Cdd:cd00267   81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 513 EATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKNSS-RIFYIDNGR 562
Cdd:cd00267  106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAAdRVIVLKDGK 157
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
351-572 7.68e-35

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: 131.15  E-value: 7.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENV--EEVTLRSL 423
Cdd:cd03260    1 IELRDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIydLDVDVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDTFIFSGTIIENIRYG------KLDATEEEIIAAA--KVvrahdfisGLKDgyytEVKER--GSTLSAGQR 493
Cdd:cd03260   80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlrKA--------ALWD----EVKDRlhALGLSGGQQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 494 QLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03260  148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
33-325 2.06e-34

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 132.25  E-value: 2.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18555    2 KLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRvVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18555   82 FEHLLKLPYSFFENRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHE---SIAGIKVT----QSFSREEENFEifTEVSNEYRRSwmkavKIQFLLWPGVQN 265
Cdd:cd18555  161 TRKKIKKLNQEEIVAQTKVQSYLTEtlyGIETIKSLgsekNIYKKWENLFK--KQLKAFKKKE-----RLSNILNSISSS 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 266 IAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18555  234 IQFIAPLLILWIGaylvING---ELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
39-325 4.31e-34

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 131.14  E-value: 4.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18557    2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18557   82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIF-TEVSNEYRRSWMKAVkiQFLLWPGVQNIAVM-TTCLIYF 276
Cdd:cd18557  162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYsEALDRSYRLARKKAL--ANALFQGITSLLIYlSLLLVLW 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18557  240 YG--GYLVlsgQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
10-575 5.34e-34

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: 138.50  E-value: 5.34e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039    10 EELETAFSAAHLKRILVYVKPYQKSIY--ITLFVILLANVA-TMIG-------PYLTKIVIDDT-------------IPN 66
Cdd:TIGR01271  842 DERENVFETTTWNTYLRYITTNRNLVFvlIFCLVIFLAEVAaSLLGlwlitdnPSAPNYVDQQHanasspdvqkpviITP 921
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039    67 KNMTQLFWIAVIFIVSVIVTGLcmrYR----IRSITLIGQDILKDMRTAIFghlqKLPFSYFDSRPHGKILIRVVNYINM 142
Cdd:TIGR01271  922 TSAYYIFYIYVGTADSVLALGF---FRglplVHTLLTVSKRLHEQMLHSVL----QAPMAVLNTMKAGRILNRFTKDMAI 994
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   143 LSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLyslALIPVLFVIVMV----IKTAQrKAYQVLSNKQSNMNAYIHES 218
Cdd:TIGR01271  995 IDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFI---AAIPVAVIFIMLrayfLRTSQ-QLKQLESEARSPIFSHLITS 1070
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   219 IAGIKVTQSFSREEENFEIFTEVSNEYRRSWMkaVKIQFLLWpgvqniaVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYV 298
Cdd:TIGR01271 1071 LKGLWTIRAFGRQSYFETLFHKALNLHTANWF--LYLSTLRW-------FQMRIDIIFVFFFIAVTFIAIGTNQDGEGEV 1141
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   299 GNFWNPVINI-GNFYNSLITATTY------LERIFETMDVEPD-----------------IKDIPNAKKMPPIVGNVDFK 354
Cdd:TIGR01271 1142 GIILTLAMNIlSTLQWAVNSSIDVdglmrsVSRVFKFIDLPQEeprpsggggkyqlstvlVIENPHAQKCWPSGGQMDVQ 1221
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   355 DVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNiNSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:TIGR01271 1222 GLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   434 TFIFSGTIIENI----RYgkldaTEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:TIGR01271 1301 VFIFSGTFRKNLdpyeQW-----SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039   510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
351-571 7.80e-34

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 128.25  E-value: 7.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRS-----LRS 425
Cdd:COG2884    2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL--SRLKRreipyLRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 426 QMGVMLQDT-FIFSGTIIENIRYGkLDATEEEIIAAAKvvRAHDFIS--GLKDgyytevKERG--STLSAGQRQLISFAR 500
Cdd:COG2884   80 RIGVVFQDFrLLPDRTVYENVALP-LRVTGKSRKEIRR--RVREVLDlvGLSD------KAKAlpHELSGGEQQRVAIAR 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 501 ALLADPKILILDEATSSIDTQT--EILlqEGLERLLEGRTSFIIA-HRLSTIKNS-SRIFYIDNGRIQEAGSHEE 571
Cdd:COG2884  151 ALVNRPELLLADEPTGNLDPETswEIM--ELLEEINRRGTTVLIAtHDLELVDRMpKRVLELEDGRLVRDEARGV 223
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
351-574 1.26e-33

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: 128.17  E-value: 1.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV---EEVTLRSLRSQM 427
Cdd:COG1127    6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSG-TIIENI-----RYGKLDATEEEIIAAAKVVRAhdfisGLKD--GYYTevkergSTLSAGQRQLISFA 499
Cdd:COG1127   85 GMLFQGGALFDSlTVFENVafplrEHTDLSEAEIRELVLEKLELV-----GLPGaaDKMP------SELSGGMRKRVALA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 500 RALLADPKILILDEATSSID--TQTEI--LLQEGLERLleGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:COG1127  154 RALALDPEILLYDEPTAGLDpiTSAVIdeLIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
35-330 2.14e-33

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 129.46  E-value: 2.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMT------QLFWIAVI-FIVSVIVTGLCMRYRIRSITLIGQDILKD 107
Cdd:cd18554    1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTldekvyKLFTIIGImFFIFLILRPPVEYYRQYFAQWIANKILYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 108 MRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLF 187
Cdd:cd18554   81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 188 VIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIA 267
Cdd:cd18554  161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 268 VMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVinignfyNSLITATTYLERIFETMD 330
Cdd:cd18554  241 DLAPLLVIGFAaylvIEG---NLTVGTLVAFVGYMERMYSPL-------RRLVNSFTTLTQSFASMD 297
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
351-574 2.31e-33

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: 127.80  E-value: 2.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:cd03295    1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIR-YGKLDATEEEIIAAakvvRAHDFIS--GLKDGYYtevKER-GSTLSAGQRQLISFARALLAD 505
Cdd:cd03295   81 IQQIGLFPHmTVEENIAlVPKLLKWPKEKIRE----RADELLAlvGLDPAEF---ADRyPHELSGGQQQRVGVARALAAD 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:cd03295  154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
351-562 4.26e-33

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: 125.66  E-value: 4.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD----ILKGINFHVDAGESIALVGPTGAGKTTIIN-LLsrfyninsGEI-LVDGEnveevtlRSLR 424
Cdd:cd03250    1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLL--------GELeKLSGS-------VSVP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSGTIIENIRYGK-LDATEEEiiaaaKVVRA---HDFISGLKDGYYTEVKERGSTLSAGQRQLISFAR 500
Cdd:cd03250   66 GSIAYVSQEPWIQNGTIRENILFGKpFDEERYE-----KVIKAcalEPDLEILPDGDLTEIGEKGINLSGGQKQRISLAR 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEG--LERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGR 562
Cdd:cd03250  141 AVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
351-567 5.92e-33

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: 125.71  E-value: 5.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVM 430
Cdd:cd03259    1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG------KLDATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARALL 503
Cdd:cd03259   78 FQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLL-----------NRYPHELSGGQQQRVALARALA 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03259  147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
344-544 1.08e-32

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 126.36  E-value: 1.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVGNVDFKDVYFRY---EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTL 420
Cdd:COG1116    1 MSAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 421 RslrsqMGVMLQDtfiFS----GTIIENIRYG--KLDATEEEIIAaakvvRAHDFIS--GLKD--GYYTevkergSTLSA 490
Cdd:COG1116   81 D-----RGVVFQE---PAllpwLTVLDNVALGleLRGVPKAERRE-----RARELLElvGLAGfeDAYP------HQLSG 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH 544
Cdd:COG1116  142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
353-576 1.25e-32

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: 125.37  E-value: 1.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGV 429
Cdd:cd03256    3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQD-TFIFSGTIIENIRYGKLDA-----------TEEEIIAAAKVVRAhdfiSGLKDGYYTevkeRGSTLSAGQRQLIS 497
Cdd:cd03256   83 IFQQfNLIERLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAALER----VGLLDKAYQ----RADQLSGGQQQRVA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 498 FARALLADPKILILDEATSSIDTQT-----EILLQEGLErllEGRTSFIIAHRLSTIK-NSSRIFYIDNGRIQEAGSHEE 571
Cdd:cd03256  155 IARALMQQPKLILADEPVASLDPASsrqvmDLLKRINRE---EGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAE 231

                 ....*
gi 346645039 572 LMAQH 576
Cdd:cd03256  232 LTDEV 236
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
344-565 2.75e-32

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 124.00  E-value: 2.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVgnvDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE---E 417
Cdd:COG1136    1 MSPLL---ELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslsE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 418 VTLRSLRSQ-MGVMLQDTFIFSG-TIIENI----RYGKLDATE--EEIIAAAKVVrahdfisGLKDgyytEVKERGSTLS 489
Cdd:COG1136   78 RELARLRRRhIGFVFQFFNLLPElTALENValplLLAGVSRKErrERARELLERV-------GLGD----RLDHRPSQLS 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIA-HRLSTIKNSSRIFYIDNGRIQE 565
Cdd:COG1136  147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
354-563 5.06e-32

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: 121.74  E-value: 5.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVMLQD 433
Cdd:cd03230    4 RNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSG-TIIENIRYgkldateeeiiaaakvvrahdfisglkdgyytevkergstlSAGQRQLISFARALLADPKILILD 512
Cdd:cd03230   82 PSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLILD 120
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 346645039 513 EATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03230  121 EPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
351-575 8.05e-32

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: 123.07  E-value: 8.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLR 424
Cdd:cd03258    2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSG-TIIENIRYG-KLDATEEEIIAAaKVVRAHDFIsGLKDgyytEVKERGSTLSAGQRQLISFARAL 502
Cdd:cd03258   82 RRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEE-RVLELLELV-GLED----KADAYPAQLSGGQKQRVGIARAL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 503 LADPKILILDEATSSIDTQTEillQEGLERLLE-----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03258  156 ANNPKVLLCDEATSALDPETT---QSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
356-567 8.57e-32

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: 122.61  E-value: 8.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVML 431
Cdd:cd03257    9 VSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 QDTF-----IFS-GTIIENI--RYGKLDATEEEIIAAAKVVRAHdfisGLKDGYYtevKERGSTLSAGQRQLISFARALL 503
Cdd:cd03257   89 QDPMsslnpRMTiGEQIAEPlrIHGKLSKKEARKEAVLLLLVGV----GLPEEVL---NRYPHELSGGQRQRVAIARALA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 504 ADPKILILDEATSSID--TQTEIL-----LQEGLerlleGRTSFIIAHRLSTIKNSS-RIFYIDNGRIQEAG 567
Cdd:cd03257  162 LNPKLLIADEPTSALDvsVQAQILdllkkLQEEL-----GLTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
351-562 1.52e-31

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: 120.37  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMG 428
Cdd:cd03229    1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSG-TIIENIRYGkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPK 507
Cdd:cd03229   80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGR 562
Cdd:cd03229  121 VLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDGK 178
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
343-584 2.21e-31

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 122.12  E-value: 2.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 343 KMPPIVgnvDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlrs 422
Cdd:COG1121    2 MMMPAI---ELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 lRSQMGVMLQDT------------FIFSGTIIENIRYGKLDATEEEIIAAA-KVVRAHDFIsglkdgyytevKERGSTLS 489
Cdd:COG1121   74 -RRRIGYVPQRAevdwdfpitvrdVVLMGRYGRRGLFRRPSRADREAVDEAlERVGLEDLA-----------DRPIGELS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTI-KNSSRIFYIDNGRI---- 563
Cdd:COG1121  142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVrEYFDRVLLLNRGLVahgp 221
                        250       260
                 ....*....|....*....|..
gi 346645039 564 -QEAGSHEELMAQHGYYYNLYQ 584
Cdd:COG1121  222 pEEVLTPENLSRAYGGPVALLA 243
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
344-576 2.42e-31

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: 127.71  E-value: 2.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVgnvDFKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN---SGEILVDGENVEEVT 419
Cdd:COG1123    1 MTPLL---EVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 420 LRSLRSQMGVMLQD--TFIFSGTIIENIRYG--KLDATEEEIIAAAKVVRAHDFISGLKDGYYTEvkergstLSAGQRQL 495
Cdd:COG1123   78 EALRGRRIGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 496 ISFARALLADPKILILDEATSSID--TQTEILlqEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHE 570
Cdd:COG1123  151 VAIAMALALDPDLLIADEPTTALDvtTQAEIL--DLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPE 228

                 ....*.
gi 346645039 571 ELMAQH 576
Cdd:COG1123  229 EILAAP 234
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
351-573 2.97e-31

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 121.74  E-value: 2.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE--EVTLRSLRSQMG 428
Cdd:PRK09493   2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSG-TIIENIRYG--------KLDATEEEIIAAAKV---VRAHDFisglkdgyytevkerGSTLSAGQRQLI 496
Cdd:PRK09493  81 MVFQQFYLFPHlTALENVMFGplrvrgasKEEAEKQARELLAKVglaERAHHY---------------PSELSGGQQQRV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 497 SFARALLADPKILILDEATSSIDTQteiLLQEGLE--RLL--EGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEE 571
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPE---LRHEVLKvmQDLaeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQV 222

                 ..
gi 346645039 572 LM 573
Cdd:PRK09493 223 LI 224
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
35-305 3.25e-31

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 122.37  E-value: 3.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNM--TQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 346645039  273 LIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPV 305
Cdd:pfam00664 241 LALWFGaylvISG---ELSVGDLVAFLSLFAQLFGPL 274
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
354-567 6.17e-31

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: 118.69  E-value: 6.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQd 433
Cdd:cd03214    3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 tfifsgtiienirygkldateeeiiaAAKVVRahdfISGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILILDE 513
Cdd:cd03214   81 --------------------------ALELLG----LAHLADRPFNE-------LSGGERQRVLLARALAQEPPILLLDE 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 514 ATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03214  124 PTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
351-563 9.05e-31

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: 119.52  E-value: 9.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE---EVTLRSLR 424
Cdd:cd03255    1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsEKELAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 -SQMGvmlqdtFIFSG-------TIIENIRYG------KLDATEEEIIAAAKVVrahdfisGLKDgyytEVKERGSTLSA 490
Cdd:cd03255   81 rRHIG------FVFQSfnllpdlTALENVELPlllagvPKKERRERAEELLERV-------GLGD----RLNHYPSELSG 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03255  144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
37-325 2.88e-29

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 117.50  E-value: 2.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18548    3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18548   83 QSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd18548  163 AIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILW 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGikGYGVD---VSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18548  243 FG--GHLINagsLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
349-575 4.16e-29

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: 116.49  E-value: 4.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINsGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03289    1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENIR-YGKLdaTEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:cd03289   80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03289  158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
366-543 5.73e-29

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: 114.11  E-value: 5.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVMLQDTFIFSG-TIIEN 444
Cdd:COG4133   17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVREN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRY----GKLDATEEEIIAAAKVVRahdfISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILDEATSSIDT 520
Cdd:COG4133   96 LRFwaalYGLRADREAIDEALEAVG----LAGLAD-------LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
                        170       180
                 ....*....|....*....|...
gi 346645039 521 QTEILLQEGLERLLEGRTSFIIA 543
Cdd:COG4133  165 AGVALLAELIAAHLARGGAVLLT 187
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
351-573 1.07e-28

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: 114.80  E-value: 1.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSG-EILVDGENVEEVTLRSLRSQMGV 429
Cdd:COG1119    4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 M---LQDTFIFSGTIIENIRYGKLD-------ATEEEIIAAAKVVRAHDfISGLKDGYYTevkergsTLSAGQRQLISFA 499
Cdd:COG1119   83 VspaLQLRFPRDETVLDVVLSGFFDsiglyrePTDEQRERARELLELLG-LAHLADRPFG-------TLSQGEQRRVLIA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 500 RALLADPKILILDEATSSID-TQTEILLQEgLERL-LEGRTSFI-IAHRLSTIKNS-SRIFYIDNGRIQEAGSHEELM 573
Cdd:COG1119  155 RALVKDPELLILDEPTAGLDlGARELLLAL-LDKLaAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
366-563 5.18e-28

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: 111.47  E-value: 5.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMGVMLQDTFIFSG-TII 442
Cdd:cd03262   15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYG--------KLDATEEEIIAAAKVvrahdfisGLKD--GYYTevkergSTLSAGQRQLISFARALLADPKILILD 512
Cdd:cd03262   95 ENITLApikvkgmsKAEAEERALELLEKV--------GLADkaDAYP------AQLSGGQQQRVAIARALAMNPKVMLFD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 513 EATSSIDTQteiLLQEGLERLL----EGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03262  161 EPTSALDPE---LVGEVLDVMKdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
354-563 1.46e-27

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 110.04  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvtlRSLRSQMGVMLQD 433
Cdd:cd03226    3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 T--FIFSGTIIENIRYGkLDATEEEIIAAAKVVRAHDfISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:cd03226   80 VdyQLFTDSVREELLLG-LKELDAGNEQAETVLKDLD-LYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 346645039 512 DEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03226  151 DEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
353-561 2.01e-27

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: 109.93  E-value: 2.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlrslRSQMGVMLQ 432
Cdd:cd03235    2 VEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFI---FSGTIIENI---RYGKL-------DATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFA 499
Cdd:cd03235   76 RRSIdrdFPISVRDVVlmgLYGHKglfrrlsKADKAKVDEALERVGLSELA-----------DRQIGELSGGQQQRVLLA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTI-KNSSRIFYIDNG 561
Cdd:cd03235  145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
363-574 2.41e-27

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: 109.83  E-value: 2.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSlRSQMGVML--QDTFIFSG- 439
Cdd:cd03224   12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIGYvpEGRRIFPEl 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG-------KLDATEEEIIAaakvvrahdfisglkdgYYTEVKER----GSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03224   91 TVEENLLLGayarrraKRKARLERVYE-----------------LFPRLKERrkqlAGTLSGGEQQMLAIARALMSRPKL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 509 LILDEATS----SIDTQTEILLQEgLERllEGRTSFIIAHRLSTIKNSSRIFYI-DNGRIQEAGSHEELMA 574
Cdd:cd03224  154 LLLDEPSEglapKIVEEIFEAIRE-LRD--EGVTILLVEQNARFALEIADRAYVlERGRVVLEGTAAELLA 221
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
363-574 8.42e-27

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: 109.06  E-value: 8.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEevTLRS-LRSQMGV--MLQDTFIFSG 439
Cdd:cd03219   12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPPhEIARLGIgrTFQIPRLFPE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIENIR----------YGKLDATEEEIIAAAKVVRAHDFIsGLKDGYYTEVkergSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03219   90 lTVLENVMvaaqartgsgLLLARARREEREARERAEELLERV-GLADLADRPA----GELSYGQQRRLEIARALATDPKL 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 509 LILDEATSSIdTQTEIllQEGLERLLE----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:cd03219  165 LLLDEPAAGL-NPEET--EELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
351-572 8.43e-27

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: 108.86  E-value: 8.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRSLRSQMGVM 430
Cdd:cd03300    1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG-KLDATEEEIIaAAKVVRAHDFI--SGLKDGYYTEvkergstLSAGQRQLISFARALLADP 506
Cdd:cd03300   78 FQNYALFPHlTVFENIAFGlRLKKLPKAEI-KERVAEALDLVqlEGYANRKPSQ-------LSGGQQQRVAIARALVNEP 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03300  150 KVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
351-563 8.49e-27

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 108.26  E-value: 8.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRS---LRSQM 427
Cdd:cd03292    1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDT-FIFSGTIIENIRYGkLDATEEEIIAAAKVVRAHDFISGLKDgyytevKERG--STLSAGQRQLISFARALLA 504
Cdd:cd03292   81 GVVFQDFrLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSH------KHRAlpAELSGGEQQRVAIARAIVN 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN--SSRIFYIDNGRI 563
Cdd:cd03292  154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
367-571 1.75e-26

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 107.81  E-value: 1.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALFPHmTVYKNI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYGKLDATEEEIIAAAKVVRAHDF--ISGLKDGYYTevkergsTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:cd03299   93 AYGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 346645039 524 ILLQEGLERLL-EGRTSFI-IAHRLSTIKN-SSRIFYIDNGRIQEAGSHEE 571
Cdd:cd03299  166 EKLREELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
59-325 5.55e-26

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 108.42  E-value: 5.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  59 VIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRYrIRSITL--IGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRV 136
Cdd:cd18565   40 VPASLGPADPRGQLWLLGGLTVAAFLLESL-FQY-LSGVLWrrFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 137 VNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIH 216
Cdd:cd18565  118 NNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLE 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 217 ESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQ---NIAVMTTCLI--YFV--GIKGYGVDVSTG 289
Cdd:cd18565  198 NNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRlvaGAGFVATFVVggYWVldGPPLFTGTLTVG 277
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 346645039 290 TLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18565  278 TLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
353-576 1.01e-25

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 105.61  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEegvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeevtLRSLRSQMGV-ML 431
Cdd:COG3840    4 LDDLTYRYG---DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVsML 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 -QDTFIFSG-TIIENIRYG-----KLDATE-EEIIAAAKVVRahdfISGLKDgyytevkERGSTLSAGQRQLISFARALL 503
Cdd:COG3840   77 fQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVG----LAGLLD-------RLPGQLSGGQRQRVALARCLV 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 504 ADPKILILDEATSSIDTqteILLQEGLERLLE-----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG3840  146 RKRPILLLDEPFSALDP---ALRQEMLDLVDElcrerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
363-574 1.16e-25

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 105.99  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTI---INLLSRFYN--INSGEILVDGE---NVEEVTLRSLRSQMGVMLQDT 434
Cdd:PRK11264  15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDTArslSQQKGLIRQLRQHVGFVFQNF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 FIFSG-TIIENIRYGKL---DATEEEIIAAAKVVRAHDFISGLKDGYytevkerGSTLSAGQRQLISFARALLADPKILI 510
Cdd:PRK11264  95 NLFPHrTVLENIIEGPVivkGEPKEEATARARELLAKVGLAGKETSY-------PRRLSGGQQQRVAIARALAMRPEVIL 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 511 LDEATSSIDTQteiLLQEGLE--RLL--EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK11264 168 FDEPTSALDPE---LVGEVLNtiRQLaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
354-574 1.48e-25

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: 105.45  E-value: 1.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRS-LRSQMGVML- 431
Cdd:COG0410    7 ENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI--TGLPPhRIARLGIGYv 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 -QDTFIFSG-TIIENIRygkldateeeiiAAAKVVRAHDFISGLKDGYYT---EVKER----GSTLSAGQRQLISFARAL 502
Cdd:COG0410   84 pEGRRIFPSlTVEENLL------------LGAYARRDRAEVRADLERVYElfpRLKERrrqrAGTLSGGEQQMLAIGRAL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 503 LADPKILILDEAT-----SSIDTQTEILLQ---EGLERLL-EGRTSFI--IAHRlstiknssriFYI-DNGRIQEAGSHE 570
Cdd:COG0410  152 MSRPKLLLLDEPSlglapLIVEEIFEIIRRlnrEGVTILLvEQNARFAleIADR----------AYVlERGRIVLEGTAA 221

                 ....
gi 346645039 571 ELMA 574
Cdd:COG0410  222 ELLA 225
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
364-578 1.88e-25

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 107.51  E-value: 1.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 364 VDilkGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTfifsgt 440
Cdd:COG4608   34 VD---GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP------ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 iienirYGKLDA--TEEEIIAAAkvVRAHdfisGLKDGyyTEVKERGSTL------------------SAGQRQLISFAR 500
Cdd:COG4608  105 ------YASLNPrmTVGDIIAEP--LRIH----GLASK--AERRERVAELlelvglrpehadryphefSGGQRQRIGIAR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 501 ALLADPKILILDEATSSIDT--QTEIL-----LQEGLerlleGRTSFIIAHRLSTIKN-SSRI--FYIdnGRIQEAGSHE 570
Cdd:COG4608  171 ALALNPKLIVCDEPVSALDVsiQAQVLnlledLQDEL-----GLTYLFISHDLSVVRHiSDRVavMYL--GKIVEIAPRD 243
                        250
                 ....*....|
gi 346645039 571 ELMA--QHGY 578
Cdd:COG4608  244 ELYArpLHPY 253
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
351-572 1.90e-25

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 107.88  E-value: 1.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT--LRslrsQMG 428
Cdd:COG3842    6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpeKR----NVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSG-TIIENIRYG----KLDATE-EEIIAAA-KVVRahdfISGLKDGYytevkerGSTLSAGQRQLISFARA 501
Cdd:COG3842   81 MVFQDYALFPHlTVAENVAFGlrmrGVPKAEiRARVAELlELVG----LEGLADRY-------PHQLSGGQQQRVALARA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 502 LLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS---TIknSSRIFYIDNGRIQEAGSHEEL 572
Cdd:COG3842  150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
351-575 2.10e-25

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 107.47  E-value: 2.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTT---IINLLSRFyniNSGEILVDGENVEEVT---LR 421
Cdd:COG1135    2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSereLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQMGVmlqdtfIF-------SGTIIENI----RYGKLDAteEEIiaAAKVVRAHDFIsGLKD--GYYTevkergSTL 488
Cdd:COG1135   79 AARRKIGM------IFqhfnllsSRTVAENValplEIAGVPK--AEI--RKRVAELLELV-GLSDkaDAYP------SQL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 489 SAGQRQLISFARALLADPKILILDEATSSIDTQT--EIL--LQEGLERLleGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:COG1135  142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETtrSILdlLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRI 219
                        250
                 ....*....|..
gi 346645039 564 QEAGSHEELMAQ 575
Cdd:COG1135  220 VEQGPVLDVFAN 231
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
363-546 3.33e-25

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 109.34  E-value: 3.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRS--QMGVML--QDTFIFS 438
Cdd:COG1129   16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDaqAAGIAIihQELNLVP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 G-TIIENI-------RYGKLDaTEEEIIAAAKVVRAHDF-ISglkdgyyteVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:COG1129   93 NlSVAENIflgreprRGGLID-WRAMRRRARELLARLGLdID---------PDTPVGDLSVAQQQLVEIARALSRDARVL 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 346645039 510 ILDEATSSIdTQTEIllqeglERLLE--------GRTSFIIAHRL 546
Cdd:COG1129  163 ILDEPTASL-TEREV------ERLFRiirrlkaqGVAIIYISHRL 200
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
363-574 5.89e-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: 104.35  E-value: 5.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRS-LRSQMGV--MLQDTFIFSG 439
Cdd:COG0411   16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI--TGLPPhRIARLGIarTFQNPRLFPE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIENI--------RYGKLDAT-------EEEIIAAAKVVRAHDFIsGLKDgyytEVKERGSTLSAGQRQLISFARALL 503
Cdd:COG0411   94 lTVLENVlvaaharlGRGLLAALlrlprarREEREARERAEELLERV-GLAD----RADEPAGNLSYGQQRRLEIARALA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 504 ADPKILILDEATSSIdTQTEIllqEGLERLL------EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:COG0411  169 TEPKLLLLDEPAAGL-NPEET---EELAELIrrlrdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
4-582 8.20e-25

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: 110.04  E-value: 8.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039     4 NKFDIDEELETAFSAAHLKR-----ILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVI----DDTIPNknmTQLFW 74
Cdd:TIGR00957  283 SQLDANEEVEALIVKSPHKPrkpslFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIrfvnDPMAPD---WQGYF 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039    75 IAVIFIVSVIVTGLCMRYRIRSITLIGQDIlkdmRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINM----LSDLLSng 150
Cdd:TIGR00957  360 YTGLLFVCACLQTLILHQYFHICFVSGMRI----KTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVdaqrFMDLAT-- 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   151 LINLI-SDILSVIVTLGFM-LMIDP-VLTLYSLALIPVLFVIVMVIKTaqrKAYQVLSNK-QSNMNAYIHESIAGIKVTQ 226
Cdd:TIGR00957  434 YINMIwSAPLQVILALYFLwLNLGPsVLAGVAVMVLMVPLNAVMAMKT---KTYQVAHMKsKDNRIKLMNEILNGIKVLK 510
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   227 SFSREEEnfeiFTEVSNEYRRSWMKAVKIQFLLwpgvqniAVMTT----CLIYFVGIKGYGVDVST---GTLIAFIGYVG 299
Cdd:TIGR00957  511 LYAWELA----FLDKVEGIRQEELKVLKKSAYL-------HAVGTftwvCTPFLVALITFAVYVTVdenNILDAEKAFVS 579
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   300 -NFWN----PVINIGNFYNSLITATTYLERIFETMDVEPDIKDIPNAKKMPPIVGN-VDFKDVYFRYEEGVD-ILKGINF 372
Cdd:TIGR00957  580 lALFNilrfPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNsITVHNATFTWARDLPpTLNGITF 659
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   373 HVDAGESIALVGPTGAGKTTIINLLsrfyninsgeiLVDGENVE-EVTLRSlrsQMGVMLQDTFIFSGTIIENIRYGKld 451
Cdd:TIGR00957  660 SIPEGALVAVVGQVGCGKSSLLSAL-----------LAEMDKVEgHVHMKG---SVAYVPQQAWIQNDSLRENILFGK-- 723
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   452 ATEEEIIAAakVVRAHDFISGLK---DGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQE 528
Cdd:TIGR00957  724 ALNEKYYQQ--VLEACALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039   529 ---GLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNL 582
Cdd:TIGR00957  802 hviGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
351-572 9.64e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 104.05  E-value: 9.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:PRK13647   5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQ--DTFIFSGTIIENIRYGKL------DATEEEIIAAAKVVRAHDFISglKDGYYtevkergstLSAGQRQLISFARAL 502
Cdd:PRK13647  85 FQdpDDQVFSSTVWDDVAFGPVnmgldkDEVERRVEEALKAVRMWDFRD--KPPYH---------LSYGQKKRVAIAGVL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 503 LADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
367-572 1.73e-24

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: 102.42  E-value: 1.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03296   18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHmTVFDNV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYG------KLDATEEEIiaAAKVVRAHDFI--SGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:cd03296   96 AFGlrvkprSERPPEAEI--RAKVHELLKLVqlDWLADRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEPFGA 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 518 IDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03296  167 LDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
356-578 2.91e-24

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: 103.59  E-value: 2.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTT----IINLLSRfYNINSGEILVDGENVEEVT---LRSLR-SQ 426
Cdd:COG0444    9 VYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPP-PGITSGEILFDGEDLLKLSekeLRKIRgRE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQDTF--------IfsGTII-ENIRY-GKLDATE--EEIIAAAKVVrahdfisGLkdgyyTEVKERGS----TLSA 490
Cdd:COG0444   88 IQMIFQDPMtslnpvmtV--GDQIaEPLRIhGGLSKAEarERAIELLERV-------GL-----PDPERRLDryphELSG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSID--TQTEIL-----LQEglerllEGRTSFI-IAHRLSTIKN-SSRI--FYid 559
Cdd:COG0444  154 GMRQRVMIARALALEPKLLIADEPTTALDvtIQAQILnllkdLQR------ELGLAILfITHDLGVVAEiADRVavMY-- 225
                        250       260
                 ....*....|....*....|.
gi 346645039 560 NGRIQEAGSHEELMA--QHGY 578
Cdd:COG0444  226 AGRIVEEGPVEELFEnpRHPY 246
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
367-567 8.66e-24

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: 99.60  E-value: 8.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRSLRSQMGVMLqDTFIFSG--TIIEN 444
Cdd:cd03268   16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALI-EAPGFYPnlTAREN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IR-----YGKLDATEEEIIAaakvvrahdfISGLKDgyytEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:cd03268   93 LRllarlLGIRKKRIDEVLD----------VVGLKD----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 346645039 520 TQTEILLQEGLERLL-EGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAG 567
Cdd:cd03268  159 PDGIKELRELILSLRdQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
350-578 1.03e-23

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: 105.15  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 350 NVDF---KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTT----IINLLSrfyniNSGEILVDGENVEEVT--- 419
Cdd:COG4172  282 KVWFpikRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSrra 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 420 LRSLRSQMGVMLQDTF-IFS-----GTIIE---NIRYGKLDATE-EEIIAAA--KVvrahdfisGLKDG----YYTEvke 483
Cdd:COG4172  357 LRPLRRRMQVVFQDPFgSLSprmtvGQIIAeglRVHGPGLSAAErRARVAEAleEV--------GLDPAarhrYPHE--- 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 484 rgstLSAGQRQLISFARALLADPKILILDEATSSID--TQTEIL-----LQE--GLERLLegrtsfiIAHRLSTIKN-SS 553
Cdd:COG4172  426 ----FSGGQRQRIAIARALILEPKLLVLDEPTSALDvsVQAQILdllrdLQRehGLAYLF-------ISHDLAVVRAlAH 494
                        250       260
                 ....*....|....*....|....*..
gi 346645039 554 RIFYIDNGRIQEAGSHEELMA--QHGY 578
Cdd:COG4172  495 RVMVMKDGKVVEQGPTEQVFDapQHPY 521
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
33-301 1.52e-23

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 101.00  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18567    2 RALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18567   82 FRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFtevSNEYRRSWMKAVKIQFL---------LWPGV 263
Cdd:cd18567  161 LYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARW---LNLLVDAINADIRLQRLqilfsaangLLFGL 237
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 346645039 264 QNIAVmttclIYFVGIKGYGVDVSTGTLIAFIGYVGNF 301
Cdd:cd18567  238 ENILV-----IYLGALLVLDGEFTVGMLFAFLAYKDQF 270
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
351-575 1.99e-23

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 100.47  E-value: 1.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI-LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:PRK13635   6 IRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQ--DTFIFSGTIIENIRYG------KLDATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARA 501
Cdd:PRK13635  86 VFQnpDNQFVGATVQDDVAFGlenigvPREEMVERVDQALRQVGMEDFL-----------NREPHRLSGGQKQRVAIAGV 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 502 LLADPKILILDEATSSIDTQTEillQEGLE--RLL--EGRTSFI-IAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGR---REVLEtvRQLkeQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
cbiO PRK13650
energy-coupling factor transporter ATPase;
351-575 2.31e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 100.19  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD--ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:PRK13650   5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQ--DTFIFSGTIIENIRYG------KLDATEEEIIAAAKVVRAHDFisglkdgyytevKERG-STLSAGQRQLISFA 499
Cdd:PRK13650  85 MVFQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDF------------KEREpARLSGGQKQRVAIA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
370-575 2.58e-23

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: 99.64  E-value: 2.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQ-MGVMLQDTFIFSG-TIIEN 444
Cdd:cd03294   43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTVLEN 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYGkLD----ATEEEIIAAAKVVRAhdfiSGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEATSSIDT 520
Cdd:cd03294  123 VAFG-LEvqgvPRAEREERAAEALEL----VGLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 521 QTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03294  194 LIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
363-563 4.58e-23

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: 95.96  E-value: 4.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRsqmgvmlqdtfifsgtii 442
Cdd:cd03216   12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPR------------------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 enirygklDAteeeiiAAAKVVRAHDfisglkdgyytevkergstLSAGQRQLISFARALLADPKILILDEATSSI-DTQ 521
Cdd:cd03216   71 --------DA------RRAGIAMVYQ-------------------LSVGERQMVEIARALARNARLLILDEPTAALtPAE 117
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 346645039 522 TEILLQEgLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03216  118 VERLFKV-IRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
351-572 5.53e-23

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: 97.58  E-value: 5.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI-LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGV 429
Cdd:cd03263    1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSG-TIIENIR-YGKLDATEEEIIAAAkvvrAHDFISGLKDGYYteVKERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03263   80 CPQFDALFDElTVREHLRfYARLKGLPKSEIKEE----VELLLRVLGLTDK--ANKRARTLSGGMKRKLSLAIALIGGPS 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03263  154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
351-572 5.88e-23

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 100.53  E-value: 5.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVM 430
Cdd:COG3839    4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIF-SGTIIENIRYG----KLDATE--EEIIAAAKVVRahdfISGLKDgyytevkERGSTLSAGQRQLISFARALL 503
Cdd:COG3839   81 FQSYALYpHMTVYENIAFPlklrKVPKAEidRRVREAAELLG----LEDLLD-------RKPKQLSGGQRQRVALGRALV 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSID----TQTEILLQEGLERLlegRTSFIIA-HRLS---TIknSSRIFYIDNGRIQEAGSHEEL 572
Cdd:COG3839  150 REPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVtHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
362-567 6.36e-23

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: 97.60  E-value: 6.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveevTLRSLRSqMGVMLQDTFifsgTI 441
Cdd:cd03220   33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLG-LGGGFNPEL----TG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYGK--LDATEEEIiaAAKVVRAHDFiSGLKDGYYTEVKergsTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:cd03220  102 RENIYLNGrlLGLSRKEI--DEKIDEIIEF-SELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 346645039 520 TQTEILLQEGLERLLEGRTSFIIA-HRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03220  175 AAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
354-575 7.81e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 98.61  E-value: 7.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMGVML 431
Cdd:PRK13639   5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 Q--DTFIFSGTIIENIRYGKL------DATEEEIIAAAKVVRAHDFisglkdgyyteVKERGSTLSAGQRQLISFARALL 503
Cdd:PRK13639  85 QnpDDQLFAPTVEEDVAFGPLnlglskEEVEKRVKEALKAVGMEGF-----------ENKPPHHLSGGQKKRVAIAGILA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
351-567 9.08e-23

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: 96.79  E-value: 9.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgvdilkgINFHVD----AGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenVEEVTLRSLRSQ 426
Cdd:cd03298    1 VRLDKIRFSYGE-------QPMHFDltfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQDTFIFSG-TIIENIRYG-----KLDATEEEIIAAAKvvrAHDFISGLKdgyytevKERGSTLSAGQRQLISFAR 500
Cdd:cd03298   72 VSMLFQENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEVAL---ARVGLAGLE-------KRLPGELSGGERQRVALAR 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 501 ALLADPKILILDEATSSIDTqteILLQEGLERLLE-----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03298  142 VLVRDKPVLLLDEPFAALDP---ALRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
345-577 1.08e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 98.72  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 345 PPIVGNVDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLR 424
Cdd:PRK13537   2 PMSVAPIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQ-DTFIFSGTIIENI----RYGKLDATEeeiiAAAKVVRAHDFiSGLKDGYYTEVKErgstLSAGQRQLISFA 499
Cdd:PRK13537  80 QRVGVVPQfDNLDPDFTVRENLlvfgRYFGLSAAA----ARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGR-IQEAGSHEELMAQH 576
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRkIAEGAPHALIESEI 230

                 .
gi 346645039 577 G 577
Cdd:PRK13537 231 G 231
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
367-572 2.05e-22

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 98.68  E-value: 2.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEeVTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:COG1118   18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFVFQHYALFPHmTVAENI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYG--KLDATEEEIIAaakvvRAHDFI-----SGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:COG1118   97 AFGlrVRPPSKAEIRA-----RVEELLelvqlEGLADRYPSQ-------LSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 519 DTQTEILLQEGLERLLE--GRTSFIIAH------RLstiknSSRIFYIDNGRIQEAGSHEEL 572
Cdd:COG1118  165 DAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEV 221
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
355-575 2.82e-22

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 96.58  E-value: 2.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEV-------------TLR 421
Cdd:PRK10619  10 DLHKRYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQMGVMLQDTFIFSG-TIIENIR--------YGKLDATEEEIIAAAKVvrahdFISGLKDGYYTevkergSTLSAGQ 492
Cdd:PRK10619  89 LLRTRLTMVFQHFNLWSHmTVLENVMeapiqvlgLSKQEARERAVKYLAKV-----GIDERAQGKYP------VHLSGGQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 493 RQLISFARALLADPKILILDEATSSIDTQT--EIL--LQEGLErllEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELvgEVLriMQQLAE---EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234

                 ....*...
gi 346645039 568 SHEELMAQ 575
Cdd:PRK10619 235 APEQLFGN 242
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
365-548 3.99e-22

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: 94.15  E-value: 3.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 365 DILKGINFHVDAGESIALVGPTGAGKTTIINLLS--RFYNINSGEILVDGENVEevtLRSLRSQMG-VMLQDTFIFSGTI 441
Cdd:cd03213   23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFRKIIGyVPQDDILHPTLTV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYgkldateeeiiaAAKVvrahdfisglkdgyytevkeRGstLSAGQRQLISFARALLADPKILILDEATSSIDTQ 521
Cdd:cd03213  100 RETLMF------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
                        170       180
                 ....*....|....*....|....*...
gi 346645039 522 TEILLQEGLERL-LEGRTSFIIAHRLST 548
Cdd:cd03213  146 SALQVMSLLRRLaDTGRTIICSIHQPSS 173
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
39-318 5.52e-22

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 96.46  E-value: 5.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQlFWIAVI-FIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQ 117
Cdd:cd18572    2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREA-FYRAVLlLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 118 KLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQ 197
Cdd:cd18572   81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 198 RKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRsWMKAVKIQFLLWPGVQNIAVM-TTCLIYF 276
Cdd:cd18572  161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALK-LSVRQALAYAGYVAVNTLLQNgTQVLVLF 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 346645039 277 VGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITA 318
Cdd:cd18572  240 YG--GHLVlsgRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQA 282
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
351-567 6.79e-22

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: 94.24  E-value: 6.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlRSLRSQMGVM 430
Cdd:cd03301    1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG-KLDATEEEIIA-----AAKVVRahdfISGLKDGYYTEvkergstLSAGQRQLISFARALL 503
Cdd:cd03301   78 FQNYALYPHmTVYDNIAFGlKLRKVPKDEIDervreVAELLQ----IEHLLDRKPKQ-------LSGGQRQRVALGRAIV 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03301  147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
PLN03232 PLN03232
ABC transporter C family member; Provisional
74-572 1.38e-21

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 99.67  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   74 WI----AVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSdLLSN 149
Cdd:PLN03232  338 WVgyvyAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQ-QIAE 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  150 GLINLISDILSVIVTLGFMLMIDPVLTLY-SLAL---IPVLFVIVMVIKTAQRKAYQVLSNKQSNMNayihESIAGIKVT 225
Cdd:PLN03232  417 QLHGLWSAPFRIIVSMVLLYQQLGVASLFgSLILfllIPLQTLIVRKMRKLTKEGLQWTDKRVGIIN----EILASMDTV 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  226 QSFSREEeNFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPV 305
Cdd:PLN03232  493 KCYAWEK-SFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPL 571
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  306 INIGNFYNSLITATTYLERIFETMDVEPDIkdIPNAKKMPPIVGNVDFKDVYFRYEEGVD--ILKGINFHVDAGESIALV 383
Cdd:PLN03232  572 NMLPNLLSQVVNANVSLQRIEELLLSEERI--LAQNPPLQPGAPAISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIV 649
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  384 GPTGAGKTTIINLLSrfyninsGEIlvdgeNVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKV 463
Cdd:PLN03232  650 GGTGEGKTSLISAML-------GEL-----SHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT 717
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  464 VRAHDFisGLKDGY-YTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQ-TEILLQEGLERLLEGRTSFI 541
Cdd:PLN03232  718 ALQHDL--DLLPGRdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVL 795
                         490       500       510
                  ....*....|....*....|....*....|.
gi 346645039  542 IAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PLN03232  796 VTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
39-297 1.97e-21

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 94.86  E-value: 1.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18575    2 LIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18575   82 LSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLwpgvqnIAVMTTC------ 272
Cdd:cd18575  162 RLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALL------TALVIFLvfgaiv 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 346645039 273 LIYFVGIKgygvDV-----STGTLIAFIGY 297
Cdd:cd18575  236 FVLWLGAH----DVlagrmSAGELSQFVFY 261
cbiO PRK13637
energy-coupling factor transporter ATPase;
367-571 2.41e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 94.34  E-value: 2.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMGVMLQ--DTFIFSGTII 442
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQypEYQLFEETIE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYG--KLDATEEEIiaAAKVVRAHDfISGLKdgyYTEVKERGS-TLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK13637 103 KDIAFGpiNLGLSEEEI--ENRVKRAMN-IVGLD---YEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 520 --TQTEILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEE 571
Cdd:PRK13637 177 pkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
354-575 2.60e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 94.14  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE--EVTLRSLRSQMGVML 431
Cdd:PRK13636   9 EELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVGMVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 Q--DTFIFSGTIIENIRYGKLDAT--EEEIIAAAKVVRAHDFISGLKDgyytevkERGSTLSAGQRQLISFARALLADPK 507
Cdd:PRK13636  89 QdpDNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 508 ILILDEATSSIDTQ--TEI--LLQEGLERLleGRTSFIIAHRLSTIK-NSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13636 162 VLVLDEPTAGLDPMgvSEImkLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
344-573 2.99e-21

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 96.06  E-value: 2.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIvgnvDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL 423
Cdd:PRK09536   1 MPMI----DVSDLSVEFGD-TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDT---FIFSG-TIIE------NIRYGKLDATE----EEIIAAAKVVRAHDfisglkdgyytevkERGSTLS 489
Cdd:PRK09536  76 SRRVASVPQDTslsFEFDVrQVVEmgrtphRSRFDTWTETDraavERAMERTGVAQFAD--------------RPVTSLS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAG 567
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221

                 ....*.
gi 346645039 568 SHEELM 573
Cdd:PRK09536 222 PPADVL 227
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
366-573 3.01e-21

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 93.30  E-value: 3.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFI-FSGTIIEN 444
Cdd:PRK13548  17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG----KLDATEEEIIAAAkVVRAHDfISGLKDGYYTevkergsTLSAGQRQLISFARALL------ADPKILILDEA 514
Cdd:PRK13548  97 VAMGraphGLSRAEDDALVAA-ALAQVD-LAHLAGRDYP-------QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 515 TSSIDtqteILLQEGLERLL------EGRTSFIIAHRLstikN-----SSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK13548 168 TSALD----LAHQHHVLRLArqlaheRGLAVIVVLHDL----NlaaryADRIVLLHQGRLVADGTPAEVL 229
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
351-567 3.04e-21

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: 92.34  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlrslRSQMGVM 430
Cdd:cd03269    1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRY-GKLDATEEEIIAAakvvRAHDFISGLKDGYYTEVKERgsTLSAGQRQLISFARALLADPKI 508
Cdd:cd03269   76 PEERGLYPKmKVIDQLVYlAQLKGLKKEEARR----RIDEWLERLELSEYANKRVE--ELSKGNQQKVQFIAAVIHDPEL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 509 LILDEATSSID-TQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03269  150 LILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
371-576 3.05e-21

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 92.72  E-value: 3.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 371 NFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENveevTLRSLRSQMGV-ML-QDTFIFSG-TIIENIRY 447
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRRPVsMLfQENNLFSHlTVAQNIGL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 448 G-----KLDATEEEIIAA-AKVVRAHDFISGLKdgyytevkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQ 521
Cdd:PRK10771  95 GlnpglKLNAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 522 teiLLQEGL--------ERLLegrTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:PRK10771 164 ---LRQEMLtlvsqvcqERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
351-575 3.84e-21

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 94.87  E-value: 3.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTT---IINLLSRfynINSGEILVDGENV---EEVTLR 421
Cdd:PRK11153   2 IELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLtalSEKELR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQMGvMlqdtfIF-------SGTIIENIRYG-KLDATEEEIIAAakvvRAHDF-----ISGLKDGYytevkerGSTL 488
Cdd:PRK11153  79 KARRQIG-M-----IFqhfnllsSRTVFDNVALPlELAGTPKAEIKA----RVTELlelvgLSDKADRY-------PAQL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 489 SAGQRQLISFARALLADPKILILDEATSSIDTQT--EIL-LQEGLERLLeGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQ 564
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATtrSILeLLKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
                        250
                 ....*....|.
gi 346645039 565 EAGSHEELMAQ 575
Cdd:PRK11153 221 EQGTVSEVFSH 231
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
351-567 5.19e-21

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: 91.49  E-value: 5.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGeSIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVM 430
Cdd:cd03264    1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQD-TFIFSGTIIENIRYgkldateeeiIAAAKVV---RAHDFISGL--KDGYYTEVKERGSTLSAGQRQLISFARALLA 504
Cdd:cd03264   78 PQEfGVYPNFTVREFLDY----------IAWLKGIpskEVKARVDEVleLVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNS-SRIFYIDNGRIQEAG 567
Cdd:cd03264  148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
32-325 5.63e-21

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 93.43  E-value: 5.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  32 QKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTA 111
Cdd:cd18782    1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 IFGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVM 191
Cdd:cd18782   81 IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 192 VIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSfsreeENFEIFT--EVSNEYRRSW---MKAVKIQFLLWPGVQNI 266
Cdd:cd18782  160 LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA-----QNAELKArwRWQNRYARSLgegFKLTVLGTTSGSLSQFL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 267 AVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18782  235 NKLSSLLVLWVGaylvLRG---ELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
33-325 5.70e-21

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 93.39  E-value: 5.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  33 KSIYITLFVI-LLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTA 111
Cdd:cd18568    1 RKLLAEILLAsLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 IFGHLQKLPFSYFDSRPHGKILIRVvnYINM-LSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIV 190
Cdd:cd18568   81 FYKHLLSLPLSFFASRKVGDIITRF--QENQkIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 191 MVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEenfEIFTEVSNEYRRSWMKAVKIQFlLWPGVQNIA--- 267
Cdd:cd18568  159 LLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAER---PIRWRWENKFAKALNTRFRGQK-LSIVLQLISsli 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 268 -VMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18568  235 nHLGTIAVLWYGaylvISG---QLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
359-576 6.86e-21

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 92.07  E-value: 6.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveevTLRSLRSQMGVMLQDtfiFS 438
Cdd:COG1134   34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLELGAGFHPE---LT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GtiIENIR-----YG----KLDATEEEIIaaakvvrahDFiSGLKDGYYTEVKergsTLSAGQRQLISFARALLADPKIL 509
Cdd:COG1134  105 G--RENIYlngrlLGlsrkEIDEKFDEIV---------EF-AELGDFIDQPVK----TYSSGMRARLAFAVATAVDPDIL 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 510 ILDEATSSIDTQteilLQE-GLERLLE----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG1134  169 LVDEVLAVGDAA----FQKkCLARIRElresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAAY 237
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
351-575 7.80e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 92.94  E-value: 7.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:PRK13652   4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQ--DTFIFSGTIIENIRYGKLD-ATEEEIIaaakvvrAHDFISGLKDGYYTEVKERGS-TLSAGQRQLISFARALLADP 506
Cdd:PRK13652  84 FQnpDDQIFSPTVEQDIAFGPINlGLDEETV-------AHRVSSALHMLGLEELRDRVPhHLSGGEKKRVAIAGVIAMEP 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
319-570 8.62e-21

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 93.74  E-value: 8.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 319 TTYLERIFETMDVEPDIKDIPNAkkMPPIVGN-----VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTI 393
Cdd:PRK13536   7 AEEAPRRLELSPIERKHQGISEA--KASIPGSmstvaIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 394 INLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVMLQ-DTFIFSGTIIENI----RYGKLDATEEEIIaaakvvrahd 468
Cdd:PRK13536  84 ARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENLlvfgRYFGMSTREIEAV---------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 469 fISGLKDGYYTEVKE--RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHR 545
Cdd:PRK13536 153 -IPSLLEFARLESKAdaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHF 231
                        250       260
                 ....*....|....*....|....*..
gi 346645039 546 LSTIKN-SSRIFYIDNGR-IQEAGSHE 570
Cdd:PRK13536 232 MEEAERlCDRLCVLEAGRkIAEGRPHA 258
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
351-573 1.69e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 91.59  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:PRK13632   8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQD---TFIFSgTIIENIRYG----KLDATE-EEIIA-AAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFAR 500
Cdd:PRK13632  88 IFQNpdnQFIGA-TVEDDIAFGlenkKVPPKKmKDIIDdLAKKVGMEDYL-----------DKEPQNLSGGQKQRVAIAS 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIA--HRLSTIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
367-572 1.72e-20

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: 90.51  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDElTGWENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 R-YGKLDATEEEiIAAAKVVRAHDFIsGLkdgyyTEVKER-GSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:cd03265   95 YiHARLYGVPGA-ERRERIDELLDFV-GL-----LEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346645039 524 ILLQEGLERLLE--GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03265  168 AHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
cbiO PRK13644
energy-coupling factor transporter ATPase;
351-574 2.71e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 91.20  E-value: 2.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT-LRSLRSQMGV 429
Cdd:PRK13644   2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQ--DTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFIsGLKDGYYTEVKergsTLSAGQRQLISFARALLADPK 507
Cdd:PRK13644  82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-GLEKYRHRSPK----TLSGGQGQCVALAGILTMEPE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
371-567 2.72e-20

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: 89.66  E-value: 2.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 371 NFHVDA-----GESIALVGPTGAGKTTIINLLSRFYNINSGEILVDG----ENVEEVTLRSLRSQMGVMLQDTFIFSG-T 440
Cdd:cd03297   12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALFPHlN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYG-KLDATEEEIIAAAKVVRAHDfISGLKDGYYtevkergSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:cd03297   92 VRENLAFGlKRKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 346645039 520 TQTEILLQEGLERLLE--GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAG 567
Cdd:cd03297  164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
310-545 3.52e-20

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 94.49  E-value: 3.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 310 NFYNSLITATTYLERI--FETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTG 387
Cdd:COG4178  320 DNYQSLAEWRATVDRLagFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSG 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 388 AGKTTIINLLSRFYNINSGEIlvdgenveevtlrSLRSQMGVML--QDTFIFSGTIIENIRY--GKLDATEEEIIAAAKV 463
Cdd:COG4178  400 SGKSTLLRAIAGLWPYGSGRI-------------ARPAGARVLFlpQRPYLPLGTLREALLYpaTAEAFSDAELREALEA 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 464 VRAHDFISGLkdgyyTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGrTSFI-I 542
Cdd:COG4178  467 VGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVIsV 540

                 ...
gi 346645039 543 AHR 545
Cdd:COG4178  541 GHR 543
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
367-567 4.43e-20

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: 88.96  E-value: 4.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03266   21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RY-GKLDATEEEIIAAakvvRAHDFISGLKDGYYTEVkeRGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEI 524
Cdd:cd03266  100 EYfAGLYGLKGDELTA----RLEELADRLGMEELLDR--RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 346645039 525 LLQEGLERLLE-GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03266  174 ALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
367-578 4.77e-20

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 90.94  E-value: 4.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV------------EEvtlRSLRSQMgvmlqdt 434
Cdd:COG4152   17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpedrrrigylpEE---RGLYPKM------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 fifsgTIIENIRY-GKL---DAteeeiiAAAKvVRAHDFIS--GLKDGYYTEVKErgstLSAGQRQLISFARALLADPKI 508
Cdd:COG4152   87 -----KVGEQLVYlARLkglSK------AEAK-RRADEWLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPEL 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 509 LILDEATSSID-TQTEILLQEGLERLLEGRTsfII--AHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQHGY 578
Cdd:COG4152  151 LILDEPFSGLDpVNVELLKDVIRELAAKGTT--VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR 222
PLN03130 PLN03130
ABC transporter C family member; Provisional
304-574 5.48e-20

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 94.80  E-value: 5.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  304 PVINIGNFYNSLITATTYLERIFETMDVEPDIKdIPNakkmPPIVGN---VDFKDVYFRYEEGVD--ILKGINFHVDAGE 378
Cdd:PLN03130  570 PLFMLPNLITQAVNANVSLKRLEELLLAEERVL-LPN----PPLEPGlpaISIKNGYFSWDSKAErpTLSNINLDVPVGS 644
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  379 SIALVGPTGAGKTTIINLLSrfyninsGEI--LVDGENVeevtlrsLRSQMGVMLQDTFIFSGTIIENIRYGK-LDATE- 454
Cdd:PLN03130  645 LVAIVGSTGEGKTSLISAML-------GELppRSDASVV-------IRGTVAYVPQVSWIFNATVRDNILFGSpFDPERy 710
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  455 EEIIAAAKVVRAHDFISGlkdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQT-EILLQEGLERL 533
Cdd:PLN03130  711 ERAIDVTALQHDLDLLPG---GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDE 787
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 346645039  534 LEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PLN03130  788 LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
366-572 8.78e-20

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 91.30  E-value: 8.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSlrSQMGVMLQDTFIFSG-TIIEN 444
Cdd:PRK10851  17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG--KLDATEEEIIAA--AKVVRAHDFI--SGLKDGYytevkerGSTLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:PRK10851  95 IAFGltVLPRRERPNAAAikAKVTQLLEMVqlAHLADRY-------PAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 519 DTQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
344-578 1.29e-19

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 90.02  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVGNVDFKDVY------FRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV-- 415
Cdd:PRK11308   2 QQPLLQAIDLKKHYpvkrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 416 -EEVTLRSLRSQMGVMLQDTFifsGTIieNIRYgKLDATEEE--II-----AAAKVVRAHDFIS--GLKDGYYtevKERG 485
Cdd:PRK11308  82 aDPEAQKLLRQKIQIVFQNPY---GSL--NPRK-KVGQILEEplLIntslsAAERREKALAMMAkvGLRPEHY---DRYP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 486 STLSAGQRQLISFARALLADPKILILDEATSSIDT--QTEIL-----LQEglerllEGRTSFI-IAHRLST---IKNSSR 554
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVsvQAQVLnlmmdLQQ------ELGLSYVfISHDLSVvehIADEVM 226
                        250       260
                 ....*....|....*....|....*.
gi 346645039 555 IFYIdnGRIQEAGSHEELMA--QHGY 578
Cdd:PRK11308 227 VMYL--GRCVEKGTKEQIFNnpRHPY 250
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
42-315 1.45e-19

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 89.50  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  42 ILLANVATMIGPYLTKIVID-----DTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18573    5 LLVSSAVTMSVPFAIGKLIDvaskeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18573   85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNE-----YRRSWMKAVKIQFLLWPGvqNIAVMtt 271
Cdd:cd18573  165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEvfdlaKKEALASGLFFGSTGFSG--NLSLL-- 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 346645039 272 CLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSL 315
Cdd:cd18573  241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSEL 284
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
367-546 1.64e-19

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 92.01  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLR--SQMGV-------MLQDTFif 437
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRdaIALGIgmvhqhfMLVPNL-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 sgTIIENIRYGkLDATEEEII---AAAKVVRAhdfIS---GLKdgyyTEVKERGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:COG3845   96 --TVAENIVLG-LEPTKGGRLdrkAARARIRE---LSeryGLD----VDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 346645039 512 DEATSSIDTQ-TEILLQEgLERLL-EGRTSFIIAHRL 546
Cdd:COG3845  166 DEPTAVLTPQeADELFEI-LRRLAaEGKSIIFITHKL 201
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
351-587 1.72e-19

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 90.39  E-value: 1.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVM 430
Cdd:PRK09452  15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG-KLDATEEEIIA-----AAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARALL 503
Cdd:PRK09452  92 FQSYALFPHmTVFENVAFGlRMQKTPAAEITprvmeALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARAVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 504 ADPKILILDEATSSID------TQTEIllqEGLERLLeGRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEELmaqh 576
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrkqMQNEL---KALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI---- 232
                        250
                 ....*....|....*
gi 346645039 577 gyyY----NLYQSQF 587
Cdd:PRK09452 233 ---YeepkNLFVARF 244
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
367-573 3.92e-19

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 87.14  E-value: 3.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENVEEVTLRS--LRSQMGVMLQDTFIFSG 439
Cdd:PRK14239  21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG----------KLDATEEEIIAAAKVvrahdfisglkdgyYTEVKER----GSTLSAGQRQLISFARALLAD 505
Cdd:PRK14239 101 SIYENVVYGlrlkgikdkqVLDEAVEKSLKGASI--------------WDEVKDRlhdsALGLSGGQQQRVCIARVLATS 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHrlsTIKNSSRI-----FYIDNGRIQEAGSHEELM 573
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRIsdrtgFFLDGDLIEYNDTKQMFM 236
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
339-519 5.90e-19

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 86.63  E-value: 5.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 339 PNAKKMPPIVgnvDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRfynIN--------SGEILV 410
Cdd:COG1117    3 APASTLEPKI---EVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNR---MNdlipgarvEGEILL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 411 DGENV--EEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYG-----KLDATE-EEIiaaakVVRAhdfisgLKD-GYYTEV 481
Cdd:COG1117   76 DGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSElDEI-----VEES------LRKaALWDEV 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 346645039 482 KER----GSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:COG1117  145 KDRlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
366-574 6.30e-19

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: 86.06  E-value: 6.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSlRSQMGV--MLQDTFIFSG-TII 442
Cdd:cd03218   15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLPQEASIFRKlTVE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIR-----YGKLDATEEEIIAAAkvvrAHDF-ISGLKdgyytevKERGSTLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:cd03218   94 ENILavleiRGLSKKEREEKLEEL----LEEFhITHLR-------KSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 517 SIDTQTEILLQEGLERLLE-GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:cd03218  163 GVDPIAVQDIQKIIKILKDrGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
364-533 8.62e-19

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 85.40  E-value: 8.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 364 VDILKGINFHVDAGESIALVGPTGAGKTTIINLLS---RFYNINSGEILVDGenvEEVTLRSLRSQMGVMLQDTFIFSG- 439
Cdd:cd03234   20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGl 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYGKLDATEEEIIAAAKVVRAHDFisGLKDGYYTEVK-ERGSTLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:cd03234   97 TVRETLTYTAILRLPRKSSDAIRKKRVEDV--LLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
                        170
                 ....*....|....*
gi 346645039 519 DTQTEILLQEGLERL 533
Cdd:cd03234  175 DSFTALNLVSTLSQL 189
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
353-564 1.00e-18

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 89.35  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveevtlRSLRsqMGVMLQ 432
Cdd:COG0488    1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYLPQ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSG-TIIENIR----------------YGKLDATEEEIIAAAKV-------------VRAHDFISGLK---DGYYT 479
Cdd:COG0488   69 EPPLDDDlTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAELqeefealggweaeARAEEILSGLGfpeEDLDR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 EVkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTeIllqEGLERLLEGRTS--FIIAH------RLSTikn 551
Cdd:COG0488  149 PV----SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-I---EWLEEFLKNYPGtvLVVSHdryfldRVAT--- 217
                        250
                 ....*....|...
gi 346645039 552 ssRIFYIDNGRIQ 564
Cdd:COG0488  218 --RILELDRGKLT 228
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
322-565 1.09e-18

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 89.35  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 322 LERIfETMDVEPDIK----DIPNAKKMPPIVgnVDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLL 397
Cdd:COG0488  286 LEKL-EREEPPRRDKtveiRFPPPERLGKKV--LELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 398 SRFYNINSGEILVdGENVEEVTLrslrSQMgvmlQDTFIFSGTIIENIRYGKLDATEEEIIAAAKvvrahDF-ISGlkdg 476
Cdd:COG0488  362 AGELEPDSGTVKL-GETVKIGYF----DQH----QEELDPDKTVLDELRDGAPGGTEQEVRGYLG-----RFlFSG---- 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 477 yyTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERlLEGrTSFIIAH-R--LSTIKNss 553
Cdd:COG0488  424 --DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdRyfLDRVAT-- 497
                        250
                 ....*....|..
gi 346645039 554 RIFYIDNGRIQE 565
Cdd:COG0488  498 RILEFEDGGVRE 509
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
329-584 1.29e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 89.38  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 329 MDVEPDIKDIPNAKKMPPIVgNVDFKDVYFRYEEG-----VD---ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF 400
Cdd:PRK15134 257 LNSEPSGDPVPLPEPASPLL-DVEQLQVAFPIRKGilkrtVDhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 401 ynINS-GEILVDGENVEEVTLRSL---RSQMGVMLQDTF------IFSGTIIEN---IRYGKLDAT--EEEIIAAAKVVr 465
Cdd:PRK15134 336 --INSqGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnprLNVLQIIEEglrVHQPTLSAAqrEQQVIAVMEEV- 412
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 466 ahdfisglkdGYYTEVKER-GSTLSAGQRQLISFARALLADPKILILDEATSSID--TQTEIL-LQEGLERllEGRTSFI 541
Cdd:PRK15134 413 ----------GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAQILaLLKSLQQ--KHQLAYL 480
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 346645039 542 -IAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA--QHGYYYNLYQ 584
Cdd:PRK15134 481 fISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAapQQEYTRQLLA 527
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
362-578 1.46e-18

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: 84.12  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNINSGEILVDGENVEEVTLrSLRSQMGVML--QDTFIF 437
Cdd:cd03217   11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPP-EERARLGIFLafQYPPEI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGtiienirygkldateeeiiaaakvVRAHDFISGLKDGyytevkergstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:cd03217   90 PG------------------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 518 IDTQTEILLQEGLERLLEGRTSF-IIAH--RLSTIKNSSRIFYIDNGRIQEAGSHE--ELMAQHGY 578
Cdd:cd03217  135 LDIDALRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
366-563 1.46e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 85.50  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveEVTLRSLRSQMGVMLQDTFIFS-GTIIEN 444
Cdd:PRK11247  27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG-KLDATEEEIIAAAKVvrahdfisGLKDgyytEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:PRK11247 102 VGLGlKGQWRDAALQALAAV--------GLAD----RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 346645039 524 ILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRI 563
Cdd:PRK11247 170 IEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
366-543 1.63e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 84.16  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL------RSQMGVMLqdtfifsg 439
Cdd:PRK13539  17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAMKPAL-------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRY--GKLDATEEEIIAAAKVVRAHDfISGLKDGYytevkergstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK13539  89 TVAENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
                        170       180
                 ....*....|....*....|....*.
gi 346645039 518 IDTQTEILLQEGLERLLEGRTSFIIA 543
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAA 183
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
363-574 1.87e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 85.92  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNI-----NSGEILVDGENVEEV-TLRSLRSQMGVMLQDTFI 436
Cdd:PRK14271  33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNP 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 FSGTIIENIRYGkldateeeiIAAAKVVRAHDFiSGLKDGYYTEV------KERGST----LSAGQRQLISFARALLADP 506
Cdd:PRK14271 113 FPMSIMDNVLAG---------VRAHKLVPRKEF-RGVAQARLTEVglwdavKDRLSDspfrLSGGQQQLLCLARTLAVNP 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLST---IKNSSRIFYidNGRIQEAGSHEELMA 574
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQaarISDRAALFF--DGRLVEEGPTEQLFS 251
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
35-325 4.97e-18

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 84.86  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLAnvatMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLC--MRYRIRSITLIGQDILKDMRtaI 112
Cdd:cd18588    8 LLASLFLQLFA----LVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLsgLRTYLFSHTTNRIDAELGAR--L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRvVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18588   82 FRHLLRLPLSYFESRQVGDTVAR-VRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18588  161 VTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTL 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 273 LIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18588  241 AILWFG--AYLVmdgELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
366-563 5.03e-18

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 84.37  E-value: 5.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeevTLRSL--RSQM-GVMLQDTFI---FSG 439
Cdd:COG1101   21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---TKLPEykRAKYiGRVFQDPMMgtaPSM 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIrygkldateeeIIAAAKVvRAHDFISGLKDGYYTEVKERGST---------------LSAGQRQLISFARALLA 504
Cdd:COG1101   98 TIEENL-----------ALAYRRG-KRRGLRRGLTKKRRELFRELLATlglglenrldtkvglLSGGQRQALSLLMATLT 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGR--TSFIIAHRLS-TIKNSSRIFYIDNGRI 563
Cdd:COG1101  166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
363-572 5.35e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 87.03  E-value: 5.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVML--QDTFIFSG- 439
Cdd:PRK15439  23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIYLvpQEPLLFPNl 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG--KLDATEEEIIAAAKVVRAHdfisglkdgyyTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK15439 102 SVKENILFGlpKRQASMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 518 ID-TQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
72-513 6.82e-18

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: 87.16  E-value: 6.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  72 LFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNgL 151
Cdd:COG4615   47 LARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-L 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 152 INLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIK-VTQSFSR 230
Cdd:COG4615  126 PELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKeLKLNRRR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 231 EEENFE-IFTEVSNEYRRSWMKAVKIQFLLWpgvqniaVMTTCLIYF-----VGIKGYGVDVSTGTLIAFIG---YVgnf 301
Cdd:COG4615  206 RRAFFDeDLQPTAERYRDLRIRADTIFALAN-------NWGNLLFFAligliLFLLPALGWADPAVLSGFVLvllFL--- 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 302 WNPVINIGNFYNSLITATTYLERI---FETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRY----EEGVDILKGINFHV 374
Cdd:COG4615  276 RGPLSQLVGALPTLSRANVALRKIeelELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYpgedGDEGFTLGPIDLTI 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 375 DAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTiienirYGKLDATE 454
Cdd:COG4615  356 RRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEAD 429
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 455 EEIIAA-------AKVVRahdfisgLKDGYYTEVKergstLSAGQRQ---LISfarALLADPKILILDE 513
Cdd:COG4615  430 PARAREllerlelDHKVS-------VEDGRFSTTD-----LSQGQRKrlaLLV---ALLEDRPILVFDE 483
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
351-574 1.04e-17

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 82.62  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEE-VTLRSLRSQMGV 429
Cdd:PRK11614   6 LSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSG-TIIENIRYGKLDATEEEIiaAAKVVRAHDFISGLkdgyYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:PRK11614  85 VPEGRRVFSRmTVEENLAMGGFFAERDQF--QERIKWVYELFPRL----HERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 509 LILDEatSSIDTQTEILLQ--EGLERLL-EGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK11614 159 LLLDE--PSLGLAPIIIQQifDTIEQLReQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
351-563 1.56e-17

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 81.84  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRS---LRSQM 427
Cdd:PRK10908   2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQD-TFIFSGTIIENIRYGKL--DATEEEIiaAAKVVRAHDfisglKDGYYTEVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK10908  82 GMIFQDhHLLMDRTVYDNVAIPLIiaGASGDDI--RRRVSAALD-----KVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 505 DPKILILDEATSSIDTQteilLQEGLERLLE-----GRTSFIIAHRLSTI-KNSSRIFYIDNGRI 563
Cdd:PRK10908 155 KPAVLLADEPTGNLDDA----LSEGILRLFEefnrvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
362-574 2.14e-17

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 85.24  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNINSGEIL------------------------------ 409
Cdd:TIGR03269  11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtle 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  410 ---VDGENVEEVTLRSLRSQMGVMLQDTFIFSG--TIIENIrygkLDATEEEIIAAAKVV-RAHDFISGLKDGYytEVKE 483
Cdd:TIGR03269  91 peeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNV----LEALEEIGYEGKEAVgRAVDLIEMVQLSH--RITH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  484 RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL--EGRTSFIIAHRLSTIKN-SSRIFYIDN 560
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLEN 244
                         250
                  ....*....|....
gi 346645039  561 GRIQEAGSHEELMA 574
Cdd:TIGR03269 245 GEIKEEGTPDEVVA 258
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
354-564 2.28e-17

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: 81.61  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGeNVEEVTLRSLRSQMGVML-- 431
Cdd:cd03267   24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgq 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 ----------QDTFIFSGTIIeNIRYGKLDATEEEIIAAAKVVRAHDfisglkdgyyTEVKErgstLSAGQRQLISFARA 501
Cdd:cd03267  103 ktqlwwdlpvIDSFYLLAAIY-DLPPARFKKRLDELSELLDLEELLD----------TPVRQ----LSLGQRMRAEIAAA 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 502 LLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFII--AHRLSTI-KNSSRIFYIDNGRIQ 564
Cdd:cd03267  168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLL 233
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
366-570 2.64e-17

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 81.60  E-value: 2.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDG------ENVEEVTLRSLRSQMGVMLQDTFIFSG 439
Cdd:PRK11124  17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPH 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIEN-----IRYGKLDatEEEIIAaakvvRAHDFISGLKdgyYTEVKERGST-LSAGQRQLISFARALLADPKILILD 512
Cdd:PRK11124  97 lTVQQNlieapCRVLGLS--KDQALA-----RAEKLLERLR---LKPYADRFPLhLSGGQQQRVAIARALMMEPQVLLFD 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 513 EATSSIDtqTEILLQ--EGLERLLE-GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHE 570
Cdd:PRK11124 167 EPTAALD--PEITAQivSIIRELAEtGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
366-513 3.08e-17

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 81.23  E-value: 3.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIinllsrFYNI------NSGEILVDGENVEEVTLrSLRSQMGV--MLQDTFIF 437
Cdd:COG1137   18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIvglvkpDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SG-TIIENIR----YGKLDATE-----EEIIAaakvvrahDF-ISGLKDgyytevkERGSTLSAGQRQLISFARALLADP 506
Cdd:COG1137   91 RKlTVEDNILavleLRKLSKKEreerlEELLE--------EFgITHLRK-------SKAYSLSGGERRRVEIARALATNP 155

                 ....*..
gi 346645039 507 KILILDE 513
Cdd:COG1137  156 KFILLDE 162
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
357-561 3.12e-17

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: 80.84  E-value: 3.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 357 YFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTII-NLLSRFYNInSGEI-----LVDGENVEEVTLRSlRSQMGVM 430
Cdd:cd03290    7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVhwsnkNESEPSFEATRSRN-RYSVAYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSGTIIENIRYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILI 510
Cdd:cd03290   85 AQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 346645039 511 LDEATSSIDTQ-TEILLQEGLERLL--EGRTSFIIAHRLSTIKNSSRIFYIDNG 561
Cdd:cd03290  164 LDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
369-572 3.14e-17

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 81.57  E-value: 3.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 369 GINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLrSQMGVMlqDTFifsgtiiENIR-Y 447
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVV--RTF-------QHVRlF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 448 GKLDATEEEIIAAAKVVRAhDFISGL-KDGYY--------------------TEVKER-GSTLSAGQRQLISFARALLAD 505
Cdd:PRK11300  93 REMTVIENLLVAQHQQLKT-GLFSGLlKTPAFrraesealdraatwlervglLEHANRqAGNLAYGQQRRLEIARCMVTQ 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
366-565 3.24e-17

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 82.04  E-value: 3.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTF------- 435
Cdd:PRK10419  27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIsavnprk 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 -IfsGTII-ENIRY-GKLDATEEEIIAAAkVVRAHDFISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILD 512
Cdd:PRK10419 107 tV--REIIrEPLRHlLSLDKAERLARASE-MLRAVDLDDSVLD-------KRPPQLSGGQLQRVCLARALAVEPKLLILD 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 513 EATSSIDtqteILLQEGLERLLE------GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQE 565
Cdd:PRK10419 177 EAVSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
366-522 3.34e-17

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 80.60  E-value: 3.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTT----IINLLSRFYNInSGEILVDGENVEevTLRSLRSQMGVMLQDTFIFSG-T 440
Cdd:COG4136   16 LLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFSA-SGEVLLNGRRLT--ALPAEQRRIGILFQDDLLFPHlS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYgkldATEEEIIAAAKVVRAHDFIS--GLkDGYYtevkERG-STLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:COG4136   93 VGENLAF----ALPPTIGRAQRRARVEQALEeaGL-AGFA----DRDpATLSGGQRARVALLRALLAEPRALLLDEPFSK 163

                 ....*
gi 346645039 518 IDTQT 522
Cdd:COG4136  164 LDAAL 168
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
359-565 3.74e-17

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 81.02  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveevTLRSLRSQMGVMLQDT- 434
Cdd:PRK11629  14 RYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-----PMSKLSSAAKAELRNQk 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 --FIFS-------GTIIENIRY-----GKLDATEEEiiaaakvvRAHDFISGLkdGYYTEVKERGSTLSAGQRQLISFAR 500
Cdd:PRK11629  89 lgFIYQfhhllpdFTALENVAMplligKKKPAEINS--------RALEMLAAV--GLEHRANHRPSELSGGERQRVAIAR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQE 565
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
39-325 6.70e-17

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 350052 [Multi-domain]  Cd Length: 294  Bit Score: 81.44  E-value: 6.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDDTIPNKNmTQLFWIAVIFIVSVIVTGLCMRYrIRSITLIG-QDIL-KDMRTAIFGHL 116
Cdd:cd18779    8 LLASLLLQLLGLALPLLTGVLVDRVIPRGD-RDLLGVLGLGLAALVLTQLLAGL-LRSHLLLRlRTRLdTQLTLGFLEHL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRvVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVL--TLYSLALIPVLFVIVMvik 194
Cdd:cd18779   86 LRLPYRFFQQRSTGDLLMR-LSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLglVVLGLAALQVALLLAT--- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 taqRKAYQVLSNK----QSNMNAYIHESIAGIKVTQSFSREEENFE----IFTEVSN-EYRRS----WMKAVK--IQF-- 257
Cdd:cd18779  162 ---RRRVRELMARelaaQAEAQSYLVEALSGIETLKASGAEDRALDrwsnLFVDQLNaSLRRGrldaLVDALLatLRLaa 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 258 ---LLWPGVQniAVMTTCLiyfvgikgygvdvSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18779  239 plvLLWVGAW--QVLDGQL-------------SLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
363-544 7.01e-17

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 80.51  E-value: 7.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlrslrSQMGVMLQDTFIFS-GTI 441
Cdd:PRK11248  13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPwRNV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYG-KLDATEEeiiaAAKVVRAHDFISglKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDT 520
Cdd:PRK11248  88 QDNVAFGlQLAGVEK----MQRLEIAHQMLK--KVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
                        170       180
                 ....*....|....*....|....*.
gi 346645039 521 QTEILLQEGLERLLE--GRTSFIIAH 544
Cdd:PRK11248 162 FTREQMQTLLLKLWQetGKQVLLITH 187
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
364-572 7.51e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 80.34  E-value: 7.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 364 VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENVEEVTLRSLRSQMGVMLQ-DTFIF 437
Cdd:PRK14247  16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGTIIENIRYG----KLDATEEEIiaAAKVVRAHDfisglKDGYYTEVKER----GSTLSAGQRQLISFARALLADPKIL 509
Cdd:PRK14247  96 NLSIFENVALGlklnRLVKSKKEL--QERVRWALE-----KAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVL 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
367-573 7.53e-17

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 82.77  E-value: 7.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTFIF--SGTI 441
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALmpHMTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYG------KLDATEEEIIAAAKVVRAHDFISGLKDgyytevkergsTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 516 SSIDTQTEILLQEGLERLL--EGRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
361-563 9.21e-17

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 83.62  E-value: 9.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL----RSQMGVMLQDTFI 436
Cdd:PRK10535  18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 FSG-TIIENIRYGKLDATEEEiiaAAKVVRAHDFISGLkdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK10535  98 LSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 346645039 516 SSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
344-565 9.38e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 80.47  E-value: 9.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVGNVDFKDVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNInSGEILVDG------ENVEE 417
Cdd:PRK14258   1 MSKLIPAIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnQNIYE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 418 --VTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKldateeEIIAAAKVVRAHDFI-SGLKDG-YYTEVKER----GSTLS 489
Cdd:PRK14258  79 rrVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGV------KIVGWRPKLEIDDIVeSALKDAdLWDEIKHKihksALDLS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSID----TQTEILLQEglERLLEGRTSFIIAHRL---STIKNSSRIFYIDNGR 562
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQS--LRLRSELTMVIVSHNLhqvSRLSDFTAFFKGNENR 230

                 ...
gi 346645039 563 IQE 565
Cdd:PRK14258 231 IGQ 233
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
370-575 1.24e-16

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: 81.69  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE----NVEEVTLRSLRSQMGVMLQDTFIFSG-TIIEN 444
Cdd:COG4148   18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHlSVRGN 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG-KLDATEEEIIAAAKVVRAHDfISGLKDgyytevkeRG-STLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:COG4148   98 LLYGrKRAPRAERRISFDEVVELLG-IGHLLD--------RRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 523 --EILlqEGLERLlegRTSF-----IIAH------RLSTiknssRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:COG4148  169 kaEIL--PYLERL---RDELdipilYVSHsldevaRLAD-----HVVLLEQGRVVASGPLAEVLSR 224
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
370-575 2.07e-16

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 80.92  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRSQ-MGVMLQDTFIFSG-TIIENIRY 447
Cdd:PRK11432  25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFPHmSLGENVGY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 448 G--KLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVkergstlSAGQRQLISFARALLADPKILILDEATSSIDTQTEIL 525
Cdd:PRK11432 102 GlkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 346645039 526 LQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK11432 175 MREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
356-578 2.64e-16

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 82.04  E-value: 2.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKT----TIINLLSRFYNINSGEILVDGENV---EEVTLRSLR-SQ 426
Cdd:COG4172   14 VAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgNR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGvmlqdtFIFS------------GT-IIENIR-YGKLDATE--EEIIAAAKVVRAHDFISGLKDgYYTEvkergstLSA 490
Cdd:COG4172   94 IA------MIFQepmtslnplhtiGKqIAEVLRlHRGLSGAAarARALELLERVGIPDPERRLDA-YPHQ-------LSG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSID--TQTEIL-----LQ--EGLERLLegrtsfiIAHRLSTIKN-SSRIFYIDN 560
Cdd:COG4172  160 GQRQRVMIAMALANEPDLLIADEPTTALDvtVQAQILdllkdLQreLGMALLL-------ITHDLGVVRRfADRVAVMRQ 232
                        250       260
                 ....*....|....*....|
gi 346645039 561 GRIQEAGSHEELMA--QHGY 578
Cdd:COG4172  233 GEIVEQGPTAELFAapQHPY 252
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
366-572 3.02e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 78.94  E-value: 3.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE------NVEEVTLRSLRSQMGVMLQDTFIFSG 439
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 519 DTQTEILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
363-575 3.62e-16

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: 79.13  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveevtlRSLRSQMgvmlqdTFIFSGTII 442
Cdd:cd03291   49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------ISFSSQF------SWIMPGTIK 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYGkLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:cd03291  116 ENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 346645039 523 EI-LLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03291  195 EKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
363-549 4.19e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 81.11  E-value: 4.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR-SLRSQMGVMLQD-TFIFSGT 440
Cdd:PRK11288  16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElHLVPEMT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKLDAT-----EEEIIAAAKVVRAHdfiSGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK11288  96 VAENLYLGQLPHKggivnRRLLNYEAREQLEH---LGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 346645039 516 SSIDTQ-TEILLQegLERLL--EGRTSFIIAHRLSTI 549
Cdd:PRK11288 169 SSLSAReIEQLFR--VIRELraEGRVILYVSHRMEEI 203
cbiO PRK13642
energy-coupling factor transporter ATPase;
351-574 5.60e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 78.60  E-value: 5.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI--LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:PRK13642   5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQ--DTFIFSGTIIENIRYGkldaTEEEIIAAAKVVRAHDfiSGLKDGYYTEVKERG-STLSAGQRQLISFARALLAD 505
Cdd:PRK13642  85 MVFQnpDNQFVGATVEDDVAFG----MENQGIPREEMIKRVD--EALLAVNMLDFKTREpARLSGGQKQRVAVAGIIALR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLEGR--TSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
367-590 5.71e-16

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: 77.51  E-value: 5.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLrsqmgVMLQDTFIFSG-TIIENI 445
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  446 RYG------KLDATEEEiiaaaKVVRAHDFISGLKDGyyteVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:TIGR01184  76 ALAvdrvlpDLSKSERR-----AIVEEHIALVGLTEA----ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  520 TQTEILLQEGLERLLE--GRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGS----------HEELMAQHGYYYNLYQSQ 586
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQilevpfprprDRLEVVEDPSYYDLRNEA 226

                  ....
gi 346645039  587 FDML 590
Cdd:TIGR01184 227 LYFL 230
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
353-560 6.98e-16

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: 75.27  E-value: 6.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILvdgenveevtlRSLRSQMGVMLQ 432
Cdd:cd03223    3 LENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLLFLPQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSGTIIENIRYgkldateeeiiaaakvvrahdfisglkdgyytevkERGSTLSAGQRQLISFARALLADPKILILD 512
Cdd:cd03223   72 RPYLPLGTLREQLIY-----------------------------------PWDDVLSGGEQQRLAFARLLLHKPKFVFLD 116
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 346645039 513 EATSSIDTQTEILLqegLERLLEGRTSFI-IAHRLSTIKNSSRIFYIDN 560
Cdd:cd03223  117 EATSALDEESEDRL---YQLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
362-572 7.61e-16

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 79.49  E-value: 7.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlrSLRSQMGVMLQDTFIFSGTI 441
Cdd:PRK11607  30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHMT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IE-NIRYG-KLDATEEEIIAAakvvRAHDFISGLKDGYYTevKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK11607 108 VEqNIAFGlKQDKLPKAEIAS----RVNEMLGLVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 520 TQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK11607 182 KKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
cbiO PRK13640
energy-coupling factor transporter ATPase;
351-572 7.66e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 78.30  E-value: 7.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY---NINSGEILVDGENVEEVTLRSLRSQ 426
Cdd:PRK13640   6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQ--DTFIFSGTIIENIRYGkldaTEEEIIAAAKVVR-AHDFISGLkdGYYTEVKERGSTLSAGQRQLISFARALL 503
Cdd:PRK13640  86 VGIVFQnpDNQFVGATVGDDVAFG----LENRAVPRPEMIKiVRDVLADV--GMLDYIDSEPANLSGGQKQRVAIAGILA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
363-575 8.70e-16

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: 81.50  E-value: 8.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveevtlrslrsQMGVMLQDTFIFSGTII 442
Cdd:TIGR01271  438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIK 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   443 ENIRYGkLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:TIGR01271  505 DNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 346645039   523 EI-LLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:TIGR01271  584 EKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
366-544 9.10e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 77.19  E-value: 9.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENV--EEVTLRSLRSQMGVMLQDTFIFS 438
Cdd:PRK14267  19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 G-TIIENI----RYGKLDATEEEIiaaAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDE 513
Cdd:PRK14267  99 HlTIYDNVaigvKLNGLVKSKKEL---DERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
                        170       180       190
                 ....*....|....*....|....*....|.
gi 346645039 514 ATSSIDTQTEILLQEGLERLLEGRTSFIIAH 544
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
362-574 1.39e-15

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 76.47  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRS-LRSQMGVMLQDTFIFSGT 440
Cdd:PRK10895  14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKL----DATEEEIIAAAKVVRAHDFISGLKDGYytevkerGSTLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:PRK10895  94 SVYDNLMAVLqirdDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 517 SIDTQTEILLQEGLERLLE-GRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
35-294 2.27e-15

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 76.85  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18566    4 LPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18566   84 HLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18566  163 PILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAV 242
                        250       260
                 ....*....|....*....|....
gi 346645039 275 YFVG----IKGygvDVSTGTLIAF 294
Cdd:cd18566  243 VAFGallvING---DLTVGALIAC 263
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
354-563 2.37e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 77.05  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEI---LVDGEN----------VE 416
Cdd:PRK13651   6 KNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNkkktkekekvLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 417 EVTL-----------RSLRSQMGVMLQ--DTFIFSGTIIENIRYG--KLDATEEEiiaAAKvvRAHDFIS--GLKDGYyt 479
Cdd:PRK13651  86 KLVIqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKK--RAAKYIElvGLDESY-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 eVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRL-STIKNSSRIFY 557
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIF 237

                 ....*.
gi 346645039 558 IDNGRI 563
Cdd:PRK13651 238 FKDGKI 243
PTZ00243 PTZ00243
ABC transporter; Provisional
343-574 3.09e-15

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 79.44  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  343 KMPPIVGnvdfkDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveevtlRS 422
Cdd:PTZ00243  658 KTPKMKT-----DDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------RS 722
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  423 LrsqmGVMLQDTFIFSGTIIENIrygkLDATEEEIIAAAKVVRAHDF---ISGLKDGYYTEVKERGSTLSAGQRQLISFA 499
Cdd:PTZ00243  723 I----AYVPQQAWIMNATVRGNI----LFFDEEDAARLADAVRVSQLeadLAQLGGGLETEIGEKGVNLSGGQKARVSLA 794
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039  500 RALLADPKILILDEATSSIDTQT-EILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PTZ00243  795 RAVYANRDVYLLDDPLSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
368-578 3.67e-15

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 77.05  E-value: 3.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 368 KGINFHVDAGESIALVGPTGAGKTT----IINLLsrfyNINSGEILVDGENV---EEVTLRSLRSQMGVMLQDTF----- 435
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTfaraIIGLV----KATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLaslnp 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 -IFSGTII-ENIR--YGKLDATE--EEIIAAAKVVrahDFISGLKDGYYTEvkergstLSAGQRQLISFARALLADPKIL 509
Cdd:PRK15079 114 rMTIGEIIaEPLRtyHPKLSRQEvkDRVKAMMLKV---GLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLI 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 510 ILDEATS----SIDTQTEILLQEgLERllEGRTSFI-IAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA--QHGY 578
Cdd:PRK15079 184 ICDEPVSaldvSIQAQVVNLLQQ-LQR--EMGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHnpLHPY 257
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
363-550 4.04e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 78.05  E-value: 4.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGENVEEVTLR-SLRSQMGVMLQD-TFIFS 438
Cdd:PRK13549  17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRdTERAGIAIIHQElALVKE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENIRYGKlDATEEEIIAAAKVV-RAHDFISGLKDGY--YTEVKERGStlsaGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK13549  97 LSVLENIFLGN-EITPGGIMDYDAMYlRAQKLLAQLKLDInpATPVGNLGL----GQQQLVEIAKALNKQARLLILDEPT 171
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 346645039 516 SSI-DTQTEILLQ--EGLERllEGRTSFIIAHRLSTIK 550
Cdd:PRK13549 172 ASLtESETAVLLDiiRDLKA--HGIACIYISHKLNEVK 207
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
366-581 7.54e-15

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 77.78  E-value: 7.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSrFYNIN----SGEILVDGENVEEVTLRsLRSQMgVMLQDTFIFSGTI 441
Cdd:TIGR00955  40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMR-AISAY-VQQDDLFIPTLTV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  442 IENI------RYGKLDATEE------EIIAAAKVVRAHDFISGlkdgyyteVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:TIGR00955 117 REHLmfqahlRMPRRVTKKEkrervdEVLQALGLRKCANTRIG--------VPGRVKGLSGGERKRLAFASELLTDPPLL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIahrlsTI-KNSSRIF-------YIDNGRIQEAGSHEEL---MAQHGY 578
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIIC-----TIhQPSSELFelfdkiiLMAEGRVAYLGSPDQAvpfFSDLGH 263

                  ....*..
gi 346645039  579 ----YYN 581
Cdd:TIGR00955 264 pcpeNYN 270
GguA NF040905
sugar ABC transporter ATP-binding protein;
363-549 9.41e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 77.14  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGenvEEVTLRSLRS--QMGVML--QD-TF 435
Cdd:NF040905  13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRDseALGIVIihQElAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 IFSGTIIENI-------RYGKLDATEEEIIAA---AKVvrahdfisGLKDGYYTEVKERGstlsAGQRQLISFARALLAD 505
Cdd:NF040905  90 IPYLSIAENIflgneraKRGVIDWNETNRRARellAKV--------GLDESPDTLVTDIG----VGKQQLVEIAKALSKD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 346645039 506 PKILILDEATSSI-DTQTEILLQEGLERLLEGRTSFIIAHRLSTI 549
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEI 202
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
353-576 9.93e-15

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 76.93  E-value: 9.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQ 432
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFT 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSGTIienirYGKLDATEEEIIAA--------AKVVRAHDFISGLKdgyytevkergstLSAGQRQLISFARALLA 504
Cdd:PRK10522 405 DFHLFDQLL-----GPEGKPANPALVEKwlerlkmaHKLELEDGRISNLK-------------LSKGQKKRLALLLALAE 466
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 505 DPKILILDEATSSIDTQ-TEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:PRK10522 467 ERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASR 540
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
366-543 1.24e-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: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI 445
Cdd:cd03231   15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYGKLDATEEEIIAAAKVVRahdfISGLKDGYYtevkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEIL 525
Cdd:cd03231   95 RFWHADHSDEQVEEALARVG----LNGFEDRPV-------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
                        170
                 ....*....|....*...
gi 346645039 526 LQEGLERLLEGRTSFIIA 543
Cdd:cd03231  164 FAEAMAGHCARGGMVVLT 181
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
367-568 1.25e-14

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 74.05  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYN-INS----GEILVDGENV--EEVTLRSLRSQMGVMLQDTFIFSG 439
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG--------KLDATEEEIIAAAkvvrahdfisGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:PRK14243 106 SIYDNIAYGaringykgDMDELVERSLRQA----------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 512 DEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGS 568
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
cbiO PRK13649
energy-coupling factor transporter ATPase;
351-568 1.69e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 74.01  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT----LRS 422
Cdd:PRK13649   3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYG--KLDATEEEiiaAAKVVRAHDFISGLKDgyytEVKERGS-TLSAGQRQLIS 497
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEE---AEALAREKLALVGISE----SLFEKNPfELSGGQMRRVA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 498 FARALLADPKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYI-DNGRIQEAGS 568
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVlEKGKLVLSGK 228
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
366-521 1.72e-14

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: 72.39  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI 445
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENL 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039  446 R-YGKLDATEEEII--AAAKVvrahdfisGLKDGYYTEVkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQ 521
Cdd:TIGR01189  95 HfWAAIHGGAQRTIedALAAV--------GLTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
cbiO PRK13641
energy-coupling factor transporter ATPase;
351-574 2.03e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 74.10  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT----LRS 422
Cdd:PRK13641   3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYGKLD--ATEEEI-IAAAKVVRahdfisglKDGYYTEVKERGS-TLSAGQRQLI 496
Cdd:PRK13641  83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAkEKALKWLK--------KVGLSEDLISKSPfELSGGQMRRV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 497 SFARALLADPKILILDEATSSIDTQT-EILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
358-588 2.74e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 73.29  E-value: 2.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 358 FRYEEG------VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE--EVTLRSLRSQMgv 429
Cdd:PRK15112  14 FRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRM-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTfifSGTIIENIRYGKL-------------DATEEEIIAAAKVVrahdfisGLKD---GYYTEVkergstLSAGQR 493
Cdd:PRK15112  92 IFQDP---STSLNPRQRISQIldfplrlntdlepEQREKQIIETLRQV-------GLLPdhaSYYPHM------LAPGQK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 494 QLISFARALLADPKILILDEATSSID----TQTEILLQEGLERllEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGS 568
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDmsmrSQLINLMLELQEK--QGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
                        250       260
                 ....*....|....*....|..
gi 346645039 569 HEELMA--QHGYYYNLYQSQFD 588
Cdd:PRK15112 234 TADVLAspLHELTKRLIAGHFG 255
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
350-580 3.09e-14

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 74.68  E-value: 3.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 350 NVDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSqMGV 429
Cdd:PRK11000   3 SVTLRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERG-VGM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSG-TIIENIRYG-KLDATEEEII-----AAAKVVR-AHdfisgLKDgyytevkERGSTLSAGQRQLISFARA 501
Cdd:PRK11000  80 VFQSYALYPHlSVAENMSFGlKLAGAKKEEInqrvnQVAEVLQlAH-----LLD-------RKPKALSGGQRQRVAIGRT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 502 LLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEELmaqhgY 578
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL-----Y 222

                 ..
gi 346645039 579 YY 580
Cdd:PRK11000 223 HY 224
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
354-535 3.22e-14

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 72.05  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:PRK10247  11 QNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSGTIIENIRYG---KLDATEEEIIaAAKVVRahdFisGLKDgyyTEVKERGSTLSAGQRQLISFARALLADPKILI 510
Cdd:PRK10247  90 PTLFGDTVYDNLIFPwqiRNQQPDPAIF-LDDLER---F--ALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
                        170       180
                 ....*....|....*....|....*
gi 346645039 511 LDEATSSIDTQTEILLQEGLERLLE 535
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVR 185
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
366-589 3.24e-14

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 72.74  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSG-TIIEN 444
Cdd:PRK11231  17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRY---------GKLDATEEEIIAAAkVVRAHdfISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK11231  97 VAYgrspwlslwGRLSAEDNARVNQA-MEQTR--INHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 516 SSIDT--QTEILlqeGLERLL--EGRTSFIIAHRLStikNSSRifYID------NGRIQEAGSHEELMAQHgyyynLYQS 585
Cdd:PRK11231 167 TYLDInhQVELM---RLMRELntQGKTVVTVLHDLN---QASR--YCDhlvvlaNGHVMAQGTPEEVMTPG-----LLRT 233

                 ....
gi 346645039 586 QFDM 589
Cdd:PRK11231 234 VFDV 237
cbiO PRK13643
energy-coupling factor transporter ATPase;
351-575 5.42e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 72.84  E-value: 5.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEI----LVDGENVEEVTLRS 422
Cdd:PRK13643   2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYGK----LDATEEEIIAAAKVVrahdfISGLKDGYYtevKERGSTLSAGQRQLI 496
Cdd:PRK13643  82 VRKKVGVVFQfpESQLFEETVLKDVAFGPqnfgIPKEKAEKIAAEKLE-----MVGLADEFW---EKSPFELSGGQMRRV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 497 SFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233

                 .
gi 346645039 575 Q 575
Cdd:PRK13643 234 E 234
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
363-550 6.27e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 74.44  E-value: 6.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR-SLRSQMGVMLQD-TFIFSGT 440
Cdd:PRK09700  17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKL-----------DATEEEIIAAAKVVRAhdfisGLKdgyyTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:PRK09700  97 VLENLYIGRHltkkvcgvniiDWREMRVRAAMMLLRV-----GLK----VDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 346645039 510 ILDEATSSIdTQTEILLQEGLERLL--EGRTSFIIAHRLSTIK 550
Cdd:PRK09700 168 IMDEPTSSL-TNKEVDYLFLIMNQLrkEGTAIVYISHKLAEIR 209
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
351-572 9.72e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 71.71  E-value: 9.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI-LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:PRK13648   8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQD-TFIFSGTIIE-NIRYGkldaTEEEIIAAAKVVRahDFISGLKD-GYYTEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:PRK13648  88 VFQNpDNQFVGSIVKyDVAFG----LENHAVPYDEMHR--RVSEALKQvDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIA--HRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
363-562 1.08e-13

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: 73.71  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGENVEEVTLRSL-RSQMGVMLQD-TFIFS 438
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQElTLVPE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  439 GTIIENIRYGKLDATEEEIIA-AAKVVRAHDFISGLKDGYYTEVKERGStLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:TIGR02633  93 LSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSS 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 346645039  518 I-DTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGR 562
Cdd:TIGR02633 172 LtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
359-578 1.25e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 73.74  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTF 435
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 -------IFSGTIIENIR-YGKLDATEeeiiAAAKVVRAHDFISGLKDGYYTEVKErgstLSAGQRQLISFARALLADPK 507
Cdd:PRK10261 412 asldprqTVGDSIMEPLRvHGLLPGKA----AAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPK 483
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 508 ILILDEATSSIDTQTE---ILLQEGLERLLeGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELM--AQHGY 578
Cdd:PRK10261 484 VIIADEAVSALDVSIRgqiINLLLDLQRDF-GIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFenPQHPY 559
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
369-535 1.46e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 69.83  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 369 GINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENveevtLRSLRSQmgvmLQDTFIFSG--------- 439
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP-----IRRQRDE----YHQDLLYLGhqpgiktel 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIR-YGKL--DATEEEIIAA-AKVvrahdfisGLKDgyYTEVKERgsTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK13538  90 TALENLRfYQRLhgPGDDEALWEAlAQV--------GLAG--FEDVPVR--QLSAGQQRRVALARLWLTRAPLWILDEPF 157
                        170       180
                 ....*....|....*....|...
gi 346645039 516 SSIDTQteillqeG---LERLLE 535
Cdd:PRK13538 158 TAIDKQ-------GvarLEALLA 173
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
329-575 1.73e-13

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: 72.91  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  329 MDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGV-DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGE 407
Cdd:TIGR03269 261 MEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  408 ILVD-GENVEEVTLRSLRSQ------MGVMLQDTFIFS-GTIIENIRygklDATEEEIIAAAKVVRAhdfISGLKDGYYT 479
Cdd:TIGR03269 341 VNVRvGDEWVDMTKPGPDGRgrakryIGILHQEYDLYPhRTVLDNLT----EAIGLELPDELARMKA---VITLKMVGFD 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  480 EVKERG------STLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN 551
Cdd:TIGR03269 414 EEKAEEildkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLD 493
                         250       260
                  ....*....|....*....|....*
gi 346645039  552 -SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:TIGR03269 494 vCDRAALMRDGKIVKIGDPEEIVEE 518
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
336-579 2.06e-13

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 71.27  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 336 KDIPNAKKMPPIVGNVdfKDVYFR-YEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEN 414
Cdd:COG4586    9 KTYRVYEKEPGLKGAL--KGLFRReYRE-VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 415 -VEEvtLRSLRSQMGVM------------LQDTFIFSGTI--IENIRYgklDATEEEIIAaakvvrahdfISGLKDGYYT 479
Cdd:COG4586   86 pFKR--RKEFARRIGVVfgqrsqlwwdlpAIDSFRLLKAIyrIPDAEY---KKRLDELVE----------LLDLGELLDT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 EVKErgstLSAGQRQLISFARALLADPKILILDEATSSIDtqteILLQEGLERLL------EGRTSFIIAHRLSTIKN-S 552
Cdd:COG4586  151 PVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTIGLD----VVSKEAIREFLkeynreRGTTILLTSHDMDDIEAlC 222
                        250       260
                 ....*....|....*....|....*..
gi 346645039 553 SRIFYIDNGRIQEAGSHEELMAQHGYY 579
Cdd:COG4586  223 DRVIVIDHGRIIYDGSLEELKERFGPY 249
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
40-318 2.36e-13

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 70.80  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  40 FVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLC--MRYRIRSITLIGQDIlkDMRTAIFGHLQ 117
Cdd:cd18784    3 FFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAagIRGGLFTLAMARLNI--RIRNLLFRSIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 118 KLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQ 197
Cdd:cd18784   81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 198 RKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMK-AVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd18784  161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKeALAYGGYVWSNELTELALTVSTLYY 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 346645039 277 VG---IKGYgvdVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITA 318
Cdd:cd18784  241 GGhlvITGQ---ISGGNLISFILYQLELGSCLESVGSVYTGLMQA 282
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
353-574 2.42e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 70.82  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGV----DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVdGENV-----EEVTLRSL 423
Cdd:PRK13634   5 FQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLKPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQ--DTFIFSGTIIENIRYGKLD--ATEEEIIAAAKVVRAhdfISGLKDgyytEVKERGS-TLSAGQRQLISF 498
Cdd:PRK13634  84 RKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPE----ELLARSPfELSGGQMRRVAI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 499 ARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
367-572 2.64e-13

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 70.43  E-value: 2.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY---NINSGEILVDGENVEEV-----TLRSLRSQMGVMLQD-TFIF 437
Cdd:PRK09984  20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlarDIRKSRANTGYIFQQfNLVN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGTIIENIRYGKLDAT---------------EEEIIAAAKVVRAHdfisglkdgyytEVKERGSTLSAGQRQLISFARAL 502
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwrtcfswftreqkQRALQALTRVGMVH------------FAHQRVSTLSGGQQQRVAIARAL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 503 LADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
33-294 2.68e-13

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350056 [Multi-domain]  Cd Length: 294  Bit Score: 70.62  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  33 KSIYITLFVI-LLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRYRIRSITLIGQDILkDMRTA 111
Cdd:cd18783    1 KRLFRDVAIAsLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGI-LGYLRRYLLLVATTRI-DARLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 --IFGHLQKLPFSYFDSRPHGKIlIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVI 189
Cdd:cd18783   79 lrTFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 190 VMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQflLWPgvQNIA-- 267
Cdd:cd18783  158 ILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLS--NWP--QTLTgp 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 346645039 268 ---VMTTCLIyFVGIkgYGV---DVSTGTLIAF 294
Cdd:cd18783  234 lekLMTVGVI-WVGA--YLVfagSLTVGALIAF 263
cbiO PRK13646
energy-coupling factor transporter ATPase;
351-591 3.11e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 70.58  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGV----DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT----LRS 422
Cdd:PRK13646   3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYG----KLDATEEEiiaaakvVRAHDFISGLkdGYYTEVKERGS-TLSAGQRQL 495
Cdd:PRK13646  83 VRKRIGMVFQfpESQLFEDTVEREIIFGpknfKMNLDEVK-------NYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 496 ISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL--EGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
                        250
                 ....*....|....*....
gi 346645039 573 MAQHGYYYNLYQSQFDMLQ 591
Cdd:PRK13646 234 FKDKKKLADWHIGLPEIVQ 252
ABC_6TM_NHLM_bacteriocin cd18569
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...
35-325 3.19e-13

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350013 [Multi-domain]  Cd Length: 294  Bit Score: 70.58  E-value: 3.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLAnVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcmryrirsITLIGQDILKDMRTAI-- 112
Cdd:cd18569    5 LFVVLAGLLLV-IPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGL--------LTWLQQYYLLRLETKLal 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 ------FGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVL 186
Cdd:cd18569   76 ssssrfFWHVLRLPVEFFSQRYAGDIASRV-QSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 187 FVIVMVIKTAQRKAYQVLSNKQSNMNAYiheSIAGIKVTQSF---SREEENFE----IFTEVSNEYRRSwmkAVKIQFL- 258
Cdd:cd18569  155 LLVLRLVSRKRVDLNRRLLQDSGKLTGT---TMSGLQMIETLkasGAESDFFSrwagYQAKVLNAQQEL---GRTNQLLg 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 259 LWPGVqnIAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18569  229 ALPTL--LSALTNAAILGLGgllvMDG---ALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
366-586 3.25e-13

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 72.43  E-value: 3.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKT----TIINLL-SRFYNINSGEILVDGENV---EEVTLRSLR-SQMGVMLQDTFI 436
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQEPMV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 fSGTIIENI-----------RYGKLDATEEEIIAAAKVVRAHDFISGLKDgyYTEvkergsTLSAGQRQLISFARALLAD 505
Cdd:PRK15134 104 -SLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLTD--YPH------QLSGGERQRVMIAMALLTR 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSIDT--QTEI--LLQEgLERLLEGRTSFiIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA--QHGY 578
Cdd:PRK15134 175 PELLIADEPTTALDVsvQAQIlqLLRE-LQQELNMGLLF-ITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSapTHPY 252

                 ....*...
gi 346645039 579 YYNLYQSQ 586
Cdd:PRK15134 253 TQKLLNSE 260
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
366-573 3.44e-13

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 70.02  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD-TFIFSGTIIEN 444
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTTPGDITVQEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYGKLDAT-------EEEIIAAAKVVRAhdfiSGLKDGYYTEVkergSTLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK10253 102 VARGRYPHQplftrwrKEDEEAVTKAMQA----TGITHLADQSV----DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 518 IDTQTEILLQEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK10253 174 LDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
366-560 4.53e-13

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 68.04  E-value: 4.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN--SGEILVDGENVEEvtlrSLRSQMG-VMLQDTFIFSGTII 442
Cdd:cd03232   22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----NFQRSTGyVEQQDVHSPNLTVR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYgkldateeeiiaAAKVvrahdfisglkdgyytevkeRGstLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:cd03232   98 EALRF------------SALL--------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 346645039 523 EILLQEGLERL-LEGRTSfiiahrLSTIKN-SSRIF-YIDN 560
Cdd:cd03232  144 AYNIVRFLKKLaDSGQAI------LCTIHQpSASIFeKFDR 178
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
363-549 4.79e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 71.57  E-value: 4.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLR-SQ---MGVMLQD-TFIF 437
Cdd:PRK10762  16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKsSQeagIGIIHQElNLIP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGTIIENI--------RYGKLDAteEEIIAAAKVVRAHdfiSGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKIL 509
Cdd:PRK10762  93 QLTIAENIflgrefvnRFGRIDW--KKMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVI 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 346645039 510 ILDEATSSI-DTQTEILLQEGLERLLEGRTSFIIAHRLSTI 549
Cdd:PRK10762 164 IMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
355-574 8.63e-13

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 68.88  E-value: 8.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE--NVEEVTLRSLRSQMGVMLQ 432
Cdd:PRK13638   6 DLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 D--TFIFSGTIIENIRYG--KLDATEEEII----AAAKVVRAHDFisglkdgyyteVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK13638  85 DpeQQIFYTDIDSDIAFSlrNLGVPEAEITrrvdEALTLVDAQHF-----------RHQPIQCLSHGQKKRVAIAGALVL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
350-519 1.04e-12

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 69.87  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 350 NVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR-------- 421
Cdd:PRK11650   3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdiamvf 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 ---SLRSQMgvmlqdtfifsgTIIENIRYG----KLDATE--EEIIAAAKVvrahdfisgLKDGYYTEVKERgsTLSAGQ 492
Cdd:PRK11650  83 qnyALYPHM------------SVRENMAYGlkirGMPKAEieERVAEAARI---------LELEPLLDRKPR--ELSGGQ 139
                        170       180
                 ....*....|....*....|....*..
gi 346645039 493 RQLISFARALLADPKILILDEATSSID 519
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLD 166
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
351-562 1.79e-12

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: 65.16  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSrfyninsgeilvdgenveevtlrslrsqmgvm 430
Cdd:cd03221    1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------------------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 lqdtfifsgtiieniryGKLDATEEEIIaaakvvrahdFISGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILI 510
Cdd:cd03221   48 -----------------GELEPDEGIVT----------WGSTVKIGYFEQ-------LSGGEKMRLALAKLLLENPNLLL 93
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 346645039 511 LDEATSSIDTQTEILLQEGLERLleGRTSFIIAHRLSTIKN-SSRIFYIDNGR 562
Cdd:cd03221   94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
361-522 1.99e-12

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 67.11  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV---EEVTLRSLRSQ-MGVMLQdTFI 436
Cdd:PRK10584  20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKhVGFVFQ-SFM 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 FSGTI--IENIRYGKLDATEEEiiaAAKVVRAHDFISGLkdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEA 514
Cdd:PRK10584  99 LIPTLnaLENVELPALLRGESS---RQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173

                 ....*...
gi 346645039 515 TSSIDTQT 522
Cdd:PRK10584 174 TGNLDRQT 181
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
327-568 2.64e-12

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: 70.04  E-value: 2.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   327 ETMDVE-PD-IKDIPNAKKMPPIVGNVDFKDVYFRYEE-GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNI 403
Cdd:TIGR01257  903 EMEDPEhPEgINDSFFERELPGLVPGVCVKNLVKIFEPsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP 982
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   404 NSGEILVDGENVEeVTLRSLRSQMGVMLQDTFIFSG-TIIENIR-YGKLDATEEEiiaAAKVvrahDFISGLKD-GYYTE 480
Cdd:TIGR01257  983 TSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHlTVAEHILfYAQLKGRSWE---EAQL----EMEAMLEDtGLHHK 1054
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   481 VKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYID 559
Cdd:TIGR01257 1055 RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIIS 1134

                   ....*....
gi 346645039   560 NGRIQEAGS 568
Cdd:TIGR01257 1135 QGRLYCSGT 1143
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
354-583 6.01e-12

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 68.38  E-value: 6.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGV--DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveEVTLRSLRSQMGVML 431
Cdd:PRK13545  25 KDLFFRSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----SAALIAISSGLNGQL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 qdtfifsgTIIENIRYGKL--DATEEEIIA-AAKVVRAHD---FIsglkdgyYTEVKergsTLSAGQRQLISFARALLAD 505
Cdd:PRK13545 101 --------TGIENIELKGLmmGLTKEKIKEiIPEIIEFADigkFI-------YQPVK----TYSSGMKSRLGFAISVHIN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSID-TQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQHGYYYNLY 583
Cdd:PRK13545 162 PDILVIDEALSVGDqTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
352-578 6.10e-12

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 67.06  E-value: 6.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 352 DFKD--VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKT----TIINLLSRFYNI------NSGEILvdgeNVEEV 418
Cdd:PRK09473  14 DVKDlrVTFSTPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIggsatfNGREIL----NLPEK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 419 TLRSLRS-QMGVMLQDTFI-------FSGTIIENI----RYGKLDATEEEI--IAAAKVVRA--------HDFisglkdg 476
Cdd:PRK09473  90 ELNKLRAeQISMIFQDPMTslnpymrVGEQLMEVLmlhkGMSKAEAFEESVrmLDAVKMPEArkrmkmypHEF------- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 477 yytevkergstlSAGQRQLISFARALLADPKILILDEATSSIDT--QTEI--LLQEgLERllEGRTSFI-IAHRLSTIKN 551
Cdd:PRK09473 163 ------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvQAQImtLLNE-LKR--EFNTAIImITHDLGVVAG 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 346645039 552 S-SRIFYIDNGRIQEAGSHEELMAQ--HGY 578
Cdd:PRK09473 228 IcDKVLVMYAGRTMEYGNARDVFYQpsHPY 257
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
351-513 7.59e-12

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 65.94  E-value: 7.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL---RSQM 427
Cdd:PRK11831   8 VDMRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSG-TIIENIRYGKLDATE--EEIIAAAKVVRAHDFisGLKDGyyteVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK11831  87 SMLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLHSTVMMKLEAV--GLRGA----AKLMPSELSGGMARRAALARAIAL 160

                 ....*....
gi 346645039 505 DPKILILDE 513
Cdd:PRK11831 161 EPDLIMFDE 169
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
367-591 1.11e-11

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 65.25  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTiinLLSRFYNI--NSGEILVDGENVEEVTLRSLrSQMGVML--QDTFIFSGTII 442
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMAGLlpGQGEILLNGRPLSDWSAAEL-ARHRAYLsqQQSPPFAMPVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYGKLDATEEEIIAAAKVVRAHDFisGLKDGYYTEVkergSTLSAGQRQLISFARALL-------ADPKILILDEAT 515
Cdd:COG4138   88 QYLALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPL----TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 516 SSID-TQteillQEGLERLLE-----GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQHgyyyNL---YQS 585
Cdd:COG4138  162 NSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPE----NLsevFGV 232

                 ....*.
gi 346645039 586 QFDMLQ 591
Cdd:COG4138  233 KFRRLE 238
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
359-544 1.21e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 63.79  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnvEEVTLRSLRSQmgvmLQDTFifS 438
Cdd:NF040873   1 GYG-GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSE----VPDSL--P 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENIRYG---------KLDATEEEIIAAA-KVVRAHDFisglkdgyyteVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:NF040873  72 LTVRDLVAMGrwarrglwrRLTRDDRAAVDDAlERVGLADL-----------AGRQLGELSGGQRQRALLAQGLAQEADL 140
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAH 544
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTH 177
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
366-545 1.73e-11

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 64.21  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveevtlrslrsqmgvMLQDTFIFSGTIIENI 445
Cdd:COG2401   45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDAI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 ryGKLDATEE--EIIAAAkvvrahdfisGLKDGYYteVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:COG2401  107 --GRKGDFKDavELLNAV----------GLSDAVL--WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
                        170       180
                 ....*....|....*....|....
gi 346645039 524 ILLQEGLERLL-EGRTSFIIA-HR 545
Cdd:COG2401  173 KRVARNLQKLArRAGITLVVAtHH 196
PLN03073 PLN03073
ABC transporter F family; Provisional
322-530 2.05e-11

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 66.81  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 322 LERIFETMDV--EPDIK---DIPNAKKMPPIVgnvDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINL 396
Cdd:PLN03073 478 LDRLGHVDAVvnDPDYKfefPTPDDRPGPPII---SFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 397 LsrfyninSGEIlvdgENVEEVTLRSLRSQMGVMLQ---DTFIFSGTIIENIRYGKLDATEEEIiaaakvvRAH--DF-I 470
Cdd:PLN03073 555 I-------SGEL----QPSSGTVFRSAKVRMAVFSQhhvDGLDLSSNPLLYMMRCFPGVPEQKL-------RAHlgSFgV 616
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 471 SG---LKDGYytevkergsTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGL 530
Cdd:PLN03073 617 TGnlaLQPMY---------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
ycf16 CHL00131
sulfate ABC transporter protein; Validated
365-578 2.52e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 64.28  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 365 DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNINSGEILVDGENVEEVTlRSLRSQMGVML--QDTFIFSGT 440
Cdd:CHL00131  21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLafQYPIEIPGV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 -------IIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGstLSAGQRQLISFARALLADPKILILDE 513
Cdd:CHL00131 100 snadflrLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELAILDE 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 514 ATSSIDTQTEILLQEGLERLLEGRTSFI-IAH--RLSTIKNSSRIFYIDNGRIQEAGSHE--ELMAQHGY 578
Cdd:CHL00131 178 TDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKGY 247
ABC_6TM_AarD_CydD cd18584
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...
64-258 2.84e-11

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350028 [Multi-domain]  Cd Length: 290  Bit Score: 64.74  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  64 IPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINML 143
Cdd:cd18584   28 LEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDAL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 144 SDLLSNGLINLIsdiLSVIVT---LGFMLMIDPV---LTLYSLALIPVLFVIV-MVIKTAQRKAYQVLSNkqsnMNAYIH 216
Cdd:cd18584  108 DGYFARYLPQLV---LAAIVPlliLVAVFPLDWVsalILLVTAPLIPLFMILIgKAAQAASRRQWAALSR----LSGHFL 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 346645039 217 ESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFL 258
Cdd:cd18584  181 DRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFL 222
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
110-325 3.38e-11

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 64.41  E-value: 3.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 110 TAIFGHLQKLPFS--------YFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLA 181
Cdd:cd18589   65 SRIHSRLQGLVFAavlrqeiaFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTAL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 182 LIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTE-VSNEYRRSWMKAVKIQFLLW 260
Cdd:cd18589  145 GLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQrLQKTYRLNKKEAAAYAVSMW 224
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 261 PGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18589  225 TSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
355-549 3.87e-11

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 64.13  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDT 434
Cdd:PRK15056  11 DVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 FIFSgTIIENI----RYGKL------DATEEEIIAAAkVVRAhdfisGLKDGYYTEVKErgstLSAGQRQLISFARALLA 504
Cdd:PRK15056  91 WSFP-VLVEDVvmmgRYGHMgwlrraKKRDRQIVTAA-LARV-----DMVEFRHRQIGE----LSGGQKKRVFLARAIAQ 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTI 549
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
39-253 4.51e-11

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 64.03  E-value: 4.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRyrirSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18577   17 LMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTA----CWTITGERQARRIRKRYLKALLR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18577   93 QDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLS 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSF---SREEENFEIFTEVSNEY--RRSWMKAV 253
Cdd:cd18577  173 KYTKKEQEAYAKAGSIAEEALSSIRTVKAFggeEKEIKRYSKALEKARKAgiKKGLVSGL 232
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
367-519 5.21e-11

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 65.04  E-value: 5.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveEVTLRSLRSQM--GVML------QDTFIFS 438
Cdd:COG1129  268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRDAIraGIAYvpedrkGEGLVLD 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENI---------RYGKLDATEEEIIAAakvvrahDFISGLK---DGYYTEVkergSTLSAGQRQLISFARALLADP 506
Cdd:COG1129  345 LSIRENItlasldrlsRGGLLDRRRERALAE-------EYIKRLRiktPSPEQPV----GNLSGGNQQKVVLAKWLATDP 413
                        170
                 ....*....|...
gi 346645039 507 KILILDEATSSID 519
Cdd:COG1129  414 KVLILDEPTRGID 426
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
351-545 1.02e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 61.50  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVM 430
Cdd:PRK13540   2 LDVIELDFDYHDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRY------GKLDATeeEIIAAAKVVRAHDFISGLkdgyytevkergstLSAGQRQLISFARALL 503
Cdd:PRK13540  80 GHRSGINPYlTLRENCLYdihfspGAVGIT--ELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWM 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 346645039 504 ADPKILILDEATSSIDtqteillqeglERLLEGRTSFIIAHR 545
Cdd:PRK13540 144 SKAKLWLLDEPLVALD-----------ELSLLTIITKIQEHR 174
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
351-575 1.20e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 62.41  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD-----ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDG-ENVEEVTLRSLR 424
Cdd:PRK13633   5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQ--DTFIFSGTIIENIRYG--KLDATEEEIiaaakvvRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFAR 500
Cdd:PRK13633  85 NKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEI-------RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
366-519 3.38e-10

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 60.25  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE---NVEEVTLRSLRSQMGVMLQDTfifsgTII 442
Cdd:PRK13543  26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatRGDRSRFMAYLGHLPGLKADL-----STL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYgkldateeeiIAAAKVVRAHDF------ISGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:PRK13543 101 ENLHF----------LCGLHGRRAKQMpgsalaIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYA 166

                 ...
gi 346645039 517 SID 519
Cdd:PRK13543 167 NLD 169
cbiO PRK13645
energy-coupling factor transporter ATPase;
382-574 3.68e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 61.18  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 382 LVGPTGAGKTTIINLLSRFYNINSGEILVDG-------ENVEEVtlRSLRSQMGVMLQ--DTFIFSGTIIENIRYGKLDA 452
Cdd:PRK13645  42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEV--KRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 453 TEEEIIAAAKVVRAHDFISgLKDGYyteVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLER 532
Cdd:PRK13645 120 GENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFER 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 346645039 533 L--LEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13645 196 LnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
PLN03211 PLN03211
ABC transporter G-25; Provisional
366-556 4.01e-10

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 62.59  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGENVEEVTLRslrsQMGVMLQDTFIFSG-TII 442
Cdd:PLN03211  83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK----RTGFVTQDDILYPHlTVR 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYGKLDATEEEIIAAAKVVRAHDFIS--GLKDGYYTEVKE---RGstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISelGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 346645039 518 IDTQTEILLQEGLERLLE-GRTSFIIAHrlstiKNSSRIF 556
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQkGKTIVTSMH-----QPSSRVY 271
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
321-559 4.66e-10

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: 62.46  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  321 YLERIFETMDV-------------EPDIKDIPNAKKMPPIV---GNVDFKDVYFRYE-------EGVDILKGINFHVDAG 377
Cdd:TIGR00954 399 FTARVDTLLQVlddvksgnfkrprVEEIESGREGGRNSNLVpgrGIVEYQDNGIKFEniplvtpNGDVLIESLSFEVPSG 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  378 ESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV-------EEVTLRSLRSQMgvmlqdtfIFSGTIIENIRYGKL 450
Cdd:TIGR00954 479 NNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKlfyvpqrPYMTLGTLRDQI--------IYPDSSEDMKRRGLS 550
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  451 DATEEEIIaaaKVVRAHDFISglKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGL 530
Cdd:TIGR00954 551 DKDLEQIL---DNVQLTHILE--REGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
                         250       260
                  ....*....|....*....|....*....
gi 346645039  531 ERLleGRTSFIIAHRLSTIKNSSRIFYID 559
Cdd:TIGR00954 626 REF--GITLFSVSHRKSLWKYHEYLLYMD 652
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
365-519 5.00e-10

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: 58.98  E-value: 5.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 365 DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSL--------------RSQMGVM 430
Cdd:cd03215   14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPrdairagiayvpedRKREGLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQdtfifsGTIIENIrygkldateeeiiaaakVVRAHdfisglkdgyytevkergstLSAGQRQLISFARALLADPKILI 510
Cdd:cd03215   91 LD------LSVAENI-----------------ALSSL--------------------LSGGNQQKVVLARWLARDPRVLI 127

                 ....*....
gi 346645039 511 LDEATSSID 519
Cdd:cd03215  128 LDEPTRGVD 136
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
37-312 5.80e-10

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350005 [Multi-domain]  Cd Length: 289  Bit Score: 60.76  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIgpyLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18561    3 LLGLLITALYIAQAW---LLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18561   80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd18561  160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 346645039 277 VGIKGY---GVDVSTGTLIAFIGyvGNFWNPVINIGNFY 312
Cdd:cd18561  240 VGALRVlggQLTLSSLLLILFLS--REFFRPLRDLGAYW 276
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
366-522 9.89e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 61.66  E-value: 9.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYN---INSGEILVDGENVEEVTLRSLrsqmG-VMLQDTFIFSGTI 441
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSFQRSI----GyVQQQDLHLPTSTV 853
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   442 IENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTE--VKERGSTLSAGQRQLISFARALLADPKILI-LDEATSSI 518
Cdd:TIGR00956  854 RESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADavVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933

                   ....
gi 346645039   519 DTQT 522
Cdd:TIGR00956  934 DSQT 937
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
35-250 1.16e-09

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 59.83  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18580    1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPvltlYSLALIPVLFVIVMVIk 194
Cdd:cd18580   81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLL- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 195 taqRKAYQVLSNK--------QSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWM 250
Cdd:cd18580  156 ---QRYYLRTSRQlrrlesesRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFY 216
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
377-564 1.44e-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: 57.00  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   377 GESIALVGPTGAGKTTIINLLSRFYNINSGE-ILVDGENVEEVTLRSLRsqmgvmlqdtfifsgtiienirygkldatee 455
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039   456 eiiaaakvvrahdfisglkdgyYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLE---- 531
Cdd:smart00382  51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 346645039   532 --RLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQ 564
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
38-312 1.66e-09

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350026 [Multi-domain]  Cd Length: 292  Bit Score: 59.05  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  38 TLFVILLANVATMIGPYLTKIVID--DTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGH 115
Cdd:cd18582    1 ALLLLVLAKLLNVAVPFLLKYAVDalSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKiLIRVVNY-INMLSDLLSNGLINLISDILSVIVTLGFML-MIDPVLTLYSLALIpVLFVIVMVI 193
Cdd:cd18582   81 LHSLSLRFHLSRKTGA-LSRAIERgTRGIEFLLRFLLFNILPTILELLLVCGILWyLYGWSYALITLVTV-ALYVAFTIK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 194 KTAQRKAYQVLSNKQSNM-NAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLwpgvqNI---AVM 269
Cdd:cd18582  159 VTEWRTKFRREMNEADNEaNAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALL-----NIgqaLII 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 346645039 270 TTCLIYFVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFY 312
Cdd:cd18582  234 SLGLTAIMLLAAQGVvagTLTVGDFVLVNTYLLQLYQPLNFLGFVY 279
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
367-581 4.43e-09

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 57.52  E-value: 4.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveEVTLRSLRSQMGVMLqdtfifsgTIIENIR 446
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAISAGLSGQL--------TGIENIE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 447 YGKL--DATEEEIIA-AAKVVRahdfISGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEATSSIDtQTe 523
Cdd:PRK13546 108 FKMLcmGFKRKEIKAmTPKIIE----FSELGEFIYQPVKK----YSSGMRAKLGFSINITVNPDILVIDEALSVGD-QT- 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 524 iLLQEGLERLLE----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQHGYYYN 581
Cdd:PRK13546 178 -FAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLN 239
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
370-573 4.46e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 57.25  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTiinLLSRFYNI--NSGEILVDGENVEEVTLRSL--------RSQMGVMLQDTFifsg 439
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELarhraylsQQQTPPFAMPVF---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 tiieniRYGKL---DATEEEIIAAAKVVRAHDFisGLKDGYYTEVkergSTLSAGQRQLISFARALL-----ADP--KIL 509
Cdd:PRK03695  88 ------QYLTLhqpDKTRTEAVASALNEVAEAL--GLDDKLGRSV----NQLSGGEWQRVRLAAVVLqvwpdINPagQLL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
GguA NF040905
sugar ABC transporter ATP-binding protein;
366-519 5.24e-09

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 58.65  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTI-INLLSRFYNIN-SGEILVDGEnveEVTLRSL--------------RSQMGV 429
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGK---EVDVSTVsdaidaglayvtedRKGYGL 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTfifsgtIIENI---------RYGKLDATEEEIIA----AAKVVRAHDfisglkdgyyteVKERGSTLSAGQRQLI 496
Cdd:NF040905 352 NLIDD------IKRNItlanlgkvsRRGVIDENEEIKVAeeyrKKMNIKTPS------------VFQKVGNLSGGNQQKV 413
                        170       180
                 ....*....|....*....|...
gi 346645039 497 SFARALLADPKILILDEATSSID 519
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGID 436
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
381-519 1.78e-08

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 56.42  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 381 ALVGPTGAGKTTIINLLSRFYNINSGEI------LVDGENveEVTLRSLRSQMGVMLQDTFIFSG-TIIENIRYGkldat 453
Cdd:PRK11144  28 AIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEK--GICLPPEKRRIGYVFQDARLFPHyKVRGNLRYG----- 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 454 eeeiiaAAKVVRAH-DFISGLKdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK11144 101 ------MAKSMVAQfDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
361-576 2.20e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 56.01  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGINFHVDAGESIALVGPTGAGKTTIIN-----LLSRFYNINSGEILVDGENVEEVTLRS-----------LR 424
Cdd:PRK13631  36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQ--DTFIFSGTIIENIRYGKLdATEEEIIAAAKVVRAHDFISGLKDGYYtevkERGS-TLSAGQRQLISFARA 501
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSYL----ERSPfGLSGGQKRRVAIAGI 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 502 LLADPKILILDEATSSIDTQTE-ILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGS-HEELMAQH 576
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTpYEIFTDQH 268
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
363-524 2.25e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 56.66  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE-EVTLRSLRSQMGVMLQD-TFIFSGT 440
Cdd:PRK10982  10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKLdATEEEIIAAAKVVRahDFISGLKD-GYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSId 519
Cdd:PRK10982  90 VMDNMWLGRY-PTKGMFVDQDKMYR--DTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165

                 ....*
gi 346645039 520 TQTEI 524
Cdd:PRK10982 166 TEKEV 170
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
355-578 2.46e-08

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 56.79  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY-----NINSGEILVDGENVEEVTL-------- 420
Cdd:PRK10261  19 NIAFMQEQQkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLeqaggLVQCDKMLLRRRSRQVIELseqsaaqm 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 421 RSLR-SQMGVMLQD-------TFIFSGTIIENIRYGKLDATEEEIIAAAKV---VRAHDFISGLkdGYYTEvkergsTLS 489
Cdd:PRK10261  99 RHVRgADMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMldqVRIPEAQTIL--SRYPH------QLS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDT--QTEILlqeGLERLLEGRTSF---IIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVtiQAQIL---QLIKVLQKEMSMgviFITHDMGVVAEiADRVLVMYQGEA 247
                        250
                 ....*....|....*..
gi 346645039 564 QEAGSHEELM--AQHGY 578
Cdd:PRK10261 248 VETGSVEQIFhaPQHPY 264
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
39-297 5.89e-08

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 54.56  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVID---------DTIPNKNMTQ-LFWIAVIFIVSVIVTGLcmryRIRSITLIGQDILKDM 108
Cdd:cd18780    2 TIALLVSSGTNLALPYFFGQVIDavtnhsgsgGEEALRALNQaVLILLGVVLIGSIATFL----RSWLFTLAGERVVARL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 109 RTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFV 188
Cdd:cd18780   78 RKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 189 IVMV----IKTAQRKAYQVLSNKQSnmnaYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQ 264
Cdd:cd18780  158 GAVIygkyVRKLSKKFQDALAAAST----VAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMG 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 346645039 265 NIAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGY 297
Cdd:cd18780  234 AAAQLAIVLVLWYGgrlvIDG---ELTTGLLTSFLLY 267
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
72-280 6.58e-08

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 54.38  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  72 LFWIAVIFIVSVI--VTGLCMRYrirSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPH--GKILIRVVNYINMLSDLL 147
Cdd:cd18578   52 NFWALMFLVLAIVagIAYFLQGY---LFGIAGERLTRRLRKLAFRAILRQDIAWFDDPENstGALTSRLSTDASDVRGLV 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 148 SNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQS 227
Cdd:cd18578  129 GDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVAS 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 228 FSREEENFEIFTE-VSNEYRRSWMKAVKIQFLLwpGV-QNIAVMTTCLIYFVGIK 280
Cdd:cd18578  209 LTLEDYFLEKYEEaLEEPLKKGLRRALISGLGF--GLsQSLTFFAYALAFWYGGR 261
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
354-573 7.25e-08

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 54.02  E-value: 7.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:PRK10575  15 RNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSGTIIENI----RY------GKLDATEEEiiaaaKVVRAHDFIsGLKDGYYTEVkergSTLSAGQRQLISFARALL 503
Cdd:PRK10575  94 LPAAEGMTVRELvaigRYpwhgalGRFGAADRE-----KVEEAISLV-GLKPLAHRLV----DSLSGGERQRAWIAMLVA 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 504 ADPKILILDEATSSIDT--QTEILLQegLERLLEGRTSFIIAhRLSTIKNSSRifYID------NGRIQEAGSHEELM 573
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIahQVDVLAL--VHRLSQERGLTVIA-VLHDINMAAR--YCDylvalrGGEMIAQGTPAELM 236
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
352-565 8.42e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 55.34  E-value: 8.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 352 DFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVdGENVEEVTLRSLRSQMgvml 431
Cdd:PRK11147 321 EMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAEL---- 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 qDTfifSGTIIENIRYGKLDATeeeiiaaakvV--RAHDFISGLKDGYY------TEVKergsTLSAGQRQLISFARALL 503
Cdd:PRK11147 395 -DP---EKTVMDNLAEGKQEVM----------VngRPRHVLGYLQDFLFhpkramTPVK----ALSGGERNRLLLARLFL 456
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSIDTQTeillQEGLERLLEGR--TSFIIAHRLSTIKN---SSRIFYiDNGRIQE 565
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVET----LELLEELLDSYqgTVLLVSHDRQFVDNtvtECWIFE-GNGKIGR 518
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
94-248 4.99e-07

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 51.78  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  94 IRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYIN----MLSDLLSNGLINLISDILSVIVtlgfML 169
Cdd:cd18574   63 ISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQefksSFKQCVSQGLRSVTQTVGCVVS----LY 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 170 MIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRS 248
Cdd:cd18574  139 LISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL 217
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
351-578 6.00e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 52.20  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVdGENveevtlrslrSQMGVM 430
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-SEN----------ANIGYY 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDT---FIFSGTIIENIRYGKLDATEEEIIAAA--KVVRAHDfisglkdgyytEVKERGSTLSAGQRQLISFARALLAD 505
Cdd:PRK15064 388 AQDHaydFENDLTLFDWMSQWRQEGDDEQAVRGTlgRLLFSQD-----------DIKKSVKVLSGGEKGRMLFGKLMMQK 456
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLErLLEGrTSFIIAH------RLSTiknssRIFYI-DNGRIQEAGSHEELMAQHGY 578
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSHdrefvsSLAT-----RIIEItPDGVVDFSGTYEEYLRSQGI 529
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
40-301 6.20e-07

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 51.19  E-value: 6.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  40 FVIL-LANVATMIGPYLTKIVID----DTIPNKNMTQLFWIAVIFIVSVIVTGLcmryRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18590    2 FLFLtLAVICETFIPYYTGRVIDilggEYQHNAFTSAIGLMCLFSLGSSLSAGL----RGGLFMCTLSRLNLRLRHQLFS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18590   78 SLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEY-----RRSWMKAVKIQF--LLWPGVQniA 267
Cdd:cd18590  158 TYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTynlkdRRDTVRAVYLLVrrVLQLGVQ--V 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 346645039 268 VMTTCLIYFVGiKGygvDVSTGTLIAFIGYVGNF 301
Cdd:cd18590  236 LMLYCGRQLIQ-SG---HLTTGSLVSFILYQKNL 265
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
372-563 6.40e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 52.26  E-value: 6.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 372 FHVDAGESIALVGPTGAGKTTIINLLSrfyninsGEILVD-GENVEEVTLRSLRSQmgvmlQD----------TFIFSGt 440
Cdd:PRK11147  24 LHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdGRIIYEQDLIVARLQ-----QDpprnvegtvyDFVAEG- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 iIENI-----RYGKL------DATEEEIIAAAKVVRAHDFISGLK-DGYYTEVKE--------RGSTLSAGQRQLISFAR 500
Cdd:PRK11147  91 -IEEQaeylkRYHDIshlvetDPSEKNLNELAKLQEQLDHHNLWQlENRINEVLAqlgldpdaALSSLSGGWLRKAALGR 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 501 ALLADPKILILDEATSSIDTQTeILLQEGLerLLEGRTSFI-IAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET-IEWLEGF--LKTFQGSIIfISHDRSFIRNmATRIVDLDRGKL 231
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
351-522 8.90e-07

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 49.95  E-value: 8.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD---ILKGINFHVDAGESIALVGPTGAGKTT----IINLLSRFYNINsGEILVDGENVEEVTLRSL 423
Cdd:cd03233    4 LSWRNISFTTGKGRSkipILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKYP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDTFIFSGTIIENIRYgkldateeeiiaAAKvVRAHDFISGlkdgyytevkergstLSAGQRQLISFARALL 503
Cdd:cd03233   83 GEIIYVSEEDVHFPTLTVRETLDF------------ALR-CKGNEFVRG---------------ISGGERKRVSIAEALV 134
                        170
                 ....*....|....*....
gi 346645039 504 ADPKILILDEATSSIDTQT 522
Cdd:cd03233  135 SRASVLCWDNSTRGLDSST 153
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
370-519 1.16e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 51.47  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFY-NINSGEILVDGEnveEVTLRSLRSQMG---VML-----QDTFIFSGT 440
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGK---PVKIRNPQQAIAqgiAMVpedrkRDGIVPVMG 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKLD--ATEEEIIAAAKVVRAHDFISGLKdgyyteVKE-----RGSTLSAGQRQLISFARALLADPKILILDE 513
Cdd:PRK13549 358 VGKNITLAALDrfTGGSRIDDAAELKTILESIQRLK------VKTaspelAIARLSGGNQQKAVLAKCLLLNPKILILDE 431

                 ....*.
gi 346645039 514 ATSSID 519
Cdd:PRK13549 432 PTRGID 437
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
370-519 1.28e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 51.21  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIE------ 443
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDaplawn 361
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 444 --NIRYGKLDATEEEIIAAAKVVRAHDFIsGLKdgyYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK15439 362 vcALTHNRRGFWIKPARENAVLERYRRAL-NIK---FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
362-569 2.44e-06

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 49.02  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLS--RFYNINSGEILVDGENVEEVTLRSlRSQMGVMLQDTF---- 435
Cdd:PRK09580  12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAFQYpvei 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 ------IFSGTIIENIR-YGKLDATE--------EEIIAAAKvvrahdfisgLKDGYYTEVKERGstLSAGQRQLISFAR 500
Cdd:PRK09580  91 pgvsnqFFLQTALNAVRsYRGQEPLDrfdfqdlmEEKIALLK----------MPEDLLTRSVNVG--FSGGEKKRNDILQ 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYID---NGRIQEAGSH 569
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHvlyQGRIVKSGDF 230
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
328-574 2.67e-06

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 50.17  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 328 TMDVEPDIKDIPNAkkMPPIVGNVDFKDVY-----FRYEEGVdiLKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYN 402
Cdd:PRK09700 239 RLMVGRELQNRFNA--MKENVSNLAHETVFevrnvTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 403 INSGEILVDGENVEEVT-LRSLRSQMGVMLQ---DTFIFSG-TIIENIR-------------YGKLDATEEEIIAAAkvv 464
Cdd:PRK09700 315 RAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRTAEN--- 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 465 rAHDFISgLKdgyYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID--TQTEILlqeGLERLL--EGRTSF 540
Cdd:PRK09700 392 -QRELLA-LK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAEIY---KVMRQLadDGKVIL 463
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 346645039 541 IIAHRLSTIKN-SSRIFYIDNGRI------QEAGSHEELMA 574
Cdd:PRK09700 464 MVSSELPEIITvCDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
hmuV PRK13547
heme ABC transporter ATP-binding protein;
366-519 3.32e-06

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 49.05  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLL---------SRFYNInSGEILVDGE---NVEEVTLRSLRSQMGVMLQD 433
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARV-TGDVTLNGEplaAIDAPRLARLRAVLPQAAQP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFS-------GTIIENIRYGKLDATEEEIIAAAkVVRAhdfisglkdGYYTEVKERGSTLSAGQRQLISFARAL---- 502
Cdd:PRK13547  95 AFAFSareivllGRYPHARRAGALTHRDGEIAWQA-LALA---------GATALVGRDVTTLSGGELARVQFARVLaqlw 164
                        170       180
                 ....*....|....*....|..
gi 346645039 503 -----LADPKILILDEATSSID 519
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALD 186
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
366-533 3.62e-06

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 48.57  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILvdgenveevtlRSLRSQMGVMLQDTFIFSGTIIENI 445
Cdd:PRK09544  19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQKLYLDTTLPLTVN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYGKL--DATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:PRK09544  88 RFLRLrpGTKKEDILPALKRVQAGHLI-----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
                        170
                 ....*....|
gi 346645039 524 ILLQEGLERL 533
Cdd:PRK09544 157 VALYDLIDQL 166
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
370-519 7.06e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 48.75  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRS--QMGVML------QDTFIFSGTI 441
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDaiRAGIMLcpedrkAEGIIPVHSV 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENI---------RYGKL--DATEEEIiaaakvvrAHDFISGLKdgyyteVKERGS-----TLSAGQRQLISFARALLAD 505
Cdd:PRK11288 349 ADNInisarrhhlRAGCLinNRWEAEN--------ADRFIRSLN------IKTPSReqlimNLSGGNQQKAILGRWLSED 414
                        170
                 ....*....|....
gi 346645039 506 PKILILDEATSSID 519
Cdd:PRK11288 415 MKVILLDEPTRGID 428
ABC_6TM_PrtD_like cd18586
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ...
38-293 7.64e-06

Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides


Pssm-ID: 350030 [Multi-domain]  Cd Length: 291  Bit Score: 47.98  E-value: 7.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  38 TLFVILLANVAtmigPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRYrIRSITL--IGQDILKDMRTAIFGH 115
Cdd:cd18586   11 SFFINLLALAP----PIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGL-LRQ-VRSRILqrVGLRLDVELGRRVFRA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFsyfDSRPHGkilirvvNYINMLSDL------LSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVI 189
Cdd:cd18586   85 VLELPL---ESRPSG-------YWQQLLRDLdtlrnfLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 190 VMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREeenfeiftevsNEYRRSWMKAVKiQFLLWP-------- 261
Cdd:cd18586  155 AWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGML-----------GNLRRRWEARHA-ETLELQirasdlag 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 346645039 262 GVQNIA----VMTTCLIYFVG----IKGygvDVSTGTLIA 293
Cdd:cd18586  223 AISAIGktlrMALQSLILGVGaylvIDG---ELTIGALIA 259
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
354-515 7.70e-06

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 48.87  E-value: 7.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRsQMGVM--- 430
Cdd:COG3845  261 ENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR-RLGVAyip 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 ---LQDTFIFSGTIIEN----------------IRYGKLDATEEEIIAAAKvVRAHDfisglkdgyyteVKERGSTLSAG 491
Cdd:COG3845  340 edrLGRGLVPDMSVAENlilgryrrppfsrggfLDRKAIRAFAEELIEEFD-VRTPG------------PDTPARSLSGG 406
                        170       180
                 ....*....|....*....|....*.
gi 346645039 492 --QRQLIsfARALLADPKILILDEAT 515
Cdd:COG3845  407 nqQKVIL--ARELSRDPKLLIAAQPT 430
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
39-324 1.05e-05

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.


Pssm-ID: 350027 [Multi-domain]  Cd Length: 290  Bit Score: 47.52  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLA----NVATmigPYLTKIVIDDTIPNKnmTQLFWIAVIF-----------IVSVIVTGLCMRyrirsitlIGQD 103
Cdd:cd18583    1 CFLCLLAervlNVLV---PRQLGIIVDSLSGGS--GKSPWKEIGLyvllrflqsggGLGLLRSWLWIP--------VEQY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 104 ILKDMRTAIFGHLQKLPFSYFDSRPHGKIlIRVVNYINMLSDLLSNGLINLISDILSVIVTLG-FMLMIDPVLTLYsLAL 182
Cdd:cd18583   68 SYRALSTAAFNHVMNLSMDFHDSKKSGEV-LKAIEQGSSINDLLEQILFQIVPMIIDLVIAIVyLYYLFDPYMGLI-VAV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 183 IPVLFVIVMVIKTA-QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSwMKAVKIQFLLWP 261
Cdd:cd18583  146 VMVLYVWSTIKLTSwRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKA-ERKYLFSLNLLN 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 262 GVQNiAVMTTCLIYFVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLER 324
Cdd:cd18583  225 AVQS-LILTLGLLAGCFLAAYQVsqgQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
ABC_6TM_peptidase_like cd18571
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ...
32-192 1.14e-05

Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350015 [Multi-domain]  Cd Length: 294  Bit Score: 47.44  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  32 QKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMT--------QLFWI----AVIFIVSVIVTGLCMRYrirSITL 99
Cdd:cd18571    1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNfiyliliaQLVLFlgstSIEFIRSWILLHISSRI---NISI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 100 IGQDILKDMRtaifghlqkLPFSYFDSRPHGKILIRVVNYiNMLSDLLSNGLINLISDILSVIVTLGfmlmidpVLTLYS 179
Cdd:cd18571   78 ISDFLIKLMR---------LPISFFDTKMTGDILQRINDH-SRIESFLTSSSLSILFSLLNLIVFSI-------VLAYYN 140
                        170
                 ....*....|...
gi 346645039 180 laliPVLFVIVMV 192
Cdd:cd18571  141 ----LTIFLIFLI 149
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
37-325 1.66e-05

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 47.10  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  37 ITLFVILLANVATMIGPYLTKIVID--DTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18579    1 LAGLLKLLEDLLSLAQPLLLGLLISylSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKIlirvvnyINMLS------DLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFV 188
Cdd:cd18579   81 KALRLSSSARQETSTGEI-------VNLMSvdvqriEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 189 IVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREeenfEIFTEVSNEYRRSWMKAVK-------IQFLLWP 261
Cdd:cd18579  154 LQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWE----KPFLKRIEELRKKELKALRkfgylraLNSFLFF 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 262 GVQNIAVMTTCLIYFVgikgYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18579  230 STPVLVSLATFATYVL----LGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
370-564 2.54e-05

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: 47.13  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  370 INFHVDAGESIALVGPTGAGKTTIINLLSRFY-NINSGEILVDGENVEEVT-LRSLRSQMGVMLQDT----FIFSGTIIE 443
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGK 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  444 NI------RYGKL----DATEEEIIAAA----KVVRAHDFISglkdgyytevkerGSTLSAGQRQLISFARALLADPKIL 509
Cdd:TIGR02633 359 NItlsvlkSFCFKmridAAAELQIIGSAiqrlKVKTASPFLP-------------IGRLSGGNQQKAVLAKMLLTNPRVL 425
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039  510 ILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQ 564
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKLK 482
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
333-551 2.76e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 46.93  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 333 PDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTiinLLSrfyninsgeiLVDG 412
Cdd:PRK10938 243 PEPDEPSARHALPANEPRIVLNNGVVSYNDRP-ILHNLSWQVNPGEHWQIVGPNGAGKST---LLS----------LITG 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 413 ENVE----EVTLRSLRSQMGVMLQDtfifsgtIIENIRY--------GKLDATEEEIIaaakvvrahdfISGLKD--GYY 478
Cdd:PRK10938 309 DHPQgysnDLTLFGRRRGSGETIWD-------IKKHIGYvssslhldYRVSTSVRNVI-----------LSGFFDsiGIY 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 479 TEVKERGS----------------------TLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL-E 535
Cdd:PRK10938 371 QAVSDRQQklaqqwldilgidkrtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsE 450
                        250       260
                 ....*....|....*....|....*...
gi 346645039 536 GRTSFI------------IAHRLSTIKN 551
Cdd:PRK10938 451 GETQLLfvshhaedapacITHRLEFVPD 478
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
374-531 5.07e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 46.32  E-value: 5.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 374 VDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE------NVEEVTL------------RSLRSQMGVMLQDTF 435
Cdd:PRK10636  24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvNQETPALpqpaleyvidgdREYRQLEAQLHDANE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 IFSGTIIENIrYGKLDATEEEIIAAakvvRAHDFISGLkdGYYTEVKERG-STLSAGQRQLISFARALLADPKILILDEA 514
Cdd:PRK10636 104 RNDGHAIATI-HGKLDAIDAWTIRS----RAASLLHGL--GFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
                        170
                 ....*....|....*..
gi 346645039 515 TSSIDTQTEILLQEGLE 531
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLK 193
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
363-574 1.79e-04

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 44.22  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDilkGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveEVTLRSLRSQM--GVML------QDT 434
Cdd:PRK10762 267 GVN---DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH---EVVTRSPQDGLanGIVYisedrkRDG 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 FIFSGTIIEN-----IRY-----GKLDAtEEEIIAAAKVVRA-------HDFISGLkdgyytevkergstLSAGQRQLIS 497
Cdd:PRK10762 341 LVLGMSVKENmsltaLRYfsragGSLKH-ADEQQAVSDFIRLfniktpsMEQAIGL--------------LSGGNQQKVA 405
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 498 FARALLADPKILILDEATSSID--TQTEI------LLQEGLERLLegrtsfIIAHRLSTIKNSSRIFYIDNGRIQ----- 564
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDvgAKKEIyqlinqFKAEGLSIIL------VSSEMPEVLGMSDRILVMHEGRISgeftr 479
                        250
                 ....*....|
gi 346645039 565 EAGSHEELMA 574
Cdd:PRK10762 480 EQATQEKLMA 489
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
371-575 3.03e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.46  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 371 NFHVDAGESIALVGPTGAGKTTIINLLSrfyninsGE-ILVDGE---NVEEVTLRSLRsQMGVMLQDTFIFSGTiiENIR 446
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALA-------GElPLLSGErqsQFSHITRLSFE-QLQKLVSDEWQRNNT--DMLS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 447 YGKLDA--TEEEII------AAAKVVRAHDF-ISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK10938  93 PGEDDTgrTTAEIIqdevkdPARCEQLAQQFgITALLD-------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 518 IDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK10938 166 LDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
370-544 5.15e-04

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


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.87  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFH-VDAGESIALVGPTGAGKTTIINLLS-RFYninsGEILVDGENVEEVTLRSLRSQ-MGVMLqdTFIFSGTIIENIR 446
Cdd:cd03279   20 IDFTgLDNNGLFLICGPTGAGKSTILDAITyALY----GKTPRYGRQENLRSVFAPGEDtAEVSF--TFQLGGKKYRVER 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 447 YGKLDATeeeiiaaakvvrahDFISG--LKDGYYTEVKERG-STLSAGQRQLISFARAL-LADP---------KILILDE 513
Cdd:cd03279   94 SRGLDYD--------------QFTRIvlLPQGEFDRFLARPvSTLSGGETFLASLSLALaLSEVlqnrggarlEALFIDE 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 346645039 514 ATSSIDTQTEILLQEGLERL-LEGRTSFIIAH 544
Cdd:cd03279  160 GFGTLDPEALEAVATALELIrTENRMVGVISH 191
AAA_17 pfam13207
AAA domain;
383-539 6.52e-04

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 40.30  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  383 VGPTGAGKTTIINLLSRFYN---INSGEIlvdgenveevtLRSLRSQMGvmlqdtfifSGTIIENIRYGKLDATEEEIIA 459
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGfphISAGDL-----------LREEAKERG---------LVEDRDEMRKLPLEPQKELQKL 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  460 AAKVVRAHDFISG-LKDGYYTEVKERGstlsAGQRQLISFARALlaDPKILILdeatssIDTQTEILlqegLERLLEGRT 538
Cdd:pfam13207  61 AAERIAEEAGEGGvIVDGHPRIKTPAG----YLPGLPVEVLREL--KPDAIIL------LEADPEEI----LERRLKDRT 124

                  .
gi 346645039  539 S 539
Cdd:pfam13207 125 R 125
ABC_6TM_McjD_like cd18556
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ...
35-315 1.03e-03

Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.


Pssm-ID: 350000  Cd Length: 298  Bit Score: 41.47  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  35 IYITLFVILLANVATMIGP-YLTKIV--IDDTIPNkNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTA 111
Cdd:cd18556    4 FFSILFISLLSSILISISPvILAKITdlLTSSSSD-SYNYIVVLAALYVITISATKLLGFLSLYLQSSLRVELIISISSS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 IFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVM 191
Cdd:cd18556   83 YFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLFVINN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 192 VIKT------------AQRKAYQVLSNKQSNMNAyihesiagIKVTQSFSREEENFEIF-TEVSNEYRRSWMKAVKIQFL 258
Cdd:cd18556  163 TIFTkkivslrndlmdAGRKSYSLLTDSVKNIVA--------AKQNNAFDFLFKRYEATlTNDRNSQKRYWKLTFKMLIL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 259 lwPGVQNIAVMTTCLIYFVgikgYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSL 315
Cdd:cd18556  235 --NSLLNVILFGLSFFYSL----YGVvngQVSIGHFVLITSYILLLSTPIESLGNMLSEL 288
PLN03073 PLN03073
ABC transporter F family; Provisional
455-519 1.23e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.77  E-value: 1.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 455 EEIIAAAKVVRAHDFISGLKdgYYTEVKERGS-TLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PLN03073 313 ELIDAYTAEARAASILAGLS--FTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
361-424 1.46e-03

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 41.30  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGInfhVDAGESIALVGPTGAGKTTIINLLSRFynINSGEILV-----------------------DGENVEE 417
Cdd:COG4962  169 PEMAEFLRAA---VRARLNILVSGGTGSGKTTLLNALSGF--IPPDERIVtiedaaelqlqhphvvrletrppNVEGAGE 243
                         90
                 ....*....|..
gi 346645039 418 VTLR-----SLR 424
Cdd:COG4962  244 VTLRdlvrnALR 255
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
358-535 2.10e-03

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 39.61  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 358 FRYEEGVDILKGINfhvdagesiALVGPTGAGKTTIIN---------------LLSRFYNINSGEILVDGE-NVEEVTLR 421
Cdd:COG0419   13 YRDTETIDFDDGLN---------LIVGPNGAGKSTILEairyalygkarsrskLRSDLINVGSEEASVELEfEHGGKRYR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQ-------------MGVMLQDtfIFSGTIIENIRyGKLDATEEEIIAAAKVVRAhdfISGLKDGYYTEVKERGS-- 486
Cdd:COG0419   84 IERRQgefaefleakpseRKEALKR--LLGLEIYEELK-ERLKELEEALESALEELAE---LQKLKQEILAQLSGLDPie 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 346645039 487 TLSAGQRQLISFARALLadpkiLILDeaTSSIDtqteillQEGLERLLE 535
Cdd:COG0419  158 TLSGGERLRLALADLLS-----LILD--FGSLD-------EERLERLLD 192
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
377-400 2.14e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 41.13  E-value: 2.14e-03
                         10        20
                 ....*....|....*....|....*
gi 346645039 377 GESIALVGPTGAGKTTII-NLLSRF 400
Cdd:PRK12727 350 GGVIALVGPTGAGKTTTIaKLAQRF 374
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
488-577 2.15e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 41.26  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 488 LSAGQRQLISFARALLADPKILILDEATSSIDTQT-----EILLQegLERlLEGRTSFIIAHRLSTIKNSSRIFYIDNGR 562
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVArdmfwRLLIE--LSR-EDGVTIFISTHFMNEAERCDRISLMHAGR 474
                         90
                 ....*....|....*
gi 346645039 563 IQEAGSHEELMAQHG 577
Cdd:NF033858 475 VLASDTPAALVAARG 489
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
120-326 2.29e-03

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350049 [Multi-domain]  Cd Length: 300  Bit Score: 40.21  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 120 PFSYFDSRPHGKILIRVVNYINMLSDLLSNglinlisdILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRK 199
Cdd:cd18605   89 KMSFFDKTPVGRILNRFSSDVYTIDDSLPF--------ILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 200 AYQVLS--------NKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRS---------WMkAVKIQFLlwpg 262
Cdd:cd18605  161 YYRATSrelkrlnsVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAqlasqaasqWL-SIRLQLL---- 235
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 263 vqNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYvgnfwnpVINIGNFYNSLITATTYLERIF 326
Cdd:cd18605  236 --GVLIVTFVALTAVVQHFFGLSIDAGLIGLALSY-------ALPITGLLSGLLNSFTETEKEM 290
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
487-572 2.41e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 41.15  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  487 TLSAGQRQLISFARALLAD---PKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIfyID--- 559
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYI--IDlgp 906
                          90
                  ....*....|....*...
gi 346645039  560 -----NGRIQEAGSHEEL 572
Cdd:TIGR00630 907 eggdgGGTVVASGTPEEV 924
ABC_6TM_CydC cd18585
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ...
104-295 2.99e-03

Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350029 [Multi-domain]  Cd Length: 290  Bit Score: 39.77  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 104 ILKDMRTAIFGHLQKLP---FSYFDSrphGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSL 180
Cdd:cd18585   66 LLSNLRVWFYRKLEPLAparLQKYRS---GDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILL 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 181 A-LIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLL 259
Cdd:cd18585  143 AgLLLAGVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLS 222
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 346645039 260 WPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFI 295
Cdd:cd18585  223 QALMILLSGLTVWLVLWLGAPLVQNGALDGALLAML 258
PRK01889 PRK01889
GTPase RsgA; Reviewed
361-397 3.46e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 39.92  E-value: 3.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 346645039 361 EEGVDILKGinfHVDAGESIALVGPTGAGKTTIINLL 397
Cdd:PRK01889 182 GEGLDVLAA---WLSGGKTVALLGSSGVGKSTLVNAL 215
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
120-232 3.74e-03

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 39.77  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 120 PFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLtlySLALIPVLFVIVMVIKTAQRK 199
Cdd:cd18606   82 PMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWF---AIALPPLLVLYYFIANYYRAS 158
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 346645039 200 AYQVL---SNKQSNMNAYIHESIAGIKVTQSFSREE 232
Cdd:cd18606  159 SRELKrleSILRSFVYANFSESLSGLSTIRAYGAQD 194
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
488-593 4.04e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 39.79  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 488 LSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQ 564
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTV 238
                         90       100       110
                 ....*....|....*....|....*....|.
gi 346645039 565 EAGSHEELMA--QHGYYYNLYQSQFDMLQAL 593
Cdd:PRK15093 239 ETAPSKELVTtpHHPYTQALIRAIPDFGSAM 269
ABC_6TM_MRP5_8_9_D2 cd18599
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ...
65-240 4.50e-03

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350043 [Multi-domain]  Cd Length: 313  Bit Score: 39.47  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  65 PNKNMTQLfwIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDmrtAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLS 144
Cdd:cd18599   55 PDLNFYQL--VYGGSILVILLLSLIRGFVFVKVTLRASSRLHN---KLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVD 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 145 DLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYsLALIPVLFVIVMVI-KTAQRKAYQVLSNKQSNMNAYIHESIAGIK 223
Cdd:cd18599  130 VRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIA-LIPLAIIFVFLSKIfRRAIRELKRLENISRSPLFSHLTATIQGLS 208
                        170
                 ....*....|....*..
gi 346645039 224 VTQSFSREEENFEIFTE 240
Cdd:cd18599  209 TIHAFNKEKEFLSKFKK 225
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
43-293 5.82e-03

Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.


Pssm-ID: 350031  Cd Length: 293  Bit Score: 38.96  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  43 LLANVATMIGPYLTKIVIDDTIPNKNMTQLfWIAVIFIVSVIVTGLCMRY-RIRSITLIGQDILKDMRTAIFGHLQKLPF 121
Cdd:cd18587   12 LLINLFALASPLFVMNVYDRVVPNNAIETL-WVLAIGVLIALLFDFILKLlRAYFIDVAGKRADVILSSRLFERVLGLRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 122 SyfdSRPhgkilIRVVNYINMLS------DLLSNGLINLISDILSVIVTLGFMLMIDPVLtlyslALIPVLFVIVMVI-- 193
Cdd:cd18587   91 E---ARP-----ASVGSFANNLRefesvrDFFTSATLTALIDLPFVLLFLAVIALIGGPL-----ALVPLVAIPLVLLyg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 194 -------KTAQRKAYQVLSNKqsnmNAYIHESIAGIKVTQSFSREeenfeiftevsNEYRRSWMKAV--------KIQFL 258
Cdd:cd18587  158 lllqkplRRLVEESMRESAQK----NALLVESLSGLETIKALGAE-----------GRMQRRWEEAVaalarsslKSRLL 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 346645039 259 lwpgvQNIAVMTTCLIY---FVGIKGYGV------DVSTGTLIA 293
Cdd:cd18587  223 -----SSSATNFAQFVQqlvTVAIVIVGVylisdgELTMGGLIA 261
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
374-422 7.53e-03

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 37.90  E-value: 7.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 346645039 374 VDAGESIALVGPTGAGKTTIINLLSRFynINSGEILVDGENVEEVTLRS 422
Cdd:cd01130    9 VRARKNILISGGTGSGKTTLLNALLSF--IPPDERIVTIEDTRELQLPH 55
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
39-210 9.73e-03

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.


Pssm-ID: 350025 [Multi-domain]  Cd Length: 300  Bit Score: 38.38  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039  39 LFVILLANVATMIGPYLTKIVIDD-TIPNKNMTQLFWIAVIFIVSVIV---------TGLCMRYRIRSITLIGQDILKDM 108
Cdd:cd18581    2 LLLLAAGRVVNVLVPILYKKIVDSlTPDSADSPLAFPWALILLYVFLKflqgggsgsVGLLSNLRSFLWIPVQQFTTREI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 109 RTAIFGHLQKLPFSYFDSRPHGKILiRVVNY-INMLSDLLSNGLINLISDILSVIVTLGFML-MIDPVLTLYSLALIpVL 186
Cdd:cd18581   82 SVKLFAHLHSLSLRWHLSRKTGEVL-RVMDRgTSSINSLLSYVLFNIGPTIADIIIAIIYFAiAFNPWFGLIVFVTM-AL 159
                        170       180
                 ....*....|....*....|....
gi 346645039 187 FVIVMVIKTAQRKAYQVLSNKQSN 210
Cdd:cd18581  160 YLILTIIITEWRTKFRREMNKLDN 183
 
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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